PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8316221-0	1993	Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines.	Cysteine	64-73	monoamine oxidase A	Homo sapiens	29-54	
8316221-1	1993	Nine cysteines are found in the deduced amino acid sequences of both human liver monoamine oxidase (MAO)-A and MAO-B.	Cysteine	5-14	monoamine oxidase A	Homo sapiens	81-106	
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.	Cysteine	18-26	monoamine oxidase A	Homo sapiens	39-51	
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.	Cysteine	126-134	monoamine oxidase A	Homo sapiens	39-51	
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.	Cysteine	22-25	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.	Cysteine	22-25	monoamine oxidase A	Homo sapiens	114-126	
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.	Cysteine	49-52	monoamine oxidase A	Homo sapiens	114-126	
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.	Cysteine	95-104	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.	Cysteine	95-104	monoamine oxidase A	Homo sapiens	253-265	
3242595-10	1988	The ability of N-C alpha MBA to undergo attachment to a cysteine residue in both MAO A and MAO B may lead the way toward peptide mapping of the two isozymes in order to determine differences in their primary structures.	Cysteine	56-64	monoamine oxidase A	Homo sapiens	81-86	
1886775-7	1991	Exon 12 (bearing the codon for cysteine, which carries the covalently bound FAD cofactor) and exon 13 are highly conserved between human MAOA and MAOB genes (92% at the amino acid level).	Cysteine	31-39	monoamine oxidase A	Homo sapiens	137-141	
12777388-0	2003	Structural comparison of human monoamine oxidases A and B: mass spectrometry monitoring of cysteine reactivities.	Cysteine	91-99	monoamine oxidase A	Homo sapiens	31-57	
12777388-3	2003	Human MAO A and MAO B each contain 9 cysteine residues (7 in conserved sequence locations).	Cysteine	37-45	monoamine oxidase A	Homo sapiens	6-11	
10877844-1	2000	The FAD binding site of human liver monoamine oxidase A (MAO A) has been investigated by mutagenesis of the amino acid site of covalent FAD attachment (Cys-406) to an alanyl residue.	Cysteine	152-155	monoamine oxidase A	Homo sapiens	36-55	
10877844-1	2000	The FAD binding site of human liver monoamine oxidase A (MAO A) has been investigated by mutagenesis of the amino acid site of covalent FAD attachment (Cys-406) to an alanyl residue.	Cysteine	152-155	monoamine oxidase A	Homo sapiens	57-62	
10438531-9	1999	A flavin peptide was isolated from MAO A containing 7-nor-7-bromo-FAD and was demonstrated to be covalently attached to Cys-406 by an 8alpha-S-thioether linkage by sequence analysis and by matrix-assisted laser desorption ionization time of flight mass spectroscopy.	Cysteine	120-123	monoamine oxidase A	Homo sapiens	35-40	
16127378-12	2005	Modification of multiple thiols results in inactivation but mutation of a single thiol, cysteine 374 in MAO A to alanine, decreased the catalytic potency (kcat/Km) by 30%.	Cysteine	88-96	monoamine oxidase A	Homo sapiens	104-109