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and the ideal choice depends on their area of application. A dataset together with implementations of a number of popular models (HMM, CRF) for activity recognition can be found here. Conventional temporal probabilistic models such as the hidden Markov model (HMM) and conditional random fields (CRF) model directly mode... | {
"page_id": 15795950,
"source": null,
"title": "Activity recognition"
} |
and descriptive features are learned efficiently through data mining (Apriori rule). === GPS-based activity recognition === Location-based activity recognition can also rely on GPS data to recognize activities. == Sensor usage == === Vision-based activity recognition === It is a very important and challenging problem t... | {
"page_id": 15795950,
"source": null,
"title": "Activity recognition"
} |
that deep learning based action recognition may suffer from adversarial attacks, where an attacker alter the input insignificantly to fool an action recognition system. Despite remarkable progress of vision-based activity recognition, its usage for most actual visual surveillance applications remains a distant aspirati... | {
"page_id": 15795950,
"source": null,
"title": "Activity recognition"
} |
to identify specific people is by how they walk. Gait-recognition software can be used to record a person's gait or gait feature profile in a database for the purpose of recognizing that person later, even if they are wearing a disguise. === Wi-Fi-based activity recognition === When activity recognition is performed in... | {
"page_id": 15795950,
"source": null,
"title": "Activity recognition"
} |
P_{t}} is the power fed into the transmitting antenna input terminals; P r {\displaystyle P_{r}} is the power available at receiving antenna output terminals; d {\displaystyle d} is the distance between antennas; G t {\displaystyle G_{t}} is transmitting antenna gain; G r {\displaystyle G_{r}} is receiving antenna gain... | {
"page_id": 15795950,
"source": null,
"title": "Activity recognition"
} |
a series of elliptical intervals whose foci are the positions of the sender and receiver. When a person is moving across different Fresnel zones, the signal path formed by the reflection of the human body changes, and if people move vertically through Fresnel zones, the change of signal will be periodic. In a pair of p... | {
"page_id": 15795950,
"source": null,
"title": "Activity recognition"
} |
dataset than the previous ones. It contains 400 human action classes, with at least 400 video clips for each action. Each clip lasts around 10s and is taken from a different YouTube video. This dataset was created by DeepMind. == Applications == By automatically monitoring human activities, home-based rehabilitation ca... | {
"page_id": 15795950,
"source": null,
"title": "Activity recognition"
} |
Americium oxide may refer to: Americium dioxide Americium(III) oxide == See also == Americium(III) hydroxide | {
"page_id": 23463663,
"source": null,
"title": "Americium oxide"
} |
Fauna (pl.: faunae or faunas) is all of the animal life present in a particular region or time. The corresponding terms for plants and fungi are flora and funga, respectively. Flora, fauna, funga and other forms of life are collectively referred to as biota. Zoologists and paleontologists use fauna to refer to a typica... | {
"page_id": 722672,
"source": null,
"title": "Fauna"
} |
a body of water, rather than on its surface. Bacteria and microalgae may also live in the interstices of bottom sediments. In general, infaunal animals become progressively smaller and less abundant with increasing water depth and distance from shore, whereas bacteria show more constancy in abundance, tending toward on... | {
"page_id": 722672,
"source": null,
"title": "Fauna"
} |
through a 1 mm mesh also depends upon whether it is alive or dead at the time of sorting. === Mesofauna === Mesofauna are macroscopic soil animals such as arthropods or nematodes. Mesofauna are extremely diverse; considering just the springtails (Collembola), as of 1998, approximately 6,500 species had been identified.... | {
"page_id": 722672,
"source": null,
"title": "Fauna"
} |
appendages. === Xenofauna === Xenofauna, theoretically, are alien organisms that can be described as animal analogues. While no alien life forms, animal-like or otherwise, are known definitively, the concept of alien life remains a subject of great interest in fields like astronomy, astrobiology, biochemistry, evolutio... | {
"page_id": 722672,
"source": null,
"title": "Fauna"
} |
This list contains a list of EC numbers for the sixth group, EC 6, ligases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintai... | {
