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looked for 5α-R2 expression in fetal liver, adrenal, testis, ovary, brain, scalp, chest, and genital skin, using immunoblotting, and were only able to find it in genital skin. After birth, the 5α-R1 is expressed in more locations, including the liver, skin, scalp and prostate. 5α-R2 is expressed in prostate, seminal vesicles, epididymis, liver, and to a lesser extent the scalp and skin. Hepatic expression of both 5α-R1 and 2 is immediate, but disappears in the skin and scalp at month 18. Then, at puberty, only 5α-R2 is reexpressed in the skin and scalp. 5α-R1 and 5α-R2 appear to be expressed in the prostate in male fetuses and throughout postnatal life. 5α-R1 and 5α-R2 are also expressed, although to different degrees in liver, genital and nongenital skin, prostate, epididymis, seminal vesicle, testis, ovary, uterus, kidney, exocrine pancreas, and the brain. In adulthood, 5α-R1-3 is ubiquitously expressed. == Substrates == Specific substrates include testosterone, progesterone, androstenedione, epitestosterone, cortisol, aldosterone, and deoxycorticosterone. Outside of dihydrotestosterone, much of the physiological role of 5α-reduced steroids is unknown. Beyond reducing testosterone to dihydrotestosterone, 5alpha-reductase enzyme isoforms I and II reduce progesterone to dihydroprogesterone (DHP) and deoxycorticosterone to dihydrodeoxycorticosterone (DHDOC). In vitro and animal models suggest subsequent 3alpha-reduction of DHT, DHP and DHDOC lead to steroid metabolites with effects on cerebral function achieved by enhancing GABAergic inhibition. These neuroactive steroid derivatives enhance GABA via allosteric modulation at GABA(A) receptors and have anticonvulsant, antidepressant and anxiolytic effects, and also alter sexual and alcohol related behavior. 5α-dihydrocortisol is present in the aqueous humor of the eye, is synthesized in the lens, and might help make the aqueous humor itself. Allopregnanolone and THDOC are neurosteroids, with the latter having effects on the susceptibility of animals to seizures. In socially isolated mice, 5α-R1 is specifically down-regulated in glutamatergic pyramidal neurons that
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converge on the amygdala from cortical and hippocampal regions. This down-regulation may account for the appearance of behavioral disorders such as anxiety, aggression, and cognitive dysfunction. 5α-dihydroaldosterone is a potent antinatriuretic agent, although different from aldosterone. Its formation in the kidney is enhanced by restriction of dietary salt, suggesting it may help retain sodium as follows: Substrate + NADPH + H + ⟶ 5 α − substrate + NADP + {\displaystyle {\ce {{Substrate}+{NADPH}+H+->{5\alpha -substrate}+NADP+}}} 5α-DHP is a major hormone in circulation of normal cycling and pregnant women. === Testosterone === 5α-Reductase is most known for converting testosterone, the male sex hormone, into the more potent dihydrotestosterone: The major difference is the Δ4,5 double-bond on the A (leftmost) ring. The other differences between the diagrams are unrelated to structure. === List of conversions === The following reactions are known to be catalyzed by 5α-reductase: Cholestenone → 5α-Cholestanone Progesterone → 5α-Dihydroprogesterone 3α-Dihydroprogesterone → Allopregnanolone 3β-Dihydroprogesterone → Isopregnanolone Deoxycorticosterone → 5α-Dihydrodeoxycorticosterone Corticosterone → 5α-Dihydrocorticosterone Aldosterone → 5α-Dihydroaldosterone Androstenedione → 5α-Androstanedione Testosterone → 5α-Dihydrotestosterone Nandrolone → 5α-Dihydronandrolone == Structure == 5α-Reductase is a membrane bound enzyme that catalyzes the NADPH dependent reduction of double bonds in steroid substrates to increase potency. The crystal structure of a homolog of 5α-reductase isoenzymes 1 and 2 has been found in Proteobacteria (proteobacteria 5α-reductase). This exists as a monomer with a seven alpha-helix transmembrane structure housing a hydrophobic pocket that holds cofactor NADPH and monoolein which occupies the steroid substrate binding pocket. In insect cells monoolein is not found, but is subbed out for other androgens and inhibitors. The integral seven transmembrane topology is likely conserved across species, with the N terminus in the endoplasmic reticulum lumen and the C terminus facing the cytosol. High conformational dynamics of the cytosolic region likely regulate NADPH/NADP+ exchange. Sequence conservation across
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"page_id": 1245377,
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known crystal structures has corroborated high conservation in enzyme structure. In the 5α-reductase from Proteobacteria bacterium, PbSRD5A, NADPH is bound by an extensive hydrogen bonding network, including residues Arg34, which hydrogen bonds to the nicotinamide group, Arg170, which hydrogen bonds to the 2'-phosphate on the ribose group bound to nicotinamide, Asn192 and His230, which hydrogen bond to the nicotinamide nucleotide phosphate group, Tyr32 and Tyr193, which hydrogen bond to the adenine nucleotide phosphate group, and Asn159, Glu196, and Thr219, which hydrogen bond to the adenine group of NADPH. The steroid-binding pocket contains a motif of Gln, Glu, and Tyr residues, which form a triad of hydrogen-bonds, which coordinate the C3 ketone of steroids into close proximity to the nicotinamide of NADPH, which allows a hydride transfer and Δ4 double-bond reduction. These residues are Gln53, Glu54, and Tyr87 in PbSRD5A. == Inhibition == The mechanism of 5α reductase inhibition is complex, but involves the binding of NADPH to the enzyme followed by the substrate. 5α-Reductase inhibitor drugs are used in benign prostatic hyperplasia, prostate cancer, pattern hair loss (androgenetic alopecia), and hormone replacement therapy for transgender women. Inhibition of the enzyme can be classified into two categories: steroidal, which are irreversible, and nonsteroidal. There are more steroidal inhibitors, with examples including finasteride (MK-906), dutasteride (GG745), 4-MA, turosteride, MK-386, MK-434, and MK-963. Researchers have pursued synthesis of nonsteroidals to inhibit 5α-reductase due to the undesired side effects of steroidals. The most potent and selective inhibitors of 5α-R1 are found in this class, and include benzoquinolones, nonsteroidal aryl acids, butanoic acid derivatives, and more recognizably, polyunsaturated fatty acids (especially linolenic acid), zinc, and green tea. Riboflavin was also identified as a 5α-reductase inhibitor . Additionally, it has been claimed that alfatradiol works through this mechanism of activity (5α-reductase), as well as the Ganoderic
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{
"page_id": 1245377,
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acids in lingzhi mushroom, and the Saw Palmetto. Inhibition of 5α-reductase results in decreased conversion of testosterone to DHT, leading to increased testosterone and estradiol. Other enzymes compensate to a degree for the absent conversion, specifically with local expression at the skin of reductive 17β-hydroxysteroid dehydrogenase, oxidative 3α-hydroxysteroid dehydrogenase, and 3β-hydroxysteroid dehydrogenase enzymes. Gynecomastia, erectile dysfunction, impaired cognitive function, fatigue, hypoglycemia, impaired liver function, constipation, and depression, are only a few of the possible side-effects of 5α-reductase inhibition. Long term side effects, that continued even after discontinuation of the drug have been reported. === Finasteride === Finasteride inhibits two 5α-reductase isoenzymes (II and III), while dutasteride inhibits all three. Finasteride potently inhibits 5α-R2 at a mean inhibitory concentration IC50 of 69 nM, but is less effective with 5α-R1 with an IC50 of 360 nM. Finasteride decreases mean serum level of DHT by 71% after 6 months, and was shown in vitro to inhibit 5α-R3 at a similar potency to 5α-R2 in transfected cell lines. === Dutasteride === Dutasteride inhibits 5α-reductase isoenzymes type 1 and 2 better than finasteride, leading to a more complete reduction in DHT at 24 weeks (94.7% versus 70.8%). It also reduces intraprostatic DHT 97% in men with prostate cancer at 5 mg/day over three months. A second study with 3.5 mg/day for 4 months decreased intraprostatic DHT even further by 99%. The suppression of DHT in vivo, and the report that dutasteride inhibits 5α-R3 in vitro suggest that dutasteride may be a triple 5α reductase inhibitor. == Congenital deficiencies == === 5α-Reductase 1 === 5α-Reductase type 1 inactivated male mice have reduced bone mass and forelimb muscle grip strength, which has been proposed to be due to lack of 5α-reductase type 1 expression in bone and muscle. In 5 alpha reductase type 2 deficient males, the
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"page_id": 1245377,
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type 1 isoenzyme is thought to be responsible for their virilization at puberty. === 5α-Reductase 2 === Impaired 5α-reductase 2 activity can result from mutations in the underlying SRD5A2 gene. The condition, known as 5α-reductase 2 deficiency, has a range of presentations as atypical appearances of the external genitalia in males. This is because 5α-reductase 2 catalyzes the transformation of testosterone to the potent androgen dihydrotestosterone, which is required for the proper masculinization of male genitalia. === 5α-Reductase 3 === When small interfering RNA is used to knock down the expression of 5α-R3 isozyme in cell lines, there is decreased cell growth, viability, and a decrease in DHT/T ratios. It has also shown the ability to reduce testosterone, androstenedione, and progesterone in androgen stimulated prostate cell lines by adenovirus vectors. Congenital deficiency of 5α-R3 at the gene SRD53A has been linked to a rare, autosomal recessive condition in which patients are born with severe intellectual dysfunction and cerebellar and ocular defects. The presumed deficiency is reduction of the terminal bond of polyprenol to dolichol, an important step in N-glycosylation of proteins, which in turn is important for proper folding of asparagine residues on nascent protein in the endoplasmic reticulum. == Nervous system == === Affective disorders === Isolation rearing has been shown to lower protein expression of 5α-reductase isoenzymes 1 and 2 in cortical and subcortical brain regions of rat models. However, the amount of 5α-reduced metabolite remained unaffected. This means isolation rearing likely leads to changes in the expression and activity of 5α-reductase in the brain, leading to dysregulation of dopamine neurotransmission, resulting in early chronic stress Treatment with finasteride, a 5α-reductase inhibitor, has been shown to mimic the effects of SSRI's causing sexual dysfunction. Research has shown that 5α-reductase is the rate-limiting enzyme in neurosteroid synthesis, specifically in
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{
"page_id": 1245377,
"source": null,
"title": "5α-Reductase"
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the conversion of progesterone to allopregnanolone, low levels of allopregnanolone has been tied to depression, anxiety and schizophrenia. Sleep deprivation can enhance 5α-reductase expression and activity in the prefrontal cortex, leading to mania-related symptoms in rats. It is also contested whether the use of 5α-reductase inhibitors is associated with suicidal ideation and depression in patient populations who use them for benign prostatic hyperplasia. These symptoms have been found during active use of inhibitors and in immediate followup. However, it is unknown if these symptoms arise naturally from benign prostatic hyperplasia. === Hypothalamic–pituitary–adrenal axis dysfunction === An alternative mechanism of cortisol regulation is regulated via 5α-reductase which catalyzes an A-ring reduction of cortisol, metabolizing the compound. Type 1 and 2 of 5α-reductase are the principal enzymes involved in cortisol clearance through the liver. Excess cortisol has been tied to metabolic dysfunction–associated steatotic liver disease (MASLD), but in-vitro studies have found that an over expression of 5α-reductase type 2 can suppress lipogenesis. The key role of 5α-reductase in cortisol breakdown and fat buildup has elucidated some of the side effects of 5α-reductase inhibitors. In randomized studies on human volunteers it was found that 5α-reductase inhibition through the use of dutasteride and finasteride can lead to hepatic lipid accumulation in men. In critical illness, overstimulation of cortisol as part of a stress response can lead to decreased clearance of cortisol through the liver via 5α-reductase and kidneys via 11β-hydroxysteroid dehydrogenase type 2, longterm elevation of cortisol can lead to Cushing's syndrome. == Nomenclature == This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-oxo-5α-steroid:acceptor Δ4-oxidoreductase. Other names in common use include: 5α-Reductase 3-Oxosteroid Δ4-dehydrogenase 3-Oxo-5α-steroid Δ4-dehydrogenase Steroid Δ4-5α-reductase Δ4-3-Keto steroid 5α-reductase Δ4-3-Oxo
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steroid reductase Δ4-3-Ketosteroid-5α-oxidoreductase Δ4-3-Oxosteroid-5α-reductase 3-Keto-Δ4-steroid-5α-reductase Testosterone 5α-reductase 4-Ene-3-ketosteroid-5α-oxidoreductase Δ4-5α-Dehydrogenase 3-Oxo-5α-steroid:(acceptor) Δ4-oxidoreductase == See also == Steroidogenic enzyme Acne vulgaris Cholestenone 5α-reductase Hirsutism Lower urinary tract symptoms Polycystic ovarian syndrome List of steroid metabolism modulators == References == == Further reading == == External links == Testosterone+5-alpha-Reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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"page_id": 1245377,
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A terricolous lichen is a lichen that grows on the soil as a substrate. Examples include some members of the genus Peltigera. == References ==
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"page_id": 5570754,
"source": null,
"title": "Terricolous lichen"
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Fever of unknown origin (FUO) refers to a condition in which the patient has an elevated temperature (fever) for which no cause can be found despite investigations by one or more qualified physicians. If the cause is found, it is usually a diagnosis of exclusion, eliminating all possibilities until only the correct explanation remains. == Causes == Worldwide, infection is the leading cause of FUO, with prevalence varying by country and geographic region. Extrapulmonary tuberculosis is the most frequent cause of FUO. Drug-induced hyperthermia, as the sole symptom of an adverse drug reaction, should always be considered. Disseminated granulomatoses such as tuberculosis, histoplasmosis, coccidioidomycosis, blastomycosis and sarcoidosis are associated with FUO. Lymphomas are the most common cause of FUO in adults. Thromboembolic disease (i.e. pulmonary embolism, deep venous thrombosis) occasionally shows fever. Although infrequent, its potentially lethal consequences warrant evaluation of this cause. Endocarditis, although uncommon, is possible. Bartonella infections are also known to cause fever of unknown origin. Human herpes viruses are a common cause of fever of unknown origin with one study showing Cytomegalovirus, Epstein–Barr virus, human herpesvirus 6 (HHV-6), human herpesvirus 7 (HHV-7) being present in 15%, 10%, 14% and 4.8% respectively with 10% of people presenting with co-infection (infection with two or more human herpes viruses). Infectious mononucleosis, most commonly caused by EBV, may present as a fever of unknown origin. Other symptoms of infectious mononucleosis vary with age with middle-aged adults and the elderly more likely to have a longer duration of fever and leukopenia, and younger adults and adolescents more likely to have splenomegaly, pharyngitis and lymphadenopathy. Endemic mycoses such as histoplasmosis, blastomycosis, coccidioidomycosis, and paracoccidioidomycosis can cause a fever of unknown origin in immunocompromised as well as immunocompetent people. These endemic mycoses may also present with pulmonary symptoms or extra-pulmonary symptoms such as
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"page_id": 4587713,
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B symptoms (such as fevers, chills, night sweats, and unexplained weight loss). The endemic mycotic infection talaromycosis primarily affects those who are immunocompromised. Invasive opportunistic mycoses may also occur in immunocompromised people; these include aspergillosis, mucormycosis, Cryptococcus neoformans. Cancer can also cause fever of unknown origin. This is thought to be due to release of pyrogenic cytokines from cancer cells as well as due to spontaneous tumor necrosis (sometimes with secondary infections). The cancer types most associated with fever of unknown origin include renal cell carcinoma, lymphoma, liver cancer, ovarian cancer atrial myxoma and Castleman disease. In those with HIV currently being treated with antiretroviral therapy and with a low or undetectable viral load; causes of fever of unknown origin are usually not associated with HIV infection. But in those with AIDS, with high viral loads, viral replication, and immune compromise; cancers and opportunistic infection are the most common cause of FUO. Approximately 2 weeks after initial HIV infection, with viral loads being high, an acute retroviral syndrome can present with fevers, rash and mono-like symptoms. Immune reconstitution inflammatory syndrome is a common cause of FUO when a previously suppressed immune system is re-activated. The newly active immune system often has an exaggerated response against opportunistic pathogens leading to a fever and other inflammatory symptoms. Immune reconstitution syndrome commonly presents after microbiological control of infection (in cases of immune-suppressing pathogens such as HIV) but the syndrome may also present after organ transplant, in the post-partum state, with formerly neutropenic hosts or withdrawing anti-TNF therapy. Auto-inflammatory and auto-immune disorders account for approximately 5-32% of fevers of unknown origin. These can be classified as purely auto-inflammatory disorders (disorders of innate immunity, with dysregulated interleukin 1 beta and/or IL-18 responses), purely auto-immune disorders (in which the adaptive immunity is dysregulated, with a dysregulated
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{
"page_id": 4587713,
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"title": "Fever of unknown origin"
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type 1 interferon response) or disorders with mixed features. Rheumatoid arthritis or adult-onset Still's disease have mixed features and are common causes of FUO. === Infection === === Neoplasm === Although most neoplasms can present with fever, malignant lymphoma is by far the most common diagnosis of FUO among the neoplasms. In some cases the fever even precedes lymphadenopathy detectable by physical examination. === Noninfectious inflammatory diseases === === Miscellaneous conditions === === Inherited and metabolic diseases === === Thermoregulatory disorders === == Diagnosis == A comprehensive and meticulous history (i.e. illness of family members, recent visit to the tropics, medication), repeated physical examination (i.e. skin rash, eschar, lymphadenopathy, heart murmur) and myriad laboratory tests (serological, blood culture, immunological) are the cornerstone of finding the cause. Other investigations may be needed. Ultrasound may show cholelithiasis, echocardiography may be needed in suspected endocarditis and a CT-scan may show infection or malignancy of internal organs. Another technique is Gallium-67 scanning which seems to visualize chronic infections more effectively. Invasive techniques (biopsy and laparotomy for pathological and bacteriological examination) may be required before a definite diagnosis is possible. Positron emission tomography using radioactively labelled fluorodeoxyglucose (FDG) has been reported to have a sensitivity of 84% and a specificity of 86% for localizing the source of fever of unknown origin. Despite all this, diagnosis may only be suggested by the therapy chosen. When a patient recovers after discontinuing medication it likely was drug fever, when antibiotics or antimycotics work it probably was infection. Empirical therapeutic trials should be used in those patients in which other techniques have failed. === Definition === There is no universal agreement with regards to time criteria or other diagnostic criteria to diagnose a fever of unknown origin and various definitions have been used. In 1961 Petersdorf and Beeson suggested
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"page_id": 4587713,
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the following criteria: Fever higher than 38.3 °C (101 °F) on several occasions Persisting without diagnosis for at least 3 weeks At least 1 week's investigation in hospital A new definition which includes the outpatient setting (which reflects current medical practice) is broader, stipulating: 3 outpatient visits or 3 days in the hospital without elucidation of a cause or 1 week of "intelligent and invasive" ambulatory investigation. Presently FUO cases are codified in four subclasses. ==== Classic ==== This refers to the original classification by Petersdorf and Beeson. Studies show there are five categories of conditions: infections (e.g. abscesses, endocarditis, tuberculosis, and complicated urinary tract infections), neoplasms (e.g. lymphomas, leukaemias), connective tissue diseases (e.g. temporal arteritis and polymyalgia rheumatica, Still's disease, systemic lupus erythematosus, and rheumatoid arthritis), miscellaneous disorders (e.g. alcoholic hepatitis, granulomatous conditions), and undiagnosed conditions. ==== Nosocomial ==== Nosocomial FUO refers to pyrexia in patients that have been admitted to hospital for at least 24 hours. This is commonly related to hospital-associated factors such as surgery, use of a urinary catheter, intravascular devices (i.e. "drip", pulmonary artery catheter), drugs (antibiotic-induced Clostridioides difficile colitis, drug fever), and/or immobilization (decubitus ulcers). Sinusitis in the intensive care unit is associated with nasogastric and orotracheal tubes. Other conditions that should be considered are deep-vein thrombophlebitis, pulmonary embolism, transfusion reactions, acalculous cholecystitis, thyroiditis, alcohol/drug withdrawal, adrenal insufficiency, and pancreatitis. ==== Immune-deficient ==== Immunodeficiency can be seen in patients receiving chemotherapy or in hematologic malignancies. Fever is concomitant with neutropenia (neutrophil <500/uL) or impaired cell-mediated immunity. The lack of immune response masks a potentially dangerous course. Infection is the most common cause. ==== Human immunodeficiency virus (HIV)-associated ==== HIV-infected patients are a subgroup of the immunodeficient FUO, and frequently have fever. The primary phase shows fever since it has a mononucleosis-like illness. In advanced
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"page_id": 4587713,
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stages of infection fever mostly is the result of a superimposed infections. == Treatment == Unless the patient is acutely ill, no therapy should be started before the cause has been found. This is because non-specific therapy is rarely effective and may delay the diagnosis. An exception is made for neutropenic (low white blood cell count) patients or patients who are severely immunocompromised in which delay could lead to serious complications. After blood cultures are taken this condition is aggressively treated with broad-spectrum antibiotics. Antibiotics are adjusted according to the results of the cultures taken. HIV-infected people with pyrexia and hypoxia will be started on medication for possible Pneumocystis jirovecii infection. Therapy is adjusted after a diagnosis is made. == Prognosis == Since there is a wide range of conditions associated with FUO, prognosis depends on the particular cause. If after six to twelve months no diagnosis is found, the chances of ever finding a specific cause diminish. Under those circumstances, the prognosis is good. == See also == Chronic fatigue syndrome Encephalitis lethargica Idiopathic chronic fatigue Idiopathic disease == References == == External links ==
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"page_id": 4587713,
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"title": "Fever of unknown origin"
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In science fiction and fantasy literatures, the term insectoid ("insect-like") denotes any fantastical fictional creature sharing physical or other traits with ordinary insects (or arachnids). Most frequently, insect-like or spider-like extraterrestrial life forms is meant; in such cases convergent evolution may presumably be responsible for the existence of such creatures. Occasionally, an earth-bound setting — such as in the film The Fly (1958), in which a scientist is accidentally transformed into a grotesque human–fly hybrid, or Kafka's famous novella The Metamorphosis (1915), which does not bother to explain how a man becomes an enormous insect — is the venue. == Etymology == The term insectoid denotes any creature or object that shares a similar body or traits with common earth insects and arachnids. The term is a combination of "insect" and "-oid" (a suffix denoting similarity). == History == Insect-like extraterrestrials have long been a part of the tradition of science fiction. In the 1902 film A Trip to the Moon, Georges Méliès portrayed the Selenites (moon inhabitants) as insectoid. The Woggle-Bug appeared in L. Frank Baum's Oz books beginning in 1904. Olaf Stapledon incorporates insectoids in his 1937 Star Maker novel. In the pulp fiction novels, insectoid creatures were frequently used as the antagonists threatening the damsel in distress. Notable later depictions of hostile insect aliens include the antagonistic "Arachnids", or "Bugs", in Robert A. Heinlein's novel Starship Troopers (1959) and the "buggers" in Orson Scott Card's Ender's Game series (from 1985). The hive mind, or group mind, is a theme in science fiction going back to the alien hive society depicted in H. G. Wells's The First Men in the Moon (1901). Hive minds often imply a lack, or loss, of individuality, identity, or personhood. The individuals forming the hive may specialize in different functions, in the manner
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"page_id": 6422724,
"source": null,
"title": "Insectoids in science fiction and fantasy"
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of social insects. The hive queen has been a figure in novels including C. J. Cherryh's Serpent's Reach (1981) and the Alien film franchise (from 1979). Insectoid sexuality has been addressed in Philip Jose Farmer's The Lovers (1952) Octavia Butler's Xenogenesis novels (from 1987) and China Miéville's Perdido Street Station (2000). == Analysis == The motif of the insect became widely used in science fiction as an "abject human/insect hybrids that form the most common enemy" in related media. Bugs or bug-like shapes have been described as a common trope in them, and the term 'insectoid' is considered "almost a cliche" with regards to the "ubiquitous way of representing alien life". In expressing his ambivalence with regard to science fiction, insectoids were on his mind when Carl Sagan complained of the type of story which "simply ignores what we know of molecular biology and Darwinian evolution.... I have...problems with films in which spiders 30 feet tall are menacing the cities of earth: Since insects and arachnids breathe by diffusion, such marauders would asphyxiate before they could savage their first metropolis". == Examples == A wide range of different fiction has featured different insectoids ranging from characters and races: === Literature === Science fiction writer Bob Olsen (1884–1956) wrote a sequence of short stories, two of which involve humans experiencing the life of ants ("The Ant with the Human Soul", Amazing Stories Quarterly, Spring/Summer 1932 and "Perils Among the Drivers", Amazing Stories, March 1934) and one ("Six-Legged Gangsters", Amazing Stories, June 1935) told from the ants' point of view. L. Sprague de Camp's novel Rogue Queen (1951), describes the methods of procreation and social mores in a humanoid society patterned after bees. === Comics === ==== Marvel Comics ==== The Arthrosians The Brood Bug The Chr'Ylites The Horde Human Fly The
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"title": "Insectoids in science fiction and fantasy"
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Klklk The Kt'kn The Sakaaran Natives Miek The Sligs The Sm'ggani The Vrellnexians ==== DC Comics ==== The Bugs of New Genesis Forager Mantis Charaxas The Circadians The Freshishs Hellgrammite Insect Queen The Kwai The Progeny Red Bee II The Tchk-Tchkii The Tyreans ==== Image Comics ==== The Thraxans === Games === The Tyranids from Warhammer 40,000 The Grekka Targs and Skrashers from StarTopia The Thri-kreen from Dungeons & Dragons and especially the Dark Sun and Spelljammer settings, "praying mantis man" appearing as antagonists and a player character race. The Rachni from Mass Effect The Zerg from StarCraft The Bugs from Helldivers and the Terminids from Helldivers 2. === Films === The Bugs from Men in Black The Bugs from Starship Troopers The Wasp Woman from Monkeybone The Xenomorph from the Alien franchise === Television === Beetlemon and Stingmon from the Digimon franchise Buzz-Off and Webstor from Masters of the Universe The Empress of the Racknoss, the Malmooth, the Time Beetle, the Vespiform, the Viperox, the Wiirn, and the Zarbi from Doctor Who The Irkens from Invader ZIM Stingfly from A.T.O.M. Sweet-Bee from She-Ra: Princess of Power The Xindi-Insectoids from Star Trek: Enterprise == See also == Bug-eyed monster Insects in mythology Insects in religion List of fictional arthropods List of reptilian humanoids List of piscine and amphibian humanoids == References == == External links ==
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"page_id": 6422724,
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Hosaka–Cohen transformation (also called H–C transformation) is a mathematical method of converting a particular two-dimensional scalar magnetic field map to a particular two-dimensional vector map. The scalar field map is of the component of magnetic field which is normal to a two-dimensional surface of a volume conductor; this volume conductor contains the currents producing the magnetic field. The resulting vector map, sometimes called "an arrowmap" roughly mimics those currents under the surface which are parallel to the surface, which produced the field. Therefore, the purpose in performing the transformation is to allow a rough visualization of the underlying, parallel currents. The transformation was proposed by Cohen and Hosaka of the biomagnetism group at MIT, then was used by Hosaka and Cohen to visualize the current sources of the magnetocardiogram. Each arrow is defined as: a → = ∂ B z ∂ y x ^ − ∂ B z ∂ x y ^ {\displaystyle {\vec {a}}={\partial Bz \over \partial y}{\hat {x}}-{\partial Bz \over \partial x}{\hat {y}}} where x {\displaystyle x} of the local x , y , z {\displaystyle x,y,z} coordinate system is normal to the volume conductor surface, x ^ {\displaystyle {\hat {x}}} and y ^ {\displaystyle {\hat {y}}} are unit vectors, and B z {\displaystyle Bz} is the normal component of magnetic field. This is a form of two-dimensional gradient of the scalar quantity B z {\displaystyle Bz} and is rotated by 90° from the conventional gradient. Almost any scalar field, magnetic or otherwise, can be displayed in this way, if desired, as an aid to the eye, to help see the underlying sources of the field. == See also == Biomagnetism Bioelectromagnetism Electrophysiology Magnetic field Magnetocardiography Magnetometer == Notes == == Further reading == Koch, H. (2004). "Recent advances in magnetocardiography". Journal of Electrocardiology. 37: 117–122. doi:10.1016/j.jelectrocard.2004.08.035. PMID
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{
"page_id": 13631685,
"source": null,
"title": "Hosaka–Cohen transformation"
}
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15534820.
