PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20159555-3 2010 Here, we show that within the Hsp70, Hsp110, and Hsp40 (DNAJ) chaperone families, members of a subclass of the DNAJB family (particularly DNAJB6b and DNAJB8) are superior suppressors of aggregation and toxicity of disease-associated polyglutamine proteins. polyglutamine 233-246 DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1 Homo sapiens 49-54 28182921-0 2007 Hsp40 Molecules That Target to the Ubiquitin-proteasome System Decrease Inclusion Formation in Models of Polyglutamine Disease. polyglutamine 105-118 DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1 Homo sapiens 0-5 15543156-0 2004 Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. polyglutamine 61-74 DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1 Homo sapiens 10-15 12714591-3 2003 Some chaperones such as Hsp40 and Hsp70 have been identified as important regulators of polyglutamine aggregation and/or cell death in neuronal cells. polyglutamine 88-101 DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1 Homo sapiens 24-29 20166962-5 2010 Indeed, a variety of molecular chaperones such as Hsp70 and Hsp40 have been demonstrated to exert therapeutic effects against various experimental models of the polyQ diseases. polyglutamine 161-166 DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1 Homo sapiens 60-65 11400322-12 2001 As for the therapeutic strategies, the overexpression of Hsp70 and Hsp40 chaperones acted together to protect a cultured neuronal cell model of SBMA from inclusion formation and cell death by mutant AR with expanded polyglutamine tract. polyglutamine 216-229 DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1 Homo sapiens 67-72 10722721-0 2000 Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. polyglutamine 158-171 DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1 Homo sapiens 21-26 27713507-3 2016 Single overexpression of almost each individual member of the Hsp40 (DNAJ) family of chaperones efficiently reduces parkin C289G aggregation and requires interaction with and activity of endogenously expressed Hsp70 s. For DNAJB6 and DNAJB8, potent suppressors of aggregation of polyglutamine proteins for which they rely mainly on an S/T-rich region, it was found that the S/T-rich region was dispensable for suppression of parkin C289G aggregation. polyglutamine 279-292 DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1 Homo sapiens 62-67