PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11114300-3	2001	Addition of phenylarsine oxide (PAO), an inhibitor of PTP, reversibly reduced K(+) current by 55% in oocytes coinjected with ROMK1 and cSrc.	oxophenylarsine	12-30	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	125-130	
11114300-3	2001	Addition of phenylarsine oxide (PAO), an inhibitor of PTP, reversibly reduced K(+) current by 55% in oocytes coinjected with ROMK1 and cSrc.	oxophenylarsine	32-35	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	125-130	
11114300-5	2001	Moreover, application of herbimycin A, an inhibitor of PTK, increased K(+) current by 120% and completely abolished the effect of PAO in oocytes coexpressing ROMK1 and cSrc.	oxophenylarsine	130-133	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	158-163	
11114300-6	2001	The effects of herbimycin A and PAO were absent in oocytes expressing the ROMK1 mutant R1Y337A in which the tyrosine residue at position 337 was mutated to alanine.	oxophenylarsine	32-35	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	74-79	
11114300-8	2001	Moreover, the effect of PAO was completely abolished by treatment of oocytes with 20% sucrose and 250 microg/ml concanavalin A, agents that inhibit the endocytosis of ROMK1 channels.	oxophenylarsine	24-27	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	167-172	
11719519-4	2002	Patch clamp studies have shown that phenylarsine oxide (PAO), an inhibitor of PTP, decreased the activity of ROMK1.	oxophenylarsine	36-54	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	109-114	
11719519-4	2002	Patch clamp studies have shown that phenylarsine oxide (PAO), an inhibitor of PTP, decreased the activity of ROMK1.	oxophenylarsine	56-59	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	109-114	
11719519-6	2002	Also, PAO treatment significantly increased the phosphorylation of ROMK1.	oxophenylarsine	6-9	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	67-72	
11719519-7	2002	The notion that the effect of PAO is mediated by stimulating tyrosine phosphorylation-induced endocytosis of ROMK1 has also been supported by findings that mutating the tyrosine residue 337 of ROMK1 to alanine abolished the effect of PAO.	oxophenylarsine	30-33	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	109-114	
11719519-7	2002	The notion that the effect of PAO is mediated by stimulating tyrosine phosphorylation-induced endocytosis of ROMK1 has also been supported by findings that mutating the tyrosine residue 337 of ROMK1 to alanine abolished the effect of PAO.	oxophenylarsine	30-33	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	193-198	
11719519-7	2002	The notion that the effect of PAO is mediated by stimulating tyrosine phosphorylation-induced endocytosis of ROMK1 has also been supported by findings that mutating the tyrosine residue 337 of ROMK1 to alanine abolished the effect of PAO.	oxophenylarsine	234-237	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	109-114	
11719519-7	2002	The notion that the effect of PAO is mediated by stimulating tyrosine phosphorylation-induced endocytosis of ROMK1 has also been supported by findings that mutating the tyrosine residue 337 of ROMK1 to alanine abolished the effect of PAO.	oxophenylarsine	234-237	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	193-198	
11719519-8	2002	Finally, the inhibitory effect of PAO on ROMK1 was completely blocked in the cells co-transfected with dominant negative dynamin (dynaminK44A).	oxophenylarsine	34-37	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	41-46