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{
"page_id": 13631685,
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"title": "Hosaka–Cohen transformation"
}
|
Cecotropes (also caecotropes, cecotrophs, caecotrophs, cecal pellets, soft feces, or night feces) are a nutrient-filled package created in the gastrointestinal (GI) tract that is expelled and eaten by many animals (such as rabbits, guinea pigs, mice, hamsters, and chinchillas) to obtain more nutrients out of their food. When food passes through the GI tract the first time, the stomach and the small intestine digest the food material, which then moves into the colon, where the food particles are sorted by size. The smaller particles of fiber are moved into the cecum where they are fermented by microbes. This creates useable nutrients which are stored and expelled in cecotropes. The nutrients from the cecotropes are absorbed in the small intestine. The nutrients gained from cecotrophy include short-chain fatty acids, vitamin B, sodium, potassium, amino acids, and protein. Lagomorphs (a grouping including rabbits, hares, and pikas) are perhaps the most well-known for producing and eating cecotropes, but other monogastric fermenters, such as rodents, also produce cecotropes. Rodents including beavers, guinea pigs, mice, hamsters, and chinchillas are known cecotrophs. Other animals also eat cecotropes, such as the common ringtail possum and the coppery ringtail possum. The act of eating cecotropes is referred to as cecotrophy, which is distinct from coprophagy which is the eating of feces proper. Similarly, cecotropes are not fecal material, so terms such as "soft feces" and "night feces" are technically incorrect. Though cecotropes are sometimes called "night feces," they are produced throughout the day and night. == Description == Cecotropes are a group of small balls clumped together that look like a thin blackberry, which exit the anus all at once. They are dark, odorous, sticky and full of nutrition. Cecotropes differ from regular feces which are larger, exit the anus one at a time, smell only slightly, have
|
{
"page_id": 3604676,
"source": null,
"title": "Cecotrope"
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|
very little moisture, and are a waste product. == Development of cecotropes == Many cecotrophs, such as rabbits, are monogastric digesters and herbivores. The majority of food absorption occurs in the small intestine, which makes up roughly 12% of the GI tract in rabbits. Any material not yet digested enters the proximal colon. In lagomorphs, a unique structure called the fusus coli separates the proximal and distal colon and regulates the separation of food material. Food particles greater than 0.3 to 0.5 millimeters (mm) are pushed down the colon through peristalsis. These larger particles consist of mostly non-fermentable materials. Meanwhile particles less than 0.3 to 0.5 mm, which predominantly consist of fermentable fibers and proteins, are moved back into the colon and cecum through retrograde peristalsis. The ileocecal valve located at the end of the small intestine ensures the material goes to the cecum and not the small intestine. Mammalian enzymes cannot break down fiber. However, microbes in the cecum have enzymes that are capable of breaking down fiber. The microbes in a rabbit's gut include bacteria (such as the genera Bacteroides, Bifidobacterium, Clostridium, Streptococcus, and Enterobacter, among others) protozoa, yeasts, and amoeba. The anaerobic fermentation in the cecum breaks down the fiber into useable food for the animal. It is also used as food for the proliferating microbes. The results of the fermentation are volatile fatty acids (VFAs), all of the B vitamins, vitamin K, microbial proteins, essential amino acids and minerals. Some of the other nutrients are also absorbed by the cecum and the colon. Four to nine hours after a meal, the cecum empties and the contents, which containing the results of fermentation along with microbes, continue down the colon. The material from the cecum is formed into cecotropes in the fusus coli, where it contracts more
|
{
"page_id": 3604676,
"source": null,
"title": "Cecotrope"
}
|
gently than when forming regular feces. Goblet cells in the fusus coli secrete mucus which covers the cecotropes, protecting them from the acidity of the stomach. The enzyme lysozyme also aids in the digestion of microbial proteins. Cecotropes continue through the colon and rectum and are expelled through the anus about eight hours after eating. == Reingestion == Cecotropes are eaten directly from the anus. They usually do not touch the ground. They are not chewed; instead, they are swallowed whole so the mucus is not disturbed. They are held in the fundic region of the stomach for 3 to 6 hours where they continue to ferment. Once that is complete, they move into the small intestine where the nutrients are absorbed, about 17 hours after the original meal. == Benefits of cecotrophy == === Nutrient reabsorption === Many herbivores have a diet that is low in nutrition and high in fiber (which is a non-starch polysaccharide carbohydrate). Fiber can be either soluble (pectins and gums) or insoluble (cellulose, hemicellulose and lignocellulose). A simple gastrointestinal tract is not capable of extracting enough nutrients for these animals. One strategy to get the needed nutrition is used by ruminants in which they chew cud in order to process their food a second time. Another strategy used by horses is to have an elongated colon to increase the time spent during digestion and absorption. Both of these strategies add substantial bulk to the animal. Since the rabbit is at the bottom of the food chain, it must be nimble in order to out run its many predators. Creating cecotropes is a way to get more nutrients out of their food without adding a lot of bulk to their GI tract (which is 10% - 20% of their body weight). Since their colons do
|
{
"page_id": 3604676,
"source": null,
"title": "Cecotrope"
}
|
not absorb the nutrients in the cecotropes, they reingest them so they can be absorbed in the small intestine. === Gain of gut microbiota === The process of cecotrophy begins when a rabbit is a newborn. Since the gastrointestinal tract of newborn rabbits is sterile and contains no microbes, the infants consume their mothers' cecotropes and feces to obtain mictrobes needed to build their cecum's microbial community. Once the infant is around 20 days of age, they begin to consume their own cecotropes. == Disorder == It is essential to maintain a balanced microbiome in the gastrointestinal tract, especially the cecum. If beneficial microbes decrease and harmful microbes proliferate, the microbiome becomes unbalanced, which is called dysbiosis. The cause of this includes a diet too high in carbohydrates and/or too low in indigestible fiber; toxins; some medications such as antibiotics; dehydration; extreme stress; dental disease and other systemic diseases (e.g., liver or kidney disease). If the balance is not maintained, there can be multiple health issues, including GI stasis, which can lead to pain, stress and death. A few cecotropes left on the ground of the living area of the animal is not cause for concern. However, if a large amount is found on the ground or stuck to the fur, a veterinarian should be consulted. Possible causes are poor diet, dental issues, arthritis, very large dewlap, obesity, or too-long fur in the anal region. If the cecotropes are similar to pudding in consistency, it is called intermittent soft cecotropes (ISC). This is different from true diarrhea, which has no form, is completely watery and is very serious. If regular feces are also produced, it is not diarrhea. ISC will stick to the hindquarters and feet of the animal and to places in the living area. Causes are a poor
|
{
"page_id": 3604676,
"source": null,
"title": "Cecotrope"
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|
diet (too many carbohydrates, too little fiber) or inappropriate antibiotics. Treatment is to feed unlimited grass hay, greens and limited pellets and to stop giving inappropriate antibiotics. == References == == External links == GI tract diagram Diagram of gastrointestinal tract of rabbit; note cecum/caecum GI tract diagram Diagram of gastrointestinal tract of rabbit; note ileocecal valve and sacculus rotundus
|
{
"page_id": 3604676,
"source": null,
"title": "Cecotrope"
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|
Don Misener (A.D. Misener) (1911–1996) was a physicist. Along with Pyotr Leonidovich Kapitsa and John F. Allen, Misener discovered the superfluid phase of matter in 1937. Misener was a graduate student at the University of Toronto in 1935. He joined Allen at Cambridge University in about 1937. Misener later returned to Canada to work at the University of Western Ontario. == Journal references == E. F. Burton, J. O. Wilhelm, and A. D. Misener, Trans. Roy. Soc. Can. 28(111) p. 65 (1934) J. F. Allen and A. D. Misener, Flow of Liquid Helium II, Nature 141(3558) p. 75 (8 Jan 1938) doi:10.1038/141075a0 A. D. Misener, The Specific Heat of Superconducting Mercury, Indium and Thallium, Proceedings of the Royal Society of London. Series A, Mathematical and Physical Sciences, 174(957) pp. 262–272 (1940) doi:10.1098/rspa.1940.0018 == See also == Timeline of low-temperature technology Allan Griffin A Brief History of Our Understanding of BEC: From Bose to Beliaev arXiv:cond-mat/9901123 p. 5 == References == == External links == U of T and the Discover of Superfluidity Reference to the late Don Misener
|
{
"page_id": 1573063,
"source": null,
"title": "Don Misener"
}
|
PWPAW A Projector Augmented Wave (PAW) code for electronic structure calculation. It is a free software package, distributed under the copyleft GNU General Public License. It is a plane wave implementation of the projector augmented wave (PAW) method developed by Peter E. Blöchl for electronic structure calculations within the framework of density functional theory. In addition to the self-consistent calculation of the electronic structure of a periodic solid, the program has a number of other capabilities, including structural geometry optimization and molecular dynamics simulations within the Born–Oppenheimer approximation. == See also == Atompaw Software package for electron configuration calculations EXCITING Bloch's theorem == References ==
|
{
"page_id": 3342537,
"source": null,
"title": "Pwpaw"
}
|
In molecular biology mir-11 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. There is an evidence to suggest that miR-11 plays a role in apoptosis. Alignment has shown that miR-11 shares the same family motif as miR-2b and miR-6, together making up the mir-2 clan. There is however little similarity in the 3' ends between these clan members. == See also == MicroRNA == References == == Further reading == == External links == Page for mir-11 microRNA precursor family at Rfam
|
{
"page_id": 36372685,
"source": null,
"title": "Mir-11 microRNA precursor family"
}
|
The molecular formula C11H8O3 (molar mass: 188.18 g/mol, exact mass: 188.0473 u) may refer to: 3-Acetylcoumarin Hydroxynaphthoic acids 2-Hydroxy-1-naphthoic acid 3-Hydroxy-2-naphthoic acid Plumbagin, or 5-hydroxy-2-methyl-1,4-naphthoquinone
|
{
"page_id": 23986389,
"source": null,
"title": "C11H8O3"
}
|
Genetic redundancy is a term typically used to describe situations where a given biochemical function is redundantly encoded by two or more genes. In these cases, mutations (or defects) in one of these genes will have a smaller effect on the fitness of the organism than expected from the genes’ function. Characteristic examples of genetic redundancy include (Enns, Kanaoka et al. 2005) and (Pearce, Senis et al. 2004). Many more examples are thoroughly discussed in (Kafri, Levy & Pilpel. 2006). The main source of genetic redundancy is the process of gene duplication which generates multiplicity in gene copy number. A second and less frequent source of genetic redundancy are convergent evolutionary processes leading to genes that are close in function but unrelated in sequence (Galperin, Walker & Koonin 1998). Genetic redundancy is typically associated with signaling networks, in which many proteins act together to accomplish teleological functions. In contrast to expectations, genetic redundancy is not associated with gene duplications [Wagner, 2007], neither do redundant genes mutate faster than essential genes [Hurst 1999]. Therefore, genetic redundancy has classically aroused much debate in the context of evolutionary biology (Nowak et al., 1997; Kafri, Springer & Pilpel . 2009). From an evolutionary standpoint, genes with overlapping functions imply minimal, if any, selective pressures acting on these genes. One therefore expects that the genes participating in such buffering of mutations will be subject to severe mutational drift diverging their functions and/or expression patterns with considerably high rates. Indeed it has been shown that the functional divergence of paralogous pairs in both yeast and human is an extremely rapid process. Taking these notions into account, the very existence of genetic buffering, and the functional redundancies required for it, presents a paradox in light of the evolutionary concepts. On one hand, for genetic buffering to take
|
{
"page_id": 2228439,
"source": null,
"title": "Genetic redundancy"
}
|
place there is a necessity for redundancies of gene function, on the other hand such redundancies are clearly unstable in face of natural selection and are therefore unlikely to be found in evolved genomes. Duplicated genes that diverge in function may undergo subfunctionalization or can become degenerate. When two protein coding genes are degenerate there will be conditions where the gene products appear functionally redundant and also conditions where the gene products take on unique functions. == References == Pearce, A. C., Y. A. Senis, et al. (2004). "Vav1 and vav3 have critical but redundant roles in mediating platelet activation by collagen." J Biol Chem 279(52): 53955-62. Enns, L. C., M. M. Kanaoka, et al. (2005). "Two callose synthases, GSL1 and GSL5, play an essential and redundant role in plant and pollen development and in fertility." Plant Mol Biol 58(3): 333-49. Kafri, R., M. Levy, et al. (2006). "The regulatory utilization of genetic redundancy through responsive backup circuits." Proc Natl Acad Sci U S A 103(31): 11653-8. Galperin, M. Y., Walker, D. R. & Koonin, E. V. (1998) Genome Res 8, 779-90. Kafri R, Springer M, Pilpel Y. Genetic redundancy: new tricks for old genes. Cell. 2009 Feb 6;136(3):389-92. Wagner A, Wright J. Alternative routes and mutational robustness in complex regulatory networks. Biosystems. 2007 Mar;88(1-2):163-72. Epub 2006 Jun 15. Hurst LD, Smith NG. Do essential genes evolve slowly? Curr Biol. 1999 Jul 15;9(14):747-50.
