PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22131404-2	2011	The androgen receptor (AR) is substantially modified, in response to hormone binding, by phosphorylation, sumoylation, and acetylation; these modifications might thus contribute to DHT-dependent polyglutamine (polyQ)-expanded AR proteotoxicity in spinal and bulbar muscular atrophy (SBMA).	polyglutamine	195-208	androgen receptor	Homo sapiens	4-21	
22131404-2	2011	The androgen receptor (AR) is substantially modified, in response to hormone binding, by phosphorylation, sumoylation, and acetylation; these modifications might thus contribute to DHT-dependent polyglutamine (polyQ)-expanded AR proteotoxicity in spinal and bulbar muscular atrophy (SBMA).	polyglutamine	195-208	androgen receptor	Homo sapiens	23-25	
22131404-2	2011	The androgen receptor (AR) is substantially modified, in response to hormone binding, by phosphorylation, sumoylation, and acetylation; these modifications might thus contribute to DHT-dependent polyglutamine (polyQ)-expanded AR proteotoxicity in spinal and bulbar muscular atrophy (SBMA).	polyglutamine	195-208	androgen receptor	Homo sapiens	283-287	
22131404-2	2011	The androgen receptor (AR) is substantially modified, in response to hormone binding, by phosphorylation, sumoylation, and acetylation; these modifications might thus contribute to DHT-dependent polyglutamine (polyQ)-expanded AR proteotoxicity in spinal and bulbar muscular atrophy (SBMA).	polyglutamine	210-215	androgen receptor	Homo sapiens	4-21	
22131404-2	2011	The androgen receptor (AR) is substantially modified, in response to hormone binding, by phosphorylation, sumoylation, and acetylation; these modifications might thus contribute to DHT-dependent polyglutamine (polyQ)-expanded AR proteotoxicity in spinal and bulbar muscular atrophy (SBMA).	polyglutamine	210-215	androgen receptor	Homo sapiens	23-25	
22131404-2	2011	The androgen receptor (AR) is substantially modified, in response to hormone binding, by phosphorylation, sumoylation, and acetylation; these modifications might thus contribute to DHT-dependent polyglutamine (polyQ)-expanded AR proteotoxicity in spinal and bulbar muscular atrophy (SBMA).	polyglutamine	210-215	androgen receptor	Homo sapiens	283-287	
22131404-4	2011	Our studies reveal that SIRT1 also offers protection against polyQ-expanded AR by deacetylating the AR at lysines 630/632/633.	polyglutamine	61-66	androgen receptor	Homo sapiens	76-78	
22131404-4	2011	Our studies reveal that SIRT1 also offers protection against polyQ-expanded AR by deacetylating the AR at lysines 630/632/633.	polyglutamine	61-66	androgen receptor	Homo sapiens	100-102	
22131404-5	2011	This finding suggested that nuclear AR acetylation plays a role in the aberrant metabolism and toxicity of polyQ-expanded AR.	polyglutamine	107-112	androgen receptor	Homo sapiens	36-38	
22131404-5	2011	This finding suggested that nuclear AR acetylation plays a role in the aberrant metabolism and toxicity of polyQ-expanded AR.	polyglutamine	107-112	androgen receptor	Homo sapiens	122-124	
22131404-6	2011	Subsequent studies revealed that the polyQ-expanded AR is hyperacetylated and that pharmacologic reduction of acetylation reduces mutant AR aggregation.	polyglutamine	37-42	androgen receptor	Homo sapiens	52-54	
22131404-7	2011	Moreover, genetic mutation to inhibit polyQ-expanded AR acetylation of lysines 630/632/633 substantially decreased its aggregation and completely abrogated its toxicity in cell lines and motor neurons.	polyglutamine	38-43	androgen receptor	Homo sapiens	53-55	
22131404-8	2011	Our studies also reveal one means by which the AR acetylation state likely modifies polyQ-expanded AR metabolism and toxicity, through its effect on DHT-dependent AR stabilization.	polyglutamine	84-89	androgen receptor	Homo sapiens	47-49	
22131404-8	2011	Our studies also reveal one means by which the AR acetylation state likely modifies polyQ-expanded AR metabolism and toxicity, through its effect on DHT-dependent AR stabilization.	polyglutamine	84-89	androgen receptor	Homo sapiens	99-101	
22131404-8	2011	Our studies also reveal one means by which the AR acetylation state likely modifies polyQ-expanded AR metabolism and toxicity, through its effect on DHT-dependent AR stabilization.	polyglutamine	84-89	androgen receptor	Homo sapiens	99-101	
22131404-9	2011	Overall, our findings reveal a neuroprotective function of SIRT1 that operates through its deacetylation of polyQ-expanded AR and highlight the potential of both SIRT1 and AR acetylation as powerful therapeutic targets in SBMA.	polyglutamine	108-113	androgen receptor	Homo sapiens	123-125