PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9699005-4	1998	The presence of 10 cysteine residues per subunit, makes liver MAT a sensitive target for oxidation/nitrosylation.	Cysteine	19-27	methionine adenosyltransferase 1A	Homo sapiens	62-65	
21994917-2	2011	For understanding and confirming the mechanism of the reaction, the electrochemical behaviors of Michael addition reaction of two model compounds, cysteine (CYS) and glutathione (GSH), towards the catechol-terminated SAMs have been studied.	Cysteine	147-155	methionine adenosyltransferase 1A	Homo sapiens	217-221	
21994917-2	2011	For understanding and confirming the mechanism of the reaction, the electrochemical behaviors of Michael addition reaction of two model compounds, cysteine (CYS) and glutathione (GSH), towards the catechol-terminated SAMs have been studied.	Cysteine	157-160	methionine adenosyltransferase 1A	Homo sapiens	217-221	
21828453-0	2009	Growth dynamics of L-cysteine SAMs on single-crystal gold surfaces: a metastable deexcitation spectroscopy study.	Cysteine	19-29	methionine adenosyltransferase 1A	Homo sapiens	30-34	
16413417-11	2006	Increased flux of (13)C-labeled methionine to S-adenosylhomocysteine (SAH) in A549 demonstrated that SAM"s methyl group was utilized, and increased formation of cystathionine indicated that at least part of SAM generated was directed toward cysteine/GSH in the transsulfuration pathway.	Cysteine	60-68	methionine adenosyltransferase 1A	Homo sapiens	101-106	
9699005-8	1998	MAT inactivation originates on the specific and covalent modification of the sulphydryl group of cysteine residue 121.	Cysteine	97-105	methionine adenosyltransferase 1A	Homo sapiens	0-3	
9337154-3	1997	In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT.	Cysteine	211-219	methionine adenosyltransferase 1A	Homo sapiens	68-71	
9337154-3	1997	In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT.	Cysteine	211-219	methionine adenosyltransferase 1A	Homo sapiens	284-287	
9337154-4	1997	Cysteine 121 is specific to the hepatic enzyme and is localized at a "flexible loop" over the active site cleft of MAT.	Cysteine	0-8	methionine adenosyltransferase 1A	Homo sapiens	115-118	
9337154-5	1997	In vivo studies, using wild-type Chinese hamster ovary (CHO) cells and CHO cells stably expressing liver MAT, demonstrate that the inactivation of MAT by H2O2 is specific to the hepatic enzyme, resulting from the modification of the cysteine residue 121, and that this effect is mediated by the generation of the hydroxyl radical.	Cysteine	233-241	methionine adenosyltransferase 1A	Homo sapiens	105-108	
9337154-5	1997	In vivo studies, using wild-type Chinese hamster ovary (CHO) cells and CHO cells stably expressing liver MAT, demonstrate that the inactivation of MAT by H2O2 is specific to the hepatic enzyme, resulting from the modification of the cysteine residue 121, and that this effect is mediated by the generation of the hydroxyl radical.	Cysteine	233-241	methionine adenosyltransferase 1A	Homo sapiens	147-150	
9337154-3	1997	In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT.	Cysteine	94-102	methionine adenosyltransferase 1A	Homo sapiens	68-71