"Catalytic Domain" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Descriptor ID |
D020134
|
MeSH Number(s) |
G02.111.570.120.704 G02.111.570.820.709.275.750.188
|
Concept/Terms |
Catalytic Domain- Catalytic Domain
- Catalytic Domains
- Domain, Catalytic
- Domains, Catalytic
- Catalytic Subunit
- Catalytic Subunits
- Subunit, Catalytic
- Subunits, Catalytic
- Catalytic Region
- Catalytic Regions
- Region, Catalytic
- Regions, Catalytic
- Catalytic Core
- Catalytic Cores
- Core, Catalytic
- Cores, Catalytic
Active Site- Active Site
- Active Sites
- Site, Active
- Sites, Active
- Catalytic Site
- Catalytic Sites
- Site, Catalytic
- Sites, Catalytic
- Reactive Site
- Reactive Sites
- Site, Reactive
- Sites, Reactive
|
Below are MeSH descriptors whose meaning is more general than "Catalytic Domain".
Below are MeSH descriptors whose meaning is more specific than "Catalytic Domain".
This graph shows the total number of publications written about "Catalytic Domain" by people in this website by year, and whether "Catalytic Domain" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
Year | Major Topic | Minor Topic | Total |
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1998 | 1 | 0 | 1 |
1999 | 0 | 2 | 2 |
2000 | 0 | 2 | 2 |
2001 | 0 | 4 | 4 |
2002 | 0 | 4 | 4 |
2004 | 0 | 4 | 4 |
2005 | 0 | 2 | 2 |
2006 | 0 | 3 | 3 |
2007 | 2 | 1 | 3 |
2008 | 0 | 3 | 3 |
2009 | 0 | 2 | 2 |
2010 | 1 | 11 | 12 |
2011 | 0 | 6 | 6 |
2012 | 0 | 12 | 12 |
2013 | 0 | 6 | 6 |
2014 | 0 | 5 | 5 |
2015 | 1 | 4 | 5 |
2016 | 0 | 3 | 3 |
2017 | 1 | 9 | 10 |
2018 | 1 | 10 | 11 |
2019 | 1 | 8 | 9 |
2020 | 0 | 7 | 7 |
2021 | 0 | 11 | 11 |
2022 | 0 | 2 | 2 |
2023 | 0 | 1 | 1 |
2024 | 2 | 3 | 5 |
2025 | 0 | 3 | 3 |
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click here.
Below are the most recent publications written about "Catalytic Domain" by people in Profiles.
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Zvornicanin SN, Shaqra AM, Flynn J, Carias Martinez H, Jia W, Moquin S, Dovala D, Bolon DN, Kurt Yilmaz N, Schiffer CA. Molecular mechanisms of drug resistance and compensation in SARS-CoV-2 main protease: the interplay between E166 and L50. mBio. 2025 May 14; 16(5):e0406824.
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Hedger AK, Myint W, Lee JM, Suchenski Loustaunau D, Balachandran V, Shaqra AM, Kurt Yilmaz N, Watts JK, Matsuo H, Schiffer CA. Next generation?APOBEC3 inhibitors: optimally designed for potency and nuclease stability. Nucleic Acids Res. 2025 Mar 20; 53(6).
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Pardhe BD, Park H, Paudel P, Jeong J, Oh TJ, Choi KY, Ahn J. In-vitro optimization and active-site mutagenesis of CYP105D18 peroxygenase enhance the production of indigo. Enzyme Microb Technol. 2025 Jun; 187:110634.
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Azzolino VN, Shaqra AM, Ali A, Kurt Yilmaz N, Schiffer CA. Elucidating the Substrate Envelope of Enterovirus 68-3C Protease: Structural Basis of Specificity and Potential Resistance. Viruses. 2024 09 05; 16(9).
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Loveland AB, Koh CS, Ganesan R, Jacobson A, Korostelev AA. Structural mechanism of angiogenin activation by the ribosome. Nature. 2024 Jun; 630(8017):769-776.
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Leo G, Leone P, Ataie Kachoie E, Tolomeo M, Galluccio M, Indiveri C, Barile M, Capaldi S. Structural insights into the bifunctional enzyme human FAD synthase. Structure. 2024 Jul 11; 32(7):953-965.e5.
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Cruz KG, Hill Eron M, Makhaik S, Savinov S, Hardy JA. A Non-Active-Site Inhibitor with Selectivity for Zika Virus NS2B-NS3 Protease. ACS Infect Dis. 2024 02 09; 10(2):412-425.
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Mpakali A, Barla I, Lu L, Ramesh KM, Thomaidis N, Stern LJ, Giastas P, Stratikos E. Mechanisms of Allosteric Inhibition of Insulin-Regulated Aminopeptidase. J Mol Biol. 2024 03 15; 436(6):168449.
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Icso JD, Barasa L, Thompson PR. SARM1, an Enzyme Involved in Axon Degeneration, Catalyzes Multiple Activities through a Ternary Complex Mechanism. Biochemistry. 2023 07 04; 62(13):2065-2078.
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Maiti A, Hedger AK, Myint W, Balachandran V, Watts JK, Schiffer CA, Matsuo H. Structure of the catalytically active APOBEC3G bound to a DNA oligonucleotide inhibitor reveals tetrahedral geometry of the transition state. Nat Commun. 2022 11 19; 13(1):7117.