PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9038938-0	1997	ATP-dependent regulation of a G protein-coupled K+ channel (GIRK1/GIRK4) expressed in oocytes.	Adenosine Triphosphate	0-3	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	60-65	
15749783-2	2005	Based on the crystal structure of the tetrameric C-terminal domain of Kir3.1, it is possible to build a homology model of the ATP-binding C-terminal domain of Kir6.2.	Adenosine Triphosphate	126-129	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	70-76	
12860923-10	2003	Based on these results and the recently published structure of Kir3.1 cytoplasmic domain, we propose a scheme where binding of the beta phosphate group of ATP to K185 induces a motion of the surrounding region, which destabilizes the open state, favouring closure of the M2 gate.	Adenosine Triphosphate	155-158	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	63-69	
12805206-6	2003	A molecular model of the C-terminus of Kir6.2 (based on the crystal structure of Kir3.1) was constructed and automated docking was used to identify residues interacting with ATP.	Adenosine Triphosphate	174-177	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	81-87	
9038938-7	1997	Addition of 1 mM ATP, but not adenylimidodiphosphate, to inside-out patches resulted in increases in NP zero (4.8-fold) and the open-time duration of GIRK1/GIRK4, such that tau zero were 1.2 +/- 0.2 (32%) and 6.2 +/- 0.6 ms (68%).	Adenosine Triphosphate	17-20	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	150-155	
9038938-11	1997	In oocytes the ATP-dependent step is dominant and thus provides a major component of the total GIRK1/GIRK4 current activated by ACh.	Adenosine Triphosphate	15-18	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	95-100