source stringlengths 32 209 | text stringlengths 18 1.5k |
|---|---|
https://en.wikipedia.org/wiki/Crystal%20Lake%20State%20Park | Crystal Lake State Park is a day-use state park and historic site in Barton, Vermont, United States. It is located at 96 Bellwater Avenue, off Willoughby Lake Road (Vermont Route 16) just east of the village, at the northwestern end of Crystal Lake. It features a sandy beach with swimming area, and a bath house built by the Civilian Conservation Corps (CCC). A cottage is available for rental. The park was added to the U.S. National Register of Historic Places on August 30, 2005, for its association with the CCC.
Features
Crystal Lake State Park is located at the northern end of Crystal Lake, a more than body of water in southeastern Barton. The park is located just southeast of the village center, and is accessed via Bellwater Avenue off Vermont Route 16. The park has a wider area at its western end, where the entrance gate and parking area are located. Also in this area are a ranger's house and a small waterfront cottage, which is available for rental when the park is open. The parking lot is separated from the beach area to the south by a low stone wall built out of locally quarried granite. This wall gradually tapers off to the east. The eastern section of the park is narrow, with a strip of beach rising to a narrow grassy area. At the back of the grassy area near the parking lot is the bathhouse. The bathhouse has restrooms, changing areas, and a concession stand. Other features are about 40 grills, almost 80 picnic tables, play areas, and boat rentals.
Act |
https://en.wikipedia.org/wiki/RPS6KA1 | Ribosomal protein S6 kinase alpha-1 is an enzyme that in humans is encoded by the RPS6KA1 gene.
Function
This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 nonidentical kinase catalytic domains and phosphorylates various substrates, including members of the mitogen-activated kinase (MAPK) signalling pathway. The activity of this protein has been implicated in controlling cell growth and differentiation. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Interactions
RPS6KA1 has been shown to interact with:
IκBα,
MAPK1,
TOB1
TSC2, and
YWHAB.
See also
Ribosomal s6 kinase
References
Further reading
EC 2.7.11 |
https://en.wikipedia.org/wiki/CDC25C | M-phase inducer phosphatase 3 is an enzyme that in humans is encoded by the CDC25C gene.
This gene is highly conserved during evolution and it plays a key role in the regulation of cell division. The encoded protein is a tyrosine phosphatase and belongs to the Cdc25 phosphatase family. It directs dephosphorylation of cyclin B-bound CDC2 (CDK1) and triggers entry into mitosis. It is also thought to suppress p53-induced growth arrest. Multiple alternatively spliced transcript variants of this gene have been described, however, the full-length nature of many of them is not known.
Interactions
CDC25C has been shown to interact with MAPK14, CHEK1, PCNA, PIN1, PLK3 and NEDD4.
See also
Cdc25
References
Further reading
External links |
https://en.wikipedia.org/wiki/Robert%20N.%20Klein%20II | Robert Nicholas "Bob" Klein II is a stem cell advocate. He initiated California Proposition 71, which succeeded in establishing the California Institute for Regenerative Medicine, of which Klein was the chairman of the governing board.
Before getting involved in stem cell advocacy, he was a housing developer and lawyer. He lives in Portola Valley, California and works in Palo Alto, where he used to live.
Stem cell advocacy
He was a chief author of Proposition 71 and was the chair of the Yes on 71 campaign. He donated $3 million to the cause, the largest donation, and ran the campaign from the Klein Financial Corporation.
After the election, Proposition 71 became Article XXXV of the California Constitution and the Yes on 71 campaign became the California Research and Cures Coalition, a stem cell advocacy organization. Klein was the head of that organization until he took the position at the California Institute for Regenerative Medicine, the organization created by the ballot initiative. In 2005, he was named as one of TIME Magazine's 100 Most Influential People; and, that same year Scientific American named Klein one of “The Scientific American 50” as a leader shaping the future of science. Klein was honored at the 2010 BIO International Convention as the second annual Biotech Humanitarian. Also, in 2010, Klein received the 2010 Research!America Gordon and Llura Gund Leadership Award for his advocacy of stem cell and diabetes research.
In 2020, the original funding for |
https://en.wikipedia.org/wiki/Sequestosome%201 | Sequestosome-1 is a protein that in humans is encoded by the SQSTM1 gene. Also known as the ubiquitin-binding protein p62, it is an autophagosome cargo protein that targets other proteins that bind to it for selective autophagy. By interacting with GATA4 and targeting it for degradation, it can inhibit GATA-4 associated senescence and senescence-associated secretory phenotype.
Model organisms
Model organisms have been used in the study of SQSTM1 function. A conditional knockout mouse line, called Sqstm1tm1a(KOMP)Wtsi was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty two tests were carried out on homozygous mutant mice and one significant abnormality was observed: females had abnormal complete blood count parameters, including an increased red blood cell distribution width and increased mean platelet volume.
Interactions
Sequestosome 1 has been shown to interact with:
MAP1LC3A,
PRKCI,
RAD23A,
RIPK1,
TRAF6
TrkA, and
TrkB.
Nrf2
References
Further reading
Feng, Lifeng et al. “Tamoxifen activates Nrf2-dependent SQSTM1 transcription to promote endometrial hyperplasia” Theranostics vol. 7,7 1890-1900. 10 Apr. 2017, doi:10.7150/thno.19135
Genes mutated in mice |
https://en.wikipedia.org/wiki/Vascular%20endothelial%20growth%20factor%20C | Vascular endothelial growth factor C (VEGF-C) is a protein that is a member of the platelet-derived growth factor / vascular endothelial growth factor (PDGF/VEGF) family. It is encoded in humans by the VEGFC gene, which is located on chromosome 4q34.
Functions
The main function of VEGF-C is to promote the growth of lymphatic vessels (lymphangiogenesis). It acts on lymphatic endothelial cells (LECs) primarily via its receptor VEGFR-3 promoting survival, growth and migration. It was discovered in 1996 as a ligand for the orphan receptor VEGFR-3. Soon thereafter, it was shown to be a specific growth factor for lymphatic vessels in a variety of models. However, in addition to its effect on lymphatic vessels, it can also promote the growth of blood vessels and regulate their permeability. The effect on blood vessels can be mediated via its primary receptor VEGFR-3 or its secondary receptor VEGFR-2. Apart from vascular targets, VEGF-C is also important for neural development and blood pressure regulation.
Biosynthesis
VEGF-C is a dimeric, secreted protein, which undergoes a complex proteolytic maturation resulting in multiple processed forms. After translation, VEGF-C consists of three domains: the central VEGF homology domain (VHD), the N-terminal domain (propeptide) and a C-terminal domain (propeptide). It is referred to as "uncleaved VEGF-C" and has a size of approximately 58 kDa. The first cleavage (which happens already before secretion) occurs between the VHD and the C-ter |
https://en.wikipedia.org/wiki/Eukaryotic%20translation%20initiation%20factor%204%20gamma%201 | Eukaryotic translation initiation factor 4 gamma 1 is a protein that in humans is encoded by the EIF4G1 gene.
Function
The protein encoded by this gene is a component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure, and recruitment of mRNA to the ribosome. Alternative splicing results in five transcript variants encoding four distinct isoforms. eIF4G serves as a scaffold, interacting with mRNA and the other components of the eIF4F complex, as well as the PABP and eIF3.
Interactions
Eukaryotic translation initiation factor 4 gamma has been shown to interact with MKNK1, EIF4A1, EIF4E, MKNK2 and PABPC1.
See also
Eukaryotic initiation factor
References
Further reading |
https://en.wikipedia.org/wiki/ALPL | Alkaline phosphatase, tissue-nonspecific isozyme is an enzyme that in humans is encoded by the ALPL gene.
Function
There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue-nonspecific). The first three are located together on chromosome 2, whereas the tissue-nonspecific form is located on chromosome 1. The product of this gene is a membrane-bound glycosylated enzyme that is expressed in a variety of tissues and is, therefore, referred to as the tissue-nonspecific form of the enzyme. A proposed function of this form of the enzyme is in regulating matrix mineralization through its ability to degrade mineralization-inhibiting pyrophosphate. Mice that lack a functional form of this enzyme (gene knockout mice) show abnormal skeletal and dental development including a mineralization deficiency called osteomalacia/odontomalacia (hypomineralization of bones and teeth).. Humans with inactivating mutations in the ALPL gene likewise have variable degrees of mineralization defects depending on the location of the mutation in the ALPL gene.
Structure
Tissue Non-Specific Alkaline Phosphatase (TNAP), encoded by the ALPL gene, exhibits an intriguing octameric structure as revealed by X-ray crystallography. This distinct arrangement consists of four individual dimeric TNAP units. Structural studies on homologs of TNAP, namely human (ALPP) and Escherichia coli (ecPhoA), have identified the dimer as the minima |
https://en.wikipedia.org/wiki/Serum%20amyloid%20A1 | Serum amyloid A1 (SAA1) is a protein that in humans is encoded by the SAA1 gene. SAA1 is a major acute-phase protein mainly produced by hepatocytes in response to infection, tissue injury and malignancy. When released into blood circulation, SAA1 is present as an apolipoprotein associated with high-density lipoprotein (HDL). SAA1 is a major precursor of amyloid A (AA), the deposit of which leads to inflammatory amyloidosis.
Gene
The gene coding for human SAA1 is one of the 4 SAA genes mapped to a region in the short arm on Chromosome 11. Two of these genes, SAA1 and SAA2, are inducible during acute-phase response, whereas SAA3 is a pseudogene in humans and SAA4 is constitutively expressed in a variety of tissues and cells. Single nucleotide polymorphisms (SNPs) are found in SAA1 in both coding and non-coding sequences, with those located in the coding sequence defining 5 isoforms of SAA1 (SAA1.1 – 1.5). Genetic studies have shown association of some of these SNPs with the disposition to several human diseases including familiar Mediterranean fever, coronary artery diseases, cerebral infarction, and osteoporosis. Mice also have 4 Saa genes. A major difference between human and mouse SAA genes is the expression of the mouse Saa3 gene for a functional protein, generally considered an inducible SAA in inflammatory tissues.
Protein structure
The product of human SAA1 is a pre-protein of 122 amino acids, with a cleavable signal peptide of 18 amino acids. Mature SAA1 consists |
https://en.wikipedia.org/wiki/TUBB2A | Tubulin beta-2A chain is a protein that in humans is encoded by the TUBB2A gene.
References
Further reading |
https://en.wikipedia.org/wiki/TYMP%20%28gene%29 | TYMP is a gene that encodes for the enzyme thymidine phosphorylase. The TYMP gene is also known as ECGF1 (endothelial cell growth factor 1, platelet-derived) and MNGIE due to its role in MNGIE syndrome.
Structure
The TYMP gene is located on chromosome 22 in humans and contains 10 exons spanning more than 4.3 kb.
Function
TYMP encodes for the enzyme thymidine phosphorylase. TYMP and thymidine phosphorylase are associated with angiogenesis, growth of endothelial cells, and mitochondrial neurogastrointestinal encephalomyopathy (MNGIE).
Thymidine phosphorylase is angiogenic growth factor which promotes angiogenesis in vivo and stimulates the in vitro growth of a variety of endothelial cells. Thymidine phosphorylase has a highly restricted target cell specificity acting only on endothelial cells, hence its alternative name of ECGF1. Because it limits glial cell proliferation, thymidine phosphorylase is also known as gliostatin. Thymidine phosphorylase activity in leukocytes from mitochondrial neurogastrointestinal encephalomyopathy (MNGIE) patients was less than 5 percent of controls, indicating that loss-of-function mutations in TYMP cause MNGIE.