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{
"page_id": 2228439,
"source": null,
"title": "Genetic redundancy"
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The following is a partial list of the "D" codes for Medical Subject Headings (MeSH), as defined by the United States National Library of Medicine (NLM). This list continues the information at List of MeSH codes (D12.644). Codes following these are found at List of MeSH codes (D13). For other MeSH codes, see List of MeSH codes. The source for this content is the set of 2006 MeSH Trees from the NLM. == MeSH D12.776 – proteins == == MeSH D12.776.034 – albumins == === MeSH D12.776.034.145 – c-reactive protein === === MeSH D12.776.034.180 – conalbumin === === MeSH D12.776.034.398 – lactalbumin === === MeSH D12.776.034.614 – ovalbumin === ==== MeSH D12.776.034.614.300 – avidin ==== === MeSH D12.776.034.700 – parvalbumins === === MeSH D12.776.034.756 – ricin === === MeSH D12.776.034.841 – serum albumin === ==== MeSH D12.776.034.841.350 – methemalbumin ==== ==== MeSH D12.776.034.841.450 – prealbumin ==== ==== MeSH D12.776.034.841.540 – serum albumin, bovine ==== ==== MeSH D12.776.034.841.665 – serum albumin, radio-iodinated ==== === MeSH D12.776.034.900 – technetium tc 99m aggregated albumin === == MeSH D12.776.037 – algal proteins == == MeSH D12.776.045 – amphibian proteins == === MeSH D12.776.045.500 – xenopus proteins === == MeSH D12.776.049 – amyloid == === MeSH D12.776.049.025 – amyloid beta-protein === ==== MeSH D12.776.049.025.150 – amyloid beta-protein precursor ==== === MeSH D12.776.049.790 – serum amyloid a protein === === MeSH D12.776.049.800 – serum amyloid p-component === == MeSH D12.776.053 – antifreeze proteins == === MeSH D12.776.053.100 – antifreeze proteins, type i === === MeSH D12.776.053.200 – antifreeze proteins, type ii === === MeSH D12.776.053.350 – antifreeze proteins, type iii === === MeSH D12.776.053.500 – antifreeze proteins, type iv === == MeSH D12.776.070 – apoproteins == === MeSH D12.776.070.290 – apoenzymes === === MeSH D12.776.070.400 – apolipoproteins === ==== MeSH D12.776.070.400.200 – apolipoprotein A ==== MeSH
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
D12.776.070.400.200.100 – apolipoprotein A1 MeSH D12.776.070.400.200.150 – apolipoprotein A2 ==== MeSH D12.776.070.400.300 – apolipoprotein B ==== ==== MeSH D12.776.070.400.400 – apolipoprotein C ==== ==== MeSH D12.776.070.400.500 – apolipoprotein E ==== == MeSH D12.776.083 – aprotinin == == MeSH D12.776.090 – archaeal proteins == === MeSH D12.776.090.200 – bacteriorhodopsins === === MeSH D12.776.090.250 – dna topoisomerases, type i, archaeal === === MeSH D12.776.090.300 – halorhodopsins === === MeSH D12.776.090.650 – periplasmic proteins === == MeSH D12.776.091 – armadillo domain proteins == === MeSH D12.776.091.249 – beta-catenin === === MeSH D12.776.091.500 – gamma catenin === === MeSH D12.776.091.750 – plakophilins === == MeSH D12.776.093 – avian proteins == == MeSH D12.776.097 – bacterial proteins == See List of MeSH codes (D12.776.097). == MeSH D12.776.124 – blood proteins == See List of MeSH codes (D12.776.124). == MeSH D12.776.157 – carrier proteins == See List of MeSH codes (D12.776.157). == MeSH D12.776.167 – cell cycle proteins == === MeSH D12.776.167.100 – cdc25 phosphatase === === MeSH D12.776.167.150 – cellular apoptosis susceptibility protein === === MeSH D12.776.167.175 – cullin proteins === === MeSH D12.776.167.187 – cyclin-dependent kinase inhibitor proteins === ==== MeSH D12.776.167.187.100 – cyclin-dependent kinase inhibitor p15 ==== ==== MeSH D12.776.167.187.200 – cyclin-dependent kinase inhibitor p16 ==== ==== MeSH D12.776.167.187.300 – cyclin-dependent kinase inhibitor p18 ==== ==== MeSH D12.776.167.187.400 – cyclin-dependent kinase inhibitor p19 ==== ==== MeSH D12.776.167.187.500 – cyclin-dependent kinase inhibitor p21 ==== ==== MeSH D12.776.167.187.600 – cyclin-dependent kinase inhibitor p27 ==== ==== MeSH D12.776.167.187.700 – cyclin-dependent kinase inhibitor p57 ==== === MeSH D12.776.167.200 – cyclin-dependent kinases === ==== MeSH D12.776.167.200.067 – cdc2-cdc28 kinases ==== MeSH D12.776.167.200.067.249 – cdc2 protein kinase MeSH D12.776.167.200.067.500 – cdc28 protein kinase, s cerevisiae MeSH D12.776.167.200.067.875 – cyclin-dependent kinase 5 MeSH D12.776.167.200.067.900 – cyclin-dependent kinase 9 ==== MeSH D12.776.167.200.323 – cyclin-dependent kinase 2 ==== ==== MeSH D12.776.167.200.451 –
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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cyclin-dependent kinase 4 ==== ==== MeSH D12.776.167.200.515 – cyclin-dependent kinase 6 ==== ==== MeSH D12.776.167.200.580 – maturation-promoting factor ==== MeSH D12.776.167.200.580.500 – cdc2 protein kinase === MeSH D12.776.167.218 – cyclins === ==== MeSH D12.776.167.218.100 – cyclin A ==== ==== MeSH D12.776.167.218.120 – cyclin B ==== ==== MeSH D12.776.167.218.161 – cyclin D1 ==== ==== MeSH D12.776.167.218.180 – cyclin E ==== === MeSH D12.776.167.600 – tumor suppressor protein p14arf === == MeSH D12.776.178 – cerebrospinal fluid proteins == == MeSH D12.776.200 – colipases == == MeSH D12.776.210 – contractile proteins == === MeSH D12.776.210.500 – muscle proteins === ==== MeSH D12.776.210.500.095 – actinin ==== ==== MeSH D12.776.210.500.100 – actins ==== ==== MeSH D12.776.210.500.154 – actomyosin ==== ==== MeSH D12.776.210.500.220 – calsequestrin ==== ==== MeSH D12.776.210.500.227 – capz actin capping protein ==== ==== MeSH D12.776.210.500.235 – caveolin 3 ==== ==== MeSH D12.776.210.500.242 – cofilin 2 ==== ==== MeSH D12.776.210.500.250 – dystrophin ==== ==== MeSH D12.776.210.500.410 – dystrophin-associated proteins ==== MeSH D12.776.210.500.410.500 – dystroglycans MeSH D12.776.210.500.410.750 – sarcoglycans ==== MeSH D12.776.210.500.570 – myogenic regulatory factors ==== MeSH D12.776.210.500.570.590 – myod protein MeSH D12.776.210.500.570.595 – myogenic regulatory factor 5 MeSH D12.776.210.500.570.600 – myogenin ==== MeSH D12.776.210.500.588 – myoglobin ==== ==== MeSH D12.776.210.500.600 – myosins ==== MeSH D12.776.210.500.600.100 – myosin heavy chains MeSH D12.776.210.500.600.200 – myosin light chains MeSH D12.776.210.500.600.300 – myosin subfragments MeSH D12.776.210.500.600.465 – myosin type i MeSH D12.776.210.500.600.470 – myosin type ii MeSH D12.776.210.500.600.470.249 – cardiac myosins MeSH D12.776.210.500.600.470.249.249 – atrial myosins MeSH D12.776.210.500.600.470.249.500 – ventricular myosins MeSH D12.776.210.500.600.470.374 – nonmuscle myosin type iia MeSH D12.776.210.500.600.470.500 – nonmuscle myosin type iib MeSH D12.776.210.500.600.470.750 – skeletal muscle myosins MeSH D12.776.210.500.600.470.875 – smooth muscle myosins ==== MeSH D12.776.210.500.750 – parvalbumins ==== ==== MeSH D12.776.210.500.775 – profilins ==== ==== MeSH D12.776.210.500.800 – ryanodine receptor calcium release channel ==== ==== MeSH D12.776.210.500.847 – tropomodulin ==== ==== MeSH
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
D12.776.210.500.895 – tropomyosin ==== ==== MeSH D12.776.210.500.910 – troponin ==== MeSH D12.776.210.500.910.900 – troponin c MeSH D12.776.210.500.910.925 – troponin i MeSH D12.776.210.500.910.962 – troponin t == MeSH D12.776.215 – cystatins == == MeSH D12.776.220 – cytoskeletal proteins == === MeSH D12.776.220.040 – adenomatous polyposis coli protein === === MeSH D12.776.220.145 – catenins === ==== MeSH D12.776.220.145.249 – alpha-catenin ==== ==== MeSH D12.776.220.145.500 – beta catenin ==== ==== MeSH D12.776.220.145.750 – gamma catenin ==== === MeSH D12.776.220.250 – dystrophin === === MeSH D12.776.220.362 – dystrophin-associated proteins === ==== MeSH D12.776.220.362.249 – dystroglycans ==== === MeSH D12.776.220.475 – intermediate filament proteins === ==== MeSH D12.776.220.475.200 – desmin ==== ==== MeSH D12.776.220.475.400 – glial fibrillary acidic protein ==== ==== MeSH D12.776.220.475.450 – keratin ==== ==== MeSH D12.776.220.475.630 – neurofilament proteins ==== ==== MeSH D12.776.220.475.900 – vimentin ==== === MeSH D12.776.220.525 – microfilament proteins === ==== MeSH D12.776.220.525.032 – actin capping proteins ==== MeSH D12.776.220.525.032.500 – capz actin capping protein MeSH D12.776.220.525.032.750 – tropomodulin ==== MeSH D12.776.220.525.212 – actin depolymerizing factors ==== MeSH D12.776.220.525.212.500 – cofilin 1 MeSH D12.776.220.525.212.750 – cofilin 2 MeSH D12.776.220.525.212.875 – destrin ==== MeSH D12.776.220.525.246 – actin-related protein 2-3 complex ==== MeSH D12.776.220.525.246.500 – actin-related protein 2 MeSH D12.776.220.525.246.750 – actin-related protein 3 ==== MeSH D12.776.220.525.250 – actinin ==== ==== MeSH D12.776.220.525.255 – actins ==== ==== MeSH D12.776.220.525.281 – cortactin ==== ==== MeSH D12.776.220.525.350 – gelsolin ==== ==== MeSH D12.776.220.525.475 – myosins ==== MeSH D12.776.220.525.475.100 – myosin heavy chains MeSH D12.776.220.525.475.200 – myosin light chains MeSH D12.776.220.525.475.300 – myosin subfragments MeSH D12.776.220.525.475.470 – myosin type i MeSH D12.776.220.525.475.475 – myosin type ii MeSH D12.776.220.525.475.475.124 – cardiac myosins MeSH D12.776.220.525.475.475.124.249 – atrial myosins MeSH D12.776.220.525.475.475.124.500 – ventricular myosins MeSH D12.776.220.525.475.475.249 – nonmuscle myosin type iia MeSH D12.776.220.525.475.475.500 – nonmuscle myosin type iib MeSH D12.776.220.525.475.475.750 – skeletal muscle myosins MeSH D12.776.220.525.475.475.875 –
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
smooth muscle myosins MeSH D12.776.220.525.475.612 – myosin type iii MeSH D12.776.220.525.475.681 – myosin type iv MeSH D12.776.220.525.475.750 – myosin type v ==== MeSH D12.776.220.525.637 – profilins ==== ==== MeSH D12.776.220.525.800 – tropomyosin ==== ==== MeSH D12.776.220.525.825 – troponin ==== MeSH D12.776.220.525.825.900 – troponin c MeSH D12.776.220.525.825.925 – troponin i MeSH D12.776.220.525.825.962 – troponin t ==== MeSH D12.776.220.525.912 – wiskott-aldrich syndrome protein family ==== MeSH D12.776.220.525.912.500 – wiskott-aldrich syndrome protein MeSH D12.776.220.525.912.550 – wiskott-aldrich syndrome protein, neuronal === MeSH D12.776.220.600 – microtubule proteins === ==== MeSH D12.776.220.600.200 – dynein atpase ==== ==== MeSH D12.776.220.600.450 – microtubule-associated proteins ==== MeSH D12.776.220.600.450.200 – dynamins MeSH D12.776.220.600.450.200.100 – dynamin i MeSH D12.776.220.600.450.200.200 – dynamin ii MeSH D12.776.220.600.450.200.300 – dynamin iii MeSH D12.776.220.600.450.450 – kinesin MeSH D12.776.220.600.450.480 – stathmin MeSH D12.776.220.600.450.510 – tau proteins ==== MeSH D12.776.220.600.800 – tubulin ==== === MeSH D12.776.220.790 – plakins === ==== MeSH D12.776.220.790.500 – desmoplakins ==== ==== MeSH D12.776.220.790.750 – plectin ==== === MeSH D12.776.220.885 – plakophilins === === MeSH D12.776.220.980 – spectrin === === MeSH D12.776.220.985 – talin === === MeSH D12.776.220.987 – utrophin === === MeSH D12.776.220.990 – vinculin === == MeSH D12.776.231 – dental enamel proteins == == MeSH D12.776.256 – dietary proteins == === MeSH D12.776.256.317 – egg proteins, dietary === ==== MeSH D12.776.256.317.180 – conalbumin ==== ==== MeSH D12.776.256.317.663 – ovalbumin ==== MeSH D12.776.256.317.663.300 – avidin ==== MeSH D12.776.256.317.675 – ovomucin ==== ==== MeSH D12.776.256.317.700 – phosvitin ==== === MeSH D12.776.256.626 – milk proteins === ==== MeSH D12.776.256.626.207 – caseins ==== ==== MeSH D12.776.256.626.506 – lactalbumin ==== ==== MeSH D12.776.256.626.632 – lactoglobulins ==== MeSH D12.776.256.626.632.507 – lactoferrin === MeSH D12.776.256.920 – vegetable proteins === == MeSH D12.776.260 – dna-binding proteins == See List of MeSH codes (D12.776.260). == MeSH D12.776.275 – dynein atpase == == MeSH D12.776.290 – egg proteins == === MeSH D12.776.290.180
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
}
|
– conalbumin === === MeSH D12.776.290.300 – egg proteins, dietary === === MeSH D12.776.290.663 – ovalbumin === ==== MeSH D12.776.290.663.100 – avidin ==== === MeSH D12.776.290.675 – ovomucin === === MeSH D12.776.290.700 – phosvitin === === MeSH D12.776.290.812 – vitellins === ==== MeSH D12.776.290.812.500 – vitellogenins ==== == MeSH D12.776.298 – epididymal secretory proteins == == MeSH D12.776.306 – eye proteins == === MeSH D12.776.306.090 – arrestins === ==== MeSH D12.776.306.090.050 – arrestin ==== === MeSH D12.776.306.366 – crystallins === ==== MeSH D12.776.306.366.100 – alpha-crystallins ==== MeSH D12.776.306.366.100.149 – alpha-crystallin a chain MeSH D12.776.306.366.100.300 – alpha-crystallin b chain ==== MeSH D12.776.306.366.300 – beta-crystallins ==== MeSH D12.776.306.366.300.100 – beta-crystallin a chain MeSH D12.776.306.366.300.200 – beta-crystallin b chain ==== MeSH D12.776.306.366.310 – delta-crystallins ==== ==== MeSH D12.776.306.366.350 – epsilon-crystallins ==== ==== MeSH D12.776.306.366.850 – gamma-crystallins ==== ==== MeSH D12.776.306.366.925 – omega-crystallins ==== ==== MeSH D12.776.306.366.962 – tau-crystallins ==== ==== MeSH D12.776.306.366.981 – zeta-crystallins ==== === MeSH D12.776.306.433 – guanylate cyclase-activating proteins === === MeSH D12.776.306.500 – opsin === ==== MeSH D12.776.306.500.700 – rhodopsin ==== === MeSH D12.776.306.750 – recoverin === === MeSH D12.776.306.875 – rhodopsin kinase === == MeSH D12.776.313 – fanconi anemia complementation group proteins == === MeSH D12.776.313.249 – brca2 protein === === MeSH D12.776.313.500 – fanconi anemia complementation group a protein === === MeSH D12.776.313.750 – fanconi anemia complementation group c protein === === MeSH D12.776.313.812 – fanconi anemia complementation group d2 protein === === MeSH D12.776.313.843 – fanconi anemia complementation group e protein === === MeSH D12.776.313.875 – fanconi anemia complementation group f protein === === MeSH D12.776.313.906 – fanconi anemia complementation group g protein === === MeSH D12.776.313.937 – fanconi anemia complementation group l protein === == MeSH D12.776.320 – fetal proteins == === MeSH D12.776.320.050 – alpha-fetoproteins === == MeSH D12.776.325 – fish proteins == ===
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
MeSH D12.776.325.500 – zebrafish proteins === == MeSH D12.776.331 – flavoproteins == === MeSH D12.776.331.049 – acetolactate synthase === === MeSH D12.776.331.099 – acyl-coa dehydrogenase === === MeSH D12.776.331.102 – acyl-coa dehydrogenase, long-chain === === MeSH D12.776.331.149 – acyl-CoA oxidase === === MeSH D12.776.331.161 – apoptosis inducing factor === === MeSH D12.776.331.174 – butyryl-coa dehydrogenase === === MeSH D12.776.331.186 – cytochrome-b(5) reductase === === MeSH D12.776.331.192 – dihydrolipoamide dehydrogenase === === MeSH D12.776.331.199 – electron-transferring flavoproteins === ==== MeSH D12.776.331.199.500 – electron transport complex i ==== ==== MeSH D12.776.331.199.750 – electron transport complex ii ==== MeSH D12.776.331.199.750.500 – succinate dehydrogenase === MeSH D12.776.331.400 – flavodoxin === === MeSH D12.776.331.737 – glutamate synthase (NADH) === === MeSH D12.776.331.775 – methylenetetrahydrofolate reductase (nadph2) === === MeSH D12.776.331.887 – nadh dehydrogenase === === MeSH D12.776.331.894 – nadph oxidase === === MeSH D12.776.331.899 – nitrate reductase (nadh) === === MeSH D12.776.331.901 – nitrate reductase (nad(p)h) === === MeSH D12.776.331.911 – nitrate reductase (nadph) === === MeSH D12.776.331.915 – retinal dehydrogenase === === MeSH D12.776.331.943 – sarcosine oxidase === === MeSH D12.776.331.971 – thioredoxin reductase (nadph) === == MeSH D12.776.354 – fungal proteins == === MeSH D12.776.354.750 – saccharomyces cerevisiae proteins === ==== MeSH D12.776.354.750.124 – cdc28 protein kinase, s cerevisiae ==== ==== MeSH D12.776.354.750.249 – cdc42 gtp-binding protein, saccharomyces cerevisiae ==== ==== MeSH D12.776.354.750.500 – mcm1 protein ==== ==== MeSH D12.776.354.750.750 – silent information regulator proteins, saccharomyces cerevisiae ==== === MeSH D12.776.354.875 – schizosaccharomyces pombe proteins === == MeSH D12.776.377 – globulins == === MeSH D12.776.377.457 – lactoglobulins === ==== MeSH D12.776.377.457.507 – lactoferrin ==== === MeSH D12.776.377.715 – serum globulins === ==== MeSH D12.776.377.715.085 – alpha-globulins ==== MeSH D12.776.377.715.085.050 – alpha 1-antichymotrypsin MeSH D12.776.377.715.085.085 – alpha 1-antitrypsin MeSH D12.776.377.715.085.100 – alpha-macroglobulins MeSH D12.776.377.715.085.118 – antiplasmin MeSH D12.776.377.715.085.125 – antithrombin iii MeSH D12.776.377.715.085.214 –
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
ceruloplasmin MeSH D12.776.377.715.085.394 – haptoglobins MeSH D12.776.377.715.085.450 – heparin cofactor ii MeSH D12.776.377.715.085.640 – orosomucoid MeSH D12.776.377.715.085.740 – progesterone-binding globulin MeSH D12.776.377.715.085.750 – retinol-binding proteins MeSH D12.776.377.715.085.901 – transcortin ==== MeSH D12.776.377.715.182 – beta-globulins ==== MeSH D12.776.377.715.182.100 – beta-2 microglobulin MeSH D12.776.377.715.182.160 – beta-thromboglobulin MeSH D12.776.377.715.182.200 – complement factor h MeSH D12.776.377.715.182.338 – hemopexin MeSH D12.776.377.715.182.580 – plasminogen MeSH D12.776.377.715.182.580.500 – angiostatins MeSH D12.776.377.715.182.624 – properdin MeSH D12.776.377.715.182.800 – sex hormone-binding globulin MeSH D12.776.377.715.182.839 – transferrin ==== MeSH D12.776.377.715.390 – fibronectins ==== ==== MeSH D12.776.377.715.548 – immunoglobulins ==== MeSH D12.776.377.715.548.114 – antibodies MeSH D12.776.377.715.548.114.071 – antibodies, anti-idiotypic MeSH D12.776.377.715.548.114.107 – antibodies, archaeal MeSH D12.776.377.715.548.114.125 – antibodies, bacterial MeSH D12.776.377.715.548.114.125.288 – antistreptolysin MeSH D12.776.377.715.548.114.134 – antibodies, bispecific MeSH D12.776.377.715.548.114.143 – antibodies, blocking MeSH D12.776.377.715.548.114.167 – antibodies, catalytic MeSH D12.776.377.715.548.114.179 – antibodies, fungal MeSH D12.776.377.715.548.114.185 – antibodies, helminth MeSH D12.776.377.715.548.114.191 – antibodies, heterophile MeSH D12.776.377.715.548.114.224 – antibodies, monoclonal MeSH D12.776.377.715.548.114.224.570 – muromonab-cd3 MeSH D12.776.377.715.548.114.240 – antibodies, neoplasm MeSH D12.776.377.715.548.114.248 – antibodies, phospho-specific MeSH D12.776.377.715.548.114.252 – antibodies, protozoan MeSH D12.776.377.715.548.114.254 – antibodies, viral MeSH D12.776.377.715.548.114.254.150 – deltaretrovirus antibodies MeSH D12.776.377.715.548.114.254.150.440 – hiv antibodies MeSH D12.776.377.715.548.114.254.150.500 – htlv-i antibodies MeSH D12.776.377.715.548.114.254.150.510 – htlv-ii antibodies MeSH D12.776.377.715.548.114.254.450 – hepatitis antibodies MeSH D12.776.377.715.548.114.254.450.251 – hepatitis a antibodies MeSH D12.776.377.715.548.114.254.450.504 – hepatitis b antibodies MeSH D12.776.377.715.548.114.254.450.510 – hepatitis c antibodies MeSH D12.776.377.715.548.114.257 – antigen-antibody complex MeSH D12.776.377.715.548.114.301 – antitoxins MeSH D12.776.377.715.548.114.301.138 – antivenins MeSH D12.776.377.715.548.114.301.268 – botulinum antitoxin MeSH D12.776.377.715.548.114.301.438 – diphtheria antitoxin MeSH D12.776.377.715.548.114.301.849 – tetanus antitoxin MeSH D12.776.377.715.548.114.323 – autoantibodies MeSH D12.776.377.715.548.114.323.190 – antibodies, antineutrophil cytoplasmic MeSH D12.776.377.715.548.114.323.204 – antibodies, antinuclear MeSH D12.776.377.715.548.114.323.210 – antibodies, antiphospholipid MeSH D12.776.377.715.548.114.323.210.100 – antibodies, anticardiolipin MeSH D12.776.377.715.548.114.323.210.600 – lupus coagulation inhibitor MeSH D12.776.377.715.548.114.323.300 – complement c3 nephritic factor MeSH D12.776.377.715.548.114.323.390 – immunoconglutinins MeSH D12.776.377.715.548.114.323.480 – immunoglobulins, thyroid-stimulating MeSH D12.776.377.715.548.114.323.480.500 – long-acting thyroid stimulator MeSH D12.776.377.715.548.114.323.732 – rheumatoid factor MeSH
|
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"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
