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Results: 1 to 20 of 99

Related Citations for PubMed (Select 23284973)

1.

Solution structure of the oncogenic MIEN1 protein reveals a thioredoxin-like fold with a redox-active motif.

Hsu CH, Shen TL, Chang CF, Chang YY, Huang LY.

PLoS One. 2012;7(12):e52292. doi: 10.1371/journal.pone.0052292. Epub 2012 Dec 20.

2.

The oxidized subunit B8 from human complex I adopts a thioredoxin fold.

Brockmann C, Diehl A, Rehbein K, Strauss H, Schmieder P, Korn B, Kühne R, Oschkinat H.

Structure. 2004 Sep;12(9):1645-54.

PMID:
15341729
3.

The Bacillus subtilis YkuV is a thiol:disulfide oxidoreductase revealed by its redox structures and activity.

Zhang X, Hu Y, Guo X, Lescop E, Li Y, Xia B, Jin C.

J Biol Chem. 2006 Mar 24;281(12):8296-304. Epub 2006 Jan 17.

4.

Structural classification of thioredoxin-like fold proteins.

Qi Y, Grishin NV.

Proteins. 2005 Feb 1;58(2):376-88.

PMID:
15558583
5.

Redox properties of a thioredoxin-like Arabidopsis protein, AtTDX.

Kim SG, Chi YH, Lee JS, Schlesinger SR, Zabet-Moghaddam M, Chung JS, Knaff DB, Kim ST, Lee SY, Kim SK.

Biochim Biophys Acta. 2010 Dec;1804(12):2213-21. doi: 10.1016/j.bbapap.2010.09.005. Epub 2010 Sep 16.

PMID:
20849982
6.

Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer.

Weichsel A, Gasdaska JR, Powis G, Montfort WR.

Structure. 1996 Jun 15;4(6):735-51.

PMID:
8805557
7.

Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif.

Watson WH, Pohl J, Montfort WR, Stuchlik O, Reed MS, Powis G, Jones DP.

J Biol Chem. 2003 Aug 29;278(35):33408-15. Epub 2003 Jun 19.

8.

Solution structure and dynamics of ERp18, a small endoplasmic reticulum resident oxidoreductase .

Rowe ML, Ruddock LW, Kelly G, Schmidt JM, Williamson RA, Howard MJ.

Biochemistry. 2009 Jun 2;48(21):4596-606. doi: 10.1021/bi9003342.

PMID:
19361226
10.

Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function.

Alphey MS, Gabrielsen M, Micossi E, Leonard GA, McSweeney SM, Ravelli RB, Tetaud E, Fairlamb AH, Bond CS, Hunter WN.

J Biol Chem. 2003 Jul 11;278(28):25919-25. Epub 2003 Apr 21.

11.
12.

The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.

Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE.

Curr Biol. 1997 Apr 1;7(4):239-45.

15.

Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.

Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ.

J Biomol NMR. 1994 May;4(3):411-32.

PMID:
8019144
16.
17.

Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site.

Collet JF, D'Souza JC, Jakob U, Bardwell JC.

J Biol Chem. 2003 Nov 14;278(46):45325-32. Epub 2003 Sep 2.

18.
19.

Crystal structure of the DsbA protein required for disulphide bond formation in vivo.

Martin JL, Bardwell JC, Kuriyan J.

Nature. 1993 Sep 30;365(6445):464-8.

PMID:
8413591
20.

High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution.

Forman-Kay JD, Clore GM, Wingfield PT, Gronenborn AM.

Biochemistry. 1991 Mar 12;30(10):2685-98.

PMID:
2001356
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