"page_id": 5506803,
"source": null,
"title": "List of EC numbers (EC 6)"
} |
cholate—CoA ligase EC 6.2.1.8: oxalate—CoA ligase EC 6.2.1.9: malate—CoA ligase EC 6.2.1.10: carboxylic acid—CoA ligase (GDP-forming) EC 6.2.1.11: biotin—CoA ligase EC 6.2.1.12: 4-coumarate—CoA ligase EC 6.2.1.13: acetate—CoA ligase (ADP-forming) EC 6.2.1.14: 6-carboxyhexanoate—CoA ligase EC 6.2.1.15: arachidonate—CoA ... | {
"page_id": 5506803,
"source": null,
"title": "List of EC numbers (EC 6)"
} |
ligase * EC 6.2.1.66: glyine—[glycyl-carrier protein] ligase * EC 6.2.1.67: L-alanine—[L-alanyl-carrier protein] ligase * EC 6.2.1.68: L-glutamate—[L-glutamyl-carrier protein] ligase * EC 6.2.1.69: L-cysteine—[L-cysteinyl-carrier protein] ligase * EC 6.2.1.70: L-threonine—[L-threonyl-carrier protein] ligase * EC 6.2.1.... | {
"page_id": 5506803,
"source": null,
"title": "List of EC numbers (EC 6)"
} |
EC 6.3.2.15: Deleted, The activity observed is due to EC 6.3.2.10, UDP-N-acetylmuramoyl-tripeptideD-alanyl-D-alanine ligase EC 6.3.2.16: D-alanine—alanyl-poly(glycerolphosphate) ligase EC 6.3.2.17: tetrahydrofolate synthase EC 6.3.2.18: γ-glutamylhistamine synthase EC 6.3.2.19: The ubiquitinylation process is now known... | {
"page_id": 5506803,
"source": null,
"title": "List of EC numbers (EC 6)"
} |
EC 6.3.2.58: D-ornithine—citrate ligase * EC 6.3.2.59: 3-methyl-D-ornithine—L-lysine ligase * EC 6.3.2.60: glutamate—[amino group carrier protein] ligase * EC 6.3.2.61: tubulin-glutamate ligase * EC 6.3.2.62: β-tubulin-glutamate ligase * * No Wikipedia article === EC 6.3.3: Cyclo-Ligases === EC 6.3.3.1: phosphoribosylf... | {
"page_id": 5506803,
"source": null,
"title": "List of EC numbers (EC 6)"
} |
(glutamine-hydrolysing) * * No Wikipedia article == EC 6.4: Forming Carbon-Carbon Bonds == === EC 6.4.1: Ligases that form carbon-carbon bonds (only sub-subclass identified to date) === EC 6.4.1.1: pyruvate carboxylase EC 6.4.1.2: acetyl-CoA carboxylase EC 6.4.1.3: propionyl-CoA carboxylase EC 6.4.1.4: methylcrotonoyl-... | {
"page_id": 5506803,
"source": null,
"title": "List of EC numbers (EC 6)"
} |
Surface photovoltage (SPV) measurements are a widely used method to determine the minority carrier diffusion length of semiconductors. Since the transport of minority carriers determines the behavior of the p-n junctions that are ubiquitous in semiconductor devices, surface photovoltage data can be very helpful in unde... | {
"page_id": 7800566,
"source": null,
"title": "Surface photovoltage"
} |
that the photogenerated majority carriers will also diffuse towards the surface but their number as a fraction of the thermally generated majority carrier density in a moderately doped semiconductor will be too small to create a measurable photovoltage. Both carrier types will also diffuse towards the rear contact wher... | {
"page_id": 7800566,
"source": null,
"title": "Surface photovoltage"
} |
surface and the smaller the photovoltage. On a semiconductor whose spectral absorption coefficient is known, the minority carrier diffusion length can in principle be extracted from a measurement of photovoltage versus wavelength. The optical properties of a novel semiconductor may not be well known or may not be homog... | {
"page_id": 7800566,
"source": null,
"title": "Surface photovoltage"
} |
(PDF) on 2005-03-12. Retrieved 2008-07-03. == External links == Freiberg Instruments vendor of industrial and scientific SPV and Minority Carrier Lifetime measurement systems Semilab vendor of commercial SPV and Minority Carrier Lifetime measurement systems KP Technology vendors of and consultants about Kelvin probes A... | {
"page_id": 7800566,
"source": null,
"title": "Surface photovoltage"
} |
The molecular formula C12H12N4O3 (molar mass: 260.25 g/mol, exact mass: 260.0909 u) may refer to: Benznidazole Furafylline | {
"page_id": 32376569,
"source": null,
"title": "C12H12N4O3"
} |
Post-acute infection syndromes (PAISs) or post-infectious syndromes are medical conditions characterized by symptoms attributed to a prior infection. While it is commonly assumed that people either recover or die from infections, long-term symptoms—or sequelae—are a possible outcome as well. Examples include long COVID... | {
"page_id": 74712827,
"source": null,
"title": "Post-acute infection syndrome"
} |
is not understood. The commonality in symptoms between illnesses may point to a common pathology. Major hypotheses include persistence of the original pathogen or its remnants, autoimmunity, chronic inflammation, reactivation of other latent infections, microbiome dysbiosis, or damage to organs, which may include the l... | {