D12.776.377.715.548.114.345 – binding sites, antibody MeSH D12.776.377.715.548.114.345.180 – complementarity determining regions MeSH D12.776.377.715.548.114.525 – hemolysins MeSH D12.776.377.715.548.114.573 – immune sera MeSH D12.776.377.715.548.114.573.203 – antilymphocyte serum MeSH D12.776.377.715.548.114.580 – immunoconjugates MeSH D12.776.377.715.548.114.580.450 – immunotoxins MeSH D12.776.377.715.548.114.606 – immunoglobulin allotypes MeSH D12.776.377.715.548.114.606.586 – immunoglobulin gm allotypes MeSH D12.776.377.715.548.114.606.587 – immunoglobulin km allotypes MeSH D12.776.377.715.548.114.619 – immunoglobulin isotypes MeSH D12.776.377.715.548.114.619.026 – immunoglobulin a MeSH D12.776.377.715.548.114.619.026.030 – immunoglobulin a, secretory MeSH D12.776.377.715.548.114.619.026.030.500 – secretory component MeSH D12.776.377.715.548.114.619.026.515 – immunoglobulin alpha-chains MeSH D12.776.377.715.548.114.619.251 – immunoglobulin d MeSH D12.776.377.715.548.114.619.251.500 – immunoglobulin delta-chains MeSH D12.776.377.715.548.114.619.312 – immunoglobulin e MeSH D12.776.377.715.548.114.619.312.500 – immunoglobulin epsilon-chains MeSH D12.776.377.715.548.114.619.393 – immunoglobulin g MeSH D12.776.377.715.548.114.619.393.522 – immunoglobulin gamma-chains MeSH D12.776.377.715.548.114.619.393.522.400 – immunoglobulin gm allotypes MeSH D12.776.377.715.548.114.619.393.550 – long-acting thyroid stimulator MeSH D12.776.377.715.548.114.619.393.570 – muromonab-cd3 MeSH D12.776.377.715.548.114.619.393.700 – rho(d) immune globulin MeSH D12.776.377.715.548.114.619.574 – immunoglobulin m MeSH D12.776.377.715.548.114.619.574.500 – immunoglobulin mu-chains MeSH D12.776.377.715.548.114.632 – immunoglobulins, intravenous MeSH D12.776.377.715.548.114.648 – immunoglobulins, thyroid-stimulating MeSH D12.776.377.715.548.114.656 – insulin antibodies MeSH D12.776.377.715.548.114.664 – isoantibodies MeSH D12.776.377.715.548.114.715 – oligoclonal bands MeSH D12.776.377.715.548.114.767 – opsonin proteins MeSH D12.776.377.715.548.114.820 – plantibodies MeSH D12.776.377.715.548.114.837 – precipitins MeSH D12.776.377.715.548.114.890 – reagins MeSH D12.776.377.715.548.397 – gamma-globulins MeSH D12.776.377.715.548.397.500 – tuftsin MeSH D12.776.377.715.548.538 – immunoglobulin constant regions MeSH D12.776.377.715.548.538.249 – immunoglobulin fab fragments MeSH D12.776.377.715.548.538.500 – immunoglobulin fc fragments MeSH D12.776.377.715.548.538.500.249 – cd4 immunoadhesins MeSH D12.776.377.715.548.680 – immunoglobulin fragments MeSH D12.776.377.715.548.680.650 – immunoglobulin fab fragments MeSH D12.776.377.715.548.680.650.500 – immunoglobulin variable region MeSH D12.776.377.715.548.680.650.500.180 – complementarity determining regions MeSH D12.776.377.715.548.680.650.500.590 – immunoglobulin joining region MeSH D12.776.377.715.548.680.650.750 – tuftsin MeSH D12.776.377.715.548.680.660 – immunoglobulin fc fragments MeSH D12.776.377.715.548.680.660.249 – cd4 immunoadhesins MeSH D12.776.377.715.548.680.660.500 – immunoglobulin constant regions MeSH D12.776.377.715.548.680.745 – immunoglobulin idiotypes MeSH D12.776.377.715.548.705 – immunoglobulin subunits MeSH D12.776.377.715.548.705.500 – immunoglobulin heavy chains MeSH D12.776.377.715.548.705.500.350 – immunoglobulin alpha-chains MeSH D12.776.377.715.548.705.500.360 – immunoglobulin delta-chains MeSH D12.776.377.715.548.705.500.370 – immunoglobulin epsilon-chains MeSH D12.776.377.715.548.705.500.380 – immunoglobulin gamma-chains MeSH D12.776.377.715.548.705.500.380.500 – immunoglobulin
|
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|
gm allotypes MeSH D12.776.377.715.548.705.500.500 – immunoglobulin mu-chains MeSH D12.776.377.715.548.705.625 – immunoglobulin j-chains MeSH D12.776.377.715.548.705.750 – immunoglobulin light chains MeSH D12.776.377.715.548.705.750.530 – immunoglobulin kappa-chains MeSH D12.776.377.715.548.705.750.530.500 – immunoglobulin km allotypes MeSH D12.776.377.715.548.705.750.550 – immunoglobulin lambda-chains MeSH D12.776.377.715.548.705.875 – secretory component MeSH D12.776.377.715.548.797 – immunoglobulin variable region MeSH D12.776.377.715.548.797.180 – complementarity determining regions MeSH D12.776.377.715.548.797.570 – immunoglobulin fab fragments MeSH D12.776.377.715.548.797.590 – immunoglobulin joining region MeSH D12.776.377.715.548.900 – paraproteins MeSH D12.776.377.715.548.900.120 – bence jones protein MeSH D12.776.377.715.548.900.225 – cryoglobulins MeSH D12.776.377.715.548.900.500 – myeloma proteins MeSH D12.776.377.715.548.900.700 – pyroglobulins MeSH D12.776.377.715.548.950 – receptors, antigen, b-cell MeSH D12.776.377.715.548.950.500 – antigens, cd79 ==== MeSH D12.776.377.715.647 – macroglobulins ==== MeSH D12.776.377.715.647.100 – alpha-macroglobulins ==== MeSH D12.776.377.715.900 – transcobalamins ==== === MeSH D12.776.377.856 – thyroglobulin === == MeSH D12.776.395 – glycoproteins == See List of MeSH codes (D12.776.395). == MeSH D12.776.402 – gtp-binding protein regulators == === MeSH D12.776.402.150 – gtpase-activating proteins === ==== MeSH D12.776.402.150.100 – chimerin proteins ==== MeSH D12.776.402.150.100.200 – chimerin 1 ==== MeSH D12.776.402.150.300 – eukaryotic initiation factor-5 ==== ==== MeSH D12.776.402.150.500 – ras gtpase-activating proteins ==== MeSH D12.776.402.150.500.460 – neurofibromin 1 MeSH D12.776.402.150.500.500 – p120 gtpase activating protein ==== MeSH D12.776.402.150.750 – rgs proteins ==== === MeSH D12.776.402.225 – guanine nucleotide dissociation inhibitors === === MeSH D12.776.402.300 – guanine nucleotide exchange factors === ==== MeSH D12.776.402.300.200 – eukaryotic initiation factor-2b ==== ==== MeSH D12.776.402.300.300 – guanine nucleotide-releasing factor 2 ==== ==== MeSH D12.776.402.300.450 – proto-oncogene proteins c-vav ==== ==== MeSH D12.776.402.300.600 – ral guanine nucleotide exchange factor ==== ==== MeSH D12.776.402.300.700 – ras guanine nucleotide exchange factors ==== MeSH D12.776.402.300.700.500 – ras-GRF1 MeSH D12.776.402.300.700.700 – son of sevenless proteins MeSH D12.776.402.300.700.700.330 – sos1 protein MeSH D12.776.402.300.700.700.600 – son of sevenless protein, drosophila == MeSH D12.776.410 – heat-shock proteins == === MeSH D12.776.410.210 – chaperonins === ==== MeSH D12.776.410.210.175 – chaperonin 10 ====
|
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"page_id": 5505240,
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|
MeSH D12.776.410.210.175.325 – groes protein ==== MeSH D12.776.410.210.180 – chaperonin 60 ==== MeSH D12.776.410.210.180.325 – groel protein === MeSH D12.776.410.270 – heat-shock proteins, small === ==== MeSH D12.776.410.270.500 – hsp20 heat-shock proteins ==== ==== MeSH D12.776.410.270.750 – hsp30 heat-shock proteins ==== === MeSH D12.776.410.292 – hsp40 heat-shock proteins === === MeSH D12.776.410.295 – hsp47 heat-shock proteins === === MeSH D12.776.410.375 – hsp70 heat-shock proteins === ==== MeSH D12.776.410.375.500 – hsc70 heat-shock proteins ==== ==== MeSH D12.776.410.375.750 – hsp72 heat-shock proteins ==== ==== MeSH D12.776.410.375.800 – hsp110 heat-shock proteins ==== === MeSH D12.776.410.380 – hsp90 heat-shock proteins === == MeSH D12.776.419 – helminth proteins == === MeSH D12.776.419.500 – caenorhabditis elegans proteins === == MeSH D12.776.422 – hemeproteins == === MeSH D12.776.422.220 – cytochromes === ==== MeSH D12.776.422.220.175 – cytochrome a group ==== MeSH D12.776.422.220.175.249 – cytochromes a MeSH D12.776.422.220.175.500 – cytochromes a1 MeSH D12.776.422.220.175.600 – cytochromes a3 ==== MeSH D12.776.422.220.187 – cytochrome b group ==== MeSH D12.776.422.220.187.124 – cytochromes b6 MeSH D12.776.422.220.187.249 – cytochromes b MeSH D12.776.422.220.187.500 – cytochromes b5 ==== MeSH D12.776.422.220.286 – cytochrome c group ==== MeSH D12.776.422.220.286.100 – cytochromes c MeSH D12.776.422.220.286.150 – cytochromes c' MeSH D12.776.422.220.286.200 – cytochromes c1 MeSH D12.776.422.220.286.300 – cytochromes c2 MeSH D12.776.422.220.286.600 – cytochromes c6 ==== MeSH D12.776.422.220.300 – cytochrome d group ==== ==== MeSH D12.776.422.220.453 – cytochrome p-450 enzyme system ==== MeSH D12.776.422.220.453.040 – aryl hydrocarbon hydroxylases MeSH D12.776.422.220.453.040.050 – aniline hydroxylase MeSH D12.776.422.220.453.040.110 – benzopyrene hydroxylase MeSH D12.776.422.220.453.040.332 – cytochrome p-450 cyp1a1 MeSH D12.776.422.220.453.040.555 – cytochrome p-450 cyp1a2 MeSH D12.776.422.220.453.040.777 – cytochrome p-450 cyp2b1 MeSH D12.776.422.220.453.040.888 – cytochrome p-450 cyp2d6 MeSH D12.776.422.220.453.040.944 – cytochrome p-450 cyp2e1 MeSH D12.776.422.220.453.040.972 – cytochrome p-450 cyp3a MeSH D12.776.422.220.453.085 – camphor 5-monooxygenase MeSH D12.776.422.220.453.915 – steroid hydroxylases MeSH D12.776.422.220.453.915.050 – aldosterone synthase MeSH D12.776.422.220.453.915.099 – aromatase MeSH D12.776.422.220.453.915.200 – cholesterol 7 alpha-hydroxylase MeSH D12.776.422.220.453.915.212 –
|
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"page_id": 5505240,
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|
cholesterol side-chain cleavage enzyme MeSH D12.776.422.220.453.915.400 – 25-hydroxyvitamin d3 1-alpha-hydroxylase MeSH D12.776.422.220.453.915.720 – steroid 11-beta-hydroxylase MeSH D12.776.422.220.453.915.730 – steroid 12-alpha-hydroxylase MeSH D12.776.422.220.453.915.737 – steroid 16-alpha-hydroxylase MeSH D12.776.422.220.453.915.748 – steroid 17-alpha-hydroxylase MeSH D12.776.422.220.453.915.760 – steroid 21-hydroxylase ==== MeSH D12.776.422.220.726 – cytochromes f ==== === MeSH D12.776.422.412 – hemocyanin === === MeSH D12.776.422.512 – hemoglobins === ==== MeSH D12.776.422.512.149 – carboxyhemoglobin ==== ==== MeSH D12.776.422.512.260 – erythrocruorins ==== ==== MeSH D12.776.422.512.320 – fetal hemoglobin ==== ==== MeSH D12.776.422.512.380 – hemoglobin A ==== MeSH D12.776.422.512.380.440 – hemoglobin a, glycosylated MeSH D12.776.422.512.380.450 – hemoglobin A2 ==== MeSH D12.776.422.512.426 – hemoglobins, abnormal ==== MeSH D12.776.422.512.426.338 – hemoglobin C MeSH D12.776.422.512.426.375 – hemoglobin E MeSH D12.776.422.512.426.463 – hemoglobin H MeSH D12.776.422.512.426.480 – hemoglobin J MeSH D12.776.422.512.426.510 – hemoglobin M MeSH D12.776.422.512.426.588 – hemoglobin, sickle ==== MeSH D12.776.422.512.571 – methemoglobin ==== ==== MeSH D12.776.422.512.687 – oxyhemoglobins ==== ==== MeSH D12.776.422.512.865 – sulfhemoglobin ==== === MeSH D12.776.422.600 – leghemoglobin === === MeSH D12.776.422.680 – methemalbumin === === MeSH D12.776.422.690 – metmyoglobin === === MeSH D12.776.422.704 – myoglobin === == MeSH D12.776.460 – immediate-early proteins == === MeSH D12.776.460.050 – adenovirus E1 proteins === ==== MeSH D12.776.460.050.100 – adenovirus E1A proteins ==== ==== MeSH D12.776.460.050.110 – adenovirus E1B proteins ==== === MeSH D12.776.460.287 – butyrate response factor 1 === === MeSH D12.776.460.525 – early growth response transcription factors === ==== MeSH D12.776.460.525.500 – early growth response protein 1 ==== ==== MeSH D12.776.460.525.750 – early growth response protein 2 ==== ==== MeSH D12.776.460.525.875 – early growth response protein 3 ==== === MeSH D12.776.460.762 – tristetraprolin === == MeSH D12.776.466 – insect proteins == === MeSH D12.776.466.462 – drosophila proteins === ==== MeSH D12.776.466.462.500 – glue proteins, drosophila ==== === MeSH D12.776.466.693 – omega-agatoxin iva === === MeSH D12.776.466.925 – vitellogenins === == MeSH D12.776.467 – intercellular signaling peptides and proteins
|
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"page_id": 5505240,
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"title": "List of MeSH codes (D12.776)"
}
|
== === MeSH D12.776.467.100 – angiogenic proteins === ==== MeSH D12.776.467.100.100 – angiopoietins ==== MeSH D12.776.467.100.100.100 – angiopoietin-1 MeSH D12.776.467.100.100.200 – angiopoietin-2 ==== MeSH D12.776.467.100.450 – angiostatic proteins ==== MeSH D12.776.467.100.450.500 – angiostatins MeSH D12.776.467.100.450.750 – endostatins ==== MeSH D12.776.467.100.800 – vascular endothelial growth factors ==== MeSH D12.776.467.100.800.200 – vascular endothelial growth factor a MeSH D12.776.467.100.800.300 – vascular endothelial growth factor b MeSH D12.776.467.100.800.400 – vascular endothelial growth factor c MeSH D12.776.467.100.800.500 – vascular endothelial growth factor d MeSH D12.776.467.100.800.600 – vascular endothelial growth factor, endocrine-gland-derived === MeSH D12.776.467.249 – bone morphogenetic proteins === === MeSH D12.776.467.374 – cytokines === ==== MeSH D12.776.467.374.050 – autocrine motility factor ==== ==== MeSH D12.776.467.374.200 – chemokines ==== MeSH D12.776.467.374.200.070 – beta-thromboglobulin MeSH D12.776.467.374.200.100 – chemokines, c MeSH D12.776.467.374.200.110 – chemokines, cc MeSH D12.776.467.374.200.120 – chemokines, cxc MeSH D12.776.467.374.200.130 – chemokines, cx3c MeSH D12.776.467.374.200.508 – interleukin-8 MeSH D12.776.467.374.200.600 – macrophage inflammatory proteins MeSH D12.776.467.374.200.600.500 – macrophage inflammatory protein-1 MeSH D12.776.467.374.200.610 – monocyte chemoattractant proteins MeSH D12.776.467.374.200.610.600 – monocyte chemoattractant protein-1 MeSH D12.776.467.374.200.700 – platelet factor 4 MeSH D12.776.467.374.200.750 – rantes ==== MeSH D12.776.467.374.400 – growth substances ==== MeSH D12.776.467.374.400.442 – hematopoietic cell growth factors MeSH D12.776.467.374.400.442.240 – colony-stimulating factors MeSH D12.776.467.374.400.442.240.075 – colony-stimulating factors, recombinant MeSH D12.776.467.374.400.442.240.075.350 – granulocyte colony stimulating factor, recombinant MeSH D12.776.467.374.400.442.240.075.350.275 – filgrastim MeSH D12.776.467.374.400.442.240.075.375 – granulocyte macrophage colony-stimulating factors, recombinant MeSH D12.776.467.374.400.442.240.150 – erythropoietin MeSH D12.776.467.374.400.442.240.150.250 – erythropoietin, recombinant MeSH D12.776.467.374.400.442.240.150.250.250 – epoetin alfa MeSH D12.776.467.374.400.442.240.350 – granulocyte colony-stimulating factor MeSH D12.776.467.374.400.442.240.350.375 – granulocyte colony stimulating factor, recombinant MeSH D12.776.467.374.400.442.240.350.375.275 – filgrastim MeSH D12.776.467.374.400.442.240.375 – granulocyte-macrophage colony-stimulating factor MeSH D12.776.467.374.400.442.240.375.275 – granulocyte macrophage colony-stimulating factors, recombinant MeSH D12.776.467.374.400.442.240.400 – interleukin-3 MeSH D12.776.467.374.400.442.240.500 – macrophage colony-stimulating factor MeSH D12.776.467.374.400.442.240.750 – thrombopoietin MeSH D12.776.467.374.400.442.800 – stem cell factor MeSH D12.776.467.374.400.505 – interleukins MeSH D12.776.467.374.400.505.501 – interleukin-1 MeSH D12.776.467.374.400.505.502 – interleukin-2 MeSH
|
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|
D12.776.467.374.400.505.503 – interleukin-3 MeSH D12.776.467.374.400.505.504 – interleukin-4 MeSH D12.776.467.374.400.505.505 – interleukin-5 MeSH D12.776.467.374.400.505.506 – interleukin-6 MeSH D12.776.467.374.400.505.507 – interleukin-7 MeSH D12.776.467.374.400.505.508 – interleukin-8 MeSH D12.776.467.374.400.505.509 – interleukin-9 MeSH D12.776.467.374.400.505.510 – interleukin-10 MeSH D12.776.467.374.400.505.511 – interleukin-11 MeSH D12.776.467.374.400.505.512 – interleukin-12 MeSH D12.776.467.374.400.505.513 – interleukin-13 MeSH D12.776.467.374.400.505.514 – interleukin-14 MeSH D12.776.467.374.400.505.515 – interleukin-15 MeSH D12.776.467.374.400.505.516 – interleukin-16 MeSH D12.776.467.374.400.505.517 – interleukin-17 MeSH D12.776.467.374.400.505.518 – interleukin-18 MeSH D12.776.467.374.400.800 – transforming growth factor beta ==== MeSH D12.776.467.374.420 – hepatocyte growth factor ==== ==== MeSH D12.776.467.374.440 – interferons ==== MeSH D12.776.467.374.440.890 – interferon type i MeSH D12.776.467.374.440.890.125 – interferon type i, recombinant MeSH D12.776.467.374.440.890.125.100 – interferon alfa-2a MeSH D12.776.467.374.440.890.125.150 – interferon alfa-2b MeSH D12.776.467.374.440.890.125.200 – interferon alfa-2c MeSH D12.776.467.374.440.890.250 – interferon-alpha MeSH D12.776.467.374.440.890.250.100 – interferon alfa-2a MeSH D12.776.467.374.440.890.250.150 – interferon alfa-2b MeSH D12.776.467.374.440.890.250.200 – interferon alfa-2c MeSH D12.776.467.374.440.890.275 – interferon-beta MeSH D12.776.467.374.440.893 – interferon type ii MeSH D12.776.467.374.440.893.510 – interferon-gamma, recombinant ==== MeSH D12.776.467.374.480 – lymphokines ==== MeSH D12.776.467.374.480.350 – interferon type ii MeSH D12.776.467.374.480.372 – interleukin-2 MeSH D12.776.467.374.480.428 – leukocyte migration-inhibitory factors MeSH D12.776.467.374.480.438 – lymphotoxin MeSH D12.776.467.374.480.615 – macrophage-activating factors MeSH D12.776.467.374.480.615.350 – interferon type ii MeSH D12.776.467.374.480.625 – macrophage migration-inhibitory factors MeSH D12.776.467.374.480.640 – neuroleukin MeSH D12.776.467.374.480.700 – suppressor factors, immunologic MeSH D12.776.467.374.480.750 – transfer factor ==== MeSH D12.776.467.374.500 – monokines ==== MeSH D12.776.467.374.500.400 – interleukin-1 MeSH D12.776.467.374.500.800 – tumor necrosis factor-alpha ==== MeSH D12.776.467.374.750 – tumor necrosis factors ==== MeSH D12.776.467.374.750.500 – lymphotoxin MeSH D12.776.467.374.750.750 – tumor necrosis factor-alpha === MeSH D12.776.467.499 – ephrins === ==== MeSH D12.776.467.499.100 – ephrin-A1 ==== ==== MeSH D12.776.467.499.200 – ephrin-A2 ==== ==== MeSH D12.776.467.499.300 – ephrin-A3 ==== ==== MeSH D12.776.467.499.400 – ephrin-A4 ==== ==== MeSH D12.776.467.499.500 – ephrin-A5 ==== ==== MeSH D12.776.467.499.600 – ephrin-b1 ==== ==== MeSH D12.776.467.499.700 – ephrin-b2 ==== ==== MeSH D12.776.467.499.800 – ephrin-b3 ==== === MeSH D12.776.467.750 – interferons === ==== MeSH
|
{
"page_id": 5505240,
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"title": "List of MeSH codes (D12.776)"
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|
D12.776.467.750.500 – interferon type i ==== MeSH D12.776.467.750.500.125 – interferon type i, recombinant MeSH D12.776.467.750.500.125.100 – interferon alfa-2a MeSH D12.776.467.750.500.125.150 – interferon alfa-2b MeSH D12.776.467.750.500.125.200 – interferon alfa-2c MeSH D12.776.467.750.500.250 – interferon-alpha MeSH D12.776.467.750.500.250.100 – interferon alfa-2a MeSH D12.776.467.750.500.250.150 – interferon alfa-2b MeSH D12.776.467.750.500.250.200 – interferon alfa-2c MeSH D12.776.467.750.500.275 – interferon-beta ==== MeSH D12.776.467.750.550 – interferon type ii ==== MeSH D12.776.467.750.550.510 – interferon-gamma, recombinant === MeSH D12.776.467.875 – nerve growth factors === ==== MeSH D12.776.467.875.100 – brain-derived neurotrophic factor ==== ==== MeSH D12.776.467.875.212 – ciliary neurotrophic factor ==== ==== MeSH D12.776.467.875.325 – glia maturation factor ==== ==== MeSH D12.776.467.875.381 – glial cell line-derived neurotrophic factors ==== MeSH D12.776.467.875.381.500 – glial cell line-derived neurotrophic factor MeSH D12.776.467.875.381.750 – neurturin ==== MeSH D12.776.467.875.437 – nerve growth factor ==== ==== MeSH D12.776.467.875.550 – neuregulins ==== MeSH D12.776.467.875.550.750 – neuregulin-1 ==== MeSH D12.776.467.875.775 – neurotrophin 3 ==== ==== MeSH D12.776.467.875.887 – pituitary adenylate cyclase-activating polypeptide ==== === MeSH D12.776.467.890 – parathyroid hormone-related protein === === MeSH D12.776.467.906 – semaphorins === ==== MeSH D12.776.467.906.374 – semaphorin-3a ==== === MeSH D12.776.467.937 – somatomedins === ==== MeSH D12.776.467.937.400 – insulin-like growth factor i ==== ==== MeSH D12.776.467.937.420 – insulin-like growth factor ii ==== === MeSH D12.776.467.968 – tumor necrosis factors === ==== MeSH D12.776.467.968.500 – lymphotoxin ==== ==== MeSH D12.776.467.968.750 – tumor necrosis factor-alpha ==== === MeSH D12.776.467.984 – wnt proteins === ==== MeSH D12.776.467.984.500 – wnt1 protein ==== ==== MeSH D12.776.467.984.750 – wnt2 protein ==== == MeSH D12.776.476 – intracellular signaling peptides and proteins == See List of MeSH codes (D12.776.476). == MeSH D12.776.486 – iodoproteins == === MeSH D12.776.486.706 – thyroglobulin === == MeSH D12.776.494 – iron-regulatory proteins == === MeSH D12.776.494.500 – iron regulatory protein 1 === === MeSH D12.776.494.750 – iron regulatory protein 2 === == MeSH D12.776.503 – lectins == === MeSH
|
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"page_id": 5505240,
