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Items: 1 to 20 of 116

1.

The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism.

Janda I, Devedjiev Y, Derewenda U, Dauter Z, Bielnicki J, Cooper DR, Graf PC, Joachimiak A, Jakob U, Derewenda ZS.

Structure. 2004 Oct;12(10):1901-7.

2.

Activation of the redox-regulated chaperone Hsp33 by domain unfolding.

Graf PC, Martinez-Yamout M, VanHaerents S, Lilie H, Dyson HJ, Jakob U.

J Biol Chem. 2004 May 7;279(19):20529-38. Epub 2004 Mar 15.

3.

Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity.

Kim SJ, Jeong DG, Chi SW, Lee JS, Ryu SE.

Nat Struct Biol. 2001 May;8(5):459-66.

PMID:
11323724
4.

The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold.

Won HS, Low LY, Guzman RD, Martinez-Yamout M, Jakob U, Dyson HJ.

J Mol Biol. 2004 Aug 20;341(4):893-9.

PMID:
15328602
5.

Activation of the redox-regulated molecular chaperone Hsp33--a two-step mechanism.

Graumann J, Lilie H, Tang X, Tucker KA, Hoffmann JH, Vijayalakshmi J, Saper M, Bardwell JC, Jakob U.

Structure. 2001 May 9;9(5):377-87.

6.

The 2.2 A crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity.

Vijayalakshmi J, Mukhergee MK, Graumann J, Jakob U, Saper MA.

Structure. 2001 May 9;9(5):367-75.

7.

Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity.

Chi SW, Jeong DG, Woo JR, Lee HS, Park BC, Kim BY, Erikson RL, Ryu SE, Kim SJ.

FEBS Lett. 2011 Feb 18;585(4):664-70. doi: 10.1016/j.febslet.2011.01.029. Epub 2011 Jan 23.

8.

Redox-regulated molecular chaperones.

Graf PC, Jakob U.

Cell Mol Life Sci. 2002 Oct;59(10):1624-31. Review.

PMID:
12475172
9.

Redox switch of hsp33 has a novel zinc-binding motif.

Jakob U, Eser M, Bardwell JC.

J Biol Chem. 2000 Dec 8;275(49):38302-10.

10.

Functional characterization of Hsp33 protein from Bacillus psychrosaccharolyticus; additional function of HSP33 on resistance to solvent stress.

Kang HJ, Heo DH, Choi SW, Kim KN, Shim J, Kim CW, Sung HC, Yun CW.

Biochem Biophys Res Commun. 2007 Jul 6;358(3):743-50. Epub 2007 May 7.

PMID:
17512907
11.

Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone.

Cremers CM, Reichmann D, Hausmann J, Ilbert M, Jakob U.

J Biol Chem. 2010 Apr 9;285(15):11243-51. doi: 10.1074/jbc.M109.084350. Epub 2010 Feb 5.

12.

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.

13.
14.

Redox-regulated chaperone function and conformational changes of Escherichia coli Hsp33.

Raman B, Siva Kumar LV, Ramakrishna T, Mohan Rao C.

FEBS Lett. 2001 Jan 26;489(1):19-24.

15.

Chaperone activity with a redox switch.

Jakob U, Muse W, Eser M, Bardwell JC.

Cell. 1999 Feb 5;96(3):341-52.

16.

Semi-Empirical Structure Determination of Escherichia coli Hsp33 and Identification of Dynamic Regulatory Elements for the Activation Process.

Lee YS, Lee J, Ryu KS, Lee Y, Jung TG, Jang JH, Sim DW, Kim EH, Seo MD, Lee KW, Won HS.

J Mol Biol. 2015 Dec 4;427(24):3850-61. doi: 10.1016/j.jmb.2015.09.029. Epub 2015 Oct 8.

PMID:
26453802
17.

Oligomeric Hsp33 with enhanced chaperone activity: gel filtration, cross-linking, and small angle x-ray scattering (SAXS) analysis.

Akhtar MW, Srinivas V, Raman B, Ramakrishna T, Inobe T, Maki K, Arai M, Kuwajima K, Rao ChM.

J Biol Chem. 2004 Dec 31;279(53):55760-9. Epub 2004 Oct 19.

18.
19.

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.

20.

Identification of a redox-regulated chaperone network.

Hoffmann JH, Linke K, Graf PC, Lilie H, Jakob U.

EMBO J. 2004 Jan 14;23(1):160-8. Epub 2003 Dec 11.

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