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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.


Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans.

Duennwald ML, Echeverria A, Shorter J.

PLoS Biol. 2012;10(6):e1001346. doi: 10.1371/journal.pbio.1001346. Epub 2012 Jun 19.


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.


Purification of hsp104, a protein disaggregase.

Sweeny EA, DeSantis ME, Shorter J.

J Vis Exp. 2011 Sep 30;(55). pii: 3190. doi: 10.3791/3190.


Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease.

Lo Bianco C, Shorter J, Régulier E, Lashuel H, Iwatsubo T, Lindquist S, Aebischer P.

J Clin Invest. 2008 Sep;118(9):3087-97. doi: 10.1172/JCI35781.


Applying Hsp104 to protein-misfolding disorders.

Vashist S, Cushman M, Shorter J.

Biochem Cell Biol. 2010 Feb;88(1):1-13. doi: 10.1139/o09-121. Review.


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.


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.


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.


Chaperone networks in protein disaggregation and prion propagation.

Winkler J, Tyedmers J, Bukau B, Mogk A.

J Struct Biol. 2012 Aug;179(2):152-60. doi: 10.1016/j.jsb.2012.05.002. Epub 2012 May 10. Review.


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.


Prion proteostasis: Hsp104 meets its supporting cast.

Sweeny EA, Shorter J.

Prion. 2008 Oct-Dec;2(4):135-40. Epub 2008 Oct 22. Review.


Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110.

Kuo Y, Ren S, Lao U, Edgar BA, Wang T.

Cell Death Dis. 2013 Oct 3;4:e833. doi: 10.1038/cddis.2013.351.


[Cooperation between heat shock proteins in organizing of proteins spatial structure].

Wyżewski Z, Gregorczyk KP, Szulc-Dąbrowska L, Struzik J, Szczepanowska J, Niemiałtowski M.

Postepy Hig Med Dosw (Online). 2014 Jun 9;68:793-807. Review. Polish.


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.


Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.

Desantis ME, Sweeny EA, Snead D, Leung EH, Go MS, Gupta K, Wendler P, Shorter J.

J Biol Chem. 2014 Jan 10;289(2):848-67. doi: 10.1074/jbc.M113.520759. Epub 2013 Nov 26.


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.

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