Interactive pathway map
References
Further reading
External links
GeneReviews/NIH/NCBI/UW entry on Mitochondrial Neurogastrointestinal Encephalopathy Disease (MNGIE) |
https://en.wikipedia.org/wiki/Y%20box%20binding%20protein%201 | Y box binding protein 1 also known as Y-box transcription factor or nuclease-sensitive element-binding protein 1 is a protein that in humans is encoded by the YBX1 gene.
Clinical significance
YBX1 is a potential drug target in cancer therapy. YB-1 helps the replication of adenovirus type 5, a commonly used vector in gene therapy. Thus, YB-1 can cause an "oncolytic" effect in YB-1 positive cancer cells treated with adenoviruses.
Interactions
Y box binding protein 1 has been shown to interact with:
ANKRD2,
CTCF,
P53,
PCNA,
RBBP6, and
SFRS9.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/IRAK1 | Interleukin-1 receptor-associated kinase 1 (IRAK-1) is an enzyme in humans encoded by the IRAK1 gene. IRAK-1 plays an important role in the regulation of the expression of inflammatory genes by immune cells, such as monocytes and macrophages, which in turn help the immune system in eliminating bacteria, viruses, and other pathogens. IRAK-1 is part of the IRAK family consisting of IRAK-1, IRAK-2, IRAK-3, and IRAK-4, and is activated by inflammatory molecules released by signaling pathways during pathogenic attack. IRAK-1 is classified as a kinase enzyme, which regulates pathways in both innate and adaptive immune systems.
Structure
IRAK-1 contains an N-terminal death domain (DD), a ProST domain, a centrally located kinase domain, and a C-terminal domain. The DD on IRAK-1 acts as an interaction platform for other DD-containing protein, most notably the adaptor protein myeloid differentiation factor 88, MyD88.
The proST domain contains serine, proline, and threonine amino acid residues and is used to facilitate IRAK-1 interaction with other IRAK family members or proteins. For example, auto-phosphorylation may occur multiple times in the ProST domain, which allows IRAK-1 to dissociate from the MyD88 bound to the DD while maintaining interactions with downstream proteins such as TNF receptor-associated factor 6 (TRAF-6) to initiate further pathway signaling.
Moreover, IRAK-1 contains an invariant lysine within the centrally located kinase domain. The invariant lysine acts as |
https://en.wikipedia.org/wiki/Mesaxon | In neurobiology, a mesaxon is a pair of parallel plasma membranes of a Schwann cell. It marks the point of edge-to-edge contact by the Schwann cell encircling the axon. A single Schwann cell of the peripheral nervous system will wrap around and support only one individual axon (then myelinated; ratio of 1:1), while the oligodendrocytes found in the central nervous system can wrap around and support 5-8 axons. Thin unmyelinated axons are often bundled, with several unmyelinated axons to a single mesaxon (and several such groups to a single Schwann cell).
The outer mesaxon (Terminologia histologica: Mesaxon externum) is the connection of the outer cell membrane to the compact myelin sheath. The inner mesaxon (Terminologia histologica: Mesaxon internum) is the connection between the myelin sheath and the inner part of the cell membrane of the Schwann cell, which is directly opposite the axolemma, i.e. the cell membrane of the nerve fibre ensheathed by the Schwann cell.
References
Glial cells |
https://en.wikipedia.org/wiki/Solar%20power%20in%20the%20European%20Union | Solar power consists of photovoltaics (PV) and solar thermal energy in the European Union.
In 2010, the €2.6 billion European solar heating sectors consisted of small and medium-sized businesses, generated 17.3 terawatt-hours (TWh) of energy, employed 33,500 workers, and created one new job for every 80 kW of added capacity.
During 2011, an additional 21.9 gigawatts (GW) of photovoltaics systems were connected to the grid in the European Union, a steep increase from 13.4 GW in 2010. Turnover of the European PV market amounted to approximately €36 billion for this period.
Photovoltaic solar power
In 2012, photovoltaic systems with a total capacity of 17.2 gigawatt (GW) were connected to the grid in Europe, less than in 2011, when 22.4 GW had been installed. In terms of total installed capacity, according to EPIA's 2012-report, Europe still led the way with more than 70 GW, or 69% of worldwide capacity, producing 85 TWh of electricity annually. This energy volume is sufficient to power the supply needs of over 20 million households.
In 2011, solar photovoltaic continued its growth trend and Italy was the top market for the year, with 9.3 GW connected, followed by Germany (7.5 GW). These two markets were followed by France (1.7 GW) and the United Kingdom (784 MW). In terms of cumulative capacity, Germany with more than 24 GW, is the leading country in Europe, followed by Italy, with more than 12 GW. PV is now a significant part of Europe's electricity mix, producing 2% of |
https://en.wikipedia.org/wiki/Characteristic%20number%20%28disambiguation%29 | Characteristic number may mean:
Characteristic number (mathematics)
Characteristic number (physics)
Characteristic number (fluid dynamics) |
https://en.wikipedia.org/wiki/Chirp%20spread%20spectrum | In digital communications, chirp spread spectrum (CSS) is a spread spectrum technique that uses wideband linear frequency modulated chirp pulses to encode information. A chirp is a sinusoidal signal whose frequency increases or decreases over time (often with a polynomial expression for the relationship between time and frequency).
Overview
As with other spread spectrum methods, chirp spread spectrum uses its entire allocated bandwidth to broadcast a signal, making it robust to channel noise. Further, because the chirps utilize a broad band of the spectrum, chirp spread spectrum is also resistant to multi-path fading even when operating at very low power. However, it is unlike direct-sequence spread spectrum (DSSS) or frequency-hopping spread spectrum (FHSS) in that it does not add any pseudo-random elements to the signal to help distinguish it from noise on the channel, instead relying on the linear nature of the chirp pulse. Additionally, chirp spread spectrum is resistant to the Doppler effect, which is typical in mobile radio applications.
Uses
Chirp spread spectrum was originally designed to compete with ultra-wideband for precision ranging and low-rate wireless networks in the 2.45 GHz band. However, since the release of IEEE 802.15.4a (also known as IEEE 802.15.4a-2007), it is no longer actively being considered by the IEEE for standardization in the area of precision ranging.
Chirp spread spectrum is ideal for applications requiring low power usage and needing |
https://en.wikipedia.org/wiki/IRF1 | Interferon regulatory factor 1 is a protein that in humans is encoded by the IRF1 gene.
Function
Interferon regulatory factor 1 was the first member of the interferon regulatory transcription factor (IRF) family identified. Initially described as a transcription factor able to activate expression of the cytokine Interferon beta, IRF-1 was subsequently shown to function as a transcriptional activator or repressor of a variety of target genes. IRF-1 regulates expression of target genes by binding to an interferon stimulated response element (ISRE) in their promoters. The IRF-1 protein binds to the ISRE via an N-terminal helix-turn-helix DNA binding domain, which is highly conserved among all IRF proteins.
Beyond its function as a transcription factor, IRF-1 has also been shown to trans-activate the tumour suppressor protein p53 through the recruitment of its co-factor p300.
IRF-1 has been shown to play roles in the immune response, regulating apoptosis, DNA damage and tumor suppression.
Regulation
It has been shown that the extreme C-terminus of IRF-1 regulates its ability to activate transcription, nanobodies targeting this domain (MF1) are able to increase IRF-1 activity.
Model organisms
Model organisms have been used in the study of IRF1 function. A conditional knockout mouse line, called Irf1tm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of |
https://en.wikipedia.org/wiki/GNB3 | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3 is a protein that in humans is encoded by the GNB3 gene.
Heterotrimeric guanine nucleotide-binding proteins ( G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. A single-nucleotide polymorphism (C825T) in this gene is associated with essential hypertension and obesity. This polymorphism is also associated with the occurrence of the splice variant GNB3-s, which appears to have increased activity. GNB3-s is an example of alternative splicing caused by a nucleotide change outside of the splice donor and acceptor sites. Additional splice variants may exist for this gene, but they have not been fully described.
References
Further reading |
https://en.wikipedia.org/wiki/GNAQ | Guanine nucleotide-binding protein G(q) subunit alpha is a protein that in humans is encoded by the GNAQ gene. Together with GNA11 (its paralogue), it functions as a Gq alpha subunit.
Function
Guanine nucleotide-binding proteins are a family of heterotrimeric proteins that couple cell surface, 7-transmembrane domain receptors to intracellular signaling pathways. Receptor activation catalyzes the exchange of GDP for GTP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit. G-alpha-q is the alpha subunit of one of the heterotrimeric GTP-binding proteins that mediates stimulation of phospholipase C-beta (MIM 600230).[supplied by OMIM]
Mutations in this gene have been found associated to cases of Sturge–Weber syndrome and port-wine stains.
Interactions
GNAQ has been shown to interact with:
Beta adrenergic receptor kinase,
Bruton's tyrosine kinase,
RGS16
RGS4
RIC8A, and
Sodium-hydrogen antiporter 3 regulator 1.
See also
List of genes mutated in pigmented cutaneous lesions
References
Further reading |
https://en.wikipedia.org/wiki/PRKCQ | Protein kinase C theta (PKC-θ) is an enzyme that in humans is encoded by the PRKCQ gene. PKC-θ, a member of serine/threonine kinases, is mainly expressed in hematopoietic cells with high levels in platelets and T lymphocytes, where plays a role in signal transduction. Different subpopulations of T cells vary in their requirements of PKC-θ, therefore PKC-θ is considered as a potential target for inhibitors in the context of immunotherapy.
Function
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipid-dependent protein kinase. This kinase is important for T-cell activation. It is required for the activation of the transcription factors NF-kappaB and AP-1, and may link the T cell receptor (TCR) signaling complex to the activation of the transcription factors. PKC-θ also play a role in the apoptosis of lymphoid cells where it negatively influence and delay the aggregation of spectrin in an early phase of apoptosis.
The role of PKC-θ in T cells |
https://en.wikipedia.org/wiki/Cav2.1 | {{DISPLAYTITLE:Cav2.1}}
Cav2.1, also called the P/Q voltage-dependent calcium channel, is a calcium channel found mainly in the brain. Specifically, it is found on the presynaptic terminals of neurons in the brain and cerebellum. Cav2.1 plays an important role in controlling the release of neurotransmitters between neurons. It is composed of multiple subunits, including alpha-1, beta, alpha-2/delta, and gamma subunits. The alpha-1 subunit is the pore-forming subunit, meaning that the calcium ions flow through it. Different kinds of calcium channels have different isoforms (versions) of the alpha-1 subunit. Cav2.1 has the alpha-1A subunit, which is encoded by the CACNA1A gene. Mutations in CACNA1A have been associated with various neurologic disorders, including familial hemiplegic migraine, episodic ataxia type 2, and spinocerebellar ataxia type 6.
Function
"Voltage-dependent calcium channels mediate the entry of calcium ions into excitable cells, and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, and gene expression. Calcium channels are multisubunit complexes composed of alpha-1, beta, alpha-2/delta, and gamma subunits. The channel activity is directed by the pore-forming alpha-1 subunit, whereas, the others act as auxiliary subunits regulating this activity. The distinctive properties of the calcium channel types are related primarily to the expression of a variety of alpha-1 isoforms, |
https://en.wikipedia.org/wiki/Marc%20M%C3%B8ller | Marc Møller (born 7 June 1986) is a retired Danish professional football defender.