"page_id": 74712827,
"source": null,
"title": "Post-acute infection syndrome"
} |
lifelong for most. == Epidemiology == Data on epidemiology is limited by the lack of large, rigorous studies; and rates vary by infection. Mononucleosis is among the best studied, and available studies found that 7-9% had persistent symptoms 12 months after infection, and 4% had serious symptoms after 2 years. The Brit... | {
"page_id": 74712827,
"source": null,
"title": "Post-acute infection syndrome"
} |
Ljungström air preheater is an air preheater invented by the Swedish engineer Fredrik Ljungström (1875–1964). The patent was achieved in 1930. The factory and workshop were in Lidingö throughout the 1920s, with about 70 employees. In the 1930s, the facilities were used as a film studio, and they were demolished in the ... | {
"page_id": 53937915,
"source": null,
"title": "Ljungström air preheater"
} |
C55-isoprenyl pyrophosphate (also known as undecaprenyl pyrophosphate or C55-PP) is an essential molecule involved in the construction of the bacterial peptidoglycan cell wall. It is a receptor found in the plasma membrane of bacteria allowing glycan tetrapeptide monomers synthesized in the cell cytoplasm to translocat... | {
"page_id": 26478333,
"source": null,
"title": "C55-isoprenyl pyrophosphate"
} |
Microbial population biology is the application of the principles of population biology to microorganisms. == Distinguishing from other biological disciplines == Microbial population biology, in practice, is the application of population ecology and population genetics toward understanding the ecology and evolution of ... | {
"page_id": 7538436,
"source": null,
"title": "Microbial population biology"
} |
retain some emphasis on the microbe since at some point this "question-driven" microbial population biology becomes instead population biology using microorganisms. Because the point of departure of these potentially disparate emphases can be somewhat arbitrary, there exist vague and not universally accepted delimits a... | {
"page_id": 7538436,
"source": null,
"title": "Microbial population biology"
} |
This list contains a list of EC numbers for the fifth group, EC 5, isomerases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and main... | {
"page_id": 5506829,
"source": null,
"title": "List of EC numbers (EC 5)"
} |
UDP-glucosamine 4-epimerase EC 5.1.3.17: heparosan-N-sulfate-glucuronate 5-epimerase EC 5.1.3.18: GDP-mannose 3,5-epimerase EC 5.1.3.19: chondroitin-glucuronate 5-epimerase EC 5.1.3.20: ADP-glyceromanno-heptose 6-epimeras EC 5.1.3.21: maltose epimerase EC 5.1.3.22: L-ribulose-5-phosphate 3-epimerase EC 5.1.3.23: UDP-2,... | {
"page_id": 5506829,
"source": null,
"title": "List of EC numbers (EC 5)"
} |
cited EC 5.2.1.12: ζ-carotene isomerase EC 5.2.1.13: prolycopene isomerase EC 5.2.1.14: β-carotene isomerase == EC 5.3: Intramolecular Oxidoreductases == === EC 5.3.1: Interconverting Aldoses and Ketoses === EC 5.3.1.1: triose-phosphate isomerase EC 5.3.1.2: deleted EC 5.3.1.3: D-arabinose isomerase EC 5.3.1.4: L-arabi... | {
"page_id": 5506829,
"source": null,
"title": "List of EC numbers (EC 5)"
} |
L-dopachrome isomerase EC 5.3.3.13: polyenoic fatty acid isomerase EC 5.3.3.14: trans-2-decenoyl-[acyl-carrier protein] isomerase EC 5.3.3.15: Now EC 5.3.2.7, ascopyrone tautomerase EC 5.3.3.16: Now EC 5.3.2.8, 4-oxalomesaconate tautomerase EC 5.3.3.17: trans-2,3-dihydro-3-hydroxyanthranilate isomerase EC 5.3.3.18: 2-(... | {
"page_id": 5506829,
"source": null,
"title": "List of EC numbers (EC 5)"
} |
5.4.3.3, lysine 5,6-aminomutase EC 5.4.3.5: D-ornithine 4,5-aminomutase EC 5.4.3.6: tyrosine 2,3-aminomutase EC 5.4.3.7: leucine 2,3-aminomutase EC 5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase EC 5.4.3.9: glutamate 2,3-aminomutase EC 5.4.3.10: phenylalanine aminomutase (L-β-phenylalanine forming) * EC 5.4.3.11: ph... | {
"page_id": 5506829,
"source": null,
"title": "List of EC numbers (EC 5)"
} |
mitochondrial tRNA pseudouridine27/28 synthase EC 5.4.99.45: tRNA pseudouridine38/39 synthase EC 5.4.99.46: shionone synthase EC 5.4.99.47: parkeol synthase EC 5.4.99.48: achilleol B synthase EC 5.4.99.49: glutinol synthase EC 5.4.99.50: friedelin synthase EC 5.4.99.51: baccharis oxide synthase EC 5.4.99.52: α-seco-amy... | {
"page_id": 5506829,
"source": null,
"title": "List of EC numbers (EC 5)"
} |
5.5.1.32: 12-epi-hapalindole U synthase * EC 5.5.1.33: 12-epi-fischerindole U synthase * EC 5.5.1.34: (+)-cis,trans-nepetalactol synthase * EC 5.5.1.35: (+)-cis,cis-nepetalactol synthase * *No Wikipedia article == EC 5.6: Isomerases altering macromolecular conformation == === EC 5.6.1: Enzymes altering polypeptide conf... | {
