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- W2138152079 endingPage "a013219" @default.
- W2138152079 startingPage "a013219" @default.
- W2138152079 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." @default.
- W2138152079 created "2016-06-24" @default.
- W2138152079 creator A5008290085 @default.
- W2138152079 date "2012-11-01" @default.
- W2138152079 modified "2023-10-15" @default.
- W2138152079 title "Disulfide Bond Formation in the Mammalian Endoplasmic Reticulum" @default.
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- W2138152079 doi "https://doi.org/10.1101/cshperspect.a013219" @default.
- W2138152079 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3536336" @default.
- W2138152079 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23125019" @default.
- W2138152079 hasPublicationYear "2012" @default.
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