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Article

Studies on the function of yeast protein disulfide isomerase in renaturation of proteins.

Biochimica et biophysica acta - 9 Jul 2001

Katiyar S, Till E A, Lennarz W J

Abstract excerpt

Renaturation of two enzymes lacking disulfide bonds, citrate synthase (CS), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and another protein containing disulfide bonds, lysozyme (LZM), were studied in order to dissect the possible chaperone function from the isomerase function of yeast protein disulfide isomerase (PDI). Our findings suggest no independent chaperone activity of yeast PDI with respect to...

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Share to Citrate (si)-Synthase
Share to Glyceraldehyde-3-Phosphate Dehydrogenases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Oxidation-Reduction

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Source

Identifiers

PMID: 11451437
DOI: 10.1016/s0167-4838(01)00214-x

Genes

GAPDH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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