"page_id": 5506829,
"source": null,
"title": "List of EC numbers (EC 5)"
} |
The molecular formula CAgNO (molar mass: 149.89 g/mol, exact mass: 148.9031 u) may refer to: Silver cyanate, cyanate salt of silver Silver fulminate, highly explosive silver salt of fulminic acid | {
"page_id": 61605645,
"source": null,
"title": "CAgNO"
} |
AI/ML development platforms—such as PyTorch and Hugging Face—are software ecosystems designed to support the creation, training, deployment, and management of artificial intelligence (AI) and machine learning (ML) models.. These platforms provide tools, frameworks, and infrastructure to streamline workflows for develop... | {
"page_id": 78972687,
"source": null,
"title": "AI/ML Development Platform"
} |
Future trends == Democratization: Low-code/no-code platforms (e.g., Google AutoML, DataRobot). Ethical AI integration: Tools for bias mitigation and transparency. Federated learning: Training models on decentralized data. Quantum machine learning: Hybrid platforms leveraging quantum computing. == See also == Automated ... | {
"page_id": 78972687,
"source": null,
"title": "AI/ML Development Platform"
} |
In the physical sciences and electrical engineering, dispersion relations describe the effect of dispersion on the properties of waves in a medium. A dispersion relation relates the wavelength or wavenumber of a wave to its frequency. Given the dispersion relation, one can calculate the frequency-dependent phase veloci... | {
"page_id": 853778,
"source": null,
"title": "Dispersion relation"
} |
these variables gives ω ( k ) = v ( k ) ⋅ k . {\displaystyle \omega (k)=v(k)\cdot k.} where we now view f as a function of k. The use of ω(k) to describe the dispersion relation has become standard because both the phase velocity ω/k and the group velocity dω/dk have convenient representations via this function. The pl... | {
"page_id": 853778,
"source": null,
"title": "Dispersion relation"
} |
frequency ω {\displaystyle \omega } in vacuum varies with wavenumber ( k = 2 π / λ {\displaystyle k=2\pi /\lambda } ) in the non-relativistic approximation. The variation has two parts: a constant part due to the de Broglie frequency of the rest mass ( ℏ ω 0 = m 0 c 2 {\displaystyle \hbar \omega _{0}=m_{0}c^{2}} ) and ... | {
"page_id": 853778,
"source": null,
"title": "Dispersion relation"
} |
≈ m 0 c 2 ℏ + ℏ k 2 2 m 0 . {\displaystyle \omega (k)\approx {\frac {m_{0}c^{2}}{\hbar }}+{\frac {\hbar k^{2}}{2m_{0}}}\,.} This gives the non-relativistic approximation discussed above. If we start with the non-relativistic Schrödinger equation we will end up without the first, rest mass, term. == Frequency versus wav... | {
"page_id": 853778,
"source": null,
"title": "Dispersion relation"
} |
is v g = d ω d k = 1 2 v p . {\displaystyle v_{g}={\frac {d\omega }{dk}}={\frac {1}{2}}v_{p}.} === Waves on a string === For an ideal string, the dispersion relation can be written as ω = k T μ , {\displaystyle \omega =k{\sqrt {\frac {T}{\mu }}},} where T is the tension force in the string, and μ is the string's mass p... | {
"page_id": 853778,
"source": null,
"title": "Dispersion relation"
} |
they correspond to classical sound in the limit of long wavelengths. The others are optical phonons, since they can be excited by electromagnetic radiation. === Electron optics === With high-energy (e.g., 200 keV, 32 fJ) electrons in a transmission electron microscope, the energy dependence of higher-order Laue zone (H... | {
"page_id": 853778,
"source": null,
"title": "Dispersion relation"
} |
Marianne Grunberg-Manago (January 6, 1921 – January 3, 2013) was a Soviet-born French biochemist. Her work helped make possible key discoveries about the nature of the genetic code. Grunberg-Manago was the first woman to lead the International Union of Biochemistry and the 400-year-old French Academy of Sciences. == Ea... | {
"page_id": 8783636,
"source": null,
"title": "Marianne Grunberg-Manago"
} |
she was also the first woman to preside over the French Academy of Sciences (1995–1996). == Later life and death == Late in her career, Grunberg-Manago was named emeritus director of research at CNRS, France's National Center for Scientific Research. Grunberg-Manago died in January 2013, three days before her 92nd birt... | {
"page_id": 8783636,
"source": null,
"title": "Marianne Grunberg-Manago"
} |
This list contains a list of EC numbers for the fourth group, EC 4, lyases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintai... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
