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Article

Thioredoxin A active-site mutants form mixed disulfide dimers that resemble enzyme-substrate reaction intermediates.

Journal of molecular biology - 6 Jun 2008

Kouwen Thijs R H M, Andréll Juni, Schrijver Rianne, Dubois Jean-Yves F, Maher Megan J, Iwata So, Carpenter Elisabeth P, van Dijl Jan Maarten

Abstract excerpt

Thioredoxin functions in nearly all organisms as the major thiol-disulfide oxidoreductase within the cytosol. Its prime purpose is to maintain cysteine-containing proteins in the reduced state by converting intramolecular disulfide bonds into dithiols in a disulfide exchange reaction. Thioredoxin has been reported to contribute to a wide variety of physiological functions by interacting with specific sets of...

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Identifiers

PMID: 18455736
DOI: 10.1016/j.jmb.2008.03.077
PMCID: PMC2896474

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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