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D12.776.503.139 – antigens, cd22 === === MeSH D12.776.503.280 – lectins, c-type === ==== MeSH D12.776.503.280.061 – antigens, cd94 ==== ==== MeSH D12.776.503.280.124 – asialoglycoprotein receptor ==== ==== MeSH D12.776.503.280.249 – collectins ==== MeSH D12.776.503.280.249.500 – mannose-binding lectin MeSH D12.776.503.280.249.600 – pulmonary surfactant-associated protein a MeSH D12.776.503.280.249.625 – pulmonary surfactant-associated protein d === MeSH D12.776.503.295 – calnexin === === MeSH D12.776.503.303 – calreticulin === === MeSH D12.776.503.307 – galectins === ==== MeSH D12.776.503.307.100 – galectin-1 ==== ==== MeSH D12.776.503.307.200 – galectin-2 ==== ==== MeSH D12.776.503.307.300 – galectin-3 ==== ==== MeSH D12.776.503.307.400 – galectin-4 ==== === MeSH D12.776.503.311 – mannose-binding lectins === ==== MeSH D12.776.503.311.500 – mannose-binding lectin ==== === MeSH D12.776.503.499 – plant lectins === ==== MeSH D12.776.503.499.249 – abrin ==== ==== MeSH D12.776.503.499.500 – concanavalin a ==== ==== MeSH D12.776.503.499.625 – peanut agglutinin ==== ==== MeSH D12.776.503.499.750 – phytohemagglutinins ==== ==== MeSH D12.776.503.499.875 – pokeweed mitogens ==== ==== MeSH D12.776.503.499.937 – ricin ==== ==== MeSH D12.776.503.499.968 – wheat germ agglutinins ==== MeSH D12.776.503.499.968.900 – wheat germ agglutinin-horseradish peroxidase conjugate === MeSH D12.776.503.687 – receptors, n-acetylglucosamine === === MeSH D12.776.503.843 – selectins === ==== MeSH D12.776.503.843.300 – e-selectin ==== ==== MeSH D12.776.503.843.510 – l-selectin ==== ==== MeSH D12.776.503.843.775 – p-selectin ==== == MeSH D12.776.521 – lipoproteins == === MeSH D12.776.521.170 – chromogranins === === MeSH D12.776.521.242 – chylomicrons === === MeSH D12.776.521.400 – lipoprotein(a) === === MeSH D12.776.521.450 – lipoprotein-X === === MeSH D12.776.521.479 – lipoproteins, hdl === ==== MeSH D12.776.521.479.470 – lipoproteins, hdl cholesterol ==== === MeSH D12.776.521.550 – lipoproteins, ldl === ==== MeSH D12.776.521.550.500 – lipoproteins, ldl cholesterol ==== === MeSH D12.776.521.622 – lipoproteins, vldl === ==== MeSH D12.776.521.622.700 – lipoproteins, vldl cholesterol ==== === MeSH D12.776.521.800 – platelet factor 3 === === MeSH D12.776.521.925 – vitellogenins === == MeSH D12.776.526 – ldl-receptor related proteins == === MeSH D12.776.526.100
|
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|
– ldl-receptor related protein 1 === === MeSH D12.776.526.200 – ldl-receptor related protein 2 === == MeSH D12.776.529 – lithostathine == == MeSH D12.776.532 – luminescent protein == === MeSH D12.776.532.020 – aequorin === === MeSH D12.776.532.265 – green fluorescent protein === === MeSH D12.776.532.510 – luciferase === ==== MeSH D12.776.532.510.249 – luciferases, bacterial ==== ==== MeSH D12.776.532.510.500 – Firefly luciferase ==== ==== MeSH D12.776.532.510.750 – Renilla luciferase ==== == MeSH D12.776.543 – membrane proteins == See List of MeSH codes (D12.776.543). == MeSH D12.776.556 – metalloproteins == === MeSH D12.776.556.080 – azurin === === MeSH D12.776.556.151 – ceruloplasmin === === MeSH D12.776.556.462 – hemocyanin === === MeSH D12.776.556.526 – hemosiderin === === MeSH D12.776.556.579 – iron-binding proteins === ==== MeSH D12.776.556.579.249 – ferritin ==== MeSH D12.776.556.579.249.290 – apoferritin ==== MeSH D12.776.556.579.311 – lactoferrin ==== ==== MeSH D12.776.556.579.374 – nonheme iron proteins ==== MeSH D12.776.556.579.374.187 – hemerythrin MeSH D12.776.556.579.374.281 – inositol oxygenase MeSH D12.776.556.579.374.375 – iron-sulfur proteins MeSH D12.776.556.579.374.375.025 – adrenodoxin MeSH D12.776.556.579.374.375.150 – ferredoxin-nitrite reductase MeSH D12.776.556.579.374.375.275 – ferredoxins MeSH D12.776.556.579.374.375.275.450 – molybdoferredoxin MeSH D12.776.556.579.374.375.275.725 – rubredoxins MeSH D12.776.556.579.374.375.637 – iron regulatory protein 1 MeSH D12.776.556.579.374.375.818 – iron regulatory protein 2 MeSH D12.776.556.579.374.375.863 – electron transport complex i MeSH D12.776.556.579.374.375.863.500 – nadh dehydrogenase MeSH D12.776.556.579.374.375.909 – electron transport complex ii MeSH D12.776.556.579.374.375.909.500 – succinate dehydrogenase MeSH D12.776.556.579.374.375.954 – electron transport complex iii MeSH D12.776.556.579.374.375.977 – nitrate reductase (nad(p)h) MeSH D12.776.556.579.374.375.988 – nitrate reductase (nadph) MeSH D12.776.556.579.374.450 – lipoxygenase MeSH D12.776.556.579.374.450.025 – arachidonate lipoxygenases MeSH D12.776.556.579.374.450.025.020 – arachidonate 5-lipoxygenase MeSH D12.776.556.579.374.450.025.025 – arachidonate 12-lipoxygenase MeSH D12.776.556.579.374.450.025.030 – arachidonate 15-lipoxygenase MeSH D12.776.556.579.374.687 – retinal dehydrogenase MeSH D12.776.556.579.374.925 – tyrosine 3-monooxygenase ==== MeSH D12.776.556.579.500 – transferrin ==== === MeSH D12.776.556.670 – metallothionein === === MeSH D12.776.556.760 – plastocyanin === == MeSH D12.776.575 – mitochondrial proteins == === MeSH D12.776.575.750 – mitochondrial membrane
|
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transport proteins === ==== MeSH D12.776.575.750.500 – mitochondrial adp, atp translocases ==== MeSH D12.776.575.750.500.100 – adenine nucleotide translocator 1 MeSH D12.776.575.750.500.200 – adenine nucleotide translocator 2 MeSH D12.776.575.750.500.300 – adenine nucleotide translocator 3 == MeSH D12.776.580 – molecular chaperones == === MeSH D12.776.580.157 – alpha-crystallins === ==== MeSH D12.776.580.157.149 – alpha-crystallin a chain ==== ==== MeSH D12.776.580.157.300 – alpha-crystallin b chain ==== === MeSH D12.776.580.210 – chaperonins === ==== MeSH D12.776.580.210.175 – chaperonin 10 ==== MeSH D12.776.580.210.175.325 – groes protein ==== MeSH D12.776.580.210.180 – chaperonin 60 ==== MeSH D12.776.580.210.180.325 – groel protein === MeSH D12.776.580.215 – clusterin === === MeSH D12.776.580.218 – heat-shock proteins, small === ==== MeSH D12.776.580.218.500 – hsp20 heat-shock proteins ==== ==== MeSH D12.776.580.218.750 – hsp30 heat-shock proteins ==== === MeSH D12.776.580.220 – hsp47 heat-shock proteins === === MeSH D12.776.580.295 – hsp70 heat-shock proteins === ==== MeSH D12.776.580.295.200 – hsc70 heat-shock proteins ==== ==== MeSH D12.776.580.295.249 – hsp110 heat-shock proteins ==== ==== MeSH D12.776.580.295.750 – hsp72 heat-shock proteins ==== === MeSH D12.776.580.380 – hsp90 heat-shock proteins === === MeSH D12.776.580.845 – neuroendocrine secretory protein 7b2 === == MeSH D12.776.602 – mutant proteins == === MeSH D12.776.602.500 – mutant chimeric proteins === ==== MeSH D12.776.602.500.500 – oncogene proteins, fusion ==== MeSH D12.776.602.500.500.100 – fusion proteins, bcr-abl MeSH D12.776.602.500.500.320 – fusion proteins, gag-onc MeSH D12.776.602.500.500.320.700 – oncogene protein p65(gag-jun) MeSH D12.776.602.500.500.660 – oncogene protein tpr-met == MeSH D12.776.624 – neoplasm proteins == === MeSH D12.776.624.050 – autocrine motility factor === === MeSH D12.776.624.100 – fusion proteins, bcr-abl === === MeSH D12.776.624.553 – myeloma proteins === === MeSH D12.776.624.664 – oncogene proteins === ==== MeSH D12.776.624.664.500 – oncogene proteins, fusion ==== MeSH D12.776.624.664.500.100 – fusion proteins, bcr-abl MeSH D12.776.624.664.500.320 – fusion proteins, gag-onc MeSH D12.776.624.664.500.320.700 – oncogene protein p65(gag-jun) MeSH D12.776.624.664.500.660 – oncogene protein tpr-met ==== MeSH D12.776.624.664.520 – oncogene
|
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proteins, viral ==== MeSH D12.776.624.664.520.045 – adenovirus early proteins MeSH D12.776.624.664.520.045.050 – adenovirus E1 proteins MeSH D12.776.624.664.520.045.050.100 – adenovirus E1A proteins MeSH D12.776.624.664.520.045.050.110 – adenovirus E1B proteins MeSH D12.776.624.664.520.045.060 – adenovirus e2 proteins MeSH D12.776.624.664.520.045.070 – adenovirus e3 proteins MeSH D12.776.624.664.520.045.080 – adenovirus e4 proteins MeSH D12.776.624.664.520.090 – antigens, polyomavirus transforming MeSH D12.776.624.664.520.420 – papillomavirus e7 proteins MeSH D12.776.624.664.520.750 – retroviridae proteins, oncogenic MeSH D12.776.624.664.520.750.320 – fusion proteins, gag-onc MeSH D12.776.624.664.520.750.320.700 – oncogene protein p65(gag-jun) MeSH D12.776.624.664.520.750.470 – gene products, rex MeSH D12.776.624.664.520.750.480 – gene products, tax MeSH D12.776.624.664.520.750.650 – oncogene protein gp140(v-fms) MeSH D12.776.624.664.520.750.710 – oncogene protein p21(ras) MeSH D12.776.624.664.520.750.750 – oncogene protein p55(v-myc) MeSH D12.776.624.664.520.750.760 – oncogene protein pp60(v-src) MeSH D12.776.624.664.520.750.788 – oncogene protein v-akt MeSH D12.776.624.664.520.750.817 – oncogene protein v-cbl MeSH D12.776.624.664.520.750.846 – oncogene protein v-crk MeSH D12.776.624.664.520.750.860 – oncogene protein v-maf MeSH D12.776.624.664.520.750.875 – oncogene proteins v-abl MeSH D12.776.624.664.520.750.882 – oncogene proteins v-erba MeSH D12.776.624.664.520.750.883 – oncogene proteins v-erbb MeSH D12.776.624.664.520.750.887 – oncogene proteins v-fos MeSH D12.776.624.664.520.750.900 – oncogene proteins v-mos MeSH D12.776.624.664.520.750.903 – oncogene proteins v-myb MeSH D12.776.624.664.520.750.920 – oncogene proteins v-raf MeSH D12.776.624.664.520.750.925 – oncogene proteins v-rel MeSH D12.776.624.664.520.750.935 – oncogene proteins v-sis ==== MeSH D12.776.624.664.700 – proto-oncogene proteins ==== MeSH D12.776.624.664.700.100 – cyclin d1 MeSH D12.776.624.664.700.110 – fibroblast growth factor 4 MeSH D12.776.624.664.700.112 – fibroblast growth factor 6 MeSH D12.776.624.664.700.114 – fms-like tyrosine kinase 3 MeSH D12.776.624.664.700.120 – receptor, fibroblast growth factor, type 3 MeSH D12.776.624.664.700.130 – muts homolog 2 protein MeSH D12.776.624.664.700.148 – myeloid-lymphoid leukemia protein MeSH D12.776.624.664.700.167 – proto-oncogene proteins c-abl MeSH D12.776.624.664.700.168 – proto-oncogene proteins c-akt MeSH D12.776.624.664.700.169 – proto-oncogene proteins c-bcl-2 MeSH D12.776.624.664.700.170 – proto-oncogene proteins c-bcl-6 MeSH D12.776.624.664.700.171 – proto-oncogene proteins c-bcr MeSH D12.776.624.664.700.172 – proto-oncogene proteins c-cbl MeSH D12.776.624.664.700.174 – proto-oncogene proteins c-crk MeSH D12.776.624.664.700.175 – proto-oncogene proteins c-ets MeSH D12.776.624.664.700.175.100 – proto-oncogene protein c-ets-1 MeSH D12.776.624.664.700.175.200
|
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"title": "List of MeSH codes (D12.776)"
}
|
– proto-oncogene protein c-ets-2 MeSH D12.776.624.664.700.175.400 – proto-oncogene protein c-fli-1 MeSH D12.776.624.664.700.175.600 – ternary complex factors MeSH D12.776.624.664.700.175.600.100 – ets-domain protein elk-1 MeSH D12.776.624.664.700.175.600.300 – ets-domain protein elk-4 MeSH D12.776.624.664.700.177 – proto-oncogene proteins c-fes MeSH D12.776.624.664.700.179 – proto-oncogene proteins c-fos MeSH D12.776.624.664.700.180 – proto-oncogene proteins c-fyn MeSH D12.776.624.664.700.181 – proto-oncogene proteins c-hck MeSH D12.776.624.664.700.182 – proto-oncogene proteins c-jun MeSH D12.776.624.664.700.183 – proto-oncogene proteins c-kit MeSH D12.776.624.664.700.184 – proto-oncogene proteins c-maf MeSH D12.776.624.664.700.185 – proto-oncogene proteins c-mdm2 MeSH D12.776.624.664.700.186 – proto-oncogene proteins c-met MeSH D12.776.624.664.700.187 – proto-oncogene proteins c-mos MeSH D12.776.624.664.700.188 – proto-oncogene proteins c-myb MeSH D12.776.624.664.700.189 – proto-oncogene proteins c-myc MeSH D12.776.624.664.700.191 – proto-oncogene proteins c-pim-1 MeSH D12.776.624.664.700.192 – proto-oncogene proteins c-rel MeSH D12.776.624.664.700.194 – proto-oncogene proteins c-ret MeSH D12.776.624.664.700.195 – proto-oncogene proteins c-sis MeSH D12.776.624.664.700.198 – proto-oncogene proteins c-vav MeSH D12.776.624.664.700.199 – proto-oncogene proteins c-yes MeSH D12.776.624.664.700.200 – proto-oncogene proteins p21(ras) MeSH D12.776.624.664.700.202 – proto-oncogene proteins pp60(c-src) MeSH D12.776.624.664.700.204 – raf kinases MeSH D12.776.624.664.700.204.200 – proto-oncogene proteins b-raf MeSH D12.776.624.664.700.204.500 – proto-oncogene proteins c-raf MeSH D12.776.624.664.700.205 – RNA-binding protein EWS MeSH D12.776.624.664.700.250 – lymphocyte specific protein tyrosine kinase p56(lck) MeSH D12.776.624.664.700.642 – receptor, erbb-2 MeSH D12.776.624.664.700.790 – receptor, erbb-3 MeSH D12.776.624.664.700.800 – receptor, macrophage colony-stimulating factor MeSH D12.776.624.664.700.830 – receptors, thyroid hormone MeSH D12.776.624.664.700.830.500 – thyroid hormone receptors alpha MeSH D12.776.624.664.700.830.750 – thyroid hormone receptors beta MeSH D12.776.624.664.700.915 – RNA-binding protein FUS MeSH D12.776.624.664.700.957 – stathmin MeSH D12.776.624.664.700.967 – wnt1 protein MeSH D12.776.624.664.700.978 – wnt2 protein === MeSH D12.776.624.776 – tumor suppressor proteins === ==== MeSH D12.776.624.776.049 – adenomatous polyposis coli protein ==== ==== MeSH D12.776.624.776.100 – brca1 protein ==== ==== MeSH D12.776.624.776.101 – brca2 protein ==== ==== MeSH D12.776.624.776.355 – cyclin-dependent kinase inhibitor proteins ==== MeSH D12.776.624.776.355.100 – cyclin-dependent kinase inhibitor p15 MeSH D12.776.624.776.355.200 – cyclin-dependent kinase inhibitor p16 MeSH D12.776.624.776.355.300 – cyclin-dependent kinase inhibitor p18 MeSH D12.776.624.776.355.400
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
– cyclin-dependent kinase inhibitor p19 MeSH D12.776.624.776.355.500 – cyclin-dependent kinase inhibitor p21 MeSH D12.776.624.776.355.600 – cyclin-dependent kinase inhibitor p27 MeSH D12.776.624.776.355.700 – cyclin-dependent kinase inhibitor p57 ==== MeSH D12.776.624.776.482 – kangai-1 protein ==== ==== MeSH D12.776.624.776.610 – neurofibromin 1 ==== ==== MeSH D12.776.624.776.612 – neurofibromin 2 ==== ==== MeSH D12.776.624.776.695 – pten phosphohydrolase ==== ==== MeSH D12.776.624.776.717 – retinoblastoma-like protein p107 ==== ==== MeSH D12.776.624.776.735 – retinoblastoma-like protein p130 ==== ==== MeSH D12.776.624.776.745 – retinoblastoma protein ==== ==== MeSH D12.776.624.776.760 – smad4 protein ==== ==== MeSH D12.776.624.776.772 – tumor suppressor protein p14arf ==== ==== MeSH D12.776.624.776.775 – tumor suppressor protein p53 ==== ==== MeSH D12.776.624.776.865 – von hippel-lindau tumor suppressor protein ==== ==== MeSH D12.776.624.776.960 – wt1 proteins ==== == MeSH D12.776.641 – nerve tissue proteins == See List of MeSH codes (D12.776.641). == MeSH D12.776.660 – nuclear proteins == See List of MeSH codes (D12.776.660). == MeSH D12.776.664 – nucleoproteins == === MeSH D12.776.664.224 – chromatin === ==== MeSH D12.776.664.224.270 – euchromatin ==== ==== MeSH D12.776.664.224.466 – heterochromatin ==== ==== MeSH D12.776.664.224.550 – nucleosomes ==== === MeSH D12.776.664.235 – chromosomal proteins, non-histone === ==== MeSH D12.776.664.235.199 – centromere protein b ==== ==== MeSH D12.776.664.235.400 – high mobility group proteins ==== MeSH D12.776.664.235.400.400 – hmgn proteins MeSH D12.776.664.235.400.400.200 – hmgn1 protein MeSH D12.776.664.235.400.400.300 – hmgn2 protein MeSH D12.776.664.235.400.500 – hmga proteins MeSH D12.776.664.235.400.500.100 – hmga1a protein MeSH D12.776.664.235.400.500.200 – hmga1b protein MeSH D12.776.664.235.400.500.300 – hmga1c protein MeSH D12.776.664.235.400.500.600 – hmga2 protein MeSH D12.776.664.235.400.600 – hmgb proteins MeSH D12.776.664.235.400.600.300 – hmgb1 protein MeSH D12.776.664.235.400.600.600 – hmgb2 protein MeSH D12.776.664.235.400.600.800 – hmgb3 protein MeSH D12.776.664.235.400.700 – sex-determining region y protein MeSH D12.776.664.235.400.800 – tcf transcription factors MeSH D12.776.664.235.400.800.500 – lymphoid enhancer-binding factor 1 MeSH D12.776.664.235.400.800.750 – t cell transcription factor 1 ==== MeSH D12.776.664.235.700 – methyl-cpg-binding protein 2 ==== === MeSH D12.776.664.275
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
– deoxyribonucleoproteins === === MeSH D12.776.664.469 – histones === === MeSH D12.776.664.750 – protamines === ==== MeSH D12.776.664.750.270 – clupeine ==== ==== MeSH D12.776.664.750.739 – salmine ==== === MeSH D12.776.664.962 – RNA-binding proteins === ==== MeSH D12.776.664.962.061 – butyrate response factor 1 ==== ==== MeSH D12.776.664.962.124 – fragile x mental retardation protein ==== ==== MeSH D12.776.664.962.249 – host factor 1 protein ==== ==== MeSH D12.776.664.962.311 – hu paraneoplastic encephalomyelitis antigens ==== ==== MeSH D12.776.664.962.374 – iron regulatory protein 1 ==== ==== MeSH D12.776.664.962.437 – iron regulatory protein 2 ==== ==== MeSH D12.776.664.962.444 – mrna cleavage and polyadenylation factors ==== MeSH D12.776.664.962.444.240 – cleavage and polyadenylation specificity factor MeSH D12.776.664.962.444.249 – cleavage stimulation factor ==== MeSH D12.776.664.962.452 – poly(a)-binding proteins ==== MeSH D12.776.664.962.452.249 – poly(a)-binding protein i MeSH D12.776.664.962.452.500 – poly(a)-binding protein ii ==== MeSH D12.776.664.962.468 – polypyrimidine tract-binding protein ==== ==== MeSH D12.776.664.962.500 – ribonucleoproteins ==== MeSH D12.776.664.962.500.500 – heterogeneous-nuclear ribonucleoproteins MeSH D12.776.664.962.500.500.061 – RNA-binding protein FUS MeSH D12.776.664.962.500.500.100 – heterogeneous-nuclear ribonucleoprotein group a-b MeSH D12.776.664.962.500.500.200 – heterogeneous-nuclear ribonucleoprotein group c MeSH D12.776.664.962.500.500.300 – heterogeneous-nuclear ribonucleoprotein d MeSH D12.776.664.962.500.500.400 – heterogeneous-nuclear ribonucleoprotein group f-h MeSH D12.776.664.962.500.500.500 – heterogeneous-nuclear ribonucleoprotein k MeSH D12.776.664.962.500.500.600 – heterogeneous-nuclear ribonucleoprotein l MeSH D12.776.664.962.500.500.700 – heterogeneous-nuclear ribonucleoprotein group m MeSH D12.776.664.962.500.500.800 – heterogeneous-nuclear ribonucleoprotein u MeSH D12.776.664.962.500.500.900 – RNA-binding protein EWS MeSH D12.776.664.962.500.625 – ribonuclease p MeSH D12.776.664.962.500.750 – ribonucleoproteins, small cytoplasmic MeSH D12.776.664.962.500.750.800 – signal recognition particle MeSH D12.776.664.962.500.875 – ribonucleoproteins, small nuclear MeSH D12.776.664.962.500.875.590 – ribonucleoproteins, small nucleolar MeSH D12.776.664.962.500.875.600 – ribonucleoprotein, u1 small nuclear MeSH D12.776.664.962.500.875.605 – ribonucleoprotein, u2 small nuclear MeSH D12.776.664.962.500.875.615 – ribonucleoprotein, u4-u6 small nuclear MeSH D12.776.664.962.500.875.620 – ribonucleoprotein, u5 small nuclear MeSH D12.776.664.962.500.875.625 – ribonucleoprotein, u7 small nuclear MeSH D12.776.664.962.500.906 – RNA-induced silencing complex MeSH D12.776.664.962.500.937 – vault ribonucleoprotein particles ==== MeSH D12.776.664.962.750 – rna cap-binding proteins ==== MeSH
|
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"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
D12.776.664.962.750.374 – eukaryotic initiation factor-4f MeSH D12.776.664.962.750.750 – nuclear cap-binding protein complex == MeSH D12.776.691 – oxidative phosphorylation coupling factors == == MeSH D12.776.719 – peptones == == MeSH D12.776.744 – phosphoproteins == === MeSH D12.776.744.049 – bcl-associated death protein === === MeSH D12.776.744.100 – brca1 protein === === MeSH D12.776.744.150 – caseins === === MeSH D12.776.744.287 – caveolin 1 === === MeSH D12.776.744.356 – caveolin 2 === === MeSH D12.776.744.360 – cdc2 protein kinase === === MeSH D12.776.744.390 – cortactin === === MeSH D12.776.744.425 – crk-associated substrate protein === === MeSH D12.776.744.459 – dopamine and camp-regulated phosphoprotein 32 === === MeSH D12.776.744.476 – fanconi anemia complementation group a protein === === MeSH D12.776.744.484 – fanconi anemia complementation group d2 protein === === MeSH D12.776.744.488 – fanconi anemia complementation group g protein === === MeSH D12.776.744.493 – focal adhesion kinase 1 === === MeSH D12.776.744.562 – interferon regulatory factor-3 === === MeSH D12.776.744.631 – interferon regulatory factor-7 === === MeSH D12.776.744.665 – paxillin === === MeSH D12.776.744.700 – phosvitin === === MeSH D12.776.744.736 – plectin === === MeSH D12.776.744.741 – smad proteins, receptor-regulated === ==== MeSH D12.776.744.741.500 – smad1 protein ==== ==== MeSH D12.776.744.741.750 – smad2 protein ==== ==== MeSH D12.776.744.741.875 – smad3 protein ==== ==== MeSH D12.776.744.741.937 – smad5 protein ==== ==== MeSH D12.776.744.741.968 – smad8 protein ==== === MeSH D12.776.744.747 – retinoblastoma-like protein p107 === === MeSH D12.776.744.755 – retinoblastoma-like protein p130 === === MeSH D12.776.744.770 – retinoblastoma protein === === MeSH D12.776.744.772 – stathmin === === MeSH D12.776.744.840 – synapsins === === MeSH D12.776.744.845 – tumor suppressor protein p53 === === MeSH D12.776.744.925 – vitellogenins === == MeSH D12.776.752 – photoreceptors, microbial == === MeSH D12.776.752.249 – bacteriochlorophylls === ==== MeSH D12.776.752.249.500 – bacteriochlorophyll a ==== === MeSH D12.776.752.812 – rhodopsins, microbial === ==== MeSH D12.776.752.812.249 –
