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Active Site Mutations in Yeast Protein Disulfide Isomerase Cause Dithiothreitol Sensitivity and a Reduced Rate of Protein Folding in the Endoplasmic Reticulum

Aspects of protein disulfide isomerase (PDI) function have been studied in yeast in vivo. PDI contains two thioredoxin-like domains, a and a′, each of which contains an active-site CXXC motif. The relative importance of the two domains was analyzed by rendering each one inactive by mutation to SGAS....

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Autores principales: Holst, Bjørn, Tachibana, Christine, Winther, Jakob R.
Formato: Artigo
Lenguaje:Inglês
Publicado: The Rockefeller University Press 1997
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC2132551/
https://ncbi.nlm.nih.gov/pubmed/9298979
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