PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12509428-10	2003	Our results suggest that the effect of pO(2) on RyR1 S-nitrosylation is exerted through an allosteric mechanism.	PO-2	39-44	ryanodine receptor 1	Homo sapiens	48-52	
23798702-2	2013	S-Oxidation of RyR1 is coupled to muscle oxygen tension (pO2) through O2-dependent production of hydrogen peroxide by SR-resident NADPH oxidase 4.	PO-2	57-60	ryanodine receptor 1	Homo sapiens	15-19	
10966111-3	2000	Here we report that PO2 dynamically controls the redox state of 6-8 out of 50 thiols in each RyR1 subunit and thereby tunes the response to NO.	PO-2	20-23	ryanodine receptor 1	Homo sapiens	93-97	
23798702-3	2013	In isolated SR (SR vesicles), an average of six to eight Cys thiols/RyR1 monomer are reversibly oxidized at high (21% O2) versus low pO2 (1% O2), but their identity among the 100 Cys residues/RyR1 monomer is unknown.	PO-2	133-136	ryanodine receptor 1	Homo sapiens	68-72	
23798702-4	2013	Here we use isotope-coded affinity tag labeling and mass spectrometry (yielding 93% coverage of RyR1 Cys residues) to identify 13 Cys residues subject to pO2-coupled S-oxidation in SR vesicles.	PO-2	154-157	ryanodine receptor 1	Homo sapiens	96-100	
19053230-6	2008	Our results indicate that both RyR1 and RyR2 are pO(2)-responsive yet point to different mechanisms by which NO and S-nitrosoglutathione influence cardiac and skeletal muscle sarcoplasmic reticulum Ca(2+) release.	PO-2	49-54	ryanodine receptor 1	Homo sapiens	31-35	
16099502-4	2005	A role for O2 was based on the observation that RyR1 can be activated by submicromolar NO at physiological ( approximately 10 mmHg) but not ambient (approximately 150 mmHg) pO2.	PO-2	173-176	ryanodine receptor 1	Homo sapiens	48-52	
16099502-5	2005	At ambient pO2, these critical thiols were oxidized but incubation at low pO2 reset the redox state of these thiols, closed RyR1 channels and made these thiols available for nitrosation by low NO concentrations.	PO-2	74-77	ryanodine receptor 1	Homo sapiens	124-128