PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8316221-2	1993	The role of these cysteine residues in MAO-A and -B catalytic activity was studied by site-directed mutagenesis, whereby each cysteine residue was converted to serine.	Serine	160-166	monoamine oxidase A	Homo sapiens	39-51	
19650872-0	2009	Serine 209 resides within a putative p38(MAPK) consensus motif and regulates monoamine oxidase-A activity.	Serine	0-6	monoamine oxidase A	Homo sapiens	77-96	
8316221-4	1993	Catalytic activities were retained in seven MAO-A cysteine to serine mutants (mutations at residues 165, 210, 266, 306, 321, 323, and 398) and in six MAO-B cysteine to serine mutants (mutations at residues 5, 172, 192, 297, 312, and 389).	Serine	62-68	monoamine oxidase A	Homo sapiens	44-49	
8316221-6	1993	Substitution of MAO-A Cys-374 and -406 and MAO-B Cys-156, -365, and -397 with serine resulted in complete loss of MAO-A and -B catalytic activity.	Serine	78-84	monoamine oxidase A	Homo sapiens	16-21	
8316221-6	1993	Substitution of MAO-A Cys-374 and -406 and MAO-B Cys-156, -365, and -397 with serine resulted in complete loss of MAO-A and -B catalytic activity.	Serine	78-84	monoamine oxidase A	Homo sapiens	114-126	
8316221-8	1993	The loss of catalytic activity in the MAO-A Ser-406 and MAO-B Ser-397 mutants may be due to the prevention of covalent binding of the enzyme to the cofactor FAD, which is necessary for catalytic activity.	Serine	44-47	monoamine oxidase A	Homo sapiens	38-43	
8316221-8	1993	The loss of catalytic activity in the MAO-A Ser-406 and MAO-B Ser-397 mutants may be due to the prevention of covalent binding of the enzyme to the cofactor FAD, which is necessary for catalytic activity.	Serine	62-65	monoamine oxidase A	Homo sapiens	38-43	
8316221-9	1993	The loss of catalytic activity of MAO-A Ser-374 and MAO-B Ser-156 and -365 suggests that these cysteines are important for catalytic activity, but whether they are involved in forming the active site or are important for the appropriate conformation of MAO-A and -B remains to be studied.	Serine	40-43	monoamine oxidase A	Homo sapiens	34-39	
8316221-9	1993	The loss of catalytic activity of MAO-A Ser-374 and MAO-B Ser-156 and -365 suggests that these cysteines are important for catalytic activity, but whether they are involved in forming the active site or are important for the appropriate conformation of MAO-A and -B remains to be studied.	Serine	40-43	monoamine oxidase A	Homo sapiens	253-265