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
}
|
bacteriorhodopsins ==== ==== MeSH D12.776.752.812.500 – halorhodopsins ==== ==== MeSH D12.776.752.812.750 – sensory rhodopsins ==== == MeSH D12.776.758 – photosynthetic reaction center complex proteins == === MeSH D12.776.758.249 – light-harvesting protein complexes === === MeSH D12.776.758.374 – cytochrome b6f complex === ==== MeSH D12.776.758.374.500 – cytochromes b6 ==== ==== MeSH D12.776.758.374.750 – cytochromes f ==== ==== MeSH D12.776.758.374.875 – plastoquinol-plastocyanin reductase ==== === MeSH D12.776.758.500 – photosystem i protein complex === === MeSH D12.776.758.750 – photosystem ii protein complex === == MeSH D12.776.765 – plant proteins == === MeSH D12.776.765.149 – arabidopsis proteins === ==== MeSH D12.776.765.149.500 – agamous protein, arabidopsis ==== === MeSH D12.776.765.249 – deficiens protein === === MeSH D12.776.765.319 – ferredoxins === === MeSH D12.776.765.365 – g-box binding factors === === MeSH D12.776.765.412 – gluten === ==== MeSH D12.776.765.412.400 – gliadin ==== === MeSH D12.776.765.500 – leghemoglobin === === MeSH D12.776.765.537 – periplasmic proteins === === MeSH D12.776.765.650 – phycocyanin === === MeSH D12.776.765.665 – phycoerythrin === === MeSH D12.776.765.675 – phytochrome === ==== MeSH D12.776.765.675.249 – phytochrome a ==== ==== MeSH D12.776.765.675.500 – phytochrome b ==== === MeSH D12.776.765.678 – plant lectins === ==== MeSH D12.776.765.678.249 – abrin ==== ==== MeSH D12.776.765.678.500 – concanavalin a ==== ==== MeSH D12.776.765.678.625 – peanut agglutinin ==== ==== MeSH D12.776.765.678.750 – phytohemagglutinins ==== ==== MeSH D12.776.765.678.875 – pokeweed mitogens ==== ==== MeSH D12.776.765.678.937 – ricin ==== ==== MeSH D12.776.765.678.968 – wheat germ agglutinins ==== MeSH D12.776.765.678.968.900 – wheat germ agglutinin-horseradish peroxidase conjugate === MeSH D12.776.765.680 – plastocyanin === === MeSH D12.776.765.741 – soybean proteins === ==== MeSH D12.776.765.741.500 – trypsin inhibitor, bowman-birk soybean ==== ==== MeSH D12.776.765.741.750 – trypsin inhibitor, kunitz soybean ==== === MeSH D12.776.765.760 – trichosanthin === === MeSH D12.776.765.836 – vegetable proteins === === MeSH D12.776.765.919 – zein === == MeSH D12.776.775 – polyproteins == === MeSH
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
D12.776.775.320 – gene products, env (gene) === === MeSH D12.776.775.330 – gene products, gag (gene) === ==== MeSH D12.776.775.330.300 – fusion proteins, gag-pol ==== === MeSH D12.776.775.360 – gene products, pol (gene) === ==== MeSH D12.776.775.360.300 – fusion proteins, gag-pol ==== == MeSH D12.776.780 – pregnancy proteins == === MeSH D12.776.780.400 – chorionic gonadotropin === ==== MeSH D12.776.780.400.125 – chorionic gonadotropin, beta subunit, human ==== === MeSH D12.776.780.451 – gonadotropins, equine === === MeSH D12.776.780.650 – placental lactogen === === MeSH D12.776.780.675 – pregnancy-associated alpha 2-macroglobulins === === MeSH D12.776.780.700 – pregnancy-associated plasma protein-a === === MeSH D12.776.780.730 – pregnancy-specific beta 1-glycoproteins === == MeSH D12.776.785 – prions == === MeSH D12.776.785.680 – prpc proteins === === MeSH D12.776.785.700 – prpsc proteins === ==== MeSH D12.776.785.700.700 – prp 27-30 protein ==== == MeSH D12.776.796 – protein hydrolysates == == MeSH D12.776.800 – protein isoforms == === MeSH D12.776.800.300 – isoenzymes === == MeSH D12.776.811 – protein precursors == === MeSH D12.776.811.050 – amyloid beta-protein precursor === === MeSH D12.776.811.070 – angiotensinogen === === MeSH D12.776.811.300 – fibrinogen === ==== MeSH D12.776.811.300.290 – fibrin fibrinogen degradation products ==== ==== MeSH D12.776.811.300.310 – fibrinopeptide a ==== ==== MeSH D12.776.811.300.320 – fibrinopeptide b ==== === MeSH D12.776.811.360 – glucagon precursors === === MeSH D12.776.811.420 – kininogens === ==== MeSH D12.776.811.420.350 – kininogen, high-molecular-weight ==== ==== MeSH D12.776.811.420.400 – kininogen, low-molecular-weight ==== === MeSH D12.776.811.690 – procollagen === === MeSH D12.776.811.706 – proinsulin === ==== MeSH D12.776.811.706.250 – c-peptide ==== === MeSH D12.776.811.730 – pro-opiomelanocortin === === MeSH D12.776.811.850 – tropoelastin === == MeSH D12.776.813 – protein subunits == == MeSH D12.776.816 – proteolipids == === MeSH D12.776.816.500 – myelin proteolipid protein === === MeSH D12.776.816.750 – pulmonary surfactant-associated protein c === == MeSH D12.776.817 – proteome == == MeSH D12.776.820 – protozoan proteins
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
== === MeSH D12.776.820.500 – merozoite surface protein 1 === == MeSH D12.776.823 – pulmonary surfactant-associated proteins == === MeSH D12.776.823.100 – pulmonary surfactant-associated protein a === === MeSH D12.776.823.124 – pulmonary surfactant-associated protein b === === MeSH D12.776.823.186 – pulmonary surfactant-associated protein c === === MeSH D12.776.823.249 – pulmonary surfactant-associated protein d === == MeSH D12.776.826 – receptors, cytoplasmic and nuclear == === MeSH D12.776.826.119 – hepatocyte nuclear factor 4 === === MeSH D12.776.826.239 – peroxisome proliferator-activated receptors === ==== MeSH D12.776.826.239.500 – PPAR-alpha ==== ==== MeSH D12.776.826.239.530 – PPAR-beta ==== ==== MeSH D12.776.826.239.555 – PPAR-delta ==== ==== MeSH D12.776.826.239.588 – PPAR-gamma ==== === MeSH D12.776.826.480 – receptors, aryl hydrocarbon === === MeSH D12.776.826.535 – receptors, calcitriol === === MeSH D12.776.826.590 – receptors, melatonin === === MeSH D12.776.826.701 – receptors, retinoic acid === ==== MeSH D12.776.826.701.500 – Retinoid X receptors ==== MeSH D12.776.826.701.500.500 – Retinoid X receptor alpha MeSH D12.776.826.701.500.625 – Retinoid X receptor beta MeSH D12.776.826.701.500.750 – Retinoid X receptor gamma === MeSH D12.776.826.750 – receptors, steroid === ==== MeSH D12.776.826.750.074 – coup transcription factors ==== MeSH D12.776.826.750.074.249 – coup transcription factor i MeSH D12.776.826.750.074.500 – coup transcription factor ii ==== MeSH D12.776.826.750.150 – receptors, androgen ==== ==== MeSH D12.776.826.750.350 – receptors, estrogen ==== MeSH D12.776.826.750.350.174 – estrogen receptor alpha MeSH D12.776.826.750.350.262 – estrogen receptor beta MeSH D12.776.826.750.350.350 – receptors, estradiol ==== MeSH D12.776.826.750.430 – receptors, glucocorticoid ==== ==== MeSH D12.776.826.750.530 – receptors, mineralocorticoid ==== MeSH D12.776.826.750.530.150 – receptors, aldosterone ==== MeSH D12.776.826.750.765 – receptors, progesterone ==== === MeSH D12.776.826.850 – receptors, thyroid hormone === ==== MeSH D12.776.826.850.500 – thyroid hormone receptors alpha ==== ==== MeSH D12.776.826.850.750 – thyroid hormone receptors beta ==== == MeSH D12.776.827 – receptors, drug == === MeSH D12.776.827.275 – immunophilins === ==== MeSH D12.776.827.275.300 – cyclophilins ==== ==== MeSH D12.776.827.275.700 – tacrolimus binding
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
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|
proteins ==== MeSH D12.776.827.275.700.500 – tacrolimus binding protein 1a === MeSH D12.776.827.550 – receptors, phencyclidine === == MeSH D12.776.828 – recombinant proteins == === MeSH D12.776.828.075 – colony-stimulating factors, recombinant === ==== MeSH D12.776.828.075.350 – granulocyte colony stimulating factor, recombinant ==== MeSH D12.776.828.075.350.275 – filgrastim ==== MeSH D12.776.828.075.375 – granulocyte macrophage colony-stimulating factors, recombinant ==== === MeSH D12.776.828.150 – erythropoietin, recombinant === ==== MeSH D12.776.828.150.250 – epoetin alfa ==== === MeSH D12.776.828.200 – interferon type i, recombinant === ==== MeSH D12.776.828.200.100 – interferon alfa-2a ==== ==== MeSH D12.776.828.200.150 – interferon alfa-2b ==== ==== MeSH D12.776.828.200.201 – interferon alfa-2c ==== === MeSH D12.776.828.210 – interferon-gamma, recombinant === === MeSH D12.776.828.300 – recombinant fusion proteins === ==== MeSH D12.776.828.300.200 – cd4 immunoadhesins ==== === MeSH D12.776.828.868 – vaccines, synthetic === ==== MeSH D12.776.828.868.910 – vaccines, dna ==== ==== MeSH D12.776.828.868.915 – vaccines, edible ==== ==== MeSH D12.776.828.868.940 – vaccines, virosome ==== == MeSH D12.776.831 – reptilian proteins == == MeSH D12.776.835 – ribosomal proteins == === MeSH D12.776.835.700 – peptide elongation factors === ==== MeSH D12.776.835.700.350 – gtp phosphohydrolase-linked elongation factors ==== MeSH D12.776.835.700.350.200 – peptide elongation factor g MeSH D12.776.835.700.350.700 – peptide elongation factor tu MeSH D12.776.835.700.350.800 – peptide elongation factor 1 MeSH D12.776.835.700.350.850 – peptide elongation factor 2 === MeSH D12.776.835.725 – peptide initiation factors === ==== MeSH D12.776.835.725.868 – eukaryotic initiation factors ==== MeSH D12.776.835.725.868.124 – eukaryotic initiation factor-1 MeSH D12.776.835.725.868.249 – eukaryotic initiation factor-2 MeSH D12.776.835.725.868.374 – eukaryotic initiation factor-2b MeSH D12.776.835.725.868.437 – eukaryotic initiation factor 3 MeSH D12.776.835.725.868.500 – eukaryotic initiation factor-4f MeSH D12.776.835.725.868.500.500 – eukaryotic initiation factor-4a MeSH D12.776.835.725.868.500.750 – eukaryotic initiation factor-4e MeSH D12.776.835.725.868.500.875 – Eukaryotic initiation factor 4G MeSH D12.776.835.725.868.750 – eukaryotic initiation factor-5 ==== MeSH D12.776.835.725.934 – prokaryotic initiation factors ==== MeSH D12.776.835.725.934.374 – prokaryotic initiation factor-1 MeSH D12.776.835.725.934.562 – prokaryotic initiation factor-2
|
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"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
}
|
MeSH D12.776.835.725.934.750 – prokaryotic initiation factor-3 === MeSH D12.776.835.862 – peptide termination factors === === MeSH D12.776.835.931 – ribosomal protein s6 === == MeSH D12.776.850 – salivary proteins == (no MeSHNumber) LAPP (leech anti-platelet protein) - presently redirects to LAMP (software bundle) where the term is not mentioned === MeSH D12.776.850.400 – glue proteins, drosophila === == MeSH D12.776.860 – scleroproteins == === MeSH D12.776.860.300 – extracellular matrix proteins === ==== MeSH D12.776.860.300.030 – activated-leukocyte cell adhesion molecule ==== ==== MeSH D12.776.860.300.250 – collagen ==== MeSH D12.776.860.300.250.300 – fibrillar collagens MeSH D12.776.860.300.250.300.100 – Type I collagen MeSH D12.776.860.300.250.300.200 – Type II collagen MeSH D12.776.860.300.250.300.300 – Type III collagen MeSH D12.776.860.300.250.300.400 – Type V collagen MeSH D12.776.860.300.250.300.500 – Type XI collagen MeSH D12.776.860.300.250.400 – non-fibrillar collagens MeSH D12.776.860.300.250.400.100 – Type IV collagen MeSH D12.776.860.300.250.400.200 – Type VI collagen MeSH D12.776.860.300.250.400.300 – Type VII collagen MeSH D12.776.860.300.250.400.400 – Type VIII collagen MeSH D12.776.860.300.250.400.500 – Type X collagen MeSH D12.776.860.300.250.400.525 – Type XIII collagen MeSH D12.776.860.300.250.400.537 – Type XVIII collagen MeSH D12.776.860.300.250.400.537.500 – endostatins MeSH D12.776.860.300.250.400.550 – fibril-associated collagens MeSH D12.776.860.300.250.400.550.200 – Type IX collagen MeSH D12.776.860.300.250.400.550.300 – Type XII collagen MeSH D12.776.860.300.250.600 – procollagen MeSH D12.776.860.300.250.700 – tropocollagen ==== MeSH D12.776.860.300.350 – elastin ==== MeSH D12.776.860.300.350.700 – tropoelastin ==== MeSH D12.776.860.300.450 – fibronectins ==== ==== MeSH D12.776.860.300.675 – laminin ==== ==== MeSH D12.776.860.300.850 – tenascin ==== ==== MeSH D12.776.860.300.920 – vitronectin ==== === MeSH D12.776.860.476 – gelatin === === MeSH D12.776.860.607 – keratin === === MeSH D12.776.860.823 – reticulin === == MeSH D12.776.861 – selenium-binding proteins == == MeSH D12.776.864 – selenoproteins == === MeSH D12.776.864.124 – selenoprotein p === === MeSH D12.776.864.249 – selenoprotein r === === MeSH D12.776.864.500 – selenoprotein w === == MeSH D12.776.866 – seminal plasma proteins == === MeSH D12.776.866.249 – prostatic secretory proteins === ==== MeSH
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
}
|
D12.776.866.249.500 – prostate-specific antigen ==== === MeSH D12.776.866.500 – seminal vesicle secretory proteins === == MeSH D12.776.872 – serpins == === MeSH D12.776.872.030 – alpha 1-antichymotrypsin === === MeSH D12.776.872.035 – alpha 1-antitrypsin === === MeSH D12.776.872.043 – angiotensinogen === === MeSH D12.776.872.050 – antiplasmin === === MeSH D12.776.872.060 – antithrombins === ==== MeSH D12.776.872.060.060 – antithrombin iii ==== ==== MeSH D12.776.872.060.380 – heparin cofactor ii ==== ==== MeSH D12.776.872.060.690 – hirudins ==== === MeSH D12.776.872.140 – complement c1 inactivator proteins === === MeSH D12.776.872.350 – hsp47 heat-shock proteins === === MeSH D12.776.872.560 – ovalbumin === === MeSH D12.776.872.695 – plasminogen inactivators === ==== MeSH D12.776.872.695.500 – plasminogen activator inhibitor 1 ==== ==== MeSH D12.776.872.695.520 – plasminogen activator inhibitor 2 ==== ==== MeSH D12.776.872.695.700 – protein c inhibitor ==== === MeSH D12.776.872.830 – thyroxine-binding proteins === == MeSH D12.776.878 – silk == === MeSH D12.776.878.500 – fibroins === === MeSH D12.776.878.750 – sericins === == MeSH D12.776.884 – silver proteins == == MeSH D12.776.915 – thioredoxin == == MeSH D12.776.922 – thymosin == == MeSH D12.776.926 – tissue inhibitor of metalloproteinases == === MeSH D12.776.926.450 – tissue inhibitor of metalloproteinase-1 === === MeSH D12.776.926.500 – tissue inhibitor of metalloproteinase-2 === === MeSH D12.776.926.550 – tissue inhibitor of metalloproteinase-3 === == MeSH D12.776.930 – transcription factors == See List of MeSH codes (D12.776.930). == MeSH D12.776.947 – ubiquitins == === MeSH D12.776.947.249 – small ubiquitin-related modifier proteins === ==== MeSH D12.776.947.249.500 – sumo-1 protein ==== === MeSH D12.776.947.500 – ubiquitin === ==== MeSH D12.776.947.500.500 – polyubiquitin ==== ==== MeSH D12.776.947.500.750 – ubiquitin C ==== == MeSH D12.776.964 – viral proteins == === MeSH D12.776.964.700 – oncogene proteins, viral === ==== MeSH D12.776.964.700.045 – adenovirus early proteins ==== MeSH D12.776.964.700.045.050 – adenovirus e1 proteins MeSH D12.776.964.700.045.050.100 – adenovirus e1a proteins MeSH D12.776.964.700.045.050.110
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
}
|
– adenovirus e1b proteins MeSH D12.776.964.700.045.060 – adenovirus e2 proteins MeSH D12.776.964.700.045.070 – adenovirus e3 proteins MeSH D12.776.964.700.045.080 – adenovirus e4 proteins ==== MeSH D12.776.964.700.090 – antigens, polyomavirus transforming ==== ==== MeSH D12.776.964.700.750 – retroviridae proteins, oncogenic ==== MeSH D12.776.964.700.750.320 – fusion proteins, gag-onc MeSH D12.776.964.700.750.320.700 – oncogene protein p65(gag-jun) MeSH D12.776.964.700.750.470 – gene products, rex MeSH D12.776.964.700.750.480 – gene products, tax (gene) MeSH D12.776.964.700.750.650 – oncogene protein gp140(v-fms) MeSH D12.776.964.700.750.710 – oncogene protein p21(ras) MeSH D12.776.964.700.750.750 – oncogene protein p55(v-myc) MeSH D12.776.964.700.750.760 – oncogene protein pp60(v-src) MeSH D12.776.964.700.750.817 – oncogene protein v-maf MeSH D12.776.964.700.750.875 – oncogene proteins v-abl MeSH D12.776.964.700.750.882 – oncogene proteins v-erba MeSH D12.776.964.700.750.883 – oncogene proteins v-erbb MeSH D12.776.964.700.750.887 – oncogene proteins v-fos MeSH D12.776.964.700.750.900 – oncogene proteins v-mos MeSH D12.776.964.700.750.903 – oncogene proteins v-myb MeSH D12.776.964.700.750.920 – oncogene proteins v-raf MeSH D12.776.964.700.750.925 – oncogene proteins v-rel MeSH D12.776.964.700.750.935 – oncogene proteins v-sis === MeSH D12.776.964.775 – retroviridae proteins === ==== MeSH D12.776.964.775.325 – gene products, env (gene) ==== MeSH D12.776.964.775.325.330 – hiv envelope protein gp41 MeSH D12.776.964.775.325.350 – hiv envelope protein gp120 MeSH D12.776.964.775.325.380 – hiv envelope protein gp160 ==== MeSH D12.776.964.775.350 – gene products, gag (gene) ==== MeSH D12.776.964.775.350.320 – fusion proteins, gag-onc MeSH D12.776.964.775.350.320.700 – oncogene protein p65(gag-jun) MeSH D12.776.964.775.350.325 – fusion proteins, gag-pol MeSH D12.776.964.775.350.400 – hiv core protein p24 ==== MeSH D12.776.964.775.375 – gene products, pol (gene) ==== MeSH D12.776.964.775.375.325 – fusion proteins, gag-pol MeSH D12.776.964.775.375.335 – hiv integrase MeSH D12.776.964.775.375.340 – HIV protease MeSH D12.776.964.775.375.750 – RNA-directed DNA polymerase MeSH D12.776.964.775.375.750.375 – hiv-1 reverse transcriptase ==== MeSH D12.776.964.775.750 – retroviridae proteins, oncogenic ==== MeSH D12.776.964.775.750.320 – fusion proteins, gag-onc MeSH D12.776.964.775.750.320.700 – oncogene protein p65(gag-jun) MeSH D12.776.964.775.750.470 – gene products, rex MeSH D12.776.964.775.750.480 – gene products, tax MeSH D12.776.964.775.750.650 – oncogene protein gp140(v-fms) MeSH D12.776.964.775.750.710 – oncogene protein p21(ras) MeSH
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
}
|
D12.776.964.775.750.750 – oncogene protein p55(v-myc) MeSH D12.776.964.775.750.760 – oncogene protein pp60(v-src) MeSH D12.776.964.775.750.817 – oncogene protein v-maf MeSH D12.776.964.775.750.875 – oncogene proteins v-abl MeSH D12.776.964.775.750.882 – oncogene proteins v-erba MeSH D12.776.964.775.750.883 – oncogene proteins v-erbb MeSH D12.776.964.775.750.887 – oncogene proteins v-fos MeSH D12.776.964.775.750.900 – oncogene proteins v-mos MeSH D12.776.964.775.750.903 – oncogene proteins v-myb MeSH D12.776.964.775.750.920 – oncogene proteins v-raf MeSH D12.776.964.775.750.925 – oncogene proteins v-rel MeSH D12.776.964.775.750.935 – oncogene proteins v-sis === MeSH D12.776.964.900 – viral nonstructural proteins === === MeSH D12.776.964.950 – viral regulatory proteins === ==== MeSH D12.776.964.950.365 – gene products, nef ==== ==== MeSH D12.776.964.950.470 – gene products, rex ==== ==== MeSH D12.776.964.950.575 – gene products, vif ==== ==== MeSH D12.776.964.950.580 – gene products, vpu ==== ==== MeSH D12.776.964.950.610 – immediate-early proteins ==== ==== MeSH D12.776.964.950.800 – trans-activators ==== MeSH D12.776.964.950.800.385 – gene products, rev (HIV) MeSH D12.776.964.950.800.400 – gene products, tat MeSH D12.776.964.950.800.410 – gene products, tax MeSH D12.776.964.950.800.430 – gene products, vpr MeSH D12.776.964.950.800.445 – herpes simplex virus protein vmw65 === MeSH D12.776.964.970 – viral structural proteins === ==== MeSH D12.776.964.970.600 – nucleocapsid proteins ==== MeSH D12.776.964.970.600.550 – capsid proteins MeSH D12.776.964.970.600.850 – viral core proteins MeSH D12.776.964.970.600.850.350 – gene products, gag MeSH D12.776.964.970.600.850.350.325 – fusion proteins, gag-pol MeSH D12.776.964.970.600.850.350.400 – hiv core protein p24 MeSH D12.776.964.970.600.850.375 – gene products, pol (gene) MeSH D12.776.964.970.600.850.375.325 – fusion proteins, gag-pol MeSH D12.776.964.970.600.850.375.335 – hiv integrase MeSH D12.776.964.970.600.850.375.340 – HIV protease MeSH D12.776.964.970.600.850.375.750 – RNA-directed DNA polymerase MeSH D12.776.964.970.600.850.375.750.375 – hiv-1 reverse transcriptase ==== MeSH D12.776.964.970.880 – viral envelope proteins ==== MeSH D12.776.964.970.880.325 – gene products, env MeSH D12.776.964.970.880.325.330 – hiv envelope protein gp41 MeSH D12.776.964.970.880.325.350 – hiv envelope protein gp120 MeSH D12.776.964.970.880.325.380 – hiv envelope protein gp160 MeSH D12.776.964.970.880.345 – hemagglutinins, viral MeSH D12.776.964.970.880.345.500 – hemagglutinin glycoproteins, influenza virus MeSH D12.776.964.970.880.350 – hn protein MeSH D12.776.964.970.880.910 –
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
}
|
viral fusion proteins MeSH D12.776.964.970.880.910.330 – hiv envelope protein gp41 MeSH D12.776.964.970.880.940 – viral matrix proteins MeSH D12.776.964.970.880.940.580 – gene products, vpu ==== MeSH D12.776.964.970.910 – viral tail proteins ==== The list continues at List of MeSH codes (D13).