External links
Lyngby BK profile
Official Danish Superliga player statistics at danskfodbold.com
1986 births
Living people
Danish men's footballers
FC Midtjylland players
Lyngby Boldklub players
Danish Superliga players
Ikast FC players
Men's association football defenders |
https://en.wikipedia.org/wiki/TIMP3 | Metalloproteinase inhibitor 3 is a protein that in humans is encoded by the TIMP3 gene.
This gene belongs to the tissue inhibitor of metalloproteinases gene family. The proteins encoded by this gene family are inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix (ECM). Expression of this gene is induced in response to mitogenic stimulation and this netrin domain-containing protein is localized to the ECM. Mutations in this gene have been associated with the autosomal dominant disorder Sorsby's fundus dystrophy.
See also
TIMP1, TIMP2, TIMP4
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: I35.003 |
https://en.wikipedia.org/wiki/HEXA | Hexosaminidase A (alpha polypeptide), also known as HEXA, is an enzyme that in humans is encoded by the HEXA gene, located on the 15th chromosome.
Hexosaminidase A and the cofactor GM2 activator protein catalyze the degradation of the GM2 gangliosides and other molecules containing terminal N-acetyl hexosamines. Hexosaminidase A is a heterodimer composed of an alpha subunit (this protein) and a beta subunit. The alpha subunit polypeptide is encoded by the HEXA gene while the beta subunit is encoded by the HEXB gene. Gene mutations in the gene encoding the beta subunit (HEXB) often result in Sandhoff disease; whereas, mutations in the gene encoding the alpha subunit (HEXA, this gene) decrease the hydrolysis of GM2 gangliosides, which is the main cause of Tay–Sachs disease.
Function
Even though the alpha and beta subunits of hexosaminidase A can both cleave GalNAc residues, only the alpha subunit is able to hydrolyze GM2 gangliosides. The alpha subunit contains a key residue, Arg-424, which is essential for binding the N-acetyl-neuramanic residue of GM2 gangliosides. The alpha subunit can hydrolyze GM2 gangliosides because it contains a loop structure consisting of the amino acids: Gly-280, Ser-281, Glu-282, and Pro-283. The loop is absent in the beta subunit, but it serves as an ideal structure for the binding of the GM2 activator protein (GM2AP) in the alpha subunit. A combination of Arg-424 and the amino acids that cause the formation of the loop allow the alpha |
https://en.wikipedia.org/wiki/Strawberry%20Perl | Strawberry Perl is a distribution of the Perl programming language for the Microsoft Windows platform. Additionally, strawberry contains a fully featured Mingw-w64 C/C++ compiler with many libraries included. While most other distributions rely on the user having software development tools already set up to install certain Perl components, Strawberry Perl ships with the most commonly used tools preconfigured and packaged. It is a dramatic departure from other Perl distributions, and has influenced other distributions (such as its primary rival, the freely available but closed source ActivePerl distribution released by ActiveState) to provide such development tools in their own distribution.
Rationale
Through the CPAN, Perl users can download any of a vast number of prepackaged modules. Many of these modules can be installed in any Perl environment; however, certain modules (XS modules) require a working C compiler and development environment to install successfully. Most Perl distributions assume that such an environment - which is usually provided with most Unix or Linux systems - already exists; however, Windows does not come with a C compiler and the required development environment, and these must be installed separately by the user or the administrator.
However, Strawberry Perl incorporates the MinGW development environment during installation. All the installed Perl tools are set up to use these built-in libraries and development tools to compile XS modules as require |
https://en.wikipedia.org/wiki/Morten%20Christiansen%20%28footballer%29 | Morten Christiansen (born 4 January 1978) is a Danish professional football midfielder, who currently plays for FC Royal.
External links
Lyngby BK profile
Danish Superliga player statistics at danskfodbold.com
1978 births
Living people
Danish men's footballers
AC Horsens players
Lyngby Boldklub players
Danish Superliga players
Footballers from Aarhus
Men's association football midfielders
VSK Aarhus players |
https://en.wikipedia.org/wiki/TRAF3 | TNF receptor-associated factor (TRAF3) is a protein that in humans is encoded by the TRAF3 gene.
Function
The protein encoded by this gene is a member of the TNF receptor associated factor (TRAF) protein family. TRAF proteins associate with, and mediate the signal transduction from, members of the TNF receptor (TNFR) superfamily. This protein participates in the signal transduction of CD40, a TNFR family member important for the activation of the immune response. This protein is found to be a critical component of the lymphotoxin-beta receptor (LTbetaR) signaling complex, which induces NF-kappaB activation and cell death initiated by LTbeta ligation. Epstein-Barr virus-encoded latent infection membrane protein-1 (LMP1) can interact with this and several other members of the TRAF family, which may be essential for the oncogenic effects of LMP1. Three alternatively spliced transcript variants encoding two distinct isoforms have been reported.
Interactions
TRAF3 has been shown to interact with:
CD27,
CD40,
Caspase 3
Lymphotoxin beta receptor,
Nucleoporin 62,
RANK,
TANK, and
TNFSF14.
References
Further reading |
https://en.wikipedia.org/wiki/SMARCB1 | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 is a protein that in humans is encoded by the SMARCB1 gene.
Function
The protein encoded by this gene is part of a complex that relieves repressive chromatin structures, allowing the transcriptional machinery to access its targets more effectively. The encoded nuclear protein may also bind to and enhance the DNA joining activity of HIV-1 integrase. This gene has been found to be a tumor suppressor and mutations in it have been associated with malignant rhabdoid tumors. Two transcript variants encoding different isoforms have been found for this gene.
Interactions
SMARCB1 has been shown to interact with:
ARID1A,
BAZ1B,
BRCA1,
CREB-binding protein,
Cyclin-dependent kinase 8,
Myc,
P53,
POLR2A,
PPP1CA,
PPP1CB,
PPP1CC,
PPP1R15A,
SMARCA2,
SMARCA4,
SMARCC1,
SMARCE1,
SS18, and
XPO1.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Nicolai%20Melchiorsen | Nicolai Melchiorsen (born 9 March 1984) is a Danish professional football midfielder.
External links
Nicolai Melchiorsen official Danish Superliga statistics at danskfodbold.com
1984 births
Living people
Danish men's footballers
Akademisk Boldklub players
Lyngby Boldklub players
Viborg FF players
Danish Superliga players
Men's association football midfielders |
https://en.wikipedia.org/wiki/GNAI2 | Guanine nucleotide-binding protein G(i), alpha-2 subunit is a protein that in humans is encoded by the GNAI2 gene.
Interactions
GNAI2 has been shown to interact with:
EYA2,
GPSM2,
Interleukin 8 receptor, alpha,
MDFI,
RGS5, and
RIC8A.
References
Further reading |
https://en.wikipedia.org/wiki/GNAI1 | Guanine nucleotide-binding protein G(i), alpha-1 subunit is a protein that in humans is encoded by the GNAI1 gene.
Interactive pathway map
Interactions
GNAI1 has been shown to interact with:
GPR143,
RGS12,
RGS14,
RGS19,
RIC8A, and
S1PR1.
References
Further reading |
https://en.wikipedia.org/wiki/Beta-defensin%202 | Beta-defensin 2 (BD-2) also known as skin-antimicrobial peptide 1 (SAP1) is a peptide that in humans is encoded by the DEFB4 (defensin, beta 4) gene.
Human beta-defensin-2 (hBD-2) is a cysteine-rich cationic low molecular weight antimicrobial peptide recently discovered in lesional skin.
Structure
hBD-2 is a protein whose primary structure is made by 64 aminoacids. At concentrations ≤2.4 mM, hBD-2 is monomeric. The structure is amphiphilic with a nonuniform surface distribution of positive charge and contains several key structural elements, including a triple-stranded, antiparallel beta sheet with strands 2 and 3 in a beta hairpin conformation.
The determination of other structural elements depends on the technique used. When X-ray crystallography is used an alpha helix can be observed at the N-terminal end of the protein (PDB codes: ,, and ). When using NMR this alpha-helix does not appear (PDB code: ), however this structure was determined using a truncated version of hBD-2 which was missing the initial 4 amino acids, and may be the reason for the discrepancy.
Function
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. Beta-defensin 2 is an antibiotic peptide which is locally regulated by inflammation.
Human beta-defensin 2 is produced by a number of epithelial cells and exhibits potent antimicrobial activity against Gram-negative bacteria and Candida, but not Gra |
https://en.wikipedia.org/wiki/TEK%20tyrosine%20kinase | Angiopoietin-1 receptor also known as CD202B (cluster of differentiation 202B) is a protein that in humans is encoded by the TEK gene. Also known as TIE2, it is an angiopoietin receptor.
Function
The TEK receptor tyrosine kinase is expressed almost exclusively in endothelial cells in mice, rats, and humans. (TEK is closely related to the TIE receptor tyrosine kinase.)
This receptor possesses a unique extracellular domain containing 2 immunoglobulin-like loops separated by 3 epidermal growth factor-like repeats that are connected to 3 fibronectin type III-like repeats. The ligand for the receptor is angiopoietin-1. TEK has also been suggested as a marker for nucleus pulposus progenitor cells, from the intervertebral disc, which upon activation by Angiopoietin-1 starts to multiply and differentiate.
Defects in TEK are associated with inherited venous malformations; the TEK signaling pathway appears to be critical for endothelial cell-smooth muscle cell communication in venous morphogenesis.
In cancer patients, TEK (Tie2) is expressed in a subpopulation of monocytes that home in on the tumor and are essential for the formation of new blood vessels there.
Interactions
TEK tyrosine kinase has been shown to interact with:
ANGPT2,
Angiopoietin 1,
DOK2.
See also
Tie-2/Ang-1 signaling
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Multiple Cutaneous and Mucosal Venous Malformations
Clusters of differentiation
Tyrosine kinase recept |
https://en.wikipedia.org/wiki/Biplot | Biplots are a type of exploratory graph used in statistics, a generalization of the simple two-variable scatterplot.
A biplot overlays a score plot with a loading plot.
A biplot allows information on both samples and variables of a data matrix to be displayed graphically. Samples are displayed as points while variables are displayed either as vectors, linear axes or nonlinear trajectories. In the case of categorical variables, category level points may be used to represent the levels of a categorical variable. A generalised biplot displays information on both continuous and categorical variables.
Introduction and history
The biplot was introduced by K. Ruben Gabriel (1971). Gower and Hand (1996) wrote a monograph on biplots. Yan and Kang (2003) described various methods which can be used in order to visualize and interpret a biplot. The book by Greenacre (2010) is a practical user-oriented guide to biplots, along with scripts in the open-source R programming language, to generate biplots associated with principal component analysis (PCA), multidimensional scaling (MDS), log-ratio analysis (LRA)—also known as spectral mapping—discriminant analysis (DA) and various forms of correspondence analysis: simple correspondence analysis (CA), multiple correspondence analysis (MCA) and canonical correspondence analysis (CCA) (Greenacre 2016). The book by Gower, Lubbe and le Roux (2011) aims to popularize biplots as a useful and reliable method for the visualization of multivariate da |
https://en.wikipedia.org/wiki/INHBA | Inhibin, beta A, also known as INHBA, is a protein which in humans is encoded by the INHBA gene. INHBA is a subunit of both activin and inhibin, two closely related glycoproteins with opposing biological effects.
Function
The inhibin beta A subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary several fold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome.
