PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7929166-2	1994	Fluorescence spectroscopy has been used to study the interaction of Tb3+ (as a Ca2+ analog) with the purified ryanodine receptor (RyR)/Ca2+ release channel of skeletal muscle sarcoplasmic reticulum.	tb3+	68-72	ryanodine receptor 1	Homo sapiens	110-128	
7929166-12	1994	The results suggest that RyR/Ca2+ release channel undergoes conformational changes due to Tb3+ binding to the low-affinity Ca2+ binding site, and this binding results in the closing of the Ca2+ release channel.	tb3+	90-94	ryanodine receptor 1	Homo sapiens	25-28	
7929166-2	1994	Fluorescence spectroscopy has been used to study the interaction of Tb3+ (as a Ca2+ analog) with the purified ryanodine receptor (RyR)/Ca2+ release channel of skeletal muscle sarcoplasmic reticulum.	tb3+	68-72	ryanodine receptor 1	Homo sapiens	130-133	
7929166-8	1994	About 20% of the bound Tb3+ was not displaced by EGTA or Ca2+; suggesting its "occlusion" in the RyR.	tb3+	23-27	ryanodine receptor 1	Homo sapiens	97-100