- 10.1110/ps.051464705Access the most recent version at doi: 2005 14: 1863-1869Protein Sci.
- The CXXC Motif Is More than a Redox Rheostat*S Received for publication,June 28, 2007, and in revised form, July 25, 2007 Published, JBC Papers in Press,August 3, 2007, DOI 10.1074/jbc.M705291200
- Key Players Involved in Bacterial Disulfide-Bond Jacqueline T. Tan and James C. A. Bardwell*[a]
- Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm
- Structure, Vol. 9, 377387, May, 2001, 2001 Elsevier Science Ltd. All rights reserved. PII S0969-2126(01)00599-8 Activation of the Redox-Regulated Molecular
- A R T I C L E S 262 VOLUME 18 NUMBER 3 MARCH 2011 NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Molecular Cell Optimizing Protein Stability In Vivo
- Disulfide bond isomerization in prokaryotes Stefan Gleiter, James C.A. Bardwell
- Laboratory Evolution of Escherichia coli Thioredoxin for Enhanced Catalysis of Protein Oxidation in the Periplasm
- Kinetic Characterization of the Disulfide Bond-forming Enzyme DsbB*S
- JOURNAL OF BACTERIOLOGY, Oct. 2006, p. 73177320 Vol. 188, No. 20 0021-9193/06/$08.00 0 doi:10.1128/JB.00383-06
- Copper Stress Causes an in Vivo Requirement for the Escherichia coli Disulfide Isomerase DsbC*
- JOURNAL OF BACTERIOLOGY, Feb. 2005, p. 15041510 Vol. 187, No. 4 0021-9193/05/$08.00 0 doi:10.1128/JB.187.4.15041510.2005
- Thioredoxin 2, an Oxidative Stress-induced Protein, Contains a High Affinity Zinc Binding Site*
- Developmental Cell that the decrease in differentiation efficiency due to ge-tissues appear to possess populations of primitive pre-
- DsbB Catalyzes Disulfide Bond Formation de Novo* Received for publication, May 31, 2002, and in revised form, June 13, 2002
- JOURNAL OF BACTERIOLOGY, May 2002, p. 26922698 Vol. 184, No. 10 0021-9193/02/$04.00 0 DOI: 10.1128/JB.184.10.26922698.2002
- 2002 Blackwell Science Ltd MicroReview
- Identification of the Ubiquinone-binding Domain in the Disulfide Catalyst Disulfide Bond Protein B*
- JOURNAL OF BACTERIOLOGY, 0021-9193/01/$04.00 0 DOI: 10.1128/JB.183.3.980988.2001
- Molecular Cell, Vol. 6, 349360, August, 2000, Copyright 2000 by Cell Press RNA Methylation under Heat Shock Control
- news and views NATURE CELL BIOLOGY | VOL 1 | JULY 1999 | cellbio.nature.com E57
- DsbC activation by the N-terminal domain of DsbD David Goldstone*, Peter W. Haebel*, Federico Katzen
- Disulfide bond formation involves a quinhydrone-type chargetransfer complex
- Cell, Vol. 96, 341352, February 5, 1999, Copyright 1999 by Cell Press Chaperone Activity with a Redox Switch
- Disulfide relays between and within proteins: the Ero1p structure
- Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway
- repressed chromatin state can be propagated in cis over short or long distances from initial
- Redox Switch of Hsp33 Has a Novel Zinc-binding Motif* Received for publication, July 6, 2000, and in revised form August 29, 2000
- from E. coli and the 3 terminator re-gion from Agrobacterium tumefaciens
- Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue*S
- DsbG, a Protein Disulfide Isomerase with Chaperone Activity* Received for publication, October 6, 1999, and in revised form, February 9, 2000
- Reconstitution of a Disulfide Isomerization System* Received for publication, March 28, 2002, and in revised form, May 8, 2002
- Disulfide-Linked Protein Folding Pathways
- A New Heat Shock Protein That Binds Nucleic Acids* (Received for publication, August 20, 1998, and in revised form, September 28, 1998)
- Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding
- Cell, Vol. 98, 217227, July 23, 1999, Copyright 1999 by Cell Press Oxidative Protein Folding Is Driven
- 10.1110/ps.062268106Access the most recent version at doi: 2006 15: 2217-2227Protein Sci.
- Disulfide Bonds Are Generated by Quinone Reduction* Received for publication, May 5, 2000, and in revised form, June 13, 2000
- Protein refolding by pH-triggered chaperone binding and release
- Leading Edge Synthetic Biology Select
- Evolving Protein Stability through Genetic Selection
- Molecular Cell Optimizing Protein Stability In Vivo
- NATURE CHEMICAL BIOLOGY | VOL 6 | FEBRUARY 2010 | www.nature.com/naturechemicalbiology 81 research highlights
- The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner
- Current Topics Disulfide Bond Isomerization in Prokaryotes
- Mutants in DsbB that Appear to Redirect Oxidation through the Disulfide Isomerization Pathway
- Laboratory evolution of one disulfide isomerase to resemble another
- Protein refolding by pH-triggered chaperone binding and release
- Vol. 170, No. 7 Ancient Heat Shock Gene Is Dispensable
- Gram-positive DsbE Proteins Function Differently from Gram-negative DsbE Homologs
- In Vivo Substrate Specificity of Periplasmic Disulfide Oxidoreductases*
- Proc. Natl. Acad. Sci. USA Vol. 84, pp. 5177-5181, August 1987
- Proc. Nati. Acad. Sci. USA Vol. 81, pp. 848-852, February 1984
- Reconstitution of a Protein Disulfide Catalytic System* (Received for publication, December 4, 1997)
- Proc. Nati. Acad. Sci. USA Vol. 82, pp. 2679-2683, May 1985
- The EMBO Journal vol.8 no. 1 1 pp. 3401 -3407, 1 989 Autoregulation of RNase III operon by mRNA processing
- Cell, Vol. 74, 769-771, September10, 1993, Copyright0 1993by Cell Press The Bonds That Tie: Catalyzed
- THEJOURNALOF BIOLOGICALCHEMISTRY 0 1986by The American Society of Biological Chemists, Inc.
- Vol. 172, No. 10JOURNAL OF BACTERIOLOGY, Oct. 1990, p. 6042-6047 0021-9193/90/106042-06$02.00/0
- Cell, Vol. 67, 581-569. November 1, 1991, Copyright 0 1991 by Cell Press Identification of a Protein Required for
- Molecular Microbioiogy (1994) 14(2). 199-205 MicroReview
- Protein Science (1997). 6:1148-1156. Cambridge University Press. Printed in the USA. Copyright 0 1997 The Protein Society
- Protein Science (1997), 6:1893-1900. Cambridge University Press. Printed in the USA. Copyright 0 1997The Protein Society
- from the cytosol markedly stimulated MVL formation, whereas control antibodies had no