Interactions
INHBA has been shown to interact with ACVR2A.
References
Further reading
sr:INHBB |
https://en.wikipedia.org/wiki/Bloom%20syndrome%20protein | Bloom syndrome protein is a protein that in humans is encoded by the BLM gene and is not expressed in Bloom syndrome.
The Bloom syndrome gene product is related to the RecQ subset of DExH box-containing DNA helicases and has both DNA-stimulated ATPase and ATP-dependent DNA helicase activities. Mutations causing Bloom syndrome delete or alter helicase motifs and may disable the 3' → 5' helicase activity. The normal protein may act to suppress inappropriate homologous recombination.
Meiosis
Recombination during meiosis is often initiated by a DNA double-strand break (DSB). During recombination, sections of DNA at the 5' ends of the break are cut away in a process called resection. In the strand invasion step that follows, an overhanging 3' end of the broken DNA molecule then "invades" the DNA of an homologous chromosome that is not broken. After strand invasion, the further sequence of events may follow either of two main pathways leading to a crossover (CO) or a non-crossover (NCO) recombinant (see Genetic recombination and bottom of Figure in this section).
The budding yeast Saccharomyces cerevisiae encodes an ortholog of the Bloom syndrome (BLM) protein that is designated Sgs1 (Small growth suppressor 1). Sgs1(BLM) is a helicase that functions in homologous recombinational repair of DSBs. The Sgs1(BLM) helicase appears to be a central regulator of most of the recombination events that occur during S. cerevisiae meiosis. During normal meiosis Sgs1(BLM) is responsible |
https://en.wikipedia.org/wiki/PIN1 | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 is an enzyme that in humans is encoded by the PIN1 gene.
Pin 1, or peptidyl-prolyl cis/trans isomerase (PPIase), isomerizes only phospho-Serine/Threonine-Proline motifs. The enzyme binds to a subset of proteins and thus plays a role as a post phosphorylation control in regulating protein function. Studies have shown that the deregulation of Pin1 may play a pivotal role in various diseases. Notably, the up-regulation of Pin1 is implicated in certain cancers, and the down-regulation of Pin1 is implicated in Alzheimer's disease. Inhibitors of Pin1 may have therapeutic implications for cancer and immune disorders.
Discovery
The gene encoding Pin1 was identified in 1996 as a result of a genetic/biochemical screen for proteins involved in mitotic regulation. It was found to be essential for cell division in some organisms. By 1999, however, it was apparent that Pin1 knockout mice had a surprisingly mild phenotype, indicating that the enzyme was not required for cell division per se. Further studies later found that loss of Pin1 in mice displays are not only neuronal degenerative phenotypes but also several abnormalities, similar to those of cyclin D1-null mice, suggesting the conformation changes mediated by Pin1 may be crucial for cell normal function.
Activation
Phosphorylation of Ser/Thr-Pro motifs in substrates is required for recognition by Pin1. Pin is a small protein at 18 kDa and does not have a nuclear locali |
https://en.wikipedia.org/wiki/FCGR2A | Low affinity immunoglobulin gamma Fc region receptor II-a is a protein that in humans is encoded by the FCGR2A gene.
Interactions
FCGR2A has been shown to interact with PIK3R1 and Syk.
See also
CD32
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Low affinity immunoglobulin gamma Fc region receptor II-a (FCGR2A)
Clusters of differentiation
Fc receptors |
https://en.wikipedia.org/wiki/SCARB1 | Scavenger receptor class B type 1 (SRB1) also known as SR-BI is a protein that in humans is encoded by the SCARB1 gene. SR-BI functions as a receptor for high-density lipoprotein.
Function
Scavenger receptor class B, type I (SR-BI) is an integral membrane protein found in numerous cell types/tissues, including enterocytes, the liver and adrenal gland. It is best known for its role in facilitating the uptake of cholesteryl esters from high-density lipoproteins in the liver. This process drives the movement of cholesterol from peripheral tissues towards the liver, where cholesterol can either be secreted via the bile duct or be used to synthesise steroid hormones. This movement of cholesterol is known as reverse cholesterol transport and is a protective mechanism against the development of atherosclerosis, which is the principal cause of heart disease and stroke.
SR-BI is crucial in carotenoid and vitamin E uptake in the small intestine. SR-B1 is upregulated in times of vitamin A deficiency and downregulated if vitamin A status is in the normal range.
In melanocytic cells SCARB1 gene expression may be regulated by the MITF.
Species distribution
SR-BI has also been identified in the livers of non-mammalian species (turtle, goldfish, shark, chicken, frog, and skate), suggesting it emerged early in vertebrate evolutionary history. The turtle also seems to upregulate SR-BI during egg development, indicating that cholesterol efflux may be at peak levels during developmen |
https://en.wikipedia.org/wiki/BCL2L11 | Bcl-2-like protein 11, commonly called BIM (Bcl-2 Interacting Mediator of cell death), is a protein that in humans is encoded by the BCL2L11 gene.
Function
The protein encoded by this gene belongs to the BCL-2 protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The protein encoded by this gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to interact with other members of the BCL-2 protein family, including BCL2, BCL2L1/BCL-X(L), and MCL1, and to act as an apoptotic activator. The expression of this gene can be induced by nerve growth factor (NGF), as well as by the forkhead transcription factor FKHR-L1 (FoxO3a), which suggests a role of this gene in neuronal and lymphocyte apoptosis. Transgenic studies of the mouse counterpart suggested that this gene functions as an essential initiator of apoptosis in thymocyte-negative selection. Several alternatively spliced transcript variants of this gene have been identified.
Regulation of Bim
Bim expression and activity are regulated at the transcriptional, translational and post-translational levels; coordinated expression and activity of Bim shape immune responses, and ensure tissue integrity. Cancer cells develop mechanisms that suppress Bim expression, which allows for tumor progression and metastasis.
Interactions
BCL2L11 has been shown to interact with:
BCL2-like 1,
BCL2L2,
Bcl-2,
DYNL |
https://en.wikipedia.org/wiki/Erythrocyte%20rosetting | Erythrocyte rosetting or E-rosetting is a phenomenon seen through a microscope where red blood cells (erythrocytes) are arranged around a central cell to form a cluster that looks like a flower. The red blood cells surrounding the cell form the petal, while the central cell forms the stigma of the flower shape. This formation occurs due to an immunological reaction between an epitope on the central cell's surface and a receptor or antibody on a red cell. The presence of E-rosetting can be used as a test for T cells although more modern tests such as immunohistochemistry are available. Rosetting is caused by parasites in the genus Plasmodium and is a cause of some malaria-associated symptoms.
Rosetting techniques
Three types of rosette techniques have been developed and used experimentally.
Rosette test for Rh factor
The Rosette test is performed on postpartum maternal blood to estimate the volume of fetal-maternal hemorrhage in case of an Rh negative mother and an Rh positive child. This estimate, in turn, also estimates the required amount of Rho(D) immune globulin to administer. In this test, a sample of maternal blood is incubated with Rho(D) immune globulin, which will bind to any fetal Rh positive red blood cells, if present. Upon addition of enzyme-treated cDE indicator cells, the presence of Rh positive fetal blood causes rosetting, which can be seen by light microscopy. The test is recommended for Rh negative mothers within 72 hours of giving birth to an Rh-posi |
https://en.wikipedia.org/wiki/Monte%20Carlo%20method%20for%20photon%20transport | Modeling photon propagation with Monte Carlo methods is a flexible yet rigorous approach to simulate photon transport. In the method, local rules of photon transport are expressed as probability distributions which describe the step size of photon movement between sites of photon-matter interaction and the angles of deflection in a photon's trajectory when a scattering event occurs. This is equivalent to modeling photon transport analytically by the radiative transfer equation (RTE), which describes the motion of photons using a differential equation. However, closed-form solutions of the RTE are often not possible; for some geometries, the diffusion approximation can be used to simplify the RTE, although this, in turn, introduces many inaccuracies, especially near sources and boundaries. In contrast, Monte Carlo simulations can be made arbitrarily accurate by increasing the number of photons traced. For example, see the movie, where a Monte Carlo simulation of a pencil beam incident on a semi-infinite medium models both the initial ballistic photon flow and the later diffuse propagation.
The Monte Carlo method is necessarily statistical and therefore requires significant computation time to achieve precision. In addition Monte Carlo simulations can keep track of multiple physical quantities simultaneously, with any desired spatial and temporal resolution. This flexibility makes Monte Carlo modeling a powerful tool. Thus, while computationally inefficient, Monte Carlo |
https://en.wikipedia.org/wiki/COUP-TFI | COUP-TF1 (COUP Transcription Factor 1) also known as NR2F1 (Nuclear Receptor subfamily 2, group F, member 1) is a protein that in humans is encoded by the NR2F1 gene. This protein is a member of nuclear hormone receptor family of steroid hormone receptors.
Function
Coup (chicken ovalbumin upstream promoter) transcription factor binds to the ovalbumin promoter and, in conjunction with another protein (S300-II) stimulates initiation of transcription. COUP-TF1 binds to both direct repeats and palindromes of the 5'-AGGTCA-3' motif.
Interactions
COUP-TFI has been shown to interact with:
BCL11A,
BCL11B,
COPS2, and
ESR1.
Clinical
Mutations in this gene have been associated with Bosch-Boonstra-Schaaf optic atrophy syndrome.
References
External links
Further reading
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/COUP-TFII | COUP-TFII (COUP transcription factor 2), also known as NR2F2 (nuclear receptor subfamily 2, group F, member 2) is a protein that in humans is encoded by the NR2F2 gene. The COUP acronym stands for chicken ovalbumin upstream promoter.
Function
COUP-TFII plays a critical role in controlling the development of a number of tissues and organs including heart, blood vessels, muscles and limbs.
The glucocorticoid receptor (GR) stimulates COUP-TFII-induced transactivation while COUP-TFII represses the GR transcriptional activity. COUP-TFII interacts with GATA2 to inhibit adipocyte differentiation.
Structure and ligands
The structure of COUP-TF2 LBD is known. Retinoic acid, although not at physiological concentrations, activate this receptor.
Interactions
COUP-TFII has been shown to interact with:
HDAC1
Lck
V-erbA-related gene.
Nucleolin
References
External links
Further reading
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/Stretching%20field | In applied mathematics, stretching fields provide the local deformation of an infinitesimal circular fluid element over a finite time interval ∆t. The logarithm of the stretching (after first dividing by ∆t) gives the finite-time Lyapunov exponent λ for separation of nearby fluid elements at each point in a flow. For periodic two-dimensional flows, stretching fields have been shown to be closely related to the mixing of a passive scalar concentration field. Until recently, however, the extension of these ideas to systems that are non-periodic or weakly turbulent has been possible only in numerical simulations.
Dynamical systems |
https://en.wikipedia.org/wiki/Climate%20of%20Kolkata | Kolkata has a Tropical wet-and-dry climate (Köppen climate classification Aw). The annual mean temperature is 26.8 °C (80 °F); monthly mean temperatures range from 15 °C to 30 °C (59 °F to 86 °F). Summers are hot and humid with temperatures in the low 30's and during dry spells the maximum temperatures often exceed 40 °C (104 °F) during May and June. Winter tends to last for only about two and a half months, with seasonal lows dipping to 9 °C – 11 °C (48.2 °F – 51.8 °F) between December and January. The highest recorded temperature is 43.9 °C (111 °F) and the lowest is 5 °C (41 °F). Often during early summer (mid March to mid May), dusty squalls followed by spells of thunderstorm and heavy rains lash the city, bringing relief from the humid heat. These thunderstorms are convective in nature, and is locally known as Kal baisakhi (, Nor'westers).
