"Allosteric Regulation" 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 modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.
| Descriptor ID |
D000494
|
| MeSH Number(s) |
G02.111.044
|
| Concept/Terms |
Allosteric Regulation- Allosteric Regulation
- Regulation, Allosteric
- Allosteric Regulations
- Regulations, Allosteric
|
Below are MeSH descriptors whose meaning is more general than "Allosteric Regulation".
Below are MeSH descriptors whose meaning is more specific than "Allosteric Regulation".
This graph shows the total number of publications written about "Allosteric Regulation" by people in this website by year, and whether "Allosteric Regulation" was a major or minor topic of these publications.
To see the data from this visualization as text,
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2014 | 0 | 1 | 1 |
| 2015 | 0 | 1 | 1 |
| 2017 | 1 | 14 | 15 |
| 2018 | 3 | 11 | 14 |
| 2019 | 0 | 4 | 4 |
| 2021 | 0 | 2 | 2 |
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Below are the most recent publications written about "Allosteric Regulation" by people in Profiles.
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Identifying SARS-CoV-2 antiviral compounds by screening for small molecule inhibitors of nsp15 endoribonuclease. Biochem J. 2021 07 16; 478(13):2465-2479.
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A SARS-CoV-2 antibody curbs viral nucleocapsid protein-induced complement hyperactivation. Nat Commun. 2021 05 11; 12(1):2697.
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Molecular basis for higher affinity of SARS-CoV-2 spike RBD for human ACE2 receptor. Proteins. 2021 09; 89(9):1134-1144.
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Comparative Perturbation-Based Modeling of the SARS-CoV-2 Spike Protein Binding with Host Receptor and Neutralizing Antibodies: Structurally Adaptable Allosteric Communication Hotspots Define Spike Sites Targeted by Global Circulating Mutations. Biochemistry. 2021 05 18; 60(19):1459-1484.
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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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The allosteric modulation of complement C5 by knob domain peptides. Elife. 2021 02 11; 10.
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Dynamic Network Modeling of Allosteric Interactions and Communication Pathways in the SARS-CoV-2 Spike Trimer Mutants: Differential Modulation of Conformational Landscapes and Signal Transmission via Cascades of Regulatory Switches. J Phys Chem B. 2021 01 28; 125(3):850-873.
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Molecular docking study of potential phytochemicals and their effects on the complex of SARS-CoV2 spike protein and human ACE2. Sci Rep. 2020 10 19; 10(1):17699.
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Allosteric Inhibition of the SARS-CoV-2 Main Protease: Insights from Mass Spectrometry Based Assays*. Angew Chem Int Ed Engl. 2020 12 21; 59(52):23544-23548.
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Molecular Simulations and Network Modeling Reveal an Allosteric Signaling in the SARS-CoV-2 Spike Proteins. J Proteome Res. 2020 11 06; 19(11):4587-4608.