"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 |
|---|
| 2000 | 0 | 1 | 1 |
| 2002 | 0 | 1 | 1 |
| 2003 | 0 | 1 | 1 |
| 2004 | 0 | 1 | 1 |
| 2005 | 2 | 1 | 3 |
| 2006 | 0 | 2 | 2 |
| 2007 | 0 | 4 | 4 |
| 2008 | 0 | 3 | 3 |
| 2009 | 1 | 5 | 6 |
| 2010 | 2 | 6 | 8 |
| 2012 | 0 | 5 | 5 |
| 2013 | 0 | 4 | 4 |
| 2014 | 0 | 1 | 1 |
| 2015 | 0 | 2 | 2 |
| 2016 | 0 | 3 | 3 |
| 2017 | 1 | 8 | 9 |
| 2018 | 0 | 5 | 5 |
| 2019 | 0 | 4 | 4 |
| 2020 | 0 | 2 | 2 |
| 2021 | 0 | 1 | 1 |
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click here.
Below are the most recent publications written about "Catalytic Domain" by people in Profiles.
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Yuan L, Lv Z, Adams MJ, Olsen SK. Crystal structures of an E1-E2-ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification. Nat Commun. 2021 04 22; 12(1):2370.
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Zuberi M, Khan I, O'Bryan JP. Inhibition of RAS: proven and potential vulnerabilities. Biochem Soc Trans. 2020 10 30; 48(5):1831-1841.
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Rut W, Lv Z, Zmudzinski M, Patchett S, Nayak D, Snipas SJ, El Oualid F, Huang TT, Bekes M, Drag M, Olsen SK. Activity profiling and crystal structures of inhibitor-bound SARS-CoV-2 papain-like protease: A framework for anti-COVID-19 drug design. Sci Adv. 2020 10; 6(42).
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Singh A, Tomberg J, Nicholas RA, Davies C. Recognition of the ß-lactam carboxylate triggers acylation of Neisseria gonorrhoeae penicillin-binding protein 2. J Biol Chem. 2019 09 20; 294(38):14020-14032.
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Ahuja LG, Aoto PC, Kornev AP, Veglia G, Taylor SS. Dynamic allostery-based molecular workings of kinase:peptide complexes. Proc Natl Acad Sci U S A. 2019 07 23; 116(30):15052-15061.
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Shanbhogue P, Hoffmann RM, Airola MV, Maini R, Hamelin DJ, Garcia-Diaz M, Burke JE, Hannun YA. The juxtamembrane linker in neutral sphingomyelinase-2 functions as an intramolecular allosteric switch that activates the enzyme. J Biol Chem. 2019 05 03; 294(18):7488-7502.
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Wang Y, V S M, Kim J, Li G, Ahuja LG, Aoto P, Taylor SS, Veglia G. Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase's enzymatic cycle. Nat Commun. 2019 02 18; 10(1):799.
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Lv Z, Yuan L, Atkison JH, Williams KM, Vega R, Sessions EH, Divlianska DB, Davies C, Chen Y, Olsen SK. Molecular mechanism of a covalent allosteric inhibitor of SUMO E1 activating enzyme. Nat Commun. 2018 12 04; 9(1):5145.
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Pearson RJ, Blake DG, Mezna M, Fischer PM, Westwood NJ, McInnes C. The Meisenheimer Complex as a Paradigm in Drug Discovery: Reversible Covalent Inhibition through C67 of the ATP Binding Site of PLK1. Cell Chem Biol. 2018 09 20; 25(9):1107-1116.e4.
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Paquette DR, Tibble RW, Daifuku TS, Gross JD. Control of mRNA decapping by autoinhibition. Nucleic Acids Res. 2018 07 06; 46(12):6318-6329.