Substrate Specificity

"Substrate Specificity" 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

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

Descriptor ID	D013379
MeSH Number(s)	G02.111.835
Concept/Terms	Substrate Specificity Substrate Specificity Specificities, Substrate Specificity, Substrate Substrate Specificities

Below are MeSH descriptors whose meaning is more general than "Substrate Specificity".

Biological Sciences [G]
Chemical Phenomena [G02]
Biochemical Phenomena [G02.111]
Substrate Specificity [G02.111.835]

Below are MeSH descriptors whose meaning is related to "Substrate Specificity".

Below are MeSH descriptors whose meaning is more specific than "Substrate Specificity".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Substrate Specificity" by people in this website by year, and whether "Substrate Specificity" was a major or minor topic of these publications.

Bar chart showing 231 publications over 30 distinct years, with a maximum of 19 publications in 2007

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

Year	Minor Topic	Total
1994	4	4
1995	8	8
1996	2	2
1997	3	3
1998	5	5
1999	6	6
2000	8	8
2001	3	3
2002	7	7
2003	7	7
2004	6	6
2005	14	14
2006	9	9
2007	19	19
2008	8	8
2009	12	12
2010	12	12
2011	12	12
2012	10	10
2013	14	14
2014	15	15
2015	5	5
2016	8	8
2017	9	9
2018	8	8
2019	10	10
2020	1	1
2021	3	3
2022	1	1
2023	2	2

Below are the most recent publications written about "Substrate Specificity" by people in Profiles.

Gainetdinov I, Vega-Badillo J, Cecchini K, Bagci A, Colpan C, De D, Bailey S, Arif A, Wu PH, MacRae IJ, Zamore PD. Relaxed targeting rules help PIWI proteins silence transposons. Nature. 2023 Jul; 619(7969):394-402.

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Magrino J, Munford V, Martins DJ, Homma TK, Page B, Gaubitz C, Freire BL, Lerario AM, Vilar JB, Amorin A, Le?o EKE, Kok F, Menck CF, Jorge AA, Kelch BA. A thermosensitive PCNA allele underlies an ataxia-telangiectasia-like disorder. J Biol Chem. 2023 05; 299(5):104656.

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Mahmoud SA, Aldikacti B, Chien P. ATP hydrolysis tunes specificity of a AAA+ protease. Cell Rep. 2022 09 20; 40(12):111405.

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Araya LE, Soni IV, Hardy JA, Julien O. Deorphanizing Caspase-3 and Caspase-9 Substrates In and Out of Apoptosis with Deep Substrate Profiling. ACS Chem Biol. 2021 11 19; 16(11):2280-2296.

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Hou S, Lee JM, Myint W, Matsuo H, Kurt Yilmaz N, Schiffer CA. Structural basis of substrate specificity in human cytidine deaminase family APOBEC3s. J Biol Chem. 2021 08; 297(2):100909.

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Mishra AK, Lambright DG. High-Throughput Assay for Profiling the Substrate Specificity of Rab GTPase-Activating Proteins. Methods Mol Biol. 2021; 2293:27-43.

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Chaves DA, Dai H, Li L, Moresco JJ, Oh ME, Conte D, Yates JR, Mello CC, Gu W. The RNA phosphatase PIR-1 regulates endogenous small RNA pathways in C.?elegans. Mol Cell. 2021 02 04; 81(3):546-557.e5.

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O'Leary BM. The Lure of Lignin: Deciphering High-value Lignin Formation in Seed Coats. Plant Cell. 2020 12; 32(12):3652-3653.

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Adams ST, Miller SC. Enzymatic promiscuity and the evolution of bioluminescence. FEBS J. 2020 04; 287(7):1369-1380.

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Das S, Malaby AW, Nawrotek A, Zhang W, Zeghouf M, Maslen S, Skehel M, Chakravarthy S, Irving TC, Bilsel O, Cherfils J, Lambright DG. Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes. Structure. 2019 12 03; 27(12):1782-1797.e7.

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