Rains brought by the Bay of Bengal branch of South-West monsoon lash the city between June and September and supplies the city with most of its annual rainfall of 1,836.5 mm (72.30 inches). The highest rainfall occurs during the monsoon in July and August interchangeably. The city receives 2578 hours of sunshine per annum, with the maximum sunlight occurring in March. Pollution is a major concern in Kolkata, and the Suspended Particulate Matter (SPM) level is high when compared to other major cities of India, leading to regular smog and haze. Severe air pollution in the city has caused rise in pollution-related respiratory ailments s |
https://en.wikipedia.org/wiki/Context%20tree%20weighting | The context tree weighting method (CTW) is a lossless compression and prediction algorithm by . The CTW algorithm is among the very few such algorithms that offer both theoretical guarantees and good practical performance (see, e.g. ).
The CTW algorithm is an “ensemble method”, mixing the predictions of many underlying variable order Markov models, where each such model is constructed using zero-order conditional probability estimators.
References
External links
Relevant CTW papers and implementations
CTW Official Homepage
Lossless compression algorithms |
https://en.wikipedia.org/wiki/Methyl-n-amylnitrosamine | Methyl-n-amylnitrosamine (MNAN) is a potential carcinogen It is metabolized in the liver by the enzyme CYP2A6.
References
Carcinogens
Nitrosamines |
https://en.wikipedia.org/wiki/Minor%20allele%20frequency | Minor allele frequency (MAF) is the frequency at which the second most common allele occurs in a given population. They play a surprising role in heritability since MAF variants which occur only once, known as "singletons", drive an enormous amount of selection.
Single nucleotide polymorphisms (SNPs) with a minor allele frequency of 0.05 (5%) or greater were targeted by the HapMap project.
MAF is widely used in population genetics studies because it provides information to differentiate between common and rare variants in the population.
As an example, a 2015 study sequenced the whole genomes of Sardinian individuals. The authors classified the variants found in the study in three classes according to their MAF. It was observed that rare variants (MAF < 0.05) appeared more frequently in coding regions than common variants (MAF > 0.05) in this population.
Interpreting MAF data
1. Introduce the reference of a SNP of interest, as an example: rs429358, in a database (dbSNP or other).
2. Find MAF/MinorAlleleCount link. MAF/MinorAlleleCount: C=0.1506/754 (1000 Genomes, where number of genomes sampled = N = 2504); where C is the minor allele for that particular locus; 0.1506 is the frequency of the C allele (MAF), i.e. 15% within the 1000 Genomes database; and 754 is the number of times this SNP has been observed in the population of the study.
See also
Allele frequency
References
Classical genetics |
https://en.wikipedia.org/wiki/Testicular%20receptor%202 | The testicular receptor 2 (TR2) also known as NR2C1 (nuclear receptor subfamily 2, group C, member 1) is protein that in humans is encoded by the NR2C1 gene. TR2 is a member of the nuclear receptor family of transcription factors.
Interactions
Testicular receptor 2 has been shown to interact with:
Androgen receptor,
Estrogen receptor alpha,
HDAC3, and
HDAC4.
See also
Testicular receptor
References
Further reading
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/1%2C5-anhydro-D-fructose%20dehydratase | The enzyme 1,5-anhydro-D-fructose dehydratase () catalyzes the chemical reaction
1,5-anhydro-D-fructose 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + HO
It catalyzes two steps in the anhydrofructose pathway process.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 1,5-anhydro-D-fructose hydro-lyase (ascopyrone-M-forming). Other names in common use include 1,5-anhydro-D-fructose 4-dehydratase, 1,5-anhydro-D-fructose hydrolyase, 1,5-anhydro-D-arabino-hex-2-ulose dehydratase, AFDH, AF dehydratase, and 1,5-anhydro-D-fructose hydro-lyase.
References
See also
Anhydrofructose pathway
Ascopyrone tautomerase
exo-(1→4)-α-D-glucan lyase
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/16-alpha-hydroxyprogesterone%20dehydratase | The enzyme 16α-hydroxyprogesterone dehydratase () catalyzes the chemical reaction
16α-hydroxyprogesterone = 16,17-didehydroprogesterone + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 16α-hydroxyprogesterone hydro-lyase (16,17-didehydroprogesterone-forming). Other names in common use include hydroxyprogesterone dehydroxylase, 16α-hydroxyprogesterone dehydroxylase, 16α-dehydroxylase, and 16α-hydroxyprogesterone hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-dehydro-3-deoxy-L-arabinonate%20dehydratase | The enzyme 2-dehydro-3-deoxy-L-arabinonate dehydratase () catalyzes the chemical reaction
2-dehydro-3-deoxy-L-arabinonate 2,5-dioxopentanoate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 2-dehydro-3-deoxy-L-arabinonate hydro-lyase (2,5-dioxopentanoate-forming). Other names in common use include 2-keto-3-deoxy-L-arabinonate dehydratase, and 2-dehydro-3-deoxy-L-arabinonate hydro-lyase. This enzyme participates in ascorbate and aldarate metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hydroxyisoflavanone%20dehydratase | The enzyme 2-hydroxyisoflavanone dehydratase () catalyzes the chemical reaction
2,7,4′-trihydroxyisoflavanone daidzein + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 2,7,4′-trihydroxyisoflavanone hydro-lyase (daidzein-forming). This enzyme is also called 2,7,4′-trihydroxyisoflavanone hydro-lyase. This enzyme participates in isoflavonoid biosynthesis.
The variant GmHID1 from Glycine max converts 2-hydroxyisoflavone to isoflavones, mostly daidzein and genistein.
References
EC 4.2.1
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/2-methylcitrate%20dehydratase | The enzyme 2-methylcitrate dehydratase () catalyzes the chemical reaction
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate (Z)-but-2-ene-1,2,3-tricarboxylate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming]. Other names in common use include 2-methylcitrate hydro-lyase, PrpD, and 2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase. This enzyme participates in propanoate metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-methylisocitrate%20dehydratase | The enzyme 2-methylisocitrate dehydratase () catalyzes the chemical reaction
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate (Z)-but-2-ene-1,2,3-tricarboxylate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming]. This enzyme is also called (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase. This enzyme participates in propanoate metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-oxopent-4-enoate%20hydratase | The enzyme 2-oxopent-4-enoate hydratase () catalyzes the chemical reaction
4-hydroxy-2-oxopentanoate 2-oxopent-4-enoate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 4-hydroxy-2-oxopentanoate hydro-lyase (2-oxopent-4-enoate-forming). Other names in common use include 2-keto-4-pentenoate hydratase, OEH, 2-keto-4-pentenoate (vinylpyruvate)hydratase, and 4-hydroxy-2-oxopentanoate hydro-lyase. This enzyme participates in nine metabolic pathways: phenylalanine metabolism, benzoate degradation via hydroxylation, biphenyl degradation, toluene and xylene degradation, 1,4-dichlorobenzene degradation, fluorene degradation, carbazole degradation, ethylbenzene degradation, and styrene degradation.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3alpha%2C7alpha%2C12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA%20hydratase | The enzyme 3α,7α,12α-trihydroxy-5β-cholest-24-enoyl-CoA hydratase () catalyzes the chemical reaction
(24R,25R)-3α,7α,12α,24-tetrahydroxy-5β-cholestanoyl-CoA
(24E)-3α,7α,12α-trihydroxy-5β-cholest-24-enoyl-CoA + H2O
Nomenclature
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (24R,25R)-3α,7α,12α,24-tetrahydroxy-5beta-cholestanoyl-CoA hydro-lyase [(24E)-3α,7α,12α-trihydroxy-5β-cholest-24-enoyl-CoA-forming]. Other names in common use include 46 kDa hydratase 2, and (24R,25R)-3α,7α,12α,24-tetrahydroxy-5β-cholestanoyl-CoA hydro-lyase.
References
Further reading
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Jim%20Otvos | James D. Otvos is an academician/researcher/entrepreneur in nuclear magnetic resonance spectroscopy who has pioneered and published, since the later 1970s, extensive research on the roles of the various lipoproteins in cardiovascular disease and led the company, LipoScience, which developed the Vantera Analyzer.
From 1950 (when the first research was published identifying lipoproteins as the primary driver of the atherosclerosis process) through the 1990s, the basic science work which led to sub-fractionation of lipoprotein particles: chylomicrons (AKA ULDL), VLDL, IDL, LDL & HDL had long remained too expensive for routine use in clinical medicine. This issue was (and is) complicated by the multiple sub-distinctions within these groupings.
While this work was a giant breakthrough in understanding how fat molecules (needed and manipulated by all cells in the body) are carried within the water-based blood and intracellular transport systems, work which led to a Nobel prize in Medicine in 1985 for identification of the LDL receptor protein via which cells ingest (termed endocytosis) LDL particles, cost (about $5,000 USD per blood sample in the 1970s for the ultracentrifugation and gradient-gel electrophoresis methods which had been developed and utilized in earlier research) remained a major barrier to clinical use of this valuable information.
In the early 1990s, given increasing evidence and understanding of the role which the many different lipoproteins (not cholesterol pe |
https://en.wikipedia.org/wiki/Testicular%20receptor%204 | Testicular receptor 4 also known as NR2C2 (nuclear receptor subfamily 2, group C, member 2) is a protein that in humans is encoded by the NR2C2 gene.
The testicular receptor 4 is a member of the nuclear receptor family of transcription factors.
Interactions
Testicular receptor 4 has been shown to interact with
Androgen receptor,
Estrogen receptor alpha, and
Hepatocyte nuclear factor 4 alpha.
See also
Testicular receptor
References
Further reading
External links
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/China%20Classification%20Society | China Classification Society (CCS; 中國船級社) is a classification society of ships, started in 1956 as a non-profit making body in the People's Republic of China to perform classification survey, certification survey and notarial survey of ships including offshore installations, containers and related industrial products both at home and abroad. CCS also conduct statutory work on behalf of the Chinese Government and other flag administrations.
CCS joined the International Association of Classification Societies (IACS) as a full member in May 1988.
References
External links
CCS China Classification Society
Ship classification societies |
https://en.wikipedia.org/wiki/3-cyanoalanine%20hydratase | The enzyme 3-cyanoalanine hydratase () catalyzes the chemical reaction
L-asparagine 3-cyanoalanine + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-asparagine hydro-lyase (3-cyanoalanine-forming). Other names in common use include β-cyanoalanine hydrolase, β-cyanoalanine hydratase, β-CNAla hydrolase, β-CNA nitrilase, and L-asparagine hydro-lyase. This enzyme participates in cyanoamino acid metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-dehydroquinate%20dehydratase | The enzyme 3-dehydroquinate dehydratase () catalyzes the chemical reaction
3-dehydroquinate 3-dehydroshikimate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
Discovery
The shikimate pathway was determined to be a major biosynthetic route for the production of aromatic amino acids through the research of Bernhard Davis and David Sprinson.
Role in the shikimate pathway
3-Dehydroquinate Dehydratase is an enzyme that catalyzes the third step of the shikimate pathway. The shikimate pathway is a biosynthetic pathway that allows plants, fungi, and bacteria to produce aromatic amino acids. Mammals do not have this pathway, meaning that they must obtain these essential amino acids through their diet. Aromatic Amino acids include Phenylalanine, Tyrosine, and Tryptophan.
