Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
Article Abstract:
Mechanisms involved in co- and post-translational protein oxidation in vivo are described. Endoplasmic-reticulum-resident oxido-reductases PDI and ERp57 are found to be directly involved in disulphide oxidation and isomerization. They are found to be central in glycoprotein folding in mammalian cells in the endoplasmic reticulum.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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LInking catalysts to chemistry
Article Abstract:
Molinari and Helenius have reported that folding catalysts from the protein disulphide isomerase (PDI) family, form transient chemical links with the proteins on which they act. The results demonstrate that PDIs show different specificities and act on both complete and incomplete proteins detected following labelling.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
User Contributions:
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