PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25918398-5	2015	We found that elevated expression of molecular chaperones, such as Hsp40 and Hsp70, in a group of cells improves proteostasis in other groups of cells, both in cultured cells and in Drosophila expressing aggregation-prone polyglutamine proteins.	polyglutamine	222-235	Heat-shock-protein-70Ab	Drosophila melanogaster	77-82	
25918398-7	2015	Addition of Hsp40/Hsp70-containing exosomes to the culture medium of the polyglutamine-expressing cells results in efficient suppression of inclusion body formation, indicating that molecular chaperones non-cell autonomously improve the protein-folding environment via exosome-mediated transmission.	polyglutamine	73-86	Heat-shock-protein-70Ab	Drosophila melanogaster	18-23	
17536173-0	2007	Polyglutamine expansion in Drosophila: thermal stress and Hsp70 as selective agents.	polyglutamine	0-13	Heat-shock-protein-70Ab	Drosophila melanogaster	58-63	
18344983-7	2008	Furthermore, it is upregulated in the brain upon overexpression of poly-glutamine expanded protein and recruited with the chaperone Hsp70 into protein aggregates.	polyglutamine	67-81	Heat-shock-protein-70Ab	Drosophila melanogaster	132-137	
17536173-7	2007	Hsp70 also promotes tolerance of natural thermal stress in Drosophila and diverse organisms,a role which may deplete the chaperone from buffering against polyQ toxicity.	polyglutamine	154-159	Heat-shock-protein-70Ab	Drosophila melanogaster	0-5	
16039613-2	2005	Constitutive overexpression of the Hsp70 molecular chaperone is capable of suppressing polyglutamine neurodegeneration.	polyglutamine	87-100	Heat-shock-protein-70Ab	Drosophila melanogaster	35-40	
16039613-5	2005	We further showed that cellular heat shock response remained intact in aged flies, indicating the decline of Hsp70 levels observed in polyglutamine-expressing flies is not due to normal ageing.	polyglutamine	134-147	Heat-shock-protein-70Ab	Drosophila melanogaster	109-114	
16039613-6	2005	In contrast to the well-documented polyglutamine suppression caused by constitutive Hsp70 overexpression, no suppression of degeneration was observed when inducible copies of hsp70 transgenes were instead coexpressed.	polyglutamine	35-48	Heat-shock-protein-70Ab	Drosophila melanogaster	84-89	
16039613-7	2005	This supports a transcriptional dysregulation of endogenous hsp70 gene induction in polyglutamine flies.	polyglutamine	84-97	Heat-shock-protein-70Ab	Drosophila melanogaster	60-65	
16009936-0	2005	cAMP-response element-binding protein and heat-shock protein 70 additively suppress polyglutamine-mediated toxicity in Drosophila.	polyglutamine	84-97	Heat-shock-protein-70Ab	Drosophila melanogaster	42-63	
16009936-6	2005	As reported previously, overexpression of heat-shock protein 70 (Hsp70) rescues polyglutamine-dependent lethality.	polyglutamine	80-93	Heat-shock-protein-70Ab	Drosophila melanogaster	42-63	
16009936-6	2005	As reported previously, overexpression of heat-shock protein 70 (Hsp70) rescues polyglutamine-dependent lethality.	polyglutamine	80-93	Heat-shock-protein-70Ab	Drosophila melanogaster	65-70	
16009936-8	2005	The protective effects of CREB and heat-shock protein 70 against polyQ are additive, suggesting that targeting multiple pathways may be effective for treatment of polyglutamine diseases.	polyglutamine	65-70	Heat-shock-protein-70Ab	Drosophila melanogaster	35-56	
10581028-0	1999	Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70.	polyglutamine	15-28	Heat-shock-protein-70Ab	Drosophila melanogaster	97-102	
10581028-6	1999	Using a Drosophila melanogaster model of polyglutamine disease, we show that directed expression of the molecular chaperone HSP70 suppresses polyglutamine-induced neurodegeneration in vivo.	polyglutamine	41-54	Heat-shock-protein-70Ab	Drosophila melanogaster	124-129	
10581028-6	1999	Using a Drosophila melanogaster model of polyglutamine disease, we show that directed expression of the molecular chaperone HSP70 suppresses polyglutamine-induced neurodegeneration in vivo.	polyglutamine	141-154	Heat-shock-protein-70Ab	Drosophila melanogaster	124-129	
10581028-7	1999	Suppression by HSP70 occurred without a visible effect on NI formation, indicating that polyglutamine toxicity can be dissociated from formation of large aggregates.	polyglutamine	88-101	Heat-shock-protein-70Ab	Drosophila melanogaster	15-20