"Isomerases" 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 class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
| Descriptor ID |
D007535
|
| MeSH Number(s) |
D08.811.399
|
| Concept/Terms |
|
Below are MeSH descriptors whose meaning is more general than "Isomerases".
Below are MeSH descriptors whose meaning is more specific than "Isomerases".
This graph shows the total number of publications written about "Isomerases" by people in this website by year, and whether "Isomerases" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 1 | 1 | 2 |
| 1995 | 2 | 0 | 2 |
| 1996 | 1 | 1 | 2 |
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Below are the most recent publications written about "Isomerases" by people in Profiles.
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Effects of mutations in genes for proteins involved in disulphide bond formation in the periplasm on the activities of anaerobically induced electron transfer chains in Escherichia coli K12. Mol Gen Genet. 1996 Nov 27; 253(1-2):95-102.
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New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol Microbiol. 1996 Aug; 21(4):871-84.
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Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 1995 Jul 17; 14(14):3415-24.
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Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry. 1995 Apr 18; 34(15):5075-89.
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The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins. Mol Endocrinol. 1994 Oct; 8(10):1407-19.
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The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 1994 Apr 15; 13(8):2013-20.
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Structure and chromosomal localization of the human gene for a brain form of prostaglandin D2 synthase. J Biol Chem. 1992 Nov 15; 267(32):23202-8.
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A helix-turn-strand structural motif common in alpha-beta proteins. Proteins. 1990; 8(4):334-40.
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Purification and properties of methylmalonyl coenzyme A mutase from human liver. Arch Biochem Biophys. 1982 Apr 01; 214(2):815-23.
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Inherited methylmalonyl CoA mutase apoenzyme deficiency in human fibroblasts: evidence for allelic heterogeneity, genetic compounds, and codominant expression. J Clin Invest. 1980 Mar; 65(3):690-8.