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- W2914706125 abstract "The formation of disulfide bonds is critical to the folding of many extracytoplasmic proteins in all domains of life. With the discovery in the early 1990s that disulfide bond formation is catalyzed by enzymes, the field of oxidative folding of proteins was born. Escherichia coli played a central role as a model organism for the elucidation of the disulfide bond-forming machinery. Since then, many of the enzymatic players and their mechanisms of forming, breaking, and shuffling disulfide bonds have become understood in greater detail. This article summarizes the discoveries of the past 3 decades, focusing on disulfide bond formation in the periplasm of the model prokaryotic host E. coli ." @default.
- W2914706125 created "2019-02-21" @default.
- W2914706125 creator A5005378529 @default.
- W2914706125 creator A5015858246 @default.
- W2914706125 creator A5025082724 @default.
- W2914706125 date "2019-02-06" @default.
- W2914706125 modified "2023-10-14" @default.
- W2914706125 title "Disulfide Bond Formation in the Periplasm of <i>Escherichia coli</i>" @default.
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