|
{
"page_id": 5505240,
"source": null,
"title": "List of MeSH codes (D12.776)"
}
|
The molecular formula C9H14O may refer to: Isophorone (α-isophorone) β-Isophorone trans,cis-2,6-Nonadienal Phorone
|
{
"page_id": 23986393,
"source": null,
"title": "C9H14O"
}
|
Monochromatization in the context of accelerator physics is a theoretical principle used to increase center-of-mass energy resolution in high-luminosity particle collisions. The decrease of the collision energy spread can be accomplished without reducing the inherent energy spread of either of the two colliding beams, introducing opposite correlations between spatial position and energy at the interaction point (IP). In beam-optical terms, this can be accomplished through a non-zero dispersion function for both beams of opposite sign at the IP. The dispersion is determined by the respective lattice. == History == Monochromatization is a technique which has been proposed since a long time for reducing the centre-of-mass energy spread at e−e+ colliders, but this has never been used in any operational collider. This technique was first proposed by 1975 by A. Renieri to improve energy resolution of Italian collider Adone. Implementation of a monochromatization scheme has been explored for several past colliders such as ADONE (National Institute of Nuclear Physics) SPEAR (SLAC National Accelerator Laboratory) LEP (CERN) but until now such a scheme has never been applied, or tested, in any operating collider. Nevertheless, studies for the FCC-ee are under development. == References ==
|
{
"page_id": 55443671,
"source": null,
"title": "Monochromatization"
}
|
In astronomy, Pulsed accretion is the periodic modulation in accretion rate of young stellar objects in binary systems, producing a periodic pulse in the observed infrared light curves of T Tauri stars. In double stars in young stellar objects, a protoplanetary disk is formed around each star, accreted from nearby matter. In such a binary star system, a strongly eccentric orbit produces strong gravitational forces on the circumstellar disks at periastron, and such disturbance can lead to a temporary increase in the accretion rate onto both stars. Simulations show that the accretion rate is likely to be highly symmetric between stars in nearly equal-mass binary systems but for systems with a mass disparity can be asymmetric. Such asymmetry may be attributable to a high eccentricity circumbinary disk which can accrete material onto the surface of one star at a rate 10-20 times greater than onto the other, with the star that experiences a higher rate of accretion alternating with its companion over large time scales. This increased accretion rate leads to a change of intensity in the infrared radiation emitted by the stars with such intensity rising by up to tenfold in the protostar LRLL 54361. Brightness changes in the light curve that have the same period as the orbital period of the binary system, are usually assumed to be due to pulsed accretion. == References ==
|
{
"page_id": 38469851,
"source": null,
"title": "Pulsed accretion"
}
|
Gravitational-wave astronomy is a subfield of astronomy concerned with the detection and study of gravitational waves emitted by astrophysical sources. Gravitational waves are minute distortions or ripples in spacetime caused by the acceleration of massive objects. They are produced by cataclysmic events such as the merger of binary black holes, the coalescence of binary neutron stars, supernova explosions and processes including those of the early universe shortly after the Big Bang. Studying them offers a new way to observe the universe, providing valuable insights into the behavior of matter under extreme conditions. Similar to electromagnetic radiation (such as light wave, radio wave, infrared radiation and X-rays) which involves transport of energy via propagation of electromagnetic field fluctuations, gravitational radiation involves fluctuations of the relatively weaker gravitational field. The existence of gravitational waves was first suggested by Oliver Heaviside in 1893 and then later conjectured by Henri Poincaré in 1905 as the gravitational equivalent of electromagnetic waves before they were predicted by Albert Einstein in 1916 as a corollary to his theory of general relativity. In 1978, Russell Alan Hulse and Joseph Hooton Taylor Jr. provided the first experimental evidence for the existence of gravitational waves by observing two neutron stars orbiting each other and won the 1993 Nobel Prize in physics for their work. In 2015, nearly a century after Einstein's forecast, the first direct observation of gravitational waves as a signal from the merger of two black holes confirmed the existence of these elusive phenomena and opened a new era in astronomy. Subsequent detections have included binary black hole mergers, neutron star collisions, and other violent cosmic events. Gravitational waves are now detected using laser interferometry, which measures tiny changes in the length of two perpendicular arms caused by passing waves. Observatories like LIGO (Laser Interferometer Gravitational-wave Observatory), Virgo
|
{
"page_id": 11084989,
"source": null,
"title": "Gravitational-wave astronomy"
}
|
and KAGRA (Kamioka Gravitational Wave Detector) use this technology to capture the faint signals from distant cosmic events. LIGO co-founders Barry C. Barish, Kip S. Thorne, and Rainer Weiss were awarded the 2017 Nobel Prize in Physics for their ground-breaking contributions in gravitational wave astronomy. When distant astronomical objects are observed using electromagnetic waves, different phenomena like scattering, absorption, reflection, refraction, etc. cause information loss. There are various regions in space only partially penetrable by photons, such as the insides of nebulae, the dense dust clouds at the galactic core, the regions near black holes, etc. Gravitational astronomy has the potential to be used in parallel with electromagnetic astronomy to study the universe at a better resolution. In an approach known as multi-messenger astronomy, gravitational wave data is combined with data from other wavelengths to get a more complete picture of astrophysical phenomena. Gravitational wave astronomy helps understand the early universe, test theories of gravity, and reveal the distribution of dark matter and dark energy. In particular, it can help find the Hubble constant, which describes the rate of accelerated expansion of the universe. All of these open doors to a physics beyond the Standard Model (BSM). Challenges that remain in the field include noise interference, the lack of ultra-sensitive instruments, and the detection of low-frequency waves. Ground-based detectors face problems with seismic vibrations produced by environmental disturbances and the limitation of the arm length of detectors due to the curvature of the Earth’s surface. In the future, the field of gravitational wave astronomy will try develop upgraded detectors and next-generation observatories, along with possible space-based detectors such as LISA (Laser Interferometer Space Antenna). LISA will be able to listen to distant sources like compact supermassive black holes in the galactic core and primordial black holes, as well as low-frequency
|
{
"page_id": 11084989,
"source": null,
"title": "Gravitational-wave astronomy"
}
|
sensitive signals sources such as binary white dwarf merger and sources from the early universe. == Introduction == Gravitational waves are waves of the intensity of gravity generated by the accelerated masses of an orbital binary system that propagate as waves outward from their source at the speed of light. They were first proposed by Oliver Heaviside in 1893 and then later by Henri Poincaré in 1905 as waves similar to electromagnetic waves but the gravitational equivalent. Gravitational waves were later predicted in 1916 by Albert Einstein on the basis of his general theory of relativity as ripples in spacetime. Later he refused to accept gravitational waves. Gravitational waves transport energy as gravitational radiation, a form of radiant energy similar to electromagnetic radiation. Newton's law of universal gravitation, part of classical mechanics, does not provide for their existence, since that law is predicated on the assumption that physical interactions propagate instantaneously (at infinite speed) – showing one of the ways the methods of Newtonian physics are unable to explain phenomena associated with relativity. The first indirect evidence for the existence of gravitational waves came in 1974 from the observed orbital decay of the Hulse–Taylor binary pulsar, which matched the decay predicted by general relativity as energy is lost to gravitational radiation. In 1993, Russell A. Hulse and Joseph Hooton Taylor Jr. received the Nobel Prize in Physics for this discovery. Direct observation of gravitational waves was not made until 2015, when a signal generated by the merger of two black holes was received by the LIGO gravitational wave detectors in Livingston, Louisiana, and in Hanford, Washington. The 2017 Nobel Prize in Physics was subsequently awarded to Rainer Weiss, Kip Thorne and Barry Barish for their role in the direct detection of gravitational waves. In gravitational-wave astronomy, observations of gravitational waves
|
{
"page_id": 11084989,
"source": null,
"title": "Gravitational-wave astronomy"
}
|
are used to infer data about the sources of gravitational waves. Sources that can be studied this way include binary star systems composed of white dwarfs, neutron stars, and black holes; events such as supernovae; and the formation of the early universe shortly after the Big Bang. == Instruments and challenges == Collaboration between detectors aids in collecting unique and valuable information, owing to different specifications and sensitivity of each. There are several ground-based laser interferometers which span several miles/kilometers, including: the two Laser Interferometer Gravitational-Wave Observatory (LIGO) detectors in Washington and Louisiana, USA; Virgo, at the European Gravitational Observatory in Italy; GEO600 in Germany, and the Kamioka Gravitational Wave Detector (KAGRA) in Japan. While LIGO, Virgo, and KAGRA have made joint observations to date, GEO600 is currently utilized for trial and test runs due to lower sensitivity of its instruments and has not participated in joint runs with the others recently. === High frequency === In 2015, the LIGO project was the first to directly observe gravitational waves using laser interferometers. The LIGO detectors observed gravitational waves from the merger of two stellar-mass black holes, matching predictions of general relativity. These observations demonstrated the existence of binary stellar-mass black hole systems, and were the first direct detection of gravitational waves and the first observation of a binary black hole merger. This finding has been characterized as revolutionary to science, because of the verification of our ability to use gravitational-wave astronomy to progress in our search and exploration of dark matter and the big bang. === Low frequency === An alternative means of observation is using pulsar timing arrays (PTAs). There are three consortia, the European Pulsar Timing Array (EPTA), the North American Nanohertz Observatory for Gravitational Waves (NANOGrav), and the Parkes Pulsar Timing Array (PPTA), which co-operate as the
|
{
"page_id": 11084989,
"source": null,
"title": "Gravitational-wave astronomy"
}
|
International Pulsar Timing Array. These use existing radio telescopes, but since they are sensitive to frequencies in the nanohertz range, many years of observation are needed to detect a signal and detector sensitivity improves gradually. Current bounds are approaching those expected for astrophysical sources. In June 2023, four PTA collaborations, the three mentioned above and the Chinese Pulsar Timing Array, delivered independent but similar evidence for a stochastic background of nanohertz gravitational waves. Each provided an independent first measurement of the theoretical Hellings-Downs curve, i.e., the quadrupolar correlation between two pulsars as a function of their angular separation in the sky, which is a telltale sign of the gravitational wave origin of the observed background. The sources of this background remain to be identified, although binaries of supermassive black holes are the most likely candidates. === Intermediate frequencies === Further in the future, there is the possibility of space-borne detectors. The European Space Agency has selected a gravitational-wave mission for its L3 mission, due to launch 2034, the current concept is the evolved Laser Interferometer Space Antenna (eLISA). Also in development is the Japanese Deci-hertz Interferometer Gravitational wave Observatory (DECIGO). == Scientific value == Astronomy has traditionally relied on electromagnetic radiation. Originating with the visible band, as technology advanced, it became possible to observe other parts of the electromagnetic spectrum, from radio to gamma rays. Each new frequency band gave a new perspective on the Universe and heralded new discoveries. During the 20th century, indirect and later direct measurements of high-energy, massive particles provided an additional window into the cosmos. Late in the 20th century, the detection of solar neutrinos founded the field of neutrino astronomy, giving an insight into previously inaccessible phenomena, such as the inner workings of the Sun. The observation of gravitational waves provides a further means
|
{
"page_id": 11084989,
"source": null,
"title": "Gravitational-wave astronomy"
}
|
of making astrophysical observations. Russell Hulse and Joseph Taylor were awarded the 1993 Nobel Prize in Physics for showing that the orbital decay of a pair of neutron stars, one of them a pulsar, fits general relativity's predictions of gravitational radiation. Subsequently, many other binary pulsars (including one double pulsar system) have been observed, all fitting gravitational-wave predictions. In 2017, the Nobel Prize in Physics was awarded to Rainer Weiss, Kip Thorne and Barry Barish for their role in the first detection of gravitational waves. Gravitational waves provide complementary information to that provided by other means. By combining observations of a single event made using different means, it is possible to gain a more complete understanding of the source's properties. This is known as multi-messenger astronomy. Gravitational waves can also be used to observe systems that are invisible (or almost impossible to detect) by any other means. For example, they provide a unique method of measuring the properties of black holes. Gravitational waves can be emitted by many systems, but, to produce detectable signals, the source must consist of extremely massive objects moving at a significant fraction of the speed of light. The main source is a binary of two compact objects. Example systems include: Compact binaries made up of two closely orbiting stellar-mass objects, such as white dwarfs, neutron stars or black holes. Wider binaries, which have lower orbital frequencies, are a source for detectors like LISA. Closer binaries produce a signal for ground-based detectors like LIGO. Ground-based detectors could potentially detect binaries containing an intermediate mass black hole of several hundred solar masses. Supermassive black hole binaries, consisting of two black holes with masses of 105–109 solar masses. Supermassive black holes are found at the centre of galaxies. When galaxies merge, it is expected that their central supermassive
|
{
"page_id": 11084989,
"source": null,
"title": "Gravitational-wave astronomy"
}
|
black holes merge too. These are potentially the loudest gravitational-wave signals. The most massive binaries are a source for PTAs. Less massive binaries (about a million solar masses) are a source for space-borne detectors like LISA. Extreme-mass-ratio systems of a stellar-mass compact object orbiting a supermassive black hole. These are sources for detectors like LISA. Systems with highly eccentric orbits produce a burst of gravitational radiation as they pass through the point of closest approach; systems with near-circular orbits, which are expected towards the end of the inspiral, emit continuously within LISA's frequency band. Extreme-mass-ratio inspirals can be observed over many orbits. This makes them excellent probes of the background spacetime geometry, allowing for precision tests of general relativity. In addition to binaries, there are other potential sources: Supernovae generate high-frequency bursts of gravitational waves that could be detected with LIGO or Virgo. Rotating neutron stars are a source of continuous high-frequency waves if they possess axial asymmetry. Early universe processes, such as inflation or a phase transition. Cosmic strings could also emit gravitational radiation if they do exist. Discovery of these gravitational waves would confirm the existence of cosmic strings. Gravitational waves interact only weakly with matter. This is what makes them difficult to detect. It also means that they can travel freely through the Universe, and are not absorbed or scattered like electromagnetic radiation. It is therefore possible to see to the center of dense systems, like the cores of supernovae or the Galactic Center. It is also possible to see further back in time than with electromagnetic radiation, as the early universe was opaque to light prior to recombination, but transparent to gravitational waves. The ability of gravitational waves to move freely through matter also means that gravitational-wave detectors, unlike telescopes, are not pointed to observe a
|
{
"page_id": 11084989,
"source": null,
"title": "Gravitational-wave astronomy"
}
|
single field of view but observe the entire sky. Detectors are more sensitive in some directions than others, which is one reason why it is beneficial to have a network of detectors. Directionalization is also poor, due to the small number of detectors. === In cosmic inflation === Cosmic inflation, a hypothesized period when the universe rapidly expanded during the first 10−36 seconds after the Big Bang, would have given rise to gravitational waves; that would have left a characteristic imprint in the polarization of the CMB radiation. It is possible to calculate the properties of the primordial gravitational waves from measurements of the patterns in the microwave radiation, and use those calculations to learn about the early universe. == Development == As a young area of research, gravitational-wave astronomy is still in development; however, there is consensus within the astrophysics community that this field will evolve to become an established component of 21st century multi-messenger astronomy. Gravitational-wave observations complement observations in the electromagnetic spectrum. These waves also promise to yield information in ways not possible via detection and analysis of electromagnetic waves. Electromagnetic waves can be absorbed and re-radiated in ways that make extracting information about the source difficult. Gravitational waves, however, only interact weakly with matter, meaning that they are not scattered or absorbed. This should allow astronomers to view the center of a supernova, stellar nebulae, and even colliding galactic cores in new ways. Ground-based detectors have yielded new information about the inspiral phase and mergers of binary systems of two stellar mass black holes, and merger of two neutron stars. They could also detect signals from core-collapse supernovae, and from periodic sources such as pulsars with small deformations. If there is truth to speculation about certain kinds of phase transitions or kink bursts from long cosmic
|
{
"page_id": 11084989,
"source": null,
"title": "Gravitational-wave astronomy"
}
|
strings in the very early universe (at cosmic times around 10−25 seconds), these could also be detectable. Space-based detectors like LISA should detect objects such as binaries consisting of two white dwarfs, and AM CVn stars (a white dwarf accreting matter from its binary partner, a low-mass helium star), and also observe the mergers of supermassive black holes and the inspiral of smaller objects (between one and a thousand solar masses) into such black holes. LISA should also be able to listen to the same kind of sources from the early universe as ground-based detectors, but at even lower frequencies and with greatly increased sensitivity. Detecting emitted gravitational waves is a difficult endeavor. It involves ultra-stable high-quality lasers and detectors calibrated with a sensitivity of at least 2·10−22 Hz−1/2 as shown at the ground-based detector, GEO600. It has also been proposed that even from large astronomical events, such as supernova explosions, these waves are likely to degrade to vibrations as small as an atomic diameter. Pinpointing the location of where the gravitational waves comes from is also a challenge. But deflected waves through gravitational lensing combined with machine learning could make it easier and more accurate. Just as the light from the SN Refsdal supernova was detected a second time almost a year after it was first discovered, due to gravitational lensing sending some of the light on a different path through the universe, the same approach could be used for gravitational waves. While still at an early stage, a technique similar to the triangulation used by cell phones to determine their location in relation to GPS satellites, will help astronomers tracking down the origin of the waves. == See also == Gravitational wave background Gravitational-wave observatory List of gravitational wave observations Matched filter#Gravitational-wave astronomy == References == == Further
|
{
"page_id": 11084989,
"source": null,
"title": "Gravitational-wave astronomy"
}
|
reading == == External links == LIGO Scientific Collaboration AstroGravS: Astrophysical Gravitational-Wave Sources Archive Video (04:36) – Detecting a gravitational wave, Dennis Overbye, NYT (11 February 2016). Video (71:29) – Press Conference announcing discovery: "LIGO detects gravitational waves", National Science Foundation (11 February 2016). Gravitational Wave Astronomy
|
{
"page_id": 11084989,
"source": null,
"title": "Gravitational-wave astronomy"
}
|
The Wellman Group is a group of manufacturing companies that make boilers and advanced defence equipment. It is one of the main boilermakers in the UK, if not the most common for large-scale industrial applications, having taken over many well-known boiler companies. == History == The main company began as the Wellman Smith Owen Engineering Corporation, a large conglomerate British engineering company. It derived from an English company of Samuel T. Wellman, a steel industry pioneer. It was based at Parnell House on Wilton Road in London, next to London Victoria station. It supplied furnaces to the British steel industry. The site at Oldbury has been making boilers since 1862. In August 1965 it split in several subsidiaries, including Wellman Machines (at Darlaston), Wellman Incandescent Furnace Company (at Darlaston, Staffordshire), Wellman Steelworks Engineering, and Wellman Incandescent International. Wellman became a private company in December 1997, when bought by Alchemy Partners for £82 million, by setting up a nominal transitional consortium company called Newmall (an anagram of Wellman). In 2003 it formed a commercial alliance with Loos International, a German boiler maker. In August 2005, Alchemy split the company into two – Newmall, for the US subsidiaries and Really Newmall for the other subsidiaries; this became Wellman Group Ltd, owned by Kwikpower International, in the Kwikpower Wellman division. In May 2009 the company formed an alliance with Wulff Energy Technologies GmbH of Husum to form Wellman Wulff. === Robey of Lincoln === Robey of Lincoln was an agricultural firm that went into making boilers in 1870. It was bought by Babcock International in July 1985 when Robey had a turnover of £7 million. == Structure == It is headquartered on the A457 on the western side of Oldbury, next to the Birmingham Canal. It has three subsidiaries. === Wellman Hunt-Graham ===
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{
"page_id": 32702686,
"source": null,
"title": "Wellman Group"
}
|
Wellman Graham merged with Hunt Thermal Engineering Ltd to form Wellman Hunt-Graham in 2012. It works in the heat transfer industry. It is the UK's largest manufacturer of shell and tube heat exchangers. Wellman Graham began in 1956 as Heat Transfer Ltd. The company changed name to Graham Manufacturing Ltd in 1977, It was sold to Wellman Group in 1995 and Changed name to Wellman Graham Ltd, and was based in Gloucester before moving its design and manufacturing facility to Oldbury in the West Midlands. Wellman Hunt Graham was acquired by Corac Group plc in 2012 and renamed to Hunt Graham Ltd, and in 2013 changed its name to Hunt Thermal Technologies. Corac Group plc was renamed as TP Group plc in 2015 and Hunt Thermal Technologies has since been renamed as TPG Engineering. === Wellman Thermal Services === This makes industrial furnaces. A division of the company, Wellman Process Engineering, makes evaporators and crystallisers. The company makes boilers for combined heat and power schemes. Wellman-Robey boilers are made at Oldbury. === Wellman Defence === This started as the research division of John Brown Engineers and Constructors Ltd in 1957. It became part of Wellman Group in 1996. Its main significance is that it developed the equipment for purified air that allows the Royal Navy's nuclear submarines to be submerged for months at a time – Submarine Atmosphere Control. This uses an electrolyser. Carbon dioxide from the submarine reacts with hydrogen from the electrolyser and is removed. It also supplies oxygen generation equipment to other countries such as France for the new Barracuda-class submarine. Wellman Defence was acquired by Corac Group plc in 2012 and renamed to Atmosphere Control International. Corac Group plc was renamed as TP Group plc in 2015 and Atmosphere Control International has since been renamed as
|
{
"page_id": 32702686,
"source": null,
"title": "Wellman Group"
}
|
TPG Maritime == Products == Boilers – 100 kW to 35MW Steam boilers Water heat recovery boilers Furnaces – now part of the Almor Group (www.wellman-furnaces.com] Combined heat and power schemes Heat exchangers Air purifiers for nuclear submarines == Installations == North British Distillery, Edinburgh == References == == External links == Wellman Defence Wellman Hunt Graham Wellman Robey Boilers EPCB Boiler Website Graces Guide Profile == See also == Wellman-Seaver-Morgan Engineering Company
|
{
"page_id": 32702686,
"source": null,
"title": "Wellman Group"
}
|
The waterhole, or water hole, is an especially quiet band of the electromagnetic spectrum between 1420 and 1662 megahertz, corresponding to wavelengths of 18–21 centimeters. It is a popular observing frequency used by radio telescopes in radio astronomy. The strongest hydroxyl radical spectral line radiates at 18 centimeters, and atomic hydrogen at 21 centimeters (the hydrogen line). These two molecules, which combine to form water, are widespread in interstellar gas, which means this gas tends to absorb radio noise at these frequencies. Therefore, the spectrum between these frequencies forms a relatively "quiet" channel in the interstellar radio noise background. Bernard M. Oliver, who coined the term in 1971, theorized that the waterhole would be an obvious band for communication with extraterrestrial intelligence, hence the name, which is a pun: in English, a watering hole is a vernacular reference to a common place to meet and talk. Several programs involved in the search for extraterrestrial intelligence, including SETI@home, search in the waterhole radio frequencies. == See also == BLC1 Wow! signal Radio source SHGb02+14a Schelling point == References == == External links == SETI: The Radio Search (page 2) "What Is the Water Hole" (has a cleaner diagram) Planetary.org: A Blueprint for SETI How SETI Works Discusses the water hole. "waterhole" entry in The Encyclopedia of Astrobiology, Astronomy, and Spaceflight' "The ABCs of SETI: the search for extraterrestrial intelligence" "SETI: The water hole" from Astronomy Now "SETI Observations" from SETI Institute
|
{
"page_id": 5439710,
"source": null,
"title": "Water hole (radio)"
}
|
Muscle atrophy is the loss of skeletal muscle mass. It can be caused by immobility, aging, malnutrition, medications, or a wide range of injuries or diseases that impact the musculoskeletal or nervous system. Muscle atrophy leads to muscle weakness and causes disability. Disuse causes rapid muscle atrophy and often occurs during injury or illness that requires immobilization of a limb or bed rest. Depending on the duration of disuse and the health of the individual, this may be fully reversed with activity. Malnutrition first causes fat loss but may progress to muscle atrophy in prolonged starvation and can be reversed with nutritional therapy. In contrast, cachexia is a wasting syndrome caused by an underlying disease such as cancer that causes dramatic muscle atrophy and cannot be completely reversed with nutritional therapy. Sarcopenia is age-related muscle atrophy and can be slowed by exercise. Finally, diseases of the muscles such as muscular dystrophy or myopathies can cause atrophy, as well as damage to the nervous system such as in spinal cord injury or stroke. Thus, muscle atrophy is usually a finding (sign or symptom) in a disease rather than being a disease by itself. However, some syndromes of muscular atrophy are classified as disease spectrums or disease entities rather than as clinical syndromes alone, such as the various spinal muscular atrophies. Muscle atrophy results from an imbalance between protein synthesis and protein degradation, although the mechanisms are incompletely understood and are variable depending on the cause. Muscle loss can be quantified with advanced imaging studies but this is not frequently pursued. Treatment depends on the underlying cause but will often include exercise and adequate nutrition. Anabolic agents may have some efficacy but are not often used due to side effects. There are multiple treatments and supplements under investigation but there are currently
