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Items: 1 to 20 of 178

1.

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.

Pan JL, Sliskovic I, Bardwell JC.

J Mol Biol. 2008 Apr 11;377(5):1433-42. doi: 10.1016/j.jmb.2008.01.058. Epub 2008 Jan 31.

2.

De novo design and evolution of artificial disulfide isomerase enzymes analogous to the bacterial DsbC.

Arredondo S, Segatori L, Gilbert HF, Georgiou G.

J Biol Chem. 2008 Nov 14;283(46):31469-76. doi: 10.1074/jbc.M803346200. Epub 2008 Sep 9.

3.

The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.

Vertommen D, Depuydt M, Pan J, Leverrier P, Knoops L, Szikora JP, Messens J, Bardwell JC, Collet JF.

Mol Microbiol. 2008 Jan;67(2):336-49. Epub 2007 Nov 25.

4.

Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA.

Bader MW, Hiniker A, Regeimbal J, Goldstone D, Haebel PW, Riemer J, Metcalf P, Bardwell JC.

EMBO J. 2001 Apr 2;20(7):1555-62.

5.

Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways.

Segatori L, Paukstelis PJ, Gilbert HF, Georgiou G.

Proc Natl Acad Sci U S A. 2004 Jul 6;101(27):10018-23. Epub 2004 Jun 25.

6.

Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine.

Inaba K, Ito K.

Biochim Biophys Acta. 2008 Apr;1783(4):520-9. Epub 2007 Nov 26. Review.

7.

Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB.

Segatori L, Murphy L, Arredondo S, Kadokura H, Gilbert H, Beckwith J, Georgiou G.

J Biol Chem. 2006 Feb 24;281(8):4911-9. Epub 2005 Nov 9.

8.

Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA.

Chng SS, Dutton RJ, Denoncin K, Vertommen D, Collet JF, Kadokura H, Beckwith J.

Mol Microbiol. 2012 Sep;85(5):996-1006. doi: 10.1111/j.1365-2958.2012.08157.x. Epub 2012 Jul 19.

10.

The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes.

Paxman JJ, Borg NA, Horne J, Thompson PE, Chin Y, Sharma P, Simpson JS, Wielens J, Piek S, Kahler CM, Sakellaris H, Pearce M, Bottomley SP, Rossjohn J, Scanlon MJ.

J Biol Chem. 2009 Jun 26;284(26):17835-45. doi: 10.1074/jbc.M109.011502. Epub 2009 Apr 22.

11.
12.

DsbB catalyzes disulfide bond formation de novo.

Regeimbal J, Bardwell JC.

J Biol Chem. 2002 Sep 6;277(36):32706-13. Epub 2002 Jun 18.

13.
14.

Mutational analysis of the disulfide catalysts DsbA and DsbB.

Tan J, Lu Y, Bardwell JC.

J Bacteriol. 2005 Feb;187(4):1504-10.

15.

Protein disulfide bond generation in Escherichia coli DsbB-DsbA.

Inaba K.

J Synchrotron Radiat. 2008 May;15(Pt 3):199-201. doi: 10.1107/S090904950706061X. Epub 2008 Apr 18.

16.

Engineered pathways for correct disulfide bond oxidation.

Ren G, Bardwell JC.

Antioxid Redox Signal. 2011 Jun 15;14(12):2399-412. doi: 10.1089/ars.2010.3782. Epub 2011 Mar 31.

17.

NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.

Zhou Y, Cierpicki T, Jimenez RH, Lukasik SM, Ellena JF, Cafiso DS, Kadokura H, Beckwith J, Bushweller JH.

Mol Cell. 2008 Sep 26;31(6):896-908. doi: 10.1016/j.molcel.2008.08.028.

18.

DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo.

Maskos K, Huber-Wunderlich M, Glockshuber R.

J Mol Biol. 2003 Jan 17;325(3):495-513.

PMID:
12498799
20.

Structure analysis of the extracellular domain reveals disulfide bond forming-protein properties of Mycobacterium tuberculosis Rv2969c.

Wang L, Li J, Wang X, Liu W, Zhang XC, Li X, Rao Z.

Protein Cell. 2013 Aug;4(8):628-40. doi: 10.1007/s13238-013-3033-x. Epub 2013 Jul 5.

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