Jon Beckwith

The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm.

J. Beckwith, L. Debarbieux, Laurent Debarbieux, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin

Paul H. Bessette, J. Beckwith, G. Georgiou, 1997, Journal of bacteriology.

An in vivo pathway for disulfide bond isomerization in Escherichia coli.

D. Belin, J. Beckwith, A. Rietsch, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA.

J. Beckwith, C. Guilhot, N. Martin, 1995, Proceedings of the National Academy of Sciences of the United States of America.

A pathway for disulfide bond formation in vivo.

D. Belin, J. Beckwith, J. Bardwell, 1993, Proceedings of the National Academy of Sciences of the United States of America.