Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference36 articles.
1. Identification of a protein required for disulfide bond formation in vivo
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4. A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae Rd.
5. A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae
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