EC 4.1.1.51: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase EC 4.1.1.52: 6-methylsalicylate decarboxylase EC 4.1.1.53: phenylalanine decarboxylase EC 4.1.1.54: dihydroxyfumarate decarboxylase EC 4.1.1.55: 4,5-dihydroxyphthalate decarboxylase EC 4.1.1.56: 3-oxolaurate decarboxylase EC 4.1.1.57: methionine ... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
decarboxylase * EC 4.1.1.118: isophthalyl-CoA decarboxylase * EC 4.1.1.119: phenylacetate decarboxylase * EC 4.1.1.120: 3-oxoisoapionate decarboxylase * EC 4.1.1.121: 3-oxoisoapionate-4-phosphate decarboxylase * *No Wikipedia article === EC 4.1.2: Aldehyde-lyases === EC 4.1.2.1: Now included with EC 4.1.3.16 4-hydroxy-... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
4-hydroxy-2-oxoheptanedioate aldolase * * EC 4.1.2.53: 2-keto-3-deoxy-L-rhamnonate aldolase * * EC 4.1.2.54: L-threo-3-deoxy-hexylosonate aldolase * * EC 4.1.2.55: 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase * * EC 4.1.2.56: 2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate syn... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
EC 4.1.3.43: 4-hydroxy-2-oxohexanoate aldolase * EC 4.1.3.44: tRNA 4-demethylwyosine synthase (AdoMet-dependent) * EC 4.1.3.45: 3-hydroxybenzoate synthase * EC 4.1.3.46: (R)-citramalyl-CoA lyase * *No Wikipedia article === EC 4.1.99: Other Carbon-Carbon Lyases === EC 4.1.99.1: tryptophanase EC 4.1.99.2: tyrosine phenol... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
4.2.1.18: methylglutaconyl-CoA hydratase EC 4.2.1.19: imidazoleglycerol-phosphate dehydratase EC 4.2.1.20: tryptophan synthase EC 4.2.1.21: Now EC 4.2.1.22 cystathionine β-synthase EC 4.2.1.22: cystathionine β-synthase EC 4.2.1.23: deleted, the reaction was due to a side-reaction of EC 4.2.1.22 cystathionine β-synthase... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
protoaphin-aglucone dehydratase (cyclizing) EC 4.2.1.74: long-chain-enoyl-CoA hydratase EC 4.2.1.75: uroporphyrinogen-III synthase EC 4.2.1.76: UDP-glucose 4,6-dehydratase EC 4.2.1.77: trans-L-3-hydroxyproline dehydratase EC 4.2.1.78: (S)-norcoclaurine synthase EC 4.2.1.79: 2-methylcitrate dehydratase EC 4.2.1.80: 2-ox... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
synthase EC 4.2.1.138: (+)-Caryolan-1-ol synthase EC 4.2.1.139: pterocarpan synthase * EC 4.2.1.140: gluconate/galactonate dehydratase * EC 4.2.1.141: 2-dehydro-3-deoxyD-arabinonate dehydratase * EC 4.2.1.142: 5′-oxoaverantin cyclase * EC 4.2.1.143: versicolorin B synthase * EC 4.2.1.144: 3-amino-5-hydroxybenzoate synt... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
4.2.2.17: inulin fructotransferase (DFA-I-forming) EC 4.2.2.18: inulin fructotransferase (DFA-III-forming) EC 4.2.2.19: chondroitin B lyase EC 4.2.2.20: chondroitin-sulfate-ABC endolyase EC 4.2.2.21: chondroitin-sulfate-ABC exolyase EC 4.2.2.22: pectate trisaccharide-lyase EC 4.2.2.23: rhamnogalacturonan endolyase EC 4... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
4.2.3.56: γ-humulene synthase EC 4.2.3.57: (–)-β-caryophyllene synthase EC 4.2.3.58: longifolene synthase EC 4.2.3.59: (E)-γ-bisabolene synthase EC 4.2.3.60: germacrene C synthase EC 4.2.3.61: 5-epiaristolochene synthase EC 4.2.3.62: (–)-γ-cadinene synthase [(2Z,6E)-farnesyl diphosphate cyclizing] EC 4.2.3.63: (+)-cube... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
(+)-sativene synthase EC 4.2.3.130: tetraprenyl-β-curcumene synthase EC 4.2.3.131: miltiradiene synthase EC 4.2.3.132: neoabietadiene synthase EC 4.2.3.133: α-copaene synthase EC 4.2.3.134: 5-phosphooxy-L-lysine phospho-lyase EC 4.2.3.135: Δ6-protoilludene synthase EC 4.2.3.136: α-isocomene synthase EC 4.2.3.137: (E)-2... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
synthase EC 4.2.3.199: (–)-5-epieremophilene synthase EC 4.2.3.200: β-pinacene synthase EC 4.2.3.201: hydropyrene synthase EC 4.2.3.202: hydropyrenol synthase EC 4.2.3.203: isoelisabethatriene synthase EC 4.2.3.204: valerianol synthase EC 4.2.3.205: sodorifen synthase === EC 4.2.99: Other Carbon-Oxygen Lyases === EC 4.... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
4.3.1.18: D-serine ammonia-lyase EC 4.3.1.19: threonine ammonia-lyase EC 4.3.1.20: erythro-3-hydroxy-L-aspartate ammonia-lyase EC 4.3.1.21: identical to EC 4.3.1.9, glucosaminate ammonia-lyase EC 4.3.1.22: 3,4-dihydroxyphenylalanine reductive deaminase EC 4.3.1.23: tyrosine ammonia-lyase EC 4.3.1.24: phenylalanine ammo... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
lyase EC 4.4.1.17: holocytochrome-c synthase EC 4.4.1.18: Now EC 1.8.3.5, prenylcysteine oxidase EC 4.4.1.19: phosphosulfolactate synthase EC 4.4.1.20: leukotriene-C4 synthase EC 4.4.1.21: S-ribosylhomocysteine lyase EC 4.4.1.22: S-(hydroxymethyl)glutathione synthase EC 4.4.1.23: 2-hydroxypropyl-CoM lyase EC 4.4.1.24: ... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
