PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25231079-3	2014	We found that the aggregates formed by polyQ-expanded Atx3 sequester its interacting partners, such as P97/VCP and ubiquitin conjugates, into the protein inclusions through specific interactions both in vitro and in cells.	polyglutamine	39-44	valosin containing protein	Homo sapiens	103-110	
18798739-11	2008	The control of VCP expression is also proposed to be a potential therapeutic target in ex-polyQ-induced neurodegenerative diseases [12].	polyglutamine	90-95	valosin containing protein	Homo sapiens	15-18	
18715868-5	2008	Co-expression of an aggregate prone protein such as expanded polyglutamine in IBMPFD mutant cells results in an increase in aggregated protein that localizes to small inclusions instead of a single perinuclear aggresome.	polyglutamine	61-74	valosin containing protein	Homo sapiens	78-84	
18715868-9	2008	Expression of HDAC6 improves aggresome formation and protects IBMPFD mutant cells from polyglutamine-induced cell death.	polyglutamine	87-100	valosin containing protein	Homo sapiens	62-68	
17584300-7	2007	VCP was involved in the clearance of pre-formed polyglutamine aggregates as well.	polyglutamine	48-61	valosin containing protein	Homo sapiens	0-3	
18208395-7	2008	VCP was also involved in the clearance of pre-formed polyglutamine aggregates.	polyglutamine	53-66	valosin containing protein	Homo sapiens	0-3	
18208395-8	2008	Paradoxically, VCP knockdown also diminished polyglutamine aggregate formation.	polyglutamine	45-58	valosin containing protein	Homo sapiens	15-18	
17584300-8	2007	Paradoxically, VCP knockdown also diminished polyglutamine aggregate formation.	polyglutamine	45-58	valosin containing protein	Homo sapiens	15-18	
16822850-7	2006	AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta.	polyglutamine	129-142	valosin containing protein	Homo sapiens	10-13	
16822850-7	2006	AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta.	polyglutamine	129-142	valosin containing protein	Homo sapiens	14-17	
16822850-7	2006	AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta.	polyglutamine	129-142	valosin containing protein	Homo sapiens	227-230	
16822850-7	2006	AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta.	polyglutamine	190-203	valosin containing protein	Homo sapiens	10-13	
16822850-7	2006	AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta.	polyglutamine	190-203	valosin containing protein	Homo sapiens	14-17	
16822850-7	2006	AT3 binds VCP/p97, a key protein responsible for extracting ERAD substrates from the ER; binding is modulated by the size of the polyglutamine tract, and mutating a sequence adjacent to the polyglutamine tract inhibits the AT3-VCP interaction and AT3-dependent accumulation of CD3delta.	polyglutamine	190-203	valosin containing protein	Homo sapiens	227-230	
12938736-6	2003	In this review, we summarize recent findings on such ambiguous effects of molecular chaperones on polyglutamine diseases, and discuss possible mechanisms by which molecular chaperones, especially VCP, are involved in the pathogenesis.	polyglutamine	98-111	valosin containing protein	Homo sapiens	196-199	
12784666-7	2002	VCP co-localizes not only with polyglutamine aggregates but also other protein aggregates and Lewy bodies.	polyglutamine	31-44	valosin containing protein	Homo sapiens	0-3	
11598795-3	2001	Endogenous VCP co-localized with expanded polyQ (ex-polyQ) aggregates in cultured cells expressing ex-polyQ, with nuclear inclusions in Huntington disease patient brains, and with Lewy bodies in patient samples.	polyglutamine	42-47	valosin containing protein	Homo sapiens	11-14	
11598795-3	2001	Endogenous VCP co-localized with expanded polyQ (ex-polyQ) aggregates in cultured cells expressing ex-polyQ, with nuclear inclusions in Huntington disease patient brains, and with Lewy bodies in patient samples.	polyglutamine	52-57	valosin containing protein	Homo sapiens	11-14	
11598795-3	2001	Endogenous VCP co-localized with expanded polyQ (ex-polyQ) aggregates in cultured cells expressing ex-polyQ, with nuclear inclusions in Huntington disease patient brains, and with Lewy bodies in patient samples.	polyglutamine	52-57	valosin containing protein	Homo sapiens	11-14