PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17884923-8	2007	PIP(2) depletion via endogenous PLC-coupled alpha1 adrenergic receptors causes inhibition of endogenous Kir3.1/3.4 channel currents by about 75%.	Phosphatidylinositol 4,5-Diphosphate	0-6	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	104-110	
18725531-4	2008	Homology modeling of this putative PIP(2)-binding linker in Kv7.2 and Kv7.3 using the solved structure of Kir2.1 and Kir3.1 channels as templates predicts a structure of Kv7.2 and 7.3 very similar to the Kir channels, and to the seven-beta-sheet barrel motif common to other PIP(2)-binding domains.	Phosphatidylinositol 4,5-Diphosphate	35-41	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	117-123	
18725531-4	2008	Homology modeling of this putative PIP(2)-binding linker in Kv7.2 and Kv7.3 using the solved structure of Kir2.1 and Kir3.1 channels as templates predicts a structure of Kv7.2 and 7.3 very similar to the Kir channels, and to the seven-beta-sheet barrel motif common to other PIP(2)-binding domains.	Phosphatidylinositol 4,5-Diphosphate	275-281	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	117-123	
10085101-9	1999	PIP2 dramatically increased the open probability of GIRK1/GIRK2 channels in the absence of Na+ or Gbetagamma but did not preclude further activation by Na+, suggesting that Na+ is not acting simply to promote PIP2 binding to GIRKs.	Phosphatidylinositol 4,5-Diphosphate	0-4	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	52-57	
18690021-5	2007	Here we test members of each of the three families, Kir3.1/Kir3.4, KCNQ1/KCNE1 and TREK-1 channels, all of which have been shown to be regulated directly by phosphatidylinositol bisphosphate (PIP2).	Phosphatidylinositol 4,5-Diphosphate	192-196	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	52-58	
11353868-6	2001	The mutated GIRK1 and GIRK2 (GIRK1/2) channels containing the high-affinity phosphatidylinositol 4,5-bisphosphate (PIP(2)) domain from IRK1, on the other hand, showed dramatically less inhibition with bupivacaine.	Phosphatidylinositol 4,5-Diphosphate	76-113	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	12-17	
10085101-9	1999	PIP2 dramatically increased the open probability of GIRK1/GIRK2 channels in the absence of Na+ or Gbetagamma but did not preclude further activation by Na+, suggesting that Na+ is not acting simply to promote PIP2 binding to GIRKs.	Phosphatidylinositol 4,5-Diphosphate	209-213	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	52-57	
9486652-6	1998	Consistent with the faster dissociation of PIP2 from the GIRK channels, the carboxy terminus of GIRK1 binds 3H-PIP2 liposomes more weakly than does that of IRK1 or ROMK1.	Phosphatidylinositol 4,5-Diphosphate	43-47	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	96-101	
9486652-9	1998	When GIRK1/4 channels are allowed to run down completely, they are not activated by addition of Gbetagamma alone, but application of PIP2 activates them in minutes without Gbetagamma and in just seconds with Gbetagamma.	Phosphatidylinositol 4,5-Diphosphate	133-137	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	5-10