PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29111377-0	2018	Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function.	polyglutamine	41-54	ataxin 3	Homo sapiens	64-72	
29111377-3	2018	In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction.	polyglutamine	101-114	ataxin 3	Homo sapiens	64-68	
29111377-3	2018	In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction.	polyglutamine	101-114	ataxin 3	Homo sapiens	71-79	
29111377-3	2018	In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction.	polyglutamine	116-121	ataxin 3	Homo sapiens	64-68	
29111377-3	2018	In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction.	polyglutamine	116-121	ataxin 3	Homo sapiens	71-79	
29111377-5	2018	Hence, we analyzed the repertoire of proteins interacting with normal and polyQ expanded ataxin-3 by mass spectrometry.	polyglutamine	74-79	ataxin 3	Homo sapiens	89-97	
29111377-6	2018	This showed that both normal and polyQ expanded ataxin-3 interacted with components of the protein quality control system and mitochondria.	polyglutamine	33-38	ataxin 3	Homo sapiens	48-56	
29111377-7	2018	Five proteins showed increased interaction with polyQ expanded ataxin-3 relative to normal and three of these were mitochondrial proteins.	polyglutamine	48-53	ataxin 3	Homo sapiens	63-71