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Int J Biochem Cell Biol. 2006;38(7):1050-62. Epub 2006 Jan 11.

Pathways of disulfide bond formation in Escherichia coli.

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  • 1Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel (VUB), Belgium.

Abstract

Disulfide bond formation is required for the correct folding of many secreted proteins. Cells possess protein-folding catalysts to ensure that the correct pairs of cysteine residues are joined during the folding process. These enzymatic systems are located in the endoplasmic reticulum of eukaryotes or in the periplasm of Gram-negative bacteria. This review focuses on the pathways of disulfide bond formation and isomerization in bacteria, taking Escherichia coli as a model.

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