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Items: 1 to 20 of 24

1.
nDsbD: a redox interaction hub in the Escherichia coli periplasm
C. U. Stirnimann, M. G. Grütter, R. Glockshuber, G. Capitani
Cell Mol Life Sci. 2006 Jul; 63(14): 1642–1648. Published online 2006 Jun 19. doi: 10.1007/s00018-006-6055-1
PMCID:
PMC11136120
AbstractArticlePDF–957K
2.
Local frustration determines loop opening during the catalytic cycle of an oxidoreductase
Lukas S Stelzl, Despoina AI Mavridou, Emmanuel Saridakis, Diego Gonzalez, Andrew J Baldwin, Stuart J Ferguson, Mark SP Sansom, Christina Redfield
eLife. 2020; 9: e54661. Published online 2020 Jun 22. doi: 10.7554/eLife.54661
PMCID:
PMC7347389
AbstractArticlePDF–4.1M
3.
TrbB from Conjugative Plasmid F Is a Structurally Distinct Disulfide Isomerase That Requires DsbD for Redox State Maintenance
Casey W. Hemmis, Mehmet Berkmen, Markus Eser, Joel F. Schildbach
J Bacteriol. 2011 Sep; 193(18): 4588–4597. doi: 10.1128/JB.00351-11
PMCID:
PMC3165698
AbstractArticlePDF–807K
4.
Control of Periplasmic Interdomain Thiol:Disulfide Exchange in the Transmembrane Oxidoreductase DsbD
Despoina A. I. Mavridou, Julie M. Stevens, Alan D. Goddard, Antony C. Willis, Stuart J. Ferguson, Christina Redfield
J Biol Chem. 2009 Jan 30; 284(5): 3219–3226. doi: 10.1074/jbc.M805963200
PMCID:
PMC2631958
AbstractArticlePDF–597K
5.
Evidence for Conformational Changes within DsbD: Possible Role for Membrane-Embedded Proline Residues
Annie Hiniker, Didier Vertommen, James C. A. Bardwell, Jean-Francois Collet
J Bacteriol. 2006 Oct; 188(20): 7317–7320. doi: 10.1128/JB.00383-06
PMCID:
PMC1636233
AbstractArticlePDF–176K
6.
Mutations of the Membrane-Bound Disulfide Reductase DsbD That Block Electron Transfer Steps from Cytoplasm to Periplasm in Escherichia coli
Seung-Hyun Cho, Jon Beckwith
J Bacteriol. 2006 Jul; 188(14): 5066–5076. doi: 10.1128/JB.00368-06
PMCID:
PMC1539965
AbstractArticlePDF–553K
7.
Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD
Federico Katzen, Jon Beckwith
Proc Natl Acad Sci U S A. 2003 Sep 2; 100(18): 10471–10476. Published online 2003 Aug 18. doi: 10.1073/pnas.1334136100
PMCID:
PMC193585
AbstractArticlePDF–459K
8.
Protein folding in the bacterial periplasm.
D Missiakas, S Raina
J Bacteriol. 1997 Apr; 179(8): 2465–2471. doi: 10.1128/jb.179.8.2465-2471.1997
PMCID:
PMC178991
SummaryPDF–174K
9.
Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD
Federico Katzen, Meenal Deshmukh, Fevzi Daldal, Jon Beckwith
EMBO J. 2002 Aug 1; 21(15): 3960–3969. doi: 10.1093/emboj/cdf405
PMCID:
PMC126151
AbstractArticlePDF–363K
10.
An in vivo pathway for disulfide bond isomerization in Escherichia coli
Arne Rietsch, Dominique Belin, Nancy Martin, Jonathan Beckwith
Proc Natl Acad Sci U S A. 1996 Nov 12; 93(23): 13048–13053. doi: 10.1073/pnas.93.23.13048
PMCID:
PMC24044
AbstractArticlePDF–338K
11.
Genetic and morphological characterization of an Escherichia coli chromosome segregation mutant.
P S Stewart, R D'Ari
J Bacteriol. 1992 Jul; 174(13): 4513–4516. doi: 10.1128/jb.174.13.4513-4516.1992
PMCID:
PMC206241
SummaryPage BrowsePDF–1.0M
12.
Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.
A Rietsch, P Bessette, G Georgiou, J Beckwith
J Bacteriol. 1997 Nov; 179(21): 6602–6608. doi: 10.1128/jb.179.21.6602-6608.1997
PMCID:
PMC179585
SummaryPDF–710K
13.
The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC–DsbDα complex
Peter W. Haebel, David Goldstone, Federico Katzen, Jon Beckwith, Peter Metcalf
EMBO J. 2002 Sep 16; 21(18): 4774–4784. doi: 10.1093/emboj/cdf489
PMCID:
PMC126285
AbstractArticlePDF–433K
14.
DsbC activation by the N-terminal domain of DsbD
David Goldstone, Peter W. Haebel, Federico Katzen, Martin W. Bader, James C. A. Bardwell, Jon Beckwith, Peter Metcalf
Proc Natl Acad Sci U S A. 2001 Aug 14; 98(17): 9551–9556. Published online 2001 Aug 7. doi: 10.1073/pnas.171315498
PMCID:
PMC55490
AbstractArticlePDF–245K
15.
Two Snapshots of Electron Transport across the Membrane: INSIGHTS INTO THE STRUCTURE AND FUNCTION OF DsbD
Seung-Hyun Cho, Jon Beckwith
J Biol Chem. 2009 Apr 24; 284(17): 11416–11424. doi: 10.1074/jbc.M900651200
PMCID:
PMC2670147
AbstractArticlePDF–660K
16.
The disulfide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner
Didier Vertommen, Matthieu Depuydt, Jonathan Pan, Pauline Leverrier, Laurent Knoops, Jean-Pierre Szikora, Joris Messens, James C.A. Bardwell, Jean-Francois Collet
Mol Microbiol. Author manuscript; available in PMC 2009 Jan 7.
Published in final edited form as: Mol Microbiol. 2008 Jan; 67(2): 336–349. Published online 2007 Nov 25. doi: 10.1111/j.1365-2958.2007.06030.x
PMCID:
PMC2614554
AbstractArticlePDF–789K
17.
Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA
John H. Bushweller
J Mol Biol. Author manuscript; available in PMC 2021 Aug 21.
Published in final edited form as: J Mol Biol. 2020 Aug 21; 432(18): 5091–5103. Published online 2020 Apr 16. doi: 10.1016/j.jmb.2020.04.008
PMCID:
PMC7485265
AbstractArticlePDF–800K
18.
Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli.
E J Stewart, F Katzen, J Beckwith
EMBO J. 1999 Nov 1; 18(21): 5963–5971. doi: 10.1093/emboj/18.21.5963
PMCID:
PMC1171662
SummaryPDF–300K
19.
Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD
Anna Rozhkova, Christian U Stirnimann, Patrick Frei, Ulla Grauschopf, René Brunisholz, Markus G Grütter, Guido Capitani, Rudi Glockshuber
EMBO J. 2004 Apr 21; 23(8): 1709–1719. Published online 2004 Apr 1. doi: 10.1038/sj.emboj.7600178
PMCID:
PMC394233
AbstractArticlePDF–425K
20.
Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes.
V Burland, G Plunkett, 3rd, H J Sofia, D L Daniels, F R Blattner
Nucleic Acids Res. 1995 Jun 25; 23(12): 2105–2119. doi: 10.1093/nar/23.12.2105
PMCID:
PMC306997
SummaryPage BrowsePDF–2.5M

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