This enzyme dehydrates 3-Dehydroquinate, converting it to 3-Dehydroshikimate, as indicated in the adjacent diagram. This is the third step in the Shikimate pathway. It belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 3-dehydroquinate hydro-lyase (3-dehydroshikimate-forming). This enzyme is one of the few examples of convergent evolution. The two separate versions of this enzyme have different amino acid sequences.
3-Dehydroquinate dehydratase is also commonly referred |
https://en.wikipedia.org/wiki/3-dehydroquinate%20synthase | The enzyme 3-dehydroquinate synthase (EC 4.2.3.4) catalyzes the chemical reaction
[[3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate]] 3-dehydroquinate + phosphate
The protein uses NAD+ to catalyze the reaction. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
3-Dehydroquinate synthase belongs to the family of lyases, to be specific those carbon-oxygen lyases acting on phosphates. This enzyme participates in phenylalanine, tyrosine, and tryptophan biosynthesis. It employs one cofactor, cobalt (Co2+).
Background
The shikimate pathway is composed of seven steps, each catalyzed by an enzyme. The shikimate pathway is responsible for producing the precursors for aromatic amino acids, which are essential to our diets because we cannot synthesize them in our bodies. Only plants, bacteria, and microbial eukaryotes are capable of producing aromatic amino acids. The pathway ultimately converts phosphoenolpyruvate and 4-erythrose phosphate into chorismate, the precursor to aromatic amino acids. 3-Dehydroquinate synthase is the enzyme that catalyzes reaction in the second step of this pathway. This second step of the reaction eliminates a phosphate from 3-deoxy-D-arabino-heptulosonate 7-phosphate, which results in 3-dehydroquinate. 3-Dehydroquinate synthase is a monomeric enzyme, and has a molecular weight of 39,000. 3-dehydroquinate synthase is activated by inorganic phosphate, and requires NAD+ for activity, although th |
https://en.wikipedia.org/wiki/3-hydroxybutyryl-CoA%20dehydratase | The enzyme 3-hydroxybutyryl-CoA dehydratase () catalyzes the chemical reaction
(3R)-3-hydroxybutanoyl-CoA crotonoyl-CoA + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (3R)-3-hydroxybutanoyl-CoA hydro-lyase (crotonoyl-CoA-forming). Other names in common use include D-3-hydroxybutyryl coenzyme A dehydratase, D-3-hydroxybutyryl-CoA dehydratase, enoyl coenzyme A hydrase (D), and (3R)-3-hydroxybutanoyl-CoA hydro-lyase. This enzyme participates in butanoate metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hepatocyte%20nuclear%20factor%204%20gamma |
Hepatocyte nuclear factor 4 gamma (HNF4G) also known as NR2A2 (nuclear receptor subfamily 2, group A, member 2) is a nuclear receptor that in humans is encoded by the HNF4G gene.
See also
Hepatocyte nuclear factor 4
Hepatocyte nuclear factors
References
Further reading
External links
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/3-hydroxyoctanoyl-%28acyl-carrier-protein%29%20dehydratase | The enzyme 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase () catalyzes the chemical reaction
(3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] oct-2-enoyl-[acyl-carrier-protein] + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase (oct-2-enoyl-[acyl-carrier protein]-forming). Other names in common use include D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase, D-3-hydroxyoctanoyl-acyl carrier protein dehydratase, beta-hydroxyoctanoyl-acyl carrier protein dehydrase, beta-hydroxyoctanoyl thioester dehydratase, beta-hydroxyoctanoyl-ACP-dehydrase, and (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase.
See also
3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxypalmitoyl-%28acyl-carrier-protein%29%20dehydratase | In enzymology, a 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase () is an enzyme that catalyzes the chemical reaction
(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] hexadec-2-enoyl-[acyl-carrier-protein] + H2O
Hence, this enzyme has one substrate, [[(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein]]], and two products, [[hexadec-2-enoyl-[acyl-carrier-protein]]] and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] hydro-lyase (hexadec-2-enoyl-[acyl-carrier protein]-forming). Other names in common use include D-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase, beta-hydroxypalmitoyl-acyl carrier protein dehydrase, beta-hydroxypalmitoyl thioester dehydratase, beta-hydroxypalmityl-ACP dehydrase, and (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] hydro-lyase. This enzyme participates in fatty acid biosynthesis.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin%20dehydratase | The enzyme 4a-hydroxytetrahydrobiopterin dehydratase () catalyzes the chemical reaction
4a-hydroxytetrahydrobiopterin 6,7-dihydrobiopterin + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 4a-hydroxytetrahydrobiopterin hydro-lyase (6,7-dihydrobiopterin-forming). Other names in common use include 4a-hydroxy-tetrahydropterin dehydratase, pterin-4α-carbinolamine dehydratase, and 4a-hydroxytetrahydrobiopterin hydro-lyase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/4-oxalmesaconate%20hydratase | The enzyme 4-oxalmesaconate hydratase () catalyzes the chemical reaction
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate 1,2-hydro-lyase (2-hydroxy-4-oxobutane-1,2,4-tricarboxylate-forming). Other names in common use include 4-carboxy-2-oxohexenedioate hydratase, 4-carboxy-2-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase, oxalmesaconate hydratase, γ-oxalmesaconate hydratase, 4-carboxy-2-oxohexenedioate hydratase, and 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase. This enzyme participates in benzoate degradation via hydroxylation.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%284S%29-limonene%20synthase | The enzyme (4S)-limonene synthase (EC 4.2.3.16) catalyzes the chemical reaction
geranyl diphosphate (−)-(4S)-limonene + diphosphate
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is geranyl-diphosphate diphosphate-lyase [cyclizing, (−)-(4S)-limonene-forming]. Other names in common use include (−)-(4S)-limonene synthase, 4S-(−)-limonene synthase, geranyldiphosphate diphosphate lyase (limonene forming), geranyldiphosphate diphosphate lyase [cyclizing,, and (4S)-limonene-forming]. This enzyme participates in monoterpenoid biosynthesis.
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5alpha-hydroxysteroid%20dehydratase | The enzyme 5α-hydroxysteroid dehydratase () catalyzes the chemical reaction
5α-ergosta-7,22-diene-3β,5-diol ergosterol + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 5α-ergosta-7,22-diene-3β,5-diol 5,6-hydro-lyase (ergosterol-forming). This enzyme is also called 5α-ergosta-7,22-diene-3β,5-diol 5,6-hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-dehydro-4-deoxyglucarate%20dehydratase | The enzyme 5-dehydro-4-deoxyglucarate dehydratase () catalyzes the chemical reaction
5-dehydro-4-deoxy-D-glucarate 2,5-dioxopentanoate + H2O + CO2
Enzyme class
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 5-dehydro-4-deoxy-D-glucarate hydro-lyase (decarboxylating 2,5-dioxopentanoate-forming). Other names in common use include 5-keto-4-deoxy-glucarate dehydratase, deoxyketoglucarate dehydratase, D-4-deoxy-5-ketoglucarate hydro-lyase, and 5-dehydro-4-deoxy-D-glucarate hydro-lyase (decarboxylating). This enzyme participates in ascorbate and aldarate metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thyroid%20hormone%20receptor%20alpha | Thyroid hormone receptor alpha (TR-alpha) also known as nuclear receptor subfamily 1, group A, member 1 (NR1A1), is a nuclear receptor protein that in humans is encoded by the THRA gene.
Function
The protein encoded by this gene is a nuclear hormone receptor for triiodothyronine. It is one of the several receptors for thyroid hormone, and has been shown to mediate the biological activities of thyroid hormone. Knockout studies in mice suggest that the different receptors, while having certain extent of redundancy, may mediate different functions of thyroid hormone. Alternatively spliced transcript variants encoding distinct isoforms have been reported.
Role in pathology
Mutations of the THRA gene may cause nongoitrous congenital hypothyroidism-6, a subtype of congenital hypothyroidism.
Interactions
THR1 has been shown to interact with:
COPS2,
EP300,
ITGB3BP,
MED1,
MED6,
MED12,
MED16,
MEF2A,
NCOA6,
TRIP11, and
UBC.
References
Further reading
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/Thyroid%20hormone%20receptor%20beta | Thyroid hormone receptor beta (TR-beta) also known as nuclear receptor subfamily 1, group A, member 2 (NR1A2), is a nuclear receptor protein that in humans is encoded by the THRB gene.
Function
The protein encoded by this gene is a nuclear hormone receptor for triiodothyronine. It is one of the several receptors for thyroid hormone, and has been shown to mediate the biological activities of thyroid hormone. Knockout studies in mice suggest that the different receptors, while having certain extent of redundancy, may mediate different functions of thyroid hormone. Defects in this gene are known to be a cause of generalized thyroid hormone resistance (GTHR), a syndrome characterized by goiter and high levels of circulating thyroid hormone (T3-T4), with normal or slightly elevated thyroid stimulating hormone (TSH). Several transcript variants have been observed for this gene, but the full-length nature of only one has been observed so far.
Interactions
Thyroid hormone receptor beta has been shown to interact with:
BRD8,
CCND1,
NCOA1,
NCOA6,
NCOR2,
NR2F6,
PPARGC1A, and
RXRA.
References
Further reading
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/6-Pyruvoyltetrahydropterin%20synthase | The enzyme 6-pyruvoyltetrahydropterin synthase (EC 4.2.3.12, PTPS) catalyzes the following chemical reaction:
7,8-Dihydroneopterin 3′-triphosphate 6-pyruvoyltetrahydropterin + triphosphate
This reaction is the second step (shown above) in the biosynthesis of tetrahydrobiopterin from GTP, which is used as a cofactor in the synthesis of aromatic amino acid monooxygenases and nitric oxide synthase PTPS converts 7,8-dihydroneopterin triphosphate to 6-pyruvoyltetrahydropterin (PTP) through the loss of the triphosphate group, a stereospecific reduction of the double bond between the top right nitrogen and carbon in the ring on the triphosphate on the right, the oxidation of the hydroxyl groups located on the first and second carbons of the side chain, and an internal base-catalyzed hydrogen transfer. ] 6-pyruvoyltetrahydropterin synthase (PTPS) can be found in the cytoplasm as well as the nucleus of cells according to immunohistochemical studies conducted. It has also been found that in higher species 6-pyruvoyltetrahydropterin synthase (PTPS) can undergo post-translational modification.
This enzyme participates in tetrahydrobiopterin biosynthesis.
Nomenclature
This enzyme belongs to the family of lyases, to be specific, those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is 6-[(1S,2R)-1,2-dihydroxy-3′-triphosphooxypropyl]-7,8-dihydropterin triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming). Other names in common use inclu |
https://en.wikipedia.org/wiki/Abietadiene%20synthase | The enzyme abieta-7,13-diene synthase (EC 4.2.3.18) catalyzes the chemical reaction
(+)-copalyl diphosphate abieta-7,13-diene + diphosphate
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is (+)-copalyl-diphosphate diphosphate-lyase [cyclizing, abieta-7,13-diene-forming]. This enzyme is also called copalyl-diphosphate diphosphate-lyase (cyclizing). This enzyme participates in diterpenoid biosynthesis.
