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Article

Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.

The Journal of biological chemistry - 9 Dec 1994

Lyles M M, Gilbert H F

Abstract excerpt

Protein disulfide isomerase (PDI), a foldase of the endoplasmic recticulum, is a multifunctional protein that catalyzes the formation and isomerization of disulfide bonds during protein folding. The wild-type protein contains two redox active thiol/disulfide sites near the N and C terminus that are homologous to the redox center of thioredoxin. Using site-directed mutagenesis, both cysteines of each of the...

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PMID: 7983029

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

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Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.PMID 7983029Read ↗

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