Allosteric Regulation

"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.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

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".

Biological Sciences [G]
Chemical Phenomena [G02]
Biochemical Phenomena [G02.111]
Allosteric Regulation [G02.111.044]

Below are MeSH descriptors whose meaning is related to "Allosteric Regulation".

Below are MeSH descriptors whose meaning is more specific than "Allosteric Regulation".

publications

Timeline | Most Recent

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.

Bar chart showing 63 publications over 27 distinct years, with a maximum of 5 publications in 2005 and 2012

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1996	0	1	1
1997	0	1	1
1998	0	2	2
1999	0	2	2
2000	0	2	2
2003	0	1	1
2004	0	1	1
2005	0	5	5
2006	1	2	3
2007	1	1	2
2008	1	1	2
2009	0	1	1
2011	1	2	3
2012	0	5	5
2013	0	1	1
2014	0	4	4
2015	1	1	2
2016	0	2	2
2017	0	4	4
2018	0	2	2
2019	2	1	3
2020	0	3	3
2021	1	0	1
2023	0	4	4
2024	0	3	3
2025	0	2	2
2026	0	1	1

Below are the most recent publications written about "Allosteric Regulation" by people in Profiles.

Maqtedar A, Rossi MA, Clerico EM, Williams RV, Gierasch LM. The nucleotide exchange factor, GrpE, modulates substrate affinity by interaction of its N-terminal tails with the DnaK substrate-binding domain. J Biol Chem. 2026 Mar; 302(3):111176.

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Smith AJ, Rahat MA, Scaramozza LJ, Eyles SJ, Hardy JA. Inhibition of Zika Virus Protease by Modulating NS2B-NS3 Interactions. Biochemistry. 2026 Jan 06; 65(1):64-76.

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Nguyen BV, ?zden C, Dong K, Koc OC, Torres-Ocampo AP, Dziedzic N, Flaherty D, Huang J, Sankara S, Abromson NL, Tomchick DR, Fissore RA, Chen J, Garman SC, Stratton MM. A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation. Nat Commun. 2025 Sep 26; 16(1):8461.

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Ogdahl JL, Chien P. Allosteric modulation of the Lon protease via ssDNA binding and local charge changes. J Biol Chem. 2025 01; 301(1):107993.

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D?az-Salinas MA, Jain A, Durham ND, Munro JB. Single-molecule imaging reveals allosteric stimulation of SARS-CoV-2 spike receptor binding domain by host sialic acid. Sci Adv. 2024 07 19; 10(29):eadk4920.

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Mpakali A, Barla I, Lu L, Ramesh KM, Thomaidis N, Stern LJ, Giastas P, Stratikos E. Mechanisms of Allosteric Inhibition of Insulin-Regulated Aminopeptidase. J Mol Biol. 2024 03 15; 436(6):168449.

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Rossi MA, Pozhidaeva AK, Clerico EM, Petridis C, Gierasch LM. New insights into the structure and function of the complex?between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE. J Biol Chem. 2024 01; 300(1):105574.

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Chen C, Zhu R, Hodge EA, D?az-Salinas MA, Nguyen A, Munro JB, Lee KK. hACE2-Induced Allosteric Activation in SARS-CoV versus SARS-CoV-2 Spike Assemblies Revealed by Structural Dynamics. ACS Infect Dis. 2023 06 09; 9(6):1180-1189.

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Pitsawong W, P?dua RAP, Grant T, Hoemberger M, Otten R, Bradshaw N, Grigorieff N, Kern D. From primordial clocks to circadian oscillators. Nature. 2023 04; 616(7955):183-189.

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Mathy CJP, Mishra P, Flynn JM, Perica T, Mavor D, Bolon DNA, Kortemme T. A complete allosteric map of a GTPase switch in its native cellular network. Cell Syst. 2023 03 15; 14(3):237-246.e7.

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