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Items: 1 to 20 of 307

1.
2.
3.

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.

4.

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.

5.

Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.

Kaimal JM, Kandasamy G, Gasser F, Andréasson C.

Mol Cell Biol. 2017 May 16;37(11). pii: e00027-17. doi: 10.1128/MCB.00027-17. Print 2017 Jun 1.

6.

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.

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 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.

9.

Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.

Shorter J, Lindquist S.

EMBO J. 2008 Oct 22;27(20):2712-24. doi: 10.1038/emboj.2008.194. Epub 2008 Oct 2.

10.

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
11.

The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner.

Sielaff B, Tsai FT.

J Mol Biol. 2010 Sep 10;402(1):30-7. doi: 10.1016/j.jmb.2010.07.030. Epub 2010 Jul 21.

12.

Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.

O'Driscoll J, Clare D, Saibil H.

J Cell Biol. 2015 Oct 12;211(1):145-58. doi: 10.1083/jcb.201505104. Epub 2015 Oct 5.

13.

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.

14.

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.

15.

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.

16.

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.

17.

The mammalian Hsp40 ERdj3 requires its Hsp70 interaction and substrate-binding properties to complement various yeast Hsp40-dependent functions.

Vembar SS, Jin Y, Brodsky JL, Hendershot LM.

J Biol Chem. 2009 Nov 20;284(47):32462-71. doi: 10.1074/jbc.M109.000729. Epub 2009 Sep 11.

18.

Human and yeast Hsp110 chaperones exhibit functional differences.

Raviol H, Bukau B, Mayer MP.

FEBS Lett. 2006 Jan 9;580(1):168-74. Epub 2005 Dec 9.

20.

[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.

Hines JK, Li X, Du Z, Higurashi T, Li L, Craig EA.

PLoS Genet. 2011 Feb;7(2):e1001309. doi: 10.1371/journal.pgen.1001309. Epub 2011 Feb 17. Erratum in: PLoS Genet. 2011 Feb;7(2). doi: 10.1371/annotation/65a80750-95f9-40a1-a509-64ee5febbaa3.

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