NDLI: Disulfide Bond Formation in the Mammalian Endoplasmic Reticulum

Content Provider	PubMed Central
Author	Bulleid, Neil J.
Copyright Year	2012
Abstract	The formation of disulfide bonds between cysteine residues occurs during the folding of many proteins that enter the secretory pathway. As the polypeptide chain collapses, cysteines brought into proximity can form covalent linkages during a process catalyzed by members of the protein disulfide isomerase family. There are multiple pathways in mammalian cells to ensure disulfides are introduced into proteins. Common requirements for this process include a disulfide exchange protein and a protein oxidase capable of forming disulfides de novo. In addition, any incorrect disulfides formed during the normal folding pathway are removed in a process involving disulfide exchange. The pathway for the reduction of disulfides remains poorly characterized. This work will cover the current knowledge in the field and discuss areas for future investigation.
Related Links	http://dx.doi.org/10.1101/cshperspect.a013219
Starting Page	13219
File Format	PDF
ISSN	19430264
e-ISSN	19430264
Journal	Cold Spring Harbor Perspectives in Biology
Issue Number	11
Volume Number	4
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2012-11-01
Access Restriction	Open
Rights Holder	Cold Spring Harbor Laboratory Press
Subject Keyword	Medicine(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry, Genetics and Molecular Biology

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Disulfide Bond Formation in the Mammalian Endoplasmic Reticulum