"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 |
---|
1999 | 0 | 1 | 1 |
2000 | 0 | 1 | 1 |
2002 | 0 | 1 | 1 |
2003 | 0 | 1 | 1 |
2004 | 0 | 3 | 3 |
2005 | 2 | 1 | 3 |
2006 | 0 | 2 | 2 |
2007 | 0 | 4 | 4 |
2008 | 0 | 3 | 3 |
2009 | 1 | 5 | 6 |
2010 | 2 | 6 | 8 |
2011 | 0 | 1 | 1 |
2012 | 0 | 5 | 5 |
2013 | 0 | 4 | 4 |
2014 | 0 | 1 | 1 |
2015 | 0 | 2 | 2 |
2016 | 1 | 4 | 5 |
2017 | 1 | 8 | 9 |
2018 | 0 | 5 | 5 |
2019 | 0 | 5 | 5 |
2020 | 0 | 3 | 3 |
2021 | 0 | 1 | 1 |
2022 | 0 | 1 | 1 |
To return to the timeline,
click here.
Below are the most recent publications written about "Catalytic Domain" by people in Profiles.
-
Crystal structures reveal catalytic and regulatory mechanisms of the dual-specificity ubiquitin/FAT10 E1 enzyme Uba6. Nat Commun. 2022 08 19; 13(1):4880.
-
Crystal structures of an E1-E2-ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification. Nat Commun. 2021 04 22; 12(1):2370.
-
Inhibition of RAS: proven and potential vulnerabilities. Biochem Soc Trans. 2020 10 30; 48(5):1831-1841.
-
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).
-
Genome Editing As an Approach to the Study of in Vivo Transcription Reprogramming. Dokl Biochem Biophys. 2020 Jan; 490(1):43-46.
-
Recognition of the ?-lactam carboxylate triggers acylation of Neisseria gonorrhoeae penicillin-binding protein 2. J Biol Chem. 2019 09 20; 294(38):14020-14032.
-
Dynamic allostery-based molecular workings of kinase:peptide complexes. Proc Natl Acad Sci U S A. 2019 07 23; 116(30):15052-15061.
-
Structural basis for adenylation and thioester bond formation in the ubiquitin E1. Proc Natl Acad Sci U S A. 2019 07 30; 116(31):15475-15484.
-
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.
-
Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase's enzymatic cycle. Nat Commun. 2019 02 18; 10(1):799.