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