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Structural alteration of Escherichia coli Hsp31 by thermal unfolding increases chaperone activity.

Choi D, Ryu KS, Park C.

Biochim Biophys Acta. 2013 Feb;1834(2):621-8. doi: 10.1016/j.bbapap.2012.11.006. Epub 2012 Nov 30.


A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function.

Quigley PM, Korotkov K, Baneyx F, Hol WG.

Protein Sci. 2004 Jan;13(1):269-77.


Integrity of N- and C-termini is important for E. coli Hsp31 chaperone activity.

Sastry MS, Zhou W, Baneyx F.

Protein Sci. 2009 Jul;18(7):1439-47. doi: 10.1002/pro.158.


Hsp31 of Escherichia coli K-12 is glyoxalase III.

Subedi KP, Choi D, Kim I, Min B, Park C.

Mol Microbiol. 2011 Aug;81(4):926-36. doi: 10.1111/j.1365-2958.2011.07736.x. Epub 2011 Jul 6.


Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures.

Sastry MS, Korotkov K, Brodsky Y, Baneyx F.

J Biol Chem. 2002 Nov 29;277(48):46026-34. Epub 2002 Sep 15.


The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures.

Sastry MS, Quigley PM, Hol WG, Baneyx F.

Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8587-92. Epub 2004 Jun 1.


Peptidase activity of the Escherichia coli Hsp31 chaperone.

Malki A, Caldas T, Abdallah J, Kern R, Eckey V, Kim SJ, Cha SS, Mori H, Richarme G.

J Biol Chem. 2005 Apr 15;280(15):14420-6. Epub 2004 Nov 18.


Structural and biochemical studies on Vibrio cholerae Hsp31 reveals a novel dimeric form and Glutathione-independent Glyoxalase activity.

Das S, Roy Chowdhury S, Dey S, Sen U.

PLoS One. 2017 Feb 24;12(2):e0172629. doi: 10.1371/journal.pone.0172629. eCollection 2017.


Heat-induced conformational change and increased chaperone activity of lens alpha-crystallin.

Das BK, Liang JJ, Chakrabarti B.

Curr Eye Res. 1997 Apr;16(4):303-9.


Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain.

Lee SJ, Kim SJ, Kim IK, Ko J, Jeong CS, Kim GH, Park C, Kang SO, Suh PG, Lee HS, Cha SS.

J Biol Chem. 2003 Nov 7;278(45):44552-9. Epub 2003 Aug 25.


The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad.

Quigley PM, Korotkov K, Baneyx F, Hol WG.

Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3137-42. Epub 2003 Mar 5.


Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process.

Tsai CJ, Aslam K, Drendel HM, Asiago JM, Goode KM, Paul LN, Rochet JC, Hazbun TR.

J Biol Chem. 2015 Oct 9;290(41):24816-34. doi: 10.1074/jbc.M115.678367. Epub 2015 Aug 25.


The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites.

Zhao Y, Liu D, Kaluarachchi WD, Bellamy HD, White MA, Fox RO.

Protein Sci. 2003 Oct;12(10):2303-11.


Protein folding intermediates of invasin protein IbeA from Escherichia coli.

Mendu DR, Dasari VR, Cai M, Kim KS.

FEBS J. 2008 Feb;275(3):458-69. doi: 10.1111/j.1742-4658.2007.06213.x. Epub 2007 Dec 20.


Structure and mechanisms of a protein-based organelle in Escherichia coli.

Tanaka S, Sawaya MR, Yeates TO.

Science. 2010 Jan 1;327(5961):81-4. doi: 10.1126/science.1179513.


Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli.

Mujacic M, Baneyx F.

Appl Environ Microbiol. 2007 Feb;73(3):1014-8. Epub 2006 Dec 8.

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