aldoxime dehydratase * EC 4.8.1.3: indoleacetaldoxime dehydratase * EC 4.8.1.4: phenylacetaldoxime dehydratase * *No Wikipedia article == EC 4.98: ATP-independent chelatases == === EC 4.98.1: Forming coordination complexes === EC 4.98.1.1: protoporphyrin ferrochelatase == EC 4.99: Other Lyases == === EC 4.99.1: Sole su... | {
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
} |
The study of electromagnetism in higher education, as a fundamental part of both physics and electrical engineering, is typically accompanied by textbooks devoted to the subject. The American Physical Society and the American Association of Physics Teachers recommend a full year of graduate study in electromagnetism fo... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
Addison-Wesley, 2002. Purcell EM, Morin DJ, Electricity and Magnetism, 3rd ed, Cambridge University, 2013. Reitz JR, Milford FJ, Christy RW, Foundations of Electromagnetic Theory, 4th ed, Pearson, 2009. Saslow W, Electricity Magnetism and Light, Academic, 2002. Schwartz M, Principles of Electrodynamics, Dover, 1987. Ta... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
most notable being Modern Electrodynamics by Andrew Zangwill published in 2013, which has been praised by many physicists like John Joannopoulos, Michael Berry, Rob Phillips, Alain Aspect, Roberto Merlin, Shirley Chiang, Roy Schwitters but also well received in the electrical engineering community. Another notable text... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
Theory of Fields and Particles, Dover, 1980. Baylis WE, Electrodynamics: A Modern Geometric Approach, Birkhäuser, 1999. Böttcher CJF, Bordewijk P, Van Belle OC, Rip A, Theory of Electric Polarization, 2nd ed, 2 vols, Elsevier, 1973, 1978. Clemmow PC, Dougherty JP, Electrodynamics of Particles and Plasmas, CRC, 2018. Cu... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
physicist Hans Schantz and based on the comparison of textbooks Electromagnetic Theory by Julius Stratton and Classical Electrodynamics by John Jackson, Schantz argues "today's physicists who are educated using curriculum out of Jackson are less informed about practical electromagnetics than their counterparts of 80 ye... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
engineering's approach to electromagnetic problems has also been noted by other physicists like Robert Dicke and more specially Julian Schwinger. Schwinger's emphasis on using electrical engineering's point of view was even more general than just in electromagnetic phenomena so that he argued for the use of engineering... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
2nd ed, Wiley, 2022. Ulaby FT, Ravaioli U, Fundamentals of Applied Electromagnetics, 8th ed, Pearson, 2020. === Graduate === Balanis CA, Advanced Engineering Electromagnetics, 3rd ed, Wiley, 2024. Chew WC, Waves and Fields in Inhomogeneous Media, IEEE, 1995. Collin RE, Field Theory of Guided Waves, 2nd ed, Wiley-IEEE, ... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
and Sources, Wiley-IEEE, 1991. Wait JR, Electromagnetic Waves in Stratified Media, 2nd ed, IEEE-Oxford University, 1996. === Radio-frequency === Balanis CA, Antenna Theory: Analysis and Design, 4th ed, Wiley, 2016. Collin RE, Foundations for Microwave Engineering, 2nd ed, Wiley-IEEE, 2001. Elliott RS, Antenna Theory an... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
2008. Sarychev AK, Shalaev VM, Electrodynamics of Metamaterials, World Scientific, 2007. Tretyakov S, Analytical Modeling in Applied Electromagnetics, Artech House, 2003. Yang F, Rahmat-Samii Y, Electromagnetic Band Gap Structures in Antenna Engineering, Cambridge University, 2009. === Computational === Booton RC, Comp... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
FA, White HE, Fundamentals of Optics, 4th ed, McGraw Hill, 2001. Lipson A, Lipson SG, Lipson H, Optical Physics, 4th ed, Cambridge University, 2010. Shiell R, McNab I, Pedrottis' Introduction to Optics, 4th ed, Cambridge University, 2024. Smith WJ, Modern Optical Engineering: The Design of Optical Systems, 4th ed, McGr... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
magnetism which some of them are listed here and they could be used in both physics and electrical engineering studies depending on the context. Aharoni A, Introduction to the Theory of Ferromagnetism, 2nd ed, Oxford University, 1996. Blundell S, Magnetism in Condensed Matter, Oxford University, 2001. Bozorth RM, Ferro... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
