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Items: 1 to 20 of 146

1.

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.

2.

Hsp110 is required for spindle length control.

Makhnevych T, Wong P, Pogoutse O, Vizeacoumar FJ, Greenblatt JF, Emili A, Houry WA.

J Cell Biol. 2012 Aug 20;198(4):623-36. doi: 10.1083/jcb.201111105.

3.

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.

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 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.

7.

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.

8.

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.

9.

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.

10.

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.

11.

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.

12.

Swapping nucleotides, tuning Hsp70.

Cyr DM.

Cell. 2008 Jun 13;133(6):945-7. doi: 10.1016/j.cell.2008.05.036.

13.

Coordinated activation of Hsp70 chaperones.

Steel GJ, Fullerton DM, Tyson JR, Stirling CJ.

Science. 2004 Jan 2;303(5654):98-101.

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Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system.

Mandal AK, Gibney PA, Nillegoda NB, Theodoraki MA, Caplan AJ, Morano KA.

Mol Biol Cell. 2010 May 1;21(9):1439-48. doi: 10.1091/mbc.E09-09-0779. Epub 2010 Mar 17.

17.

The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis.

Shaner L, Gibney PA, Morano KA.

Curr Genet. 2008 Jul;54(1):1-11. doi: 10.1007/s00294-008-0193-y. Epub 2008 May 14.

PMID:
18478233
18.

Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro.

Rauch JN, Gestwicki JE.

J Biol Chem. 2014 Jan 17;289(3):1402-14. doi: 10.1074/jbc.M113.521997. Epub 2013 Dec 5.

19.

Chaperone-assisted protein aggregate reactivation: Different solutions for the same problem.

Aguado A, Fernández-Higuero JA, Moro F, Muga A.

Arch Biochem Biophys. 2015 Aug 15;580:121-34. doi: 10.1016/j.abb.2015.07.006. Epub 2015 Jul 6. Review.

PMID:
26159839
20.

Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.

Abrams JL, Verghese J, Gibney PA, Morano KA.

J Biol Chem. 2014 May 9;289(19):13155-67. doi: 10.1074/jbc.M113.530014. Epub 2014 Mar 26.

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