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A cytosolic network suppressing mitochondria-mediated proteostatic stress and cell death.

Wang X, Chen XJ.

Nature. 2015 Aug 27;524(7566):481-4. doi: 10.1038/nature14859. Epub 2015 Jul 20.


Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients.

Erives AJ, Fassler JS.

PLoS One. 2015 Feb 24;10(2):e0117192. doi: 10.1371/journal.pone.0117192. eCollection 2015.


Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation.

Dulle JE, Stein KC, True HL.

PLoS One. 2014 Jan 23;9(1):e87521. doi: 10.1371/journal.pone.0087521. eCollection 2014.


The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.

Wolfe KJ, Ren HY, Trepte P, Cyr DM.

Mol Biol Cell. 2013 Dec;24(23):3588-602. doi: 10.1091/mbc.E13-06-0315. Epub 2013 Oct 9.


COPII machinery cooperates with ER-localized Hsp40 to sequester misfolded membrane proteins into ER-associated compartments.

Kakoi S, Yorimitsu T, Sato K.

Mol Biol Cell. 2013 Mar;24(5):633-42. doi: 10.1091/mbc.E12-08-0639. Epub 2013 Jan 9.


Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity.

Mathur V, Seuring C, Riek R, Saupe SJ, Liebman SW.

Mol Cell Biol. 2012 Jan;32(1):139-53. doi: 10.1128/MCB.06125-11. Epub 2011 Oct 28.


Molecular chaperone Hsp104 can promote yeast prion generation.

Kryndushkin DS, Engel A, Edskes H, Wickner RB.

Genetics. 2011 Jun;188(2):339-48. doi: 10.1534/genetics.111.127779. Epub 2011 Apr 5.


[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.


Influence of Hsp70s and their regulators on yeast prion propagation.

Masison DC, Kirkland PA, Sharma D.

Prion. 2009 Apr-Jun;3(2):65-73. Epub 2009 Apr 29. Review.


Prion propagation by Hsp40 molecular chaperones.

Summers DW, Douglas PM, Cyr DM.

Prion. 2009 Apr-Jun;3(2):59-64. Epub 2009 Apr 20. Review.


Hsp70 structure, function, regulation and influence on yeast prions.

Sharma D, Masison DC.

Protein Pept Lett. 2009;16(6):571-81. Review.


Prion proteostasis: Hsp104 meets its supporting cast.

Sweeny EA, Shorter J.

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


Chaperone effects on prion and nonprion aggregates.

Rikhvanov EG, Romanova NV, Chernoff YO.

Prion. 2007 Oct-Dec;1(4):217-22. Epub 2007 Oct 6. Review.


The yeast Sup35NM domain propagates as a prion in mammalian cells.

Krammer C, Kryndushkin D, Suhre MH, Kremmer E, Hofmann A, Pfeifer A, Scheibel T, Wickner RB, Schätzl HM, Vorberg I.

Proc Natl Acad Sci U S A. 2009 Jan 13;106(2):462-7. doi: 10.1073/pnas.0811571106. Epub 2008 Dec 29.


The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype.

Pezza JA, Langseth SX, Raupp Yamamoto R, Doris SM, Ulin SP, Salomon AR, Serio TR.

Mol Biol Cell. 2009 Feb;20(3):1068-80. doi: 10.1091/mbc.E08-04-0436. Epub 2008 Dec 10.


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.


Curing of the [URE3] prion by Btn2p, a Batten disease-related protein.

Kryndushkin DS, Shewmaker F, Wickner RB.

EMBO J. 2008 Oct 22;27(20):2725-35. doi: 10.1038/emboj.2008.198. Epub 2008 Oct 2.


Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.

Wickner RB, Shewmaker F, Kryndushkin D, Edskes HK.

Bioessays. 2008 Oct;30(10):955-64. doi: 10.1002/bies.20821. Review.


Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.

Needham PG, Masison DC.

Arch Biochem Biophys. 2008 Oct 15;478(2):167-74. doi: 10.1016/ Epub 2008 Aug 6.


Functionally redundant isoforms of a yeast Hsp70 chaperone subfamily have different antiprion effects.

Sharma D, Masison DC.

Genetics. 2008 Jul;179(3):1301-11. doi: 10.1534/genetics.108.089458. Epub 2008 Jun 18.

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