Structural and Functional Characterization of DsbC, a Protein Involved in Disulfide Bond Formation in Escherichia coli
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00015a019
Reference55 articles.
1. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product.
2. Identification of a protein required for disulfide bond formation in vivo
3. A pathway for disulfide bond formation in vivo.
4. Direct identification of the primary nucleophile of thioredoxin f.
5. Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes
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