It has recently been shown (Keeling, et al., 2011) that the orthologous gene in Norway spruce (Picea abies) does not produce abietadiene directly, but instead produces a thermally unstable allylic tertiary alcohol 13-hydroxy-8(14)- abietene, which readily dehydrates to abietadiene, levopimaradiene, palustradiene, and neoabietadiene, when analyzed by the commonly used gas chromatography. This has been confirmed in the other conifer species, lodgepole pine (Pinus contorta) and Jack pine (Pinus banksiana) (Hall et al., 2013).
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetylenecarboxylate%20hydratase | The enzyme acetylenecarboxylate hydratase () catalyzes the chemical reaction
3-oxopropanoate propynoate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 3-oxopropanoate hydro-lyase (propynoate-forming). Other names in common use include acetylenemonocarboxylate hydratase, alkynoate hydratase, acetylenemonocarboxylate hydrase, acetylenemonocarboxylic acid hydrase, malonate-semialdehyde dehydratase, and 3-oxopropanoate hydro-lyase. This enzyme participates in 3 metabolic pathways: beta-alanine metabolism, propanoate metabolism, and butanoate metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetylene%20hydratase | Acetylene hydratase (, AH) is a bacterial enzyme, originally discovered in the anaerobic microorganism Pelobactor acetylenicus, that catalyzes the non-redox hydration of acetylene to form acetaldehyde.
C2H2 + H2O → CH3CHO
The mechanism is thought to involve attachment of acetylene to the metal followed by nucleophilic attack of water. Because acetylene binding to the Mo in nitrogenase lends some support that the mechanism involves a Mo→CH2=CH2 bond. Acetylene inhibits several microbial transformations where it interacts with the active site of the metal-dependent enzymes including hydrogenase and nitrogenase. This enzyme relies on tungsten as the metal center and is the heaviest metal that plays a prominent part in the nitrogen, sulfur and carbon metabolic processes. The [4Fe-4S] cubane keeps the W in the reduced W(IV) state, the most stable reduced oxidation state, while W(VI) is the other stable oxidation state (2nd and 3rd row transition metals are usually most stable in their highest oxidation state). Mo and W enzymes ubiquitously involve W(IV)/W(VI) in the catalysis, however AH is very unique since the tungstoenzyme stays as W(IV) in the catalysis. The tungstoenzyme stays as W(IV) throughout the catalysis because the enzyme catalyzes a non-redox reaction described as the hydration of acetylene to acetaldehyde. The active site tungsten has a distorted octahedral geometry that is coordinated by molybdopterin co-factors along with a cysteine residue coordinated by a water |
https://en.wikipedia.org/wiki/Retinoic%20acid%20receptor%20beta | Retinoic acid receptor beta (RAR-beta), also known as NR1B2 (nuclear receptor subfamily 1, group B, member 2) is a nuclear receptor that in humans is encoded by the RARB gene.
Function
This gene encodes retinoic acid receptor beta, a member of the thyroid-steroid hormone receptor superfamily of nuclear transcriptional regulators. This receptor localizes to the cytoplasm and to subnuclear compartments. It binds retinoic acid, the biologically active form of vitamin A which mediates cellular signalling in embryonic morphogenesis, cell growth and differentiation. It is thought that this protein limits growth of many cell types by regulating gene expression. The gene was first identified in a hepatocellular carcinoma where it flanks a hepatitis B virus integration site. A deregulation of this gene has also been detected in uterine cervical carcinoma preneoplastic lesions. The gene expresses at least two transcript variants; one additional transcript has been described, but its full length nature has not been determined.
Epigenetics
The Retinoic acid receptor beta aberrant promoter DNA hypermethylation has been observed associated with cancer onset/progression. Indeed, this improper epigenetic phenomenon has been observed in women affected by Vulvar Squamous cell carcinoma arose from vulver lichen sclerosus. Methylation of the Retinoic acid receptor beta promoter may be a marker of cancer risk in patients affected by this disease.
Interactions
Retinoic acid receptor beta |
https://en.wikipedia.org/wiki/Altronate%20dehydratase | The enzyme altronate dehydratase () catalyzes the chemical reaction
D-altronate 2-dehydro-3-deoxy-D-gluconate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-altronate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming). This enzyme is also called D-altronate hydro-lyase. This enzyme participates in pentose and glucuronate interconversions.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Retinoic%20acid%20receptor%20gamma | Retinoic acid receptor gamma (RAR-γ), also known as NR1B3 (nuclear receptor subfamily 1, group B, member 3) is a nuclear receptor encoded by the RARG gene. Adapalene selectively targets retinoic acid receptor beta and retinoic acid receptor gamma and its agonism of the gamma subtype is largely responsible for adapalene's observed effects.
Interactions
Retinoic acid receptor gamma has been shown to interact with NCOR1.
See also
Retinoic acid receptor
References
Further reading
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/Amorpha-4%2C11-diene%20synthase | The enzyme amorpha-4,11-diene synthase (EC 4.2.3.24) (ADS) catalyzes the chemical reaction
(2E,6E)-farnesyl diphosphate ⇌ amorpha-4,11-diene + diphosphate
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is (2E,6E)-farnesyl-diphosphate diphosphate-lyase (amorpha-4,11-diene-forming). This enzyme is also called amorphadiene synthase.
This enzyme is mainly found in Artemisia annua, a temperate Asian native flowering plant, and ADS catalyzes the first committed step in the antimalarial drug artemisinin synthesis.
Enzyme Properties
Physical Properties
Amorpha-4,11-diene synthase is a 533 amino acid long protein with a molecular weight of 62.2 kDa and isoelectric point of 5.25.
ADS shows a pH optimum at pH 6.5 and a minimum at pH 7.5.
With Mg2+, Mn2+ and Co2+ as cofactors, large enzyme activity observed, with Ni2+, low activity observed, and with Cu2+ and Zn2+, essentially no activity observed.
Evolution
ADS is a highly conserved protein similar to other proteins with analogous functionality. The deduced amino acid sequence is 32 to 51% identical with the sequence of other known sesquiterpene cyclases from angiosperms (flowering plants) meaning the enzymes have a common ancestry. More specifically, it has a highly conserved substrate binding site with an aspartate rich DDxxD motif.
Expression
ADS is expressed 16-fold higher in the leaves than in roots of the Artemisia annu |
https://en.wikipedia.org/wiki/Liver%20X%20receptor%20beta | Liver X receptor beta (LXR-β) is a member of the nuclear receptor family of transcription factors. LXR-β is encoded by the gene (nuclear receptor subfamily 1, group H, member 2).
Function
The liver X receptors (LXRs) were originally identified as orphan members of the nuclear receptor superfamily because their ligands were unknown. Like other receptors in the family, LXRs heterodimerize with retinoid X receptor and bind to specific response elements (LXREs) characterized by direct repeats separated by 4 nucleotides. Two genes, alpha (LXRA) and beta, are known to encode LXR proteins.
Structure
Crystal structure of human liver X receptor β(LXRβ) forming heterodimer with its partner retinoid X receptor α(RXRα) on its cognate element, an AGGTCA direct repeat spaced by 4 nt shows an extended X-shaped arrangement, with DNA- and ligand-binding domains crossed. The LXRβ core binds DNA via canonical contacts and auxiliary DNA contacts that enhance affinity for the response element.
Interactions
Liver X receptor beta has been shown to interact with NCOA6 and Retinoid X receptor alpha.
References
Further reading
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/RAR-related%20orphan%20receptor%20gamma | RAR-related orphan receptor gamma (RORγ) is a protein that in humans is encoded by the (RAR-related orphan receptor C) gene. RORγ is a member of the nuclear receptor family of transcription factors. It is mainly expressed in immune cells (Th17 cells) and it also regulates circadian rhythms. It may be involved in the progression of certain types of cancer.
Gene expression
Two isoforms are produced from the same RORC gene, probably by selection of alternative promoters.
RORγ (also referred to as RORγ1) – produced from an mRNA containing exons 1 to 11.
RORγt (also known as RORγ2) – produced from an mRNA identical to that of RORγ, except that the two 5'-most exons are replaced by an alternative exon, located downstream in the gene. This causes a different, shorter N-terminus.
RORγ
The mRNA of the first isoform, RORγ is expressed in many tissues, including thymus, lung, liver, kidney, muscle, and brown fat. While RORγ mRNA is abundantly expressed, attempts to detect RORγ protein have not been successful; therefore it is not clear whether RORγ protein is actually expressed. Consistent with this, the main phenotypes identified in RORγ-/- knockout mice (where neither isoform is expressed) are those associated with RORγt immune system function and an isoform specific RORγt knockout displayed a phenotype identical to the RORγ-/- knockout. On the other hand, circadian phenotypes of RORγ-/- mice in tissues where the RORγt isoform is expressed in minute amounts argues for the exp |
https://en.wikipedia.org/wiki/QUAD%20%28compressor%29 | QUAD is a high-performance data compressor based on the LZ algorithms (LZ77, LZ78, LZW). It's designed to produce small files but still decompress fast and with little memory. QUAD is licensed under the LGPL.
External links
http://quad.sourceforge.net/
Archive formats
Free data compression software
Lossless compression algorithms |
https://en.wikipedia.org/wiki/GRIN2B | Glutamate [NMDA] receptor subunit epsilon-2, also known as N-methyl D-aspartate receptor subtype 2B (NMDAR2B or NR2B), is a protein that in humans is encoded by the GRIN2B gene.
NMDA receptors
N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. The NMDA receptor channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heterotetramers composed of two molecules of the key receptor subunit NMDAR1 (GRIN1) and two drawn from one or more of the four NMDAR2 subunits: NMDAR2A (GRIN2A), NMDAR2B (GRIN2B), NMDAR2C (GRIN2C), and NMDAR2D (GRIN2D). The NR2 subunit acts as the agonist binding site for glutamate, one of the predominant excitatory neurotransmitter receptors in the mammalian brain.
Function
NR2B has been associated with age- and visual-experience-dependent plasticity in the neocortex of rats, where an increased NR2B/NR2A ratio correlates directly with the stronger excitatory LTP in young animals. This is thought to contribute to experience-dependent refinement of developing cortical circuits.
Engineered to overexpress GRIN2B in their brains, mice and rats exhibit improved mental function. The "Doogie" mouse performed twice as well on one learning test.
Ligands
Besonprodil
CERC-301, a selective NR2B receptor antagonist
Eliprodil
Ethanol - apparent induction of dephosphor |
https://en.wikipedia.org/wiki/PTGS1 | Cyclooxygenase 1 (COX-1), also known as prostaglandin G/H synthase 1, prostaglandin-endoperoxide synthase 1 or prostaglandin H2 synthase 1, is an enzyme that in humans is encoded by the PTGS1 gene. In humans it is one of two cyclooxygenases.
History
Cyclooxygenase (COX) is the central enzyme in the biosynthetic pathway to prostaglandins from arachidonic acid. This protein was isolated more than 40 years ago and cloned in 1988.
Gene and isozymes
There are two isozymes of COX encoded by distinct gene products: a constitutive COX-1 (this enzyme) and an inducible COX-2, which differ in their regulation of expression and tissue distribution. The expression of these two transcripts is differentially regulated by relevant cytokines and growth factors. This gene encodes COX-1, which regulates angiogenesis in endothelial cells. COX-1 is also involved in cell signaling and maintaining tissue homeostasis. A splice variant of COX-1 termed COX-3 was identified in the central nervous system of dogs, but does not result in a functional protein in humans. Two smaller COX-1-derived proteins (the partial COX-1 proteins PCOX-1A and PCOX-1B) have also been discovered, but their precise roles are yet to be described.
