| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1951313 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2008 | 5 Pages |
Abstract
Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase. This review discusses the current knowledge about disulfide isomerization in prokaryotes.
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Authors
Stefan Gleiter, James C.A. Bardwell,