|
{
"page_id": 5308641,
"source": null,
"title": "Muscle atrophy"
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limited treatment options in clinical practice. Given the implications of muscle atrophy and limited treatment options, minimizing immobility is critical in injury or illness. == Signs and symptoms == The hallmark sign of muscle atrophy is loss of lean muscle mass. This change may be difficult to detect due to obesity, changes in fat mass or edema. Changes in weight, limb or waist circumference are not reliable indicators of muscle mass changes. The predominant symptom is increased weakness which may result in difficulty or inability in performing physical tasks depending on what muscles are affected. Atrophy of the core or leg muscles may cause difficulty standing from a seated position, walking or climbing stairs and can cause increased falls. Atrophy of the throat muscles may cause difficulty swallowing and diaphragm atrophy can cause difficulty breathing. Muscle atrophy can be asymptomatic and may go undetected until a significant amount of muscle is lost. == Causes == Skeletal muscle serves as a storage site for amino acids, creatine, myoglobin, and adenosine triphosphate, which can be used for energy production when demands are high or supplies are low. If metabolic demands remain greater than protein synthesis, muscle mass is lost. Many diseases and conditions can lead to this imbalance, either through the disease itself or disease associated appetite-changes, such as loss of taste due to Covid-19. Causes of muscle atrophy, include immobility, aging, malnutrition, certain systemic diseases (cancer, congestive heart failure; chronic obstructive pulmonary disease; AIDS, liver disease, etc.), deinnervation, intrinsic muscle disease or medications (such as glucocorticoids). === Immobility === Disuse is a common cause of muscle atrophy and can be local (due to injury or casting) or general (bed-rest). The rate of muscle atrophy from disuse (10–42 days) is approximately 0.5–0.6% of total muscle mass per day although there is considerable
|
{
"page_id": 5308641,
"source": null,
"title": "Muscle atrophy"
}
|
variation between people. The elderly are the most vulnerable to dramatic muscle loss with immobility. Much of the established research has investigated prolonged disuse (>10 days), in which the muscle is compromised primarily by declines in muscle protein synthesis rates rather than changes in muscle protein breakdown. There is evidence to suggest that there may be more active protein breakdown during short term immobility (<10 days). === Cachexia === Certain diseases can cause a complex muscle wasting syndrome known as cachexia. It is commonly seen in cancer, congestive heart failure, chronic obstructive pulmonary disease, chronic kidney disease and AIDS although it is associated with many disease processes, usually with a significant inflammatory component. Cachexia causes ongoing muscle loss that is not entirely reversed with nutritional therapy. The pathophysiology is incompletely understood but inflammatory cytokines are considered to play a central role. In contrast to weight loss from inadequate caloric intake, cachexia causes predominantly muscle loss instead of fat loss and it is not as responsive to nutritional intervention. Cachexia can significantly compromise quality of life and functional status and is associated with poor outcomes. === Sarcopenia === Sarcopenia is the degenerative loss of skeletal muscle mass, quality, and strength associated with aging. This involves muscle atrophy, reduction in number of muscle fibers and a shift towards "slow twitch" or type I skeletal muscle fibers over "fast twitch" or type II fibers. The rate of muscle loss is dependent on exercise level, co-morbidities, nutrition and other factors. There are many proposed mechanisms of sarcopenia, such as a decreased capacity for oxidative phosphorylation, cellular senescence or an altered signaling of pathways regulating protein synthesis, and is considered to be the result of changes in muscle synthesis signalling pathways and gradual failure in the satellite cells which help to regenerate skeletal muscle fibers,
|
{
"page_id": 5308641,
"source": null,
"title": "Muscle atrophy"
}
|
specifically in "fast twitch" myofibers. Sarcopenia can lead to reduction in functional status and cause significant disability but is a distinct condition from cachexia although they may co-exist. In 2016 an ICD code for sarcopenia was released, contributing to its acceptance as a disease entity. === Intrinsic muscle diseases === Muscle diseases, such as muscular dystrophy, amyotrophic lateral sclerosis (ALS), or myositis such as inclusion body myositis can cause muscle atrophy. === Central nervous system damage === Damage to neurons in the brain or spinal cord can cause prominent muscle atrophy. This can be localized muscle atrophy and weakness or paralysis such as in stroke or spinal cord injury. More widespread damage such as in traumatic brain injury or cerebral palsy can cause generalized muscle atrophy. === Peripheral nervous system damage === Injuries or diseases of peripheral nerves supplying specific muscles can also cause muscle atrophy. This is seen in nerve injury due to trauma or surgical complication, nerve entrapment, or inherited diseases such as Charcot-Marie-Tooth disease. === Medications === Some medications are known to cause muscle atrophy, usually due to direct effect on muscles. This includes glucocorticoids causing glucocorticoid myopathy or medications toxic to muscle such as doxorubicin. === Endocrinopathies === Disorders of the endocrine system such as Cushing's disease or hypothyroidism are known to cause muscle atrophy. == Pathophysiology == Muscle atrophy occurs due to an imbalance between the normal balance between protein synthesis and protein degradation. This involves complex cell signalling that is incompletely understood and muscle atrophy is likely the result of multiple contributing mechanisms. Mitochondrial function is crucial to skeletal muscle health and detrimental changes at the level of the mitochondria may contribute to muscle atrophy. A decline in mitochondrial density as well as quality is consistently seen in muscle atrophy due to disuse. The
|
{
"page_id": 5308641,
"source": null,
"title": "Muscle atrophy"
}
|
ATP-dependent ubiquitin/proteasome pathway is one mechanism by which proteins are degraded in muscle. This involves specific proteins being tagged for destruction by a small peptide called ubiquitin which allows recognition by the proteasome to degrade the protein. == Diagnosis == Screening for muscle atrophy is limited by a lack of established diagnostic criteria, although many have been proposed. Diagnostic criteria for other conditions such as sarcopenia or cachexia can be used. These syndromes can also be identified with screening questionnaires. Muscle mass and changes can be quantified on imaging studies such as CT scans or Magnetic resonance imaging (MRI). Biomarkers such as urine urea can be used to roughly estimate muscle loss during circumstances of rapid muscle loss. Other biomarkers are currently under investigation but are not used in clinical practice. == Treatment == Muscle atrophy can be delayed, prevented and sometimes reversed with treatment. Treatment approaches include impacting the signaling pathways that induce muscle hypertrophy or slow muscle breakdown as well as optimizing nutritional status. Physical activity provides a significant anabolic muscle stimulus and is a crucial component to slowing or reversing muscle atrophy. It is still unknown regarding the ideal exercise "dosing." Resistance exercise has been shown to be beneficial in reducing muscle atrophy in older adults. In patients who cannot exercise due to physical limitations such as paraplegia, functional electrical stimulation can be used to externally stimulate the muscles. Adequate calories and protein is crucial to prevent muscle atrophy. Protein needs may vary dramatically depending on metabolic factors and disease state, so high-protein supplementation may be beneficial. Supplementation of protein or branched-chain amino acids, especially leucine, can provide a stimulus for muscle synthesis and inhibit protein breakdown and has been studied for muscle atrophy for sarcopenia and cachexia. β-Hydroxy β-methylbutyrate (HMB), a metabolite of leucine which is
|
{
"page_id": 5308641,
"source": null,
"title": "Muscle atrophy"
}
|
sold as a dietary supplement, has demonstrated efficacy in preventing the loss of muscle mass in several muscle wasting conditions in humans, particularly sarcopenia. Based upon a meta-analysis of seven randomized controlled trials that was published in 2015, HMB supplementation has efficacy as a treatment for preserving lean muscle mass in older adults. More research is needed to determine the precise effects of HMB on muscle strength and function in various populations. In severe cases of muscular atrophy, the use of an anabolic steroid such as methandrostenolone may be administered to patients as a potential treatment although use is limited by side effects. A novel class of drugs, called selective androgen receptor modulators, is being investigated with promising results. They would have fewer side effects, while still promoting muscle and bone tissue growth and regeneration. These effects have yet to be confirmed in larger clinical trials. == Outcomes == Outcomes of muscle atrophy depend on the underlying cause and the health of the patient. Immobility or bed rest in populations predisposed to muscle atrophy, such as the elderly or those with disease states that commonly cause cachexia, can cause dramatic muscle atrophy and impact on functional outcomes. In the elderly, this often leads to decreased biological reserve and increased vulnerability to stressors known as the "frailty syndrome." Loss of lean body mass is also associated with increased risk of infection, decreased immunity, and poor wound healing. The weakness that accompanies muscle atrophy leads to higher risk of falls, fractures, physical disability, need for institutional care, reduced quality of life, increased mortality, and increased healthcare costs. == Other animals == Inactivity and starvation in mammals lead to atrophy of skeletal muscle, accompanied by a smaller number and size of the muscle cells as well as lower protein content. In humans, prolonged
|
{
"page_id": 5308641,
"source": null,
"title": "Muscle atrophy"
}
|
periods of immobilization, as in the cases of bed rest or astronauts flying in space, are known to result in muscle weakening and atrophy. Such consequences are also noted in small hibernating mammals like the golden-mantled ground squirrels and brown bats. A striking example of human-induced atrophy is seen in Amar Bharati, an Indian sadhu who held his arm raised for decades as a spiritual devotion, resulting in severe muscle atrophy and loss of function in the limb. Bears are an exception to this rule; species in the family Ursidae are famous for their ability to survive unfavorable environmental conditions of low temperatures and limited nutrition availability during winter by means of hibernation. During that time, bears go through a series of physiological, morphological, and behavioral changes. Their ability to maintain skeletal muscle number and size during disuse is of significant importance. During hibernation, bears spend 4–7 months of inactivity and anorexia without undergoing muscle atrophy and protein loss. A few known factors contribute to the sustaining of muscle tissue. During the summer, bears take advantage of the nutrition availability and accumulate muscle protein. The protein balance at time of dormancy is also maintained by lower levels of protein breakdown during the winter. At times of immobility, muscle wasting in bears is also suppressed by a proteolytic inhibitor that is released in circulation. Another factor that contributes to the sustaining of muscle strength in hibernating bears is the occurrence of periodic voluntary contractions and involuntary contractions from shivering during torpor. The three to four daily episodes of muscle activity are responsible for the maintenance of muscle strength and responsiveness in bears during hibernation. == Pre-clinical models == Muscle-atrophy can be induced in pre-clinical models (e.g. mice) to study the effects of therapeutic interventions against muscle-atrophy. Restriction of the diet, i.e.
|
{
"page_id": 5308641,
"source": null,
"title": "Muscle atrophy"
}
|
caloric restriction, leads to a significant loss of muscle mass within two weeks, and loss of muscle-mass can be rescued by a nutritional intervention. Immobilization of one of the hindlegs of mice leads to muscle-atrophy as well, and is hallmarked by loss of both muscle mass and strength. Food restriction and immobilization may be used in mouse models and have been shown to overlap with mechanisms associated to sarcopenia in humans. == See also == == References == == External links == Media related to Muscle atrophy at Wikimedia Commons Muscular atrophy at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
|
{
"page_id": 5308641,
"source": null,
"title": "Muscle atrophy"
}
|
Sutton's law states that when diagnosing, one should first consider the obvious. It suggests that one should first conduct those tests which could confirm (or rule out) the most likely diagnosis. It is taught in medical schools to suggest to medical students that they might best order tests in that sequence which is most likely to result in a quick diagnosis, hence treatment, while minimizing unnecessary costs. It is also applied in pharmacology, when choosing a drug to treat a specific disease you want the drug to reach the disease. It is applicable to any process of diagnosis, e.g. debugging computer programs. Computer-aided diagnosis provides a statistical and quantitative approach. A more thorough analysis will consider the false positive rate of the test and the possibility that a less likely diagnosis might have more serious consequences. A competing principle is the idea of performing simple tests before more complex and expensive tests, moving from bedside tests to blood results and simple imaging such as ultrasound and then more complex such as MRI then specialty imaging. The law can also be applied in prioritizing tests when resources are limited, so a test for a treatable condition should be performed before an equally probable but less treatable condition. The law is named after the bank robber Willie Sutton, who reputedly replied to a reporter's inquiry as to why he robbed banks by saying "because that's where the money is." In Sutton's 1976 book Where the Money Was, Sutton denies having said this, but added that "If anybody had asked me, I'd have probably said it. That's what almost anybody would say.... it couldn't be more obvious." A similar idea is contained in the physician's adage, "When you hear hoofbeats, think horses, not zebras." == See also == Occam's razor == References ==
|
{
"page_id": 2949345,
"source": null,
"title": "Sutton's law"
}
|
Altman, Lawrence (1970-01-03). "A Law Named for Willie Sutton Assists Physicians". The New York Times. Rytand, David (1980). "Sutton's or Dock's Law?". New England Journal of Medicine. 302 (17): 972. doi:10.1056/NEJM198004243021726. PMID 6987522.
|
{
"page_id": 2949345,
"source": null,
"title": "Sutton's law"
}
|
The British Society for Developmental Biology (BSDB) is a scientific society promoting developmental biology research; it is open to anyone with an interest in the subject who agrees with the principles of the Society. == History == The British Society for Developmental Biology was founded in 1948 as the London Embryologists’ Club. In 1964, the club was expanded into a scientific society, named the Society for Developmental Biology. In 1964, the Society for the Study of Growth and Development in the United States had also voted to take on the same name, and they took over sponsorship of the journal Developmental Biology in 1966. Consequently, the smaller British society changed to its current name in 1969. == Awards == The society administers four annual awards and a studentship. The Waddington Medal was first awarded in 1998. It is named after C. H. Waddington, a leading British embryologist and geneticist, and is awarded to "an outstanding individual who has made major contributions to any aspect of Developmental Biology in the UK". Award winners include: 1998 Cheryll Tickle 1999 Rosa Beddington 2000 Peter Lawrence 2001 Mike Bate 2002 Jonathan Slack 2003 Julian Lewis 2004 Jeff Williams 2005 Michael Akam 2006 Claudio Stern 2007 David Ish-Horowicz 2008 Pat Simpson 2009 Liz Robertson 2010 Robin Lovell-Badge 2011 Christopher Wylie 2012 Alfonso Martinez Arias 2013 Jim Smith 2014 Philip Ingham 2015 Lewis Wolpert 2016 Enrico Coen 2017 William Harris 2018 Richard Lavenham Gardner In 2016, the society added the Cheryll Tickle Medal, which is awarded to a mid-career female scientist. It is named after the embryologist Cheryll Tickle, the first winner of the Waddington Medal. Winners include: 2016 Abigail Saffron Tucker 2017 Jenny Nichols 2018 Christiana Ruhrberg 2019 Bénédicte Sanson The society also has awards for early career scientists: The Beddington Medal is awarded annually
|
{
"page_id": 53936355,
"source": null,
"title": "British Society for Developmental Biology"
}
|
for the "best PhD thesis in developmental biology" defended in the year prior to the award; the Dennis Summerbell Lecture is an award that is delivered annually by a junior researcher at either PhD or postdoctoral level; and summer studentships are available for undergraduate students. == References == == External links == Official website
|
{
"page_id": 53936355,
"source": null,
"title": "British Society for Developmental Biology"
}
|
In molecular biology mir-14 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. == See also == MicroRNA == References == == Further reading == == External links == Page for mir-14 microRNA precursor family at Rfam
|
{
"page_id": 36372711,
"source": null,
"title": "Mir-14 microRNA precursor family"
}
|
CCD8 (gene) may refer to: Carlactone synthase All-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase
|
{
"page_id": 38338791,
"source": null,
"title": "CCD8"
}
|
Elda Miriam Aldasoro Maya is a Mexican biologist, anthropologist and popularizer. She is a pioneer in the study of ethnoentomology in Mexico and of interdisciplinary research that uses theoretical approaches from biology and anthropology to study ethnobiology from a political, economic, social and cultural perspective. Her work has contributed to the documentation of indigenous knowledge, the promotion of activities around community development, the implementation and design of participatory methodologies, as well as biocultural education activities. She has taught at the National Autonomous University of Mexico (UNAM), University of Washington, University of the Valley of Mexico, and at the Intercultural Universities of the State of Mexico. She has also been a collaborator of the CONACyT Network of Ethnoecology and Cultural Heritage, and a consultant in the field of microfinance for work with indigenous peoples. She is currently a CONACYT chair at the Colegio de la Frontera Sur (ECOSUR) in Villahermosa and a member of the national system of researchers of CONACYT Mexico. == Career == She obtained a bachelor's degree in biology from the Iztacala Faculty of Higher Studies of the National Autonomous University of Mexico conducting one of the first investigations in Hñä hñu (Otomi) ethnoentomology in the Mezquital Valley in Mexico. She then studied a master's degree at the Environmental Anthropology Program at the University of Washington, she also obtained her Ph. Tlahuicas through a participatory research project in which it offers novel models for the study of ethnobiology. During 2012 to 2014 she worked as a consultant in the field of microfinance for work with indigenous peoples for the development and international trade company DAI. In 2014 she obtained the CONACYT chair to work on the project "Massification of Agroecology" in the Department of Agriculture, Society and Environment of the Colegio de la Frontera Sur (ECOSUR) in Villahermosa;
|
{
"page_id": 70123754,
"source": null,
"title": "Elda Miriam Aldasoro Maya"
}
|
where she currently works. In 2015, she was coordinator of the declaration of the Latin American ethnobiological meeting of women (EELAM) that sought to recognize, make visible and protect the contribution of Latin American women to the knowledge of the use of biological resources. == References == == External links == Elda Miriam Aldasoro Maya publications indexed by Google Scholar
|
{
"page_id": 70123754,
"source": null,
"title": "Elda Miriam Aldasoro Maya"
}
|
The molecular formula C14H19NO may refer to: Alpha-Pyrrolidinobutiophenone Ethoxyquin, a food preservative Eticyclidone 2'-Oxo-PCE 4'-Methyl-α-pyrrolidinopropiophenone
|
{
"page_id": 23920875,
"source": null,
"title": "C14H19NO"
}
|
In quantum chromodynamics (QCD), the gluon condensate is a non-perturbative property of the QCD vacuum which could be partly responsible for giving masses to light mesons. If the gluon field tensor is represented as Gμν, then the gluon condensate is the vacuum expectation value ⟨ G μ ν G μ ν ⟩ {\displaystyle \langle G_{\mu \nu }G^{\mu \nu }\rangle } . It is not clear yet whether this condensate is related to any of the known phase changes in quark matter. There have been scattered studies of other types of gluon condensates, involving a different number of gluon fields. For more on the context in which this quantity occurs, see the article on the QCD vacuum. == See also == Quantum chromodynamics QCD vacuum and chiral condensates Vacuum in quantum field theory Quark–gluon plasma QCD matter == References ==
|
{
"page_id": 1966314,
"source": null,
"title": "Gluon condensate"
}
|
John Peter Novembre (born 1977 or 1978) is a computational biologist at the University of Chicago. He received a MacArthur Fellowship in 2015. Novembre has developed data visualization and analysis techniques to investigate correlations between genomic diversity, geography, and demographic structure. == Education == Novembre completed his undergraduate education in biochemistry at Colorado College in 2000. He then received a PhD in population genetics in 2006 at UC Berkeley; he was supervised by Montgomery Slatkin. He then went on to do postdoctoral research with Matthew Stephens in Chicago. In 2008, Novembre joined the Department of Ecology and Evolutionary Biology at the University of California, Los Angeles. == References ==
|
{
"page_id": 47972591,
"source": null,
"title": "John Novembre"
}
|
Reinforcement is a process within speciation where natural selection increases the reproductive isolation between two populations of species by reducing the production of hybrids. Evidence for speciation by reinforcement has been gathered since the 1990s, and along with data from comparative studies and laboratory experiments, has overcome many of the objections to the theory.: 354 Differences in behavior or biology that inhibit formation of hybrid zygotes are termed prezygotic isolation. Reinforcement can be shown to be occurring (or to have occurred in the past) by measuring the strength of prezygotic isolation in a sympatric population in comparison to an allopatric population of the same species.: 357 Comparative studies of this allow for determining large-scale patterns in nature across various taxa.: 362 Mating patterns in hybrid zones can also be used to detect reinforcement. Reproductive character displacement is seen as a result of reinforcement, so many of the cases in nature express this pattern in sympatry. Reinforcement's prevalence is unknown, but the patterns of reproductive character displacement are found across numerous taxa (vertebrates, invertebrates, plants, and fungi), and is considered to be a common occurrence in nature. Studies of reinforcement in nature often prove difficult, as alternative explanations for the detected patterns can be asserted.: 358 Nevertheless, empirical evidence exists for reinforcement occurring across various taxa and its role in precipitating speciation is conclusive. == Evidence from nature == === Amphibians === The two frog species Litoria ewingi and L. verreauxii live in southern Australia with their two ranges overlapping. The species have very similar calls in allopatry, but express clinal variation in sympatry, with notable distinctness in calls that generate female preference discrimination. The zone of overlap sometimes forms hybrids and is thought to originate by secondary contact of once fully allopatric populations. Allopatric populations of Gastrophryne olivacea and G.
|
{
"page_id": 56754417,
"source": null,
"title": "Evidence for speciation by reinforcement"
}
|
carolinensis have recently come into secondary contact due to forest clearing. The calls that the males make to attract females differ significantly in frequency and duration in the area where the two species overlap, despite them having similar calls where they do not.: 359 Further, the hybrids that form in sympatry have calls that are intermediate between the two. Similar patterns of reproductive character displacement involving acoustic displays have been found in Hyla cinerea and H. gratiosa, with greater female preference for conspecific males in areas of sympatry. Three species of true frogs (Lithobates sphenocephalus, L. berlandieri, and L. blairi) are temporally isolated in that their breeding seasons are spaced out in areas where they live in sympatry, but not where they live in allopatry. Selection against interspecific mating due to low hybrid fitness and low hybrid fertility has reinforced the observed character displacement of breeding times. The rainforests of northeast Queensland, Australia were separated into north and south refugia by climate fluctuations of the Pliocene and Pleistocene. About 6500 years ago, the rainforests reconnected, bringing the diverged, incipient populations of Litoria genimaculata into secondary contact. The species contact zones exhibit, "strong postzygotic selection against hybrids" and enhanced isolation from differences in mating call. An alternative to detecting reproductive character displacement in populations that overlap in sympatry is measuring rates of hybridization in contact zones. The frog species Anaxyrus americanus and Anaxyrus woodhousii have shown a decrease in hybridization from 9% to 0% over approximately 30 years. A similar pattern was detected in the sympatric spadefoot toads Spea multiplicata and S. bombifrons have hybridized with decreasing frequency over a 27-year period (about 13 generations). === Birds === The Ficedula flycatchers exhibit a pattern that suggests premating isolation is being reinforced by sexual selection. The pied flycatcher (Ficedula hypoleuca) has brown
|
{
"page_id": 56754417,
"source": null,
"title": "Evidence for speciation by reinforcement"
}
|
females, brown males, and black-and-white males. The related collard flycatcher (Ficedula albicollis) has brown females and only black-and-white males. The two species exist in separate populations that overlap in a zone of sympatry. In the range of overlap, only brown males of F. hypoleuca exist and are thought to have evolved the brown plumage to prevent hybridization, though there is also evidence indicating that such character displacement is explained by heterospecific competition for territory rather than reinforcement. Mating choice tests of the species find that females of both species choose conspecific males in sympatry, but heterospecific males in allopatry (see conspecific song preference). The patterns could suggest mimicry, driven by interspecific competition;: 361 however, song divergence has been detected that shows a similar pattern to the mating preferences. Geospiza fuliginosa and G. difficilis males on the Galápagos Islands show a noted preference for conspecific females where they meet in sympatry, but not in allopatry. Other birds such as the dark and light subspecies of the western grebe show enhanced prezygotic isolation. It has been argued that reinforcement is extremely common in birds and has been documented in a wide range of bird species. === Crustaceans === Reproductive character displacement in body size was detected in sympatric populations of Orconectes rusticus and O. sanbornii. === Echinoderms === An example of gametic isolation involves the allopatric sea urchins (Arbacia) have minimal bindin differences (bindin is a protein involved in the process of sea urchin fertilization, used for species-specific recognition of the egg by the sperm) and have insufficient barriers to fertilization.: 243 Comparison with the sympatric species Echinometra and Strongylocentrotus of the Indo-Pacific finds that they have significant differences in bindin proteins for fertilization and marked fertilization barriers. Laboratory matings of closely related sea urchin species Echinometra oblonga and E. sp. C
|
{
"page_id": 56754417,
"source": null,
"title": "Evidence for speciation by reinforcement"
}
|
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