Methyl-Accepting Chemotaxis Proteins
"Methyl-Accepting Chemotaxis Proteins" 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.
Transmembrane sensor receptor proteins that are central components of the chemotactic systems of a number of motile bacterial species which include ESCHERICHIA COLI and SALMONELLA TYPHIMURIUM. Methyl-accepting chemotaxis proteins derive their name from a sensory adaptation process which involves methylation at several glutamyl residues in their cytoplasmic domain. Methyl-accepting chemotaxis proteins trigger chemotactic responses across spatial chemical gradients, causing organisms to move either toward favorable stimuli or away from toxic ones.
| Descriptor ID |
D000072236
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| MeSH Number(s) |
D12.644.360.420 D12.776.097.533 D12.776.476.420 D12.776.543.750.054
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| Concept/Terms |
Methyl-Accepting Chemotaxis Proteins- Methyl-Accepting Chemotaxis Proteins
- Chemotaxis Proteins, Methyl-Accepting
- Methyl Accepting Chemotaxis Proteins
- Proteins, Methyl-Accepting Chemotaxis
|
Below are MeSH descriptors whose meaning is more general than "Methyl-Accepting Chemotaxis Proteins".
Below are MeSH descriptors whose meaning is more specific than "Methyl-Accepting Chemotaxis Proteins".
This graph shows the total number of publications written about "Methyl-Accepting Chemotaxis Proteins" by people in this website by year, and whether "Methyl-Accepting Chemotaxis Proteins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1999 | 0 | 1 | 1 |
| 2000 | 0 | 1 | 1 |
| 2016 | 1 | 0 | 1 |
| 2020 | 1 | 0 | 1 |
| 2021 | 1 | 0 | 1 |
| 2022 | 0 | 2 | 2 |
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Below are the most recent publications written about "Methyl-Accepting Chemotaxis Proteins" by people in Profiles.
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Analysis of CheW-like domains provides insights into organization of prokaryotic chemotaxis systems. Proteins. 2023 03; 91(3):315-329.
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Generalizable strategy to analyze domains in the context of parent protein architecture: A CheW case study. Proteins. 2022 11; 90(11):1973-1986.
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Role of Position K+4 in the Phosphorylation and Dephosphorylation Reaction Kinetics of the CheY Response Regulator. Biochemistry. 2021 07 06; 60(26):2130-2151.
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Modulation of Response Regulator CheY Reaction Kinetics by Two Variable Residues That Affect Conformation. J Bacteriol. 2020 07 09; 202(15).
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Use of restrained molecular dynamics to predict the conformations of phosphorylated receiver domains in two-component signaling systems. Proteins. 2017 01; 85(1):155-176.
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Functional roles of conserved amino acid residues surrounding the phosphorylatable histidine of the yeast phosphorelay protein YPD1. Mol Microbiol. 2000 Jul; 37(1):136-44.
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Differential stabilities of phosphorylated response regulator domains reflect functional roles of the yeast osmoregulatory SLN1 and SSK1 proteins. J Bacteriol. 1999 Jan; 181(2):411-7.
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Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry. 1993 Dec 14; 32(49):13375-80.