"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 |
|---|
| 1998 | 2 | 4 | 6 |
| 1999 | 0 | 4 | 4 |
| 2000 | 0 | 6 | 6 |
| 2001 | 0 | 7 | 7 |
| 2002 | 2 | 9 | 11 |
| 2003 | 2 | 8 | 10 |
| 2004 | 1 | 13 | 14 |
| 2005 | 0 | 9 | 9 |
| 2006 | 1 | 9 | 10 |
| 2007 | 1 | 5 | 6 |
| 2008 | 0 | 8 | 8 |
| 2009 | 2 | 11 | 13 |
| 2010 | 0 | 5 | 5 |
| 2011 | 0 | 13 | 13 |
| 2012 | 1 | 12 | 13 |
| 2013 | 0 | 6 | 6 |
| 2014 | 2 | 12 | 14 |
| 2015 | 0 | 9 | 9 |
| 2016 | 0 | 11 | 11 |
| 2017 | 1 | 7 | 8 |
| 2018 | 1 | 7 | 8 |
| 2019 | 3 | 2 | 5 |
| 2020 | 0 | 5 | 5 |
| 2021 | 2 | 8 | 10 |
| 2022 | 0 | 3 | 3 |
| 2023 | 1 | 4 | 5 |
| 2024 | 0 | 2 | 2 |
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click here.
Below are the most recent publications written about "Catalytic Domain" by people in Profiles.
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Effects of the Y432S Cancer-Associated Variant on the Reaction Mechanism of Human DNA Polymerase ?. J Chem Inf Model. 2024 May 27; 64(10):4231-4249.
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Network of epistatic interactions in an enzyme active site revealed by large-scale deep mutational scanning. Proc Natl Acad Sci U S A. 2024 Mar 19; 121(12):e2313513121.
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Klebsiella pneumoniae carbapenemase variant 44 acquires ceftazidime-avibactam resistance by altering the conformation of active-site loops. J Biol Chem. 2024 Jan; 300(1):105493.
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Opposing Roles for the a Isoform of the Catalytic Subunit of Protein Phosphatase 1 in Inside-Out and Outside-In Integrin Signaling in Murine Platelets. Cells. 2023 10 10; 12(20).
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Identification of levomenthol derivatives as potential dipeptidyl peptidase-4 inhibitors: a comparative study with gliptins. J Biomol Struct Dyn. 2024 May; 42(8):4029-4047.
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Mutagenesis and structural analysis reveal the CTX-M ?-lactamase active site is optimized for cephalosporin catalysis and drug resistance. J Biol Chem. 2023 05; 299(5):104630.
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Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator megacomplex. Nature. 2023 02; 614(7948):572-579.
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An active site loop toggles between conformations to control antibiotic hydrolysis and inhibition potency for CTX-M ?-lactamase drug-resistance enzymes. Nat Commun. 2022 11 07; 13(1):6726.
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HIV-1 subtype F integrase polymorphisms external to the catalytic core domain contribute to severe loss of replication capacity in context of the integrase inhibitor resistance mutation Q148H. J Antimicrob Chemother. 2022 09 30; 77(10):2793-2802.
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Structural characterization of dicyanopyridine containing DNMT1-selective, non-nucleoside inhibitors. Structure. 2022 06 02; 30(6):793-802.e5.