"Allosteric Site" 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.
A site on an enzyme which upon binding of a modulator, causes the enzyme to undergo a conformational change that may alter its catalytic or binding properties.
Descriptor ID |
D000495
|
MeSH Number(s) |
G02.111.570.120.147
|
Concept/Terms |
Allosteric Site- Allosteric Site
- Allosteric Sites
- Site, Allosteric
- Sites, Allosteric
|
Below are MeSH descriptors whose meaning is more general than "Allosteric Site".
Below are MeSH descriptors whose meaning is more specific than "Allosteric Site".
This graph shows the total number of publications written about "Allosteric Site" by people in this website by year, and whether "Allosteric Site" 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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2008 | 1 | 0 | 1 |
2017 | 1 | 7 | 8 |
2018 | 1 | 3 | 4 |
2019 | 0 | 1 | 1 |
2020 | 0 | 1 | 1 |
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Below are the most recent publications written about "Allosteric Site" by people in Profiles.
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Free Energy Landscapes from SARS-CoV-2 Spike Glycoprotein Simulations Suggest that RBD Opening Can Be Modulated via Interactions in an Allosteric Pocket. J Am Chem Soc. 2021 08 04; 143(30):11349-11360.
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Repurposing of FDA-approved drugs against active site and potential allosteric drug-binding sites of COVID-19 main protease. Proteins. 2021 11; 89(11):1425-1441.
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Interfacial Water Many-Body Effects Drive Structural Dynamics and Allosteric Interactions in SARS-CoV-2 Main Protease Dimerization Interface. J Phys Chem Lett. 2021 Jul 08; 12(26):6218-6226.
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Discovery of chebulagic acid and punicalagin as novel allosteric inhibitors of SARS-CoV-2 3CLpro. Antiviral Res. 2021 06; 190:105075.
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Exploring the Allosteric Territory of Protein Function. J Phys Chem B. 2021 04 22; 125(15):3763-3780.
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X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease. Science. 2021 05 07; 372(6542):642-646.
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Mapping major SARS-CoV-2 drug targets and assessment of druggability using computational fragment screening: Identification of an allosteric small-molecule binding site on the Nsp13 helicase. PLoS One. 2021; 16(2):e0246181.
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SARS-CoV-2 S protein:ACE2 interaction reveals novel allosteric targets. Elife. 2021 02 08; 10.
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Dynamics and electrostatics define an allosteric druggable site within the receptor-binding domain of SARS-CoV-2 spike protein. FEBS Lett. 2021 02; 595(4):442-451.
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Drug Repurposing for Candidate SARS-CoV-2 Main Protease Inhibitors by a Novel In Silico Method. Molecules. 2020 Aug 23; 25(17).