Function
Prostaglandin-endoperoxide synthase (PTGS), also known as cyclooxygenase (COX), is the key enzyme in prostaglandin biosynthesis. It converts free arachidonic acid, released from membrane phospholipids at the sn-2 ester binding site by the enzymatic activity of phosphol |
https://en.wikipedia.org/wiki/PHS1 | PHS1 may refer to:
PTGS1, an enzyme
Very-long-chain (3R)-3-hydroxyacyl-(acyl-carrier protein) dehydratase, an enzyme
Beta-phellandrene synthase (neryl-diphosphate-cyclizing), an enzyme |
https://en.wikipedia.org/wiki/Cornell%20University%20Satellite | The Cornell University Satellite (CUSat) is a nanosatellite developed by Cornell University that launched on 29 September 2013. It used a new algorithm called Carrier-phase Differential GPS (CDGPS) to calibrate global positioning systems to an accuracy of 3 millimeters. This technology can allow multiple spacecraft to travel in close proximity.
The CUSat project began in 2005 and was the winner of the University Nanosat-4 Program which aims to educate the future aerospace workforce and develop new space technologies. As part of this program, CUSat completed environmental testing and other aspects of final I&T in the AFRL Aerospace Engineering Facility at Kirtland Air Force Base. CUSat worked with AFRL to complete the Department of Defense SERB process in preparation for a launch with the Space Test Program. The satellite launched as a secondary payload to CASSIOPE on a SpaceX Falcon 9 rocket on 29 September 2013.
Operation details
The space segment was originally designed to consist of two functionally identical satellites that would launch together and separate on orbit in a target-inspector configuration. Once in orbit, CUSat would use microthrust Pulsed Plasma Thrusters (PPTs) and sub-centimeter level accurate carrier-phase differential GPS (CDGPS) to navigate the satellites to within ten meters of each other. The inspector satellite would use cameras to gather imagery of the target satellite while performing relative navigation. Target satellite imagery would be trans |
https://en.wikipedia.org/wiki/Fibrinogen%20beta%20chain | Fibrinogen beta chain, also known as FGB, is a gene found in humans and most other vertebrates with a similar system of blood coagulation.
The protein encoded by this gene is the beta component of fibrinogen, a blood-borne glycoprotein composed of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including afibrinogenemia, dysfibrinogenemia, hypodysfibrinogenemia and thrombotic tendency.
Interactions
Fibrinogen beta chain has been shown to interact with Lipoprotein(a).
See also
Fibrin
Fibrinogen alpha chain
Fibrinogen gamma chain
References
Further reading |
https://en.wikipedia.org/wiki/BCAR1 | Breast cancer anti-estrogen resistance protein 1 is a protein that in humans is encoded by the BCAR1 gene.
Gene
BCAR1 is localized on chromosome 16 on region q, on the negative strand and it consists of seven exons. Eight different gene isoforms have been identified that share the same sequence starting from the second exon onwards but are characterized by different starting sites. The longest isoform is called BCAR1-iso1 (RefSeq NM_001170714.1) and is 916 amino acids long, the other shorter isoforms start with an alternative first exon.
Function
BCAR1 is a ubiquitously expressed adaptor molecule originally identified as the major substrate of v-Src and v-Crk . p130Cas/BCAR1 belongs to the Cas family of adaptor proteins and can act as a docking protein for several signalling partners. Due to its ability to associate with multiple signaling partners, p130Cas/BCAR1 contributes to the regulation to a variety of signaling pathways leading to cell adhesion, migration, invasion, apoptosis, hypoxia and mechanical forces. p130Cas/BCAR1 plays a role in cell transformation and cancer progression and alterations of p130Cas/BCAR1 expression and the resulting activation of selective signalling are determinants for the occurrence of different types of human tumors.
Due to the capacity of p130Cas/BCAR1, as an adaptor protein, to interact with multiple partners and to be regulated by phosphorylation and dephosphorylation, its expression and phosphorylation can lead to a wide range o |
https://en.wikipedia.org/wiki/Actin%2C%20cytoplasmic%202 | Actin, cytoplasmic 2, or gamma-actin is a protein that in humans is encoded by the ACTG1 gene. Gamma-actin is widely expressed in cellular cytoskeletons of many tissues; in adult striated muscle cells, gamma-actin is localized to Z-discs and costamere structures, which are responsible for force transduction and transmission in muscle cells. Mutations in ACTG1 have been associated with nonsyndromic hearing loss and Baraitser-Winter syndrome, as well as susceptibility of adolescent patients to vincristine toxicity.
Structure
Human gamma-actin is 41.8 kDa in molecular weight and 375 amino acids in length. Actins are highly conserved proteins that are involved in various types of cell motility, and maintenance of the cytoskeleton. In vertebrates, three main groups of actin paralogs, alpha, beta, and gamma, have been identified.
The alpha actins are found in muscle tissues and are a major constituent of the sarcomere contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. Actin, gamma 1, encoded by this gene, is found in non-muscle cells in the cytoplasm, and in muscle cells at costamere structures, or transverse points of cell-cell adhesion that run perpendicular to the long axis of myocytes.
Function
In myocytes, sarcomeres adhere to the sarcolemma via costameres, which align at Z-discs and M-lines. The two primary cytoskeletal components of costameres are desmin intermedia |
https://en.wikipedia.org/wiki/Heparanase | Heparanase, also known as HPSE, is an enzyme that acts both at the cell-surface and within the extracellular matrix to degrade polymeric heparan sulfate molecules into shorter chain length oligosaccharides.
Synthesis and structure
The protein is originally synthesised in an inactive 65 kDa proheparanase form in the golgi apparatus and transferred to late endosomes/lysosomes for transport to the cell-surface. In the lysosome it is proteolytically processed into its active form. Proteolytic processing results in the production of three products,
a linker peptide
an 8 kDa proheparanase fragment and
a 50 kDa proheparanase fragment
The 8 kDa and 50 kDa fragments form a heterodimer and it is this heterodimer that constitutes the active heparanase molecule. The linker protein is so called because prior to its excision it physically links the 8 kDa and 50 kDa proheparanase fragments. Complete excision of the linker peptide appears to be a prerequisite to the complete activation of the heparanase enzyme.
Crystal structures of both proheparanase and mature heparanase are available, showing that the linker peptide forms a large helical domain which blocks heparan sulfate molecules from interacting with heparanase. Removal of the linker reveals an extended cleft on the enzyme surface, which contains the heparanase active site.
Function
Heparanase has endoglycosidase activity and cleaves polymeric heparan sulfate molecules at sites which are internal within the polymeric chain |
https://en.wikipedia.org/wiki/RAC3 | Ras-related C3 botulinum toxin substrate 3 (Rac3) is a G protein that in humans is encoded by the RAC3 gene. It is an important component of intracellular signalling pathways. Rac3 is a member of the Rac subfamily of the Rho family of small G proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases.
Interactions
RAC3 has been shown to interact with CIB1 and HNF1A. RAC3 also interacts with Nrf2 proteins. ETAR, ILK, and β-arr1 interact with RAC3 as well.
Location
RAC3 gene is located in the third sub-band of the fifth band in the second region of the q arm on chromosome 17. There's many tumor suppressor genes that are located around the RAC3 gene.
Therapeutic Use
Since the RAC3 gene is over-expressed in carcinoma cells, it can function as a therapeutic target for the treatment of different cancer such as lung adenocarcinoma. To become invasive, epithelial cells have to transform into mesenchymal cells and the transformation is regulated by the RAC3 gene. As a result, if the RAC3 gene is silenced, lung adenocarcinoma cells cannot metastasize. In addition, drugs designed to silence the RAC3 gene lead to the apoptosis of tumor cells, thus preventing the cells from colonizing.
Pathological mutations
Mutations of the RAC3 gene may result in neurodevelopmental disorder with structural brain anomalies and dysmorphic facies, first describe |
https://en.wikipedia.org/wiki/Orthotospovirus | Orthotospovirus is a genus of negative-strand RNA viruses, in the family Tospoviridae of the order Bunyavirales, which infects plants. Tospoviruses take their name from the species Tomato spotted wilt orthotospovirus (TSWV) which was discovered in Australia in 1919. TSWV remained the only known member of the family until the early 1990s when genetic characterisation of plant viruses became more common. There are now at least twenty species in the genus with more being discovered on a regular basis. Member viruses infect over eight hundred plant species from 82 different families.
Genome
Tospoviruses have a negative-sense, single-strand RNA genome. The genome resembles that of the genus Phlebovirus. It is linear and is 17.2 kb in size. It is divided into three segments termed S (2.9kb), M (5.4kb), and L (8.9kb). The M and S RNA segments encode for proteins in an ambisense direction.
Transmission
Tospoviruses are arboviruses usually vectored by thrips. At least ten species of thrips belonging to family Thripidae have been confirmed as vectors for the transmission of thirteen or more tospoviruses. The thrips vectors are not closely related, implying an independent origin of infection for each thrips, possibly transmitted horizontally through shared hosts. There may be other species of thrips competent to transmit similar viruses, but they have not been documented on crops of economic significance.
Recent research concludes that thrips can only be infected by tospovirus du |
https://en.wikipedia.org/wiki/HPSE | HPSE may refer to:
Heparanase, an enzyme
Blood group B branched chain alpha-1,3-galactosidase, an enzyme |
https://en.wikipedia.org/wiki/Ocean%20pout | The ocean pout (Zoarces americanus) is an eelpout in the family Zoarcidae. It is found in the Northwest Atlantic Ocean, off the coast of New England and eastern Canada. The fish has antifreeze proteins in its blood, giving it the ability to survive in near-freezing waters.
Taxonomy
The ocean pout was first formally described in 1801 by the German naturalists Marcus Elieser Bloch and Johann Gottlob Theaenus Schneider with its type locality given as "American seas". It is one of six species in the genus Zoarces, the only genus in the subfamily Zoarcinae which is one of four subfamilies in the eelpout family Zoarcidae.
Description
The ocean pout has an elongated, tapering body with a wide mouth with fleshy lips, the upper lip protruding further than the lower. This species varies in color from yellow through to reddish brown and to grayish-green and is marked with a series of cross like markings running the length of the eel-like body. There is a dark brown line on each side of the head running from the upper rear margin of the eye to the edge of the operculum. The long, continuous dorsal fin does not connect with the caudal fin, however, the anal fin does. The teeth are robust, blunt and conical in shape. The ocean pout is the largest species of eelpout and has reached a maximum published total length of .
Distribution and habitat
The ocean pout is found in the western Atlantic Ocean where it occurs from Labrador in Canada south to Delaware. They are bottom living species ty |
https://en.wikipedia.org/wiki/Baiu%20Mountains | The Baiu Mountains (, ) are mountains in central Romania, a few kilometers south of Brașov.
Within traditional Romanian classification the Baiu Mountains belong to the Curvature Carpathians. According to the geological divisions of the Carpathians, they belong to the Outer Eastern Carpathians.
The Baiu Mountains run from the Azuga Valley in the North and to the Posada Gorges in the South, and from the Doftana Valley in the East to the Prahova Valley in the West. The mountains have an average elevation of and a maximum height of at Neamțu Peak, covering an area of about .
The Baiu Mountains lie immediately south of the Gârbova Mountains, a long north-south ridge.
See also
List of mountain peaks in Romania
Baiu Mare River
References
External links
Information on Baiu Mountains at tourist-informator.info
Mountain ranges of Romania
Mountain ranges of the Eastern Carpathians |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.