10.1111/j.1365-2958.1994.tb01281.x
Crossref journal-article
Wiley
Molecular Microbiology (311)
Abstract

SummaryDisulphides are often vital for the folding and stability of proteins. Dedicated enzymatic systems have been discovered that catalyse the formation of disulphides in the periplasm of prokaryotes. These discoveries provide compelling evidence for the actual catalysis of protein foldingin vivo.Disulphide bond formation inEscherichia coliis catalysed by at least three ‘Dsb’ proteins; DsbA, ‐B and ‐C. The DsbA protein has an extremely reactive, oxidizing disulphide which it simply donates directly to other proteins. DsbB is required for the reoxidation of DsbA. DsbC is active in disulphide rearrangements and appears to work synergistically with DsbA. The relative rarity of disulphides in cytoplasmic proteins appears to be dependent upon a disulphide‐destruction machine. One pivotal cog in this machine is thioredoxin reductase.

Bibliography

Bardwell, J. C. A. (1994). Building bridges: disulphide bond formation in the cell. Molecular Microbiology, 14(2), 199–205. Portico.

Authors 1
  1. James C. A. Bardwell (first)
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Dates
Type When
Created 18 years, 10 months ago (Oct. 27, 2006, 10:44 p.m.)
Deposited 1 year, 6 months ago (Feb. 7, 2024, 5:05 p.m.)
Indexed 6 days, 13 hours ago (Aug. 28, 2025, 7:59 a.m.)
Issued 30 years, 11 months ago (Oct. 1, 1994)
Published 30 years, 11 months ago (Oct. 1, 1994)
Published Online 18 years, 10 months ago (Oct. 27, 2006)
Published Print 30 years, 11 months ago (Oct. 1, 1994)
Funders 0

None

@article{Bardwell_1994, title={Building bridges: disulphide bond formation in the cell}, volume={14}, ISSN={1365-2958}, url={http://dx.doi.org/10.1111/j.1365-2958.1994.tb01281.x}, DOI={10.1111/j.1365-2958.1994.tb01281.x}, number={2}, journal={Molecular Microbiology}, publisher={Wiley}, author={Bardwell, James C. A.}, year={1994}, month=oct, pages={199–205} }