PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20621156-12	2010	GSH should combine with the hAS3MT after the methylation to reduce the disulfide bond formed during the catalytic cycle in the hAS3MT to resume the active form of the enzyme.	Glutathione	0-3	arsenite methyltransferase	Homo sapiens	28-34	
31355259-8	2019	There was a positive correlation between the content of intracellular GSH/AS3MT and methyl arsenic.	Glutathione	70-73	arsenite methyltransferase	Homo sapiens	74-79	
25349987-9	2014	In this work, we clarified both the functional roles of GSH and the crucial Cys residues in iAs3+ methylation catalyzed by hAS3MT.	Glutathione	56-59	arsenite methyltransferase	Homo sapiens	123-129	
20621156-5	2010	hAS3MT showed the greatest activity at pH 8.5 with glutathione (GSH) as the reductant.	Glutathione	51-62	arsenite methyltransferase	Homo sapiens	0-6	
20621156-5	2010	hAS3MT showed the greatest activity at pH 8.5 with glutathione (GSH) as the reductant.	Glutathione	64-67	arsenite methyltransferase	Homo sapiens	0-6	
22868225-6	2012	Without GSH, V(max) and K(m) values were significantly lower for AS3MT/M287T than for wtAS3MT.	Glutathione	8-11	arsenite methyltransferase	Homo sapiens	65-70	
22868225-8	2012	Thus, 1mM GSH modulates AS3MT activity, increasing both methylation rates and yield of DMAs(III).	Glutathione	10-13	arsenite methyltransferase	Homo sapiens	24-29	
22868225-9	2012	AS3MT genotype exemplified by differences in regulation of wtAS3MT and AS3MT/M287T-catalyzed reactions by GSH may contribute to differences in the phenotype for arsenic methylation and, ultimately, to differences in the disease susceptibility in individuals chronically exposed to inorganic arsenic.	Glutathione	106-109	arsenite methyltransferase	Homo sapiens	0-5	
22868225-9	2012	AS3MT genotype exemplified by differences in regulation of wtAS3MT and AS3MT/M287T-catalyzed reactions by GSH may contribute to differences in the phenotype for arsenic methylation and, ultimately, to differences in the disease susceptibility in individuals chronically exposed to inorganic arsenic.	Glutathione	106-109	arsenite methyltransferase	Homo sapiens	61-66	
21537954-1	2011	It has been suggested that arsenic (+3 oxidation state) methyltransferase (AS3MT) plays a critical role in methylation of arsenic, and that arsenic-glutathione conjugate is a substrate for AS3MT-catalyzed methylation of arsenic.	Glutathione	148-159	arsenite methyltransferase	Homo sapiens	27-73	
21537954-1	2011	It has been suggested that arsenic (+3 oxidation state) methyltransferase (AS3MT) plays a critical role in methylation of arsenic, and that arsenic-glutathione conjugate is a substrate for AS3MT-catalyzed methylation of arsenic.	Glutathione	148-159	arsenite methyltransferase	Homo sapiens	75-80	
21537954-1	2011	It has been suggested that arsenic (+3 oxidation state) methyltransferase (AS3MT) plays a critical role in methylation of arsenic, and that arsenic-glutathione conjugate is a substrate for AS3MT-catalyzed methylation of arsenic.	Glutathione	148-159	arsenite methyltransferase	Homo sapiens	189-194	
15526190-0	2005	A new metabolic pathway of arsenite: arsenic-glutathione complexes are substrates for human arsenic methyltransferase Cyt19.	Glutathione	45-56	arsenite methyltransferase	Homo sapiens	100-123	
15526190-10	2005	These results suggest that As-GSH complexes such as ATG and MADG were converted by Cyt19 to MADG and DMAG, respectively.	Glutathione	30-33	arsenite methyltransferase	Homo sapiens	83-88