Pathways of disulfide bond formation in Escherichia coli
(2006) The International Journal of Biochemistry & Cell Biology — Vol. 38, n° 7, p. 1050-1062 (2006)
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- 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. (c) 2005 Elsevier Ltd. All rights reserved.
- Affiliations
Université catholique de Louvain Christian de Duve Institute of Cellular Pathology
Citations
Messens, J., & Collet, J.-F. (2006). Pathways of disulfide bond formation in Escherichia coli. The International Journal of Biochemistry & Cell Biology, 38(7), 1050-1062. https://doi.org/10.1016/j.biocel.2005.12.011 (Original work published 2006)