"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 |
|---|
| 2002 | 0 | 2 | 2 |
| 2003 | 0 | 4 | 4 |
| 2004 | 0 | 2 | 2 |
| 2005 | 0 | 2 | 2 |
| 2006 | 0 | 5 | 5 |
| 2008 | 0 | 1 | 1 |
| 2010 | 0 | 2 | 2 |
| 2011 | 0 | 2 | 2 |
| 2012 | 0 | 1 | 1 |
| 2013 | 0 | 2 | 2 |
| 2014 | 0 | 4 | 4 |
| 2015 | 0 | 4 | 4 |
| 2016 | 0 | 4 | 4 |
| 2017 | 1 | 31 | 32 |
| 2018 | 4 | 29 | 33 |
| 2019 | 0 | 14 | 14 |
| 2020 | 1 | 25 | 26 |
| 2021 | 1 | 14 | 15 |
To return to the timeline, click here.
Below are the most recent publications written about "Catalytic Domain" by people in Profiles.
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Repurposing existing drugs: identification of SARS-CoV-2 3C-like protease inhibitors. J Enzyme Inhib Med Chem. 2021 Dec; 36(1):147-153.
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Structure of the multiple functional domains from coronavirus nonstructural protein 3. Emerg Microbes Infect. 2021 Dec; 10(1):66-80.
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Zinc thiotropolone combinations as inhibitors of the SARS-CoV-2 main protease. Dalton Trans. 2021 Sep 14; 50(35):12226-12233.
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NMPylation and de-NMPylation of SARS-CoV-2 nsp9 by the NiRAN domain. Nucleic Acids Res. 2021 09 07; 49(15):8822-8835.
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OFF-State-Specific Inhibition of the Proprotein Convertase Furin. ACS Chem Biol. 2021 09 17; 16(9):1692-1700.
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Discovery of juglone and its derivatives as potent SARS-CoV-2 main proteinase inhibitors. Eur J Med Chem. 2021 Dec 05; 225:113789.
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Pharmacophore-Based Virtual Screening, Quantum Mechanics Calculations, and Molecular Dynamics Simulation Approaches Identified Potential Natural Antiviral Drug Candidates against MERS-CoV S1-NTD. Molecules. 2021 Aug 17; 26(16).
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Near-physiological-temperature serial crystallography reveals conformations of SARS-CoV-2 main protease active site for improved drug repurposing. Structure. 2021 12 02; 29(12):1382-1396.e6.
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Inhibition of Cysteine Proteases by 6,6'-Dihydroxythiobinupharidine (DTBN) from Nuphar lutea. Molecules. 2021 Aug 05; 26(16).
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1,10/1,11-Cyclization catalyzed by diverged plant sesquiterpene synthases is dependent on a single residue. Org Biomol Chem. 2021 08 05; 19(30):6650-6656.