PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21415529-7	2011	These results indicate that reactivity (stability) of the thiol in MGST1 is affected by surrounding lipids, namely CL which prevents MGST1 activation by thiol modification.	Sulfhydryl Compounds	58-63	microsomal glutathione S-transferase 1	Homo sapiens	67-72	
21428695-6	2011	Membrane-bound MGST1 is activated through the thiol modification in oxidative conditions.	Sulfhydryl Compounds	46-51	microsomal glutathione S-transferase 1	Homo sapiens	15-20	
21415529-1	2011	Membrane-bound glutathione transferases (MGST1) distributed mostly in liver microsomal and mitochondrial membranes are activated by the thiol modification.	Sulfhydryl Compounds	136-141	microsomal glutathione S-transferase 1	Homo sapiens	41-46	
21415529-4	2011	Although MGST1 was activated by the thiol alkylation with N-ethylmaleimide (NEM), the activation was suppressed in the presence of anionic phospholipids as clearly observed in the presence of CL.	Sulfhydryl Compounds	36-41	microsomal glutathione S-transferase 1	Homo sapiens	9-14	
21415529-7	2011	These results indicate that reactivity (stability) of the thiol in MGST1 is affected by surrounding lipids, namely CL which prevents MGST1 activation by thiol modification.	Sulfhydryl Compounds	58-63	microsomal glutathione S-transferase 1	Homo sapiens	133-138	
21415529-7	2011	These results indicate that reactivity (stability) of the thiol in MGST1 is affected by surrounding lipids, namely CL which prevents MGST1 activation by thiol modification.	Sulfhydryl Compounds	153-158	microsomal glutathione S-transferase 1	Homo sapiens	67-72	
21415529-7	2011	These results indicate that reactivity (stability) of the thiol in MGST1 is affected by surrounding lipids, namely CL which prevents MGST1 activation by thiol modification.	Sulfhydryl Compounds	153-158	microsomal glutathione S-transferase 1	Homo sapiens	133-138	
11258959-1	2001	An important aspect of the catalytic mechanism of microsomal glutathione transferase (MGST1) is the activation of the thiol of bound glutathione (GSH).	Sulfhydryl Compounds	118-123	microsomal glutathione S-transferase 1	Homo sapiens	86-91	
19348782-11	2009	In addition, the activity could be increased by thiol reagents (a hallmark of MGST1).	Sulfhydryl Compounds	48-53	microsomal glutathione S-transferase 1	Homo sapiens	78-83	
16386761-5	2006	In addition, the MGST1 activity increased by nitric oxide (NO) donors such as S-nitrosoglutathione, S-nitrosocysteine or the non-thiol NO donor 1-hydroxy-2-oxo-3 (3-aminopropyl)-3-isopropyl was restored by the DTT treatment.	Sulfhydryl Compounds	129-134	microsomal glutathione S-transferase 1	Homo sapiens	17-22