PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24039611-0 2013 Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model. polyglutamine 18-31 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 0-6 24039611-5 2013 Importantly, in staging experiments, Hsp104 suppressed toxicity of a C-terminal MJD fragment when expressed after the onset of PolyQ-induced degeneration, whereas Hsp70 was ineffective. polyglutamine 127-132 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 37-43 18381282-9 2008 The presence of tyrosines within polyglutamine stretches dramatically enhanced polymer fragmentation and allowed polymer propagation in the absence of Rnq1 and, in some cases, of Hsp104. polyglutamine 33-46 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 179-185 22723742-7 2012 In vitro, sHsps enhance Hsp104-catalyzed disaggregation of pathological amyloid forms of alpha-synuclein and polyglutamine. polyglutamine 109-122 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 24-30 21969373-0 2011 Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes. polyglutamine 86-99 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 66-72 21969373-1 2011 In Saccharomyces cerevisae, expanded polyglutamine (polyQ) fragments are assembled into discrete cytosolic aggregates in a process regulated by the molecular chaperones Hsp26, Hsp70, Hsp90, and Hsp104. polyglutamine 37-50 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 194-200 21969373-1 2011 In Saccharomyces cerevisae, expanded polyglutamine (polyQ) fragments are assembled into discrete cytosolic aggregates in a process regulated by the molecular chaperones Hsp26, Hsp70, Hsp90, and Hsp104. polyglutamine 52-57 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 194-200 19995551-0 2010 Hsp104 is essential for the selective degradation in yeast of polyglutamine expanded ataxin-1 but not most misfolded proteins generally. polyglutamine 62-75 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 0-6 19768774-5 2010 In yeast models of Huntington"s disease, Hsp104 is required for the aggregation and toxicity of polyglutamine (polyQ), but the expression of Hsp104 in cellular and animal models of Huntington"s and Parkinson"s disease protects against polyQ and alpha-synuclein toxicity. polyglutamine 96-109 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 41-47 19768774-5 2010 In yeast models of Huntington"s disease, Hsp104 is required for the aggregation and toxicity of polyglutamine (polyQ), but the expression of Hsp104 in cellular and animal models of Huntington"s and Parkinson"s disease protects against polyQ and alpha-synuclein toxicity. polyglutamine 111-116 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 41-47 19768774-5 2010 In yeast models of Huntington"s disease, Hsp104 is required for the aggregation and toxicity of polyglutamine (polyQ), but the expression of Hsp104 in cellular and animal models of Huntington"s and Parkinson"s disease protects against polyQ and alpha-synuclein toxicity. polyglutamine 235-240 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 141-147 15298677-0 2004 The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions. polyglutamine 56-69 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 39-45 16973603-4 2006 Strikingly, deletion of Hsp104 increases the size of inclusions formed by expanded poly(Q) lacking the proline-rich region and abolishes toxicity. polyglutamine 83-90 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 24-30 16204350-0 2005 Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington"s disease. polyglutamine 39-52 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 24-30 15845535-10 2005 Small Hsps also facilitate the Hsp104-mediated solubilization of polyglutamine in yeast. polyglutamine 65-78 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 31-37 15298677-2 2004 The molecular chaperone Hsp104 has been shown to be necessary for the aggregate formation of polyglutamine in yeast, and for the maintenance of several yeast prion phenotypes through the formation of self-propagating aggregates. polyglutamine 93-106 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 24-30 15298677-3 2004 In this paper, we show that the polyglutamine aggregates that are formed independently of Hsp104, are required for Hsp104 to efficiently produce more aggregates. polyglutamine 32-45 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 90-96 15298677-3 2004 In this paper, we show that the polyglutamine aggregates that are formed independently of Hsp104, are required for Hsp104 to efficiently produce more aggregates. polyglutamine 32-45 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 115-121 12161426-5 2002 In this study, we found that the co-expression of a long polyglutamine tract, which formed aggregates independently of the function of Hsp104, enhanced the formation of aggregates of a short polyglutamine tract in wild-type cells as well as in Deltahsp104 mutant cells. polyglutamine 57-70 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 135-141 10811890-5 2000 The toxic effect of polyglutamine expression and the formation of aggregates can be reversed by coexpression of the yeast chaperone Hsp104. polyglutamine 20-33 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 132-138 11683917-10 2001 Moreover, the dependency on Hsp104 for aggregate formation was strong with the short polyglutamine tract, and decreased with the long polyglutamine tract. polyglutamine 85-98 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 28-34 11683917-10 2001 Moreover, the dependency on Hsp104 for aggregate formation was strong with the short polyglutamine tract, and decreased with the long polyglutamine tract. polyglutamine 134-147 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 28-34 11683917-11 2001 CONCLUSION: For polyglutamine aggregate formation, a balance of parameters including the length of the polyglutamine tract, Hsp104, and level of polyglutamine expression determined its efficiency. polyglutamine 16-29 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 124-130 12058016-3 2002 Our data indicated that deficiencies in molecular chaperones Sis1 and Hsp104 inhibited seeding of polyQ aggregates, whereas ssa1, ssa2, and ydj1-151 mutations inhibited expansion of aggregates. polyglutamine 98-103 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 70-76 30595457-8 2019 We also establish that CtHsp104 antagonizes several toxic protein-misfolding events in vivo where S. cerevisiae Hsp104 is ineffective, including rescue of TDP-43, polyglutamine, and alpha-synuclein toxicity. polyglutamine 163-176 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 25-31 34424055-0 2021 Huntingtin Polyglutamine Fragments Are a Substrate for Hsp104 in Yeast. polyglutamine 11-24 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 55-61 33175887-0 2020 Hsp104-dependent ability to assimilate mannitol and sorbitol conferred by a truncated Cyc8 with a C-terminal polyglutamine in Saccharomyces cerevisiae. polyglutamine 109-122 chaperone ATPase HSP104 Saccharomyces cerevisiae S288C 0-6