list of some important textbooks in different areas of electro-magneto-ferro-hydrodynamics. Alfvén H, Fälthammar CG, Cosmical Electrodynamics: Fundamental Principles, 2nd ed, Oxford University, 1963. Biskamp D, Magnetohydrodynamic Turbulence, Cambridge University, 2003. Biskamp D, Nonlinear Magnetohydrodynamics, Cambri... | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
2nd ed, 2 vols, Thomas Nelson, 1951. == See also == == Notes == == References == | {
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
} |
Ammonium polyphosphate is an inorganic salt of polyphosphoric acid and ammonia containing both chains and possibly branching. Its chemical formula is H(NH4PO3)nOH showing that each monomer consists of an orthophosphate radical of a phosphorus atom with three oxygens and one negative charge neutralized by an ammonium ca... | {
"page_id": 15664920,
"source": null,
"title": "Ammonium polyphosphate"
} |
flame retard polyurethane foams. Ammonium polyphosphates used as flame retardants in polymers have long chains and a specific crystallinity (Form II). They start to decompose at 240 °C to form ammonia and phosphoric acid. The phosphoric acid acts as an acid catalyst in the dehydration of carbon-based poly-alcohols, suc... | {
"page_id": 15664920,
"source": null,
"title": "Ammonium polyphosphate"
} |
This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and main... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
deacetylase EC 3.1.1.55: acetylsalicylate deacetylase EC 3.1.1.56: methylumbelliferyl-acetate deacetylase EC 3.1.1.57: 2-pyrone-4,6-dicarboxylate lactonase EC 3.1.1.58: N-acetylgalactosaminoglycan deacetylase EC 3.1.1.59: juvenile-hormone esterase EC 3.1.1.60: bis(2-ethylhexyl)phthalate esterase EC 3.1.1.61: protein-gl... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
esterase * EC 3.1.1.118: phospholipid sn-1 acylhydrolase * *No Wikipedia article === EC 3.1.2: Thioester Hydrolases === EC 3.1.2.1: acetyl-CoA hydrolase EC 3.1.2.2: palmitoyl-CoA hydrolase EC 3.1.2.3: succinyl-CoA hydrolase EC 3.1.2.4: 3-hydroxyisobutyryl-CoA hydrolase EC 3.1.2.5: hydroxymethylglutaryl-CoA hydrolase EC... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
EC 3.1.3.30: The activity may be that of an acid phosphatase EC 3.1.3.31: The activity may be that of an acid phosphatase EC 3.1.3.32: polynucleotide 3′-phosphatase EC 3.1.3.33: polynucleotide 5′-phosphatase EC 3.1.3.34: deoxynucleotide 3′-phosphatase EC 3.1.3.35: thymidylate 5′-phosphatase EC 3.1.3.36: phosphoinositid... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
3.1.4.7: Now EC 3.1.31.1, micrococcal nuclease EC 3.1.4.8: Now EC 3.1.27.3, ribonuclease T1 EC 3.1.4.9: Now EC 3.1.30.2, Serratia marcescens nuclease EC 3.1.4.10: Now EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase EC 3.1.4.11: phosphoinositide phospholipase C EC 3.1.4.12: sphingomyelin phosphodiesterase EC 3.1.... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
EC 3.1.6: Sulfuric Ester Hydrolases === EC 3.1.6.1: arylsulfatase (type I) EC 3.1.6.2: steryl-sulfatase EC 3.1.6.3: glycosulfatase EC 3.1.6.4: N-acetylgalactosamine-6-sulfatase EC 3.1.6.5: deleted EC 3.1.6.6: choline-sulfatase EC 3.1.6.7: cellulose-polysulfatase EC 3.1.6.8: cerebroside-sulfatase EC 3.1.6.9: chondro-4-s... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 3'-Phosphomonoesters === EC 3.1.16.1: spleen exonuclease === EC 3.1.21: Endodeoxyribonucleases Producing 5'-Phosphomonoesters === EC 3.1.21.1: deoxyribonuclease I EC 3.1.21.2: deoxyribonuclease IV EC 3.1.21.3: type I site-specific deoxyribonu... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
reaction is that of a lyase EC 3.1.27.7: ribonuclease F EC 3.1.27.8: ribonuclease V EC 3.1.27.9: Now EC 4.6.1.16, tRNA-intron lyase EC 3.1.27.10: Now EC 4.6.1.23, ribotoxin, === EC 3.1.30: Endoribonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 5'-Phosphomonoesters === EC 3.1.30.1: Aspergillu... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
EC 3.2.1.56: glucuronosyl-disulfoglucosamine glucuronidase EC 3.2.1.57: isopullulanase EC 3.2.1.58: glucan 1,3-β-glucosidase EC 3.2.1.59: glucan endo-1,3-α-glucosidase EC 3.2.1.60: glucan 1,4-α-maltotetraohydrolase EC 3.2.1.61: mycodextranase EC 3.2.1.62: glycosylceramidase EC 3.2.1.63: 1,2-α-L-fucosidase EC 3.2.1.64: ... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
glycoprotein endo-α-1,2-mannosidase EC 3.2.1.131: xylan α-1,2-glucuronosidase EC 3.2.1.132: chitosanase EC 3.2.1.133: glucan 1,4-α-maltohydrolase EC 3.2.1.134: difructose-anhydride synthase EC 3.2.1.135: neopullulanase EC 3.2.1.136: glucuronoarabinoxylan endo-1,4-β-xylanase EC 3.2.1.137: mannan exo-1,2-1,6-α-mannosidas... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
