PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23977830-2	2013	While in vitro or in vivo eNOS S-glutathionylation with modification of Cys689 and Cys908 of its reductase domain is triggered by high levels of glutathione disulfide (GSSG) or oxidative thiyl radical formation, it remains unclear how this process may be reversed.	thiyl radical	187-200	nitric oxide synthase 3	Homo sapiens	26-30	
21666221-0	2011	Superoxide induces endothelial nitric-oxide synthase protein thiyl radical formation, a novel mechanism regulating eNOS function and coupling.	thiyl radical	61-74	nitric oxide synthase 3	Homo sapiens	19-52	
21666221-0	2011	Superoxide induces endothelial nitric-oxide synthase protein thiyl radical formation, a novel mechanism regulating eNOS function and coupling.	thiyl radical	61-74	nitric oxide synthase 3	Homo sapiens	115-119	
21666221-3	2011	We demonstrate endothelial NOS (eNOS) oxidant-induced protein thiyl radical formation from tetrahydrobiopterin-free enzyme or following exposure to exogenous superoxide using immunoblotting, immunostaining, and mass spectrometry.	thiyl radical	62-75	nitric oxide synthase 3	Homo sapiens	15-30	
21666221-3	2011	We demonstrate endothelial NOS (eNOS) oxidant-induced protein thiyl radical formation from tetrahydrobiopterin-free enzyme or following exposure to exogenous superoxide using immunoblotting, immunostaining, and mass spectrometry.	thiyl radical	62-75	nitric oxide synthase 3	Homo sapiens	32-36	
21666221-8	2011	Protein thiyl radical formation leads to oxidation or modification of cysteine with either disulfide bond formation or S-glutathionylation, which induces eNOS uncoupling.	thiyl radical	8-21	nitric oxide synthase 3	Homo sapiens	154-158