PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24631257-2	2014	Barium blocks the inward Kir2.1 currents in a voltage-dependent manner.	Barium	0-6	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	25-31	
25205110-9	2015	To further demonstrate the role of the Kir2.1 channels during the osteogenesis, we inhibited Kir2.1 channel activity in healthy patient cells by applying extracellular Ba(2+) or using adenoviruses carrying mutant Kir2.1 channels.	Barium	168-170	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	93-99	
25205110-9	2015	To further demonstrate the role of the Kir2.1 channels during the osteogenesis, we inhibited Kir2.1 channel activity in healthy patient cells by applying extracellular Ba(2+) or using adenoviruses carrying mutant Kir2.1 channels.	Barium	168-170	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	93-99	
25223803-11	2014	Snake KIR2.1 channels became expressed at the plasmamembrane and produced typical barium sensitive (IC50 ~6muM) inward rectifier currents.	Barium	82-88	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	6-12	
24631257-3	2014	However, in this study we found that barium would impair the rectification and open Kir2.1 outward currents at a depolarized voltage, causing increment of outward current amplitudes by 43+-7% (n=5, P<0.01) after 200s barium application.	Barium	37-43	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	84-90	
24631257-6	2014	The rectification of Kir2.1 was not recovered by washing barium off, which suggested a non-competitive mechanism.	Barium	57-63	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	21-27	
17394572-8	2007	The effect of K(+) was totally inhibited by infusion (27 micromol min(-1)) of Ba(2+), an inhibitor of Kir2.1 channels.	Barium	78-80	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	102-108	
20676672-7	2010	Similarly, the sensitivity to block by barium also depended on the proportions of Kir2.1 to Kir2.2 subunits.	Barium	39-45	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	82-88	
19834614-6	2009	Studies of the analogous mutation in the mammalian inward rectifier Kir2.1 show that the T-->S mutation affects barium block as well as the stability of the conductive state.	Barium	115-121	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	68-74	
19834614-7	2009	Comparison of the effects of similar barium resistant mutations in Kcv and Kir2.1 shows that neighboring amino acids in the Kcv selectivity filter affect blocker binding.	Barium	37-43	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	75-81	
15465033-2	2004	Compared to cells which only expressed alpha(1G) (HEK293/alpha(1G)), HEK293/alpha(1G)/Kir2.1 cells produced an enormous inward rectifying current which was blocked by external Ba(2+) and Cs(+) in a concentration-dependent manner.	Barium	176-178	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	86-92	
17347781-7	2006	In 60 mM extracellular K(+), Ba(2+) blocked K(IR) currents in HPASM cells with a 50% inhibitory concentration of 39.1 microM at -100 mV compared to 3.9 microM and 65.6 microM for Kir2.1 and Kir2.4, respectively.	Barium	29-31	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	179-185	
16157278-3	2005	Here, using genetic selections to probe interactions of an exemplar potassium channel blocker, barium, with the inward rectifier Kir2.1, we identify mutants bearing positively charged residues in the potassium channel signature sequence at the pore helix C terminus.	Barium	95-101	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	129-135