β-1,2-mannosidase * EC 3.2.1.198: α-mannan endo-1,2-α-mannanase * EC 3.2.1.199: sulfoquinovosidase * EC 3.2.1.200: exo-chitinase (non-reducing end) * EC 3.2.1.201: exo-chitinase (reducing end) * EC 3.2.1.202: endo-chitodextinase * EC 3.2.1.203: carboxymethylcellulase * EC 3.2.1.204: 1,3-α-isomaltosidase * EC 3.2.1.205:... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
hydrolase EC 3.3.2.3: Now known to comprise two enzymes, microsomal epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC 3.3.2.10) EC 3.3.2.4: trans-epoxysuccinate hydrolase EC 3.3.2.5: Now included in EC 3.3.2.2, lysoplasmalogenase EC 3.3.2.6: leukotriene-A4 hydrolase EC 3.3.2.7: hepoxilin-epoxide hydrolas... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
3.4.4.11: Now EC 3.4.22.6, chymopapain EC 3.4.4.12: Now EC 3.4.22.3, ficain EC 3.4.4.13: Now EC 3.4.21.5, thrombin EC 3.4.4.14: Now EC 3.4.21.7, plasmin EC 3.4.4.15: Now EC 3.4.23.15, renin EC 3.4.4.16: Now covered by the microbial serine proteinases EC 3.4.21.62 (subtilisin), EC 3.4.21.63 (oryzin), EC 3.4.21.64 (endop... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
D) EC 3.4.12.2: Now EC 3.4.17.1, carboxypeptidase A EC 3.4.12.3: Now EC 3.4.17.2, carboxypeptidase B EC 3.4.12.4: Now EC 3.4.16.2, lysosomal Pro-Xaa carboxypeptidase EC 3.4.12.5: Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase EC 3.4.12.6: Now EC 3.4.17.8, muramoyl-pentapeptidase carboxypeptidase EC 3.4.12.7: Now E... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
=== EC 3.4.15 Peptidyl dipeptidases === EC 3.4.15.1: peptidyl-dipeptidase A EC 3.4.15.2: Now EC 3.4.19.2, peptidyl-glycinamidase EC 3.4.15.3: Now EC 3.4.15.5, peptidyl-dipeptidase Dcp EC 3.4.15.4: Peptidyl-dipeptidase B EC 3.4.15.5: Peptidyl-dipeptidase Dcp EC 3.4.15.6: cyanophycinase === EC 3.4.16 Serine type carboxyp... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
3.4.21.3: metridin EC 3.4.21.4: trypsin EC 3.4.21.5: thrombin EC 3.4.21.6: coagulation factor Xa EC 3.4.21.7: plasmin EC 3.4.21.8: Now EC 3.4.21.34 (plasma kallikrein) and EC 3.4.21.35 (tissue kallikrein) EC 3.4.21.9: enteropeptidase EC 3.4.21.10: acrosin EC 3.4.21.11: Now EC 3.4.21.37, leukocyte elastase EC 3.4.21.12:... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
II EC 3.4.21.72: IgA-specific serine endopeptidase EC 3.4.21.73: u-plasminogen activator EC 3.4.21.74: venombin A EC 3.4.21.75: furin EC 3.4.21.76: myeloblastin EC 3.4.21.77: semenogelase EC 3.4.21.78: granzyme A EC 3.4.21.79: granzyme B EC 3.4.21.80: streptogrisin A EC 3.4.21.81: streptogrisin B EC 3.4.21.82: glutamyl... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
3.4.22.16: cathepsin H EC 3.4.22.17: Now EC 3.4.22.53, calpain-2 EC 3.4.22.18: Now EC 3.4.21.26, prolyl oligopeptidase EC 3.4.22.19: Now EC 3.4.24.15, thimet oligopeptidase EC 3.4.22.20: Deleted EC 3.4.22.21: Now EC 3.4.25.1, proteasome endopeptidase complex EC 3.4.22.22: Now EC 3.4.24.37, saccharolysin EC 3.4.22.23: N... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
3.4.23.19: aspergillopepsin II EC 3.4.23.20: penicillopepsin EC 3.4.23.21: rhizopuspepsin EC 3.4.23.22: endothiapepsin EC 3.4.23.23: mucorpepsin EC 3.4.23.24: candidapepsin EC 3.4.23.25: saccharopepsin EC 3.4.23.26: rhodotorulapepsin EC 3.4.23.27: Now EC 3.4.21.103, physarolisin EC 3.4.23.28: acrocylindropepsin EC 3.4.... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
EC 3.4.24.37: saccharolysin EC 3.4.24.38: gametolysin EC 3.4.24.39: deuterolysin EC 3.4.24.40: serralysin EC 3.4.24.41: atrolysin B EC 3.4.24.42: atrolysin C EC 3.4.24.43: atroxase EC 3.4.24.44: atrolysin E EC 3.4.24.45: atrolysin F EC 3.4.24.46: adamalysin EC 3.4.24.47: horrilysin EC 3.4.24.48: ruberlysin EC 3.4.24.49... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
3.4.99.20: Deleted entry: scopulariopsis proteinase EC 3.4.99.21: Deleted entry: solanain. Now considered EC 3.4.21.25, cucumisin EC 3.4.99.22: Transferred entry: staphylokinase. EC 3.4.24.29, aureolysin EC 3.4.99.23: Deleted entry: tabernamontanain. Now considered EC 3.4.21.25, cucumisin EC 3.4.99.24: Deleted entry: T... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
deformylase EC 3.5.1.11: penicillin amidase EC 3.5.1.12: biotinidase EC 3.5.1.13: aryl-acylamidase EC 3.5.1.14: N-acyl-aliphatic-L-amino acid amidohydrolase EC 3.5.1.15: aspartoacylase EC 3.5.1.16: acetylornithine deacetylase EC 3.5.1.17: acyl-lysine deacylase EC 3.5.1.18: succinyl-diaminopimelate desuccinylase EC 3.5.... | {
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
} |
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