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Items: 1 to 20 of 104

1.

The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.

Goeckeler JL, Petruso AP, Aguirre J, Clement CC, Chiosis G, Brodsky JL.

FEBS Lett. 2008 Jul 9;582(16):2393-6. doi: 10.1016/j.febslet.2008.05.047. Epub 2008 Jun 6.

2.

Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.

Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU.

EMBO J. 2006 Jun 7;25(11):2519-28. Epub 2006 May 11.

3.
4.

Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.

Polier S, Dragovic Z, Hartl FU, Bracher A.

Cell. 2008 Jun 13;133(6):1068-79. doi: 10.1016/j.cell.2008.05.022.

5.

Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.

Shaner L, Sousa R, Morano KA.

Biochemistry. 2006 Dec 19;45(50):15075-84.

6.

Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.

Mattoo RU, Sharma SK, Priya S, Finka A, Goloubinoff P.

J Biol Chem. 2013 Jul 19;288(29):21399-411. doi: 10.1074/jbc.M113.479253. Epub 2013 Jun 4.

7.

Hsp110 is a nucleotide-activated exchange factor for Hsp70.

Andréasson C, Fiaux J, Rampelt H, Mayer MP, Bukau B.

J Biol Chem. 2008 Apr 4;283(14):8877-84. doi: 10.1074/jbc.M710063200. Epub 2008 Jan 24.

8.

Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.

Raviol H, Sadlish H, Rodriguez F, Mayer MP, Bukau B.

EMBO J. 2006 Jun 7;25(11):2510-8. Epub 2006 May 11.

9.

Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae.

Kryndushkin D, Wickner RB.

Mol Biol Cell. 2007 Jun;18(6):2149-54. Epub 2007 Mar 28.

10.

Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding.

Yam AY, Albanèse V, Lin HT, Frydman J.

J Biol Chem. 2005 Dec 16;280(50):41252-61. Epub 2005 Oct 11.

11.

The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb.

Shaner L, Wegele H, Buchner J, Morano KA.

J Biol Chem. 2005 Dec 16;280(50):41262-9. Epub 2005 Oct 12.

12.

Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein.

Polier S, Hartl FU, Bracher A.

J Mol Biol. 2010 Sep 3;401(5):696-707. doi: 10.1016/j.jmb.2010.07.004. Epub 2010 Jul 17.

PMID:
20624400
13.

The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.

Andréasson C, Rampelt H, Fiaux J, Druffel-Augustin S, Bukau B.

J Biol Chem. 2010 Apr 16;285(16):12445-53. doi: 10.1074/jbc.M109.096735. Epub 2010 Feb 20.

14.

Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity.

Andréasson C, Fiaux J, Rampelt H, Druffel-Augustin S, Bukau B.

Proc Natl Acad Sci U S A. 2008 Oct 28;105(43):16519-24. doi: 10.1073/pnas.0804187105. Epub 2008 Oct 23.

15.
16.

Metazoan Hsp70 machines use Hsp110 to power protein disaggregation.

Rampelt H, Kirstein-Miles J, Nillegoda NB, Chi K, Scholz SR, Morimoto RI, Bukau B.

EMBO J. 2012 Nov 5;31(21):4221-35. doi: 10.1038/emboj.2012.264. Epub 2012 Sep 18.

17.

Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity.

Goeckeler JL, Stephens A, Lee P, Caplan AJ, Brodsky JL.

Mol Biol Cell. 2002 Aug;13(8):2760-70.

18.

The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates.

Ziegelhoffer T, Lopez-Buesa P, Craig EA.

J Biol Chem. 1995 May 5;270(18):10412-9.

19.

The control of spindle length by Hsp70 and Hsp110 molecular chaperones.

Makhnevych T, Houry WA.

FEBS Lett. 2013 Apr 17;587(8):1067-72. doi: 10.1016/j.febslet.2013.02.018. Epub 2013 Feb 19. Review.

20.

The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s.

Easton DP, Kaneko Y, Subjeck JR.

Cell Stress Chaperones. 2000 Oct;5(4):276-90. Review.

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