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Items: 1 to 20 of 124

1.

Comparative sequence, structure and redox analyses of Klebsiella pneumoniae DsbA show that anti-virulence target DsbA enzymes fall into distinct classes.

Kurth F, Rimmer K, Premkumar L, Mohanty B, Duprez W, Halili MA, Shouldice SR, Heras B, Fairlie DP, Scanlon MJ, Martin JL.

PLoS One. 2013 Nov 14;8(11):e80210. doi: 10.1371/journal.pone.0080210.

2.

Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar typhimurium.

Heras B, Totsika M, Jarrott R, Shouldice SR, Guncar G, Achard ME, Wells TJ, Argente MP, McEwan AG, Schembri MA.

J Biol Chem. 2010 Jun 11;285(24):18423-32. doi: 10.1074/jbc.M110.101360.

3.

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.

4.

Four structural subclasses of the antivirulence drug target disulfide oxidoreductase DsbA provide a platform for design of subclass-specific inhibitors.

McMahon RM, Premkumar L, Martin JL.

Biochim Biophys Acta. 2014 Aug;1844(8):1391-401. doi: 10.1016/j.bbapap.2014.01.013. Review.

PMID:
24487020
5.

Structure and function of DsbA, a key bacterial oxidative folding catalyst.

Shouldice SR, Heras B, Walden PM, Totsika M, Schembri MA, Martin JL.

Antioxid Redox Signal. 2011 May 1;14(9):1729-60. doi: 10.1089/ars.2010.3344. Review.

PMID:
21241169
6.

Structure and function of the oxidoreductase DsbA1 from Neisseria meningitidis.

Vivian JP, Scoullar J, Rimmer K, Bushell SR, Beddoe T, Wilce MC, Byres E, Boyle TP, Doak B, Simpson JS, Graham B, Heras B, Kahler CM, Rossjohn J, Scanlon MJ.

J Mol Biol. 2009 Dec 18;394(5):931-43. doi: 10.1016/j.jmb.2009.09.065.

PMID:
19815019
7.

Characterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uropathogenic Escherichia coli CFT073.

Totsika M, Heras B, Wurpel DJ, Schembri MA.

J Bacteriol. 2009 Jun;191(12):3901-8. doi: 10.1128/JB.00143-09.

8.

Peptide inhibitors of the Escherichia coli DsbA oxidative machinery essential for bacterial virulence.

Duprez W, Premkumar L, Halili MA, Lindahl F, Reid RC, Fairlie DP, Martin JL.

J Med Chem. 2015 Jan 22;58(2):577-87. doi: 10.1021/jm500955s.

PMID:
25470204
9.

Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae.

Hu SH, Peek JA, Rattigan E, Taylor RK, Martin JL.

J Mol Biol. 1997 Apr 25;268(1):137-46.

PMID:
9149147
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.

11.

Characterization of the DsbA oxidative folding catalyst from Pseudomonas aeruginosa reveals a highly oxidizing protein that binds small molecules.

Shouldice SR, Heras B, Jarrott R, Sharma P, Scanlon MJ, Martin JL.

Antioxid Redox Signal. 2010 Apr 15;12(8):921-31. doi: 10.1089/ars.2009.2736.

PMID:
19788398
12.

The oxidase DsbA folds a protein with a nonconsecutive disulfide.

Messens J, Collet JF, Van Belle K, Brosens E, Loris R, Wyns L.

J Biol Chem. 2007 Oct 26;282(43):31302-7.

13.

Isolation and characterization of a chromosomally encoded disulphide oxidoreductase from Salmonella enterica serovar Typhimurium.

Turcot I, Ponnampalam TV, Bouwman CW, Martin NL.

Can J Microbiol. 2001 Aug;47(8):711-21.

PMID:
11575497
14.

Rv2969c, essential for optimal growth in Mycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases.

Premkumar L, Heras B, Duprez W, Walden P, Halili M, Kurth F, Fairlie DP, Martin JL.

Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):1981-94. doi: 10.1107/S0907444913017800.

15.
16.

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.

17.

[Study on disulfide bond formation protein A in Escherichia coli].

Luo M, Guan YX, Yao SJ.

Sheng Wu Gong Cheng Xue Bao. 2007 Jan;23(1):7-15. Review. Chinese.

PMID:
17366881
18.

Application of fragment-based screening to the design of inhibitors of Escherichia coli DsbA.

Adams LA, Sharma P, Mohanty B, Ilyichova OV, Mulcair MD, Williams ML, Gleeson EC, Totsika M, Doak BC, Caria S, Rimmer K, Horne J, Shouldice SR, Vazirani M, Headey SJ, Plumb BR, Martin JL, Heras B, Simpson JS, Scanlon MJ.

Angew Chem Int Ed Engl. 2015 Feb 9;54(7):2179-84. doi: 10.1002/anie.201410341.

PMID:
25556635
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