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Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast.

Kochneva-Pervukhova NV, Alexandrov AI, Ter-Avanesyan MD.

PLoS One. 2012;7(1):e29832. doi: 10.1371/journal.pone.0029832. Epub 2012 Jan 11.


Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast.

Gong H, Romanova NV, Allen KD, Chandramowlishwaran P, Gokhale K, Newnam GP, Mieczkowski P, Sherman MY, Chernoff YO.

PLoS Genet. 2012;8(4):e1002634. doi: 10.1371/journal.pgen.1002634. Epub 2012 Apr 19.


Sequestration of Sup35 by aggregates of huntingtin fragments causes toxicity of [PSI+] yeast.

Zhao X, Park YN, Todor H, Moomau C, Masison D, Eisenberg E, Greene LE.

J Biol Chem. 2012 Jul 6;287(28):23346-55. doi: 10.1074/jbc.M111.287748. Epub 2012 May 9.


Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1.

Meriin AB, Zhang X, He X, Newnam GP, Chernoff YO, Sherman MY.

J Cell Biol. 2002 Jun 10;157(6):997-1004. Epub 2002 Jun 10. Erratum in: J Cell Biol 2002 Aug 5;158(3):591.


Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model.

Gokhale KC, Newnam GP, Sherman MY, Chernoff YO.

J Biol Chem. 2005 Jun 17;280(24):22809-18. Epub 2005 Apr 11.


Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro.

Derkatch IL, Uptain SM, Outeiro TF, Krishnan R, Lindquist SL, Liebman SW.

Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12934-9. Epub 2004 Aug 23.


Protein aggregation and polyasparagine-mediated cellular toxicity in Saccharomyces cerevisiae.

Peters TW, Huang M.

Prion. 2007 Apr-Jun;1(2):144-53. Epub 2007 Apr 26.


Suppression of polyglutamine toxicity by the yeast Sup35 prion domain in Drosophila.

Li LB, Xu K, Bonini NM.

J Biol Chem. 2007 Dec 28;282(52):37694-701. Epub 2007 Oct 23.


A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates.

Kurahashi H, Ishiwata M, Shibata S, Nakamura Y.

Mol Cell Biol. 2008 May;28(10):3313-23. doi: 10.1128/MCB.01900-07. Epub 2008 Mar 10.


Appearance and propagation of polyglutamine-based amyloids in yeast: tyrosine residues enable polymer fragmentation.

Alexandrov IM, Vishnevskaya AB, Ter-Avanesyan MD, Kushnirov VV.

J Biol Chem. 2008 May 30;283(22):15185-92. doi: 10.1074/jbc.M802071200. Epub 2008 Apr 1.


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.


Biochemical and genetic methods for characterization of [PIN+] prions in yeast.

Liebman SW, Bagriantsev SN, Derkatch IL.

Methods. 2006 May;39(1):23-34.


Pathogenic polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis.

Goehler H, Dröge A, Lurz R, Schnoegl S, Chernoff YO, Wanker EE.

PLoS One. 2010 Mar 10;5(3):e9642. doi: 10.1371/journal.pone.0009642.


Aggregation-prone proteins modulate huntingtin inclusion body formation in yeast.

Kantcheva RB, Mason R, Giorgini F.

PLoS Curr. 2014 Apr 23;6. pii: ecurrents.hd.501008f3051342c9a5c0cd0f3a5bf3a4. doi: 10.1371/currents.hd.501008f3051342c9a5c0cd0f3a5bf3a4.


Wild type huntingtin toxicity in yeast: Implications for the role of amyloid cross-seeding in polyQ diseases.

Alexandrov AI, Serpionov GV, Kushnirov VV, Ter-Avanesyan MD.

Prion. 2016 May 3;10(3):221-7. doi: 10.1080/19336896.2016.1176659.


Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions.

Urakov VN, Vishnevskaya AB, Alexandrov IM, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD.

Prion. 2010 Jan-Mar;4(1):45-52. Epub 2010 Jan 18.


Cellular toxicity of yeast prion protein Rnq1 can be modulated by N-terminal wild type huntingtin.

Sethi R, Patel V, Saleh AA, Roy I.

Arch Biochem Biophys. 2016 Jan 15;590:82-9. doi: 10.1016/ Epub 2015 Nov 26.


Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.

Mathur V, Taneja V, Sun Y, Liebman SW.

Mol Biol Cell. 2010 May 1;21(9):1449-61. doi: 10.1091/mbc.E09-11-0927. Epub 2010 Mar 10.


Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models.

Ehrnhoefer DE, Duennwald M, Markovic P, Wacker JL, Engemann S, Roark M, Legleiter J, Marsh JL, Thompson LM, Lindquist S, Muchowski PJ, Wanker EE.

Hum Mol Genet. 2006 Sep 15;15(18):2743-51. Epub 2006 Aug 7.


A network of protein interactions determines polyglutamine toxicity.

Duennwald ML, Jagadish S, Giorgini F, Muchowski PJ, Lindquist S.

Proc Natl Acad Sci U S A. 2006 Jul 18;103(29):11051-6. Epub 2006 Jul 10.

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