PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28460566-2	2018	Extensive MD simulation studies of dopamine-docked hMAO B structures have revealed the stabilization of amino-terminal of the substrate by a direct and water-mediated interaction of catalytic tyrosines, Gln206, and Leu171 residues.	Tyrosine	192-201	monoamine oxidase B	Homo sapiens	51-57	
9724550-3	1998	Previously, Glu-34 and Tyr-44 of MAO B have been identified as residues which engage in noncovalent interactions with FAD that are required for subsequent covalent FAD binding and generation of catalytic activity.	Tyrosine	23-26	monoamine oxidase B	Homo sapiens	33-38	
2153484-1	1990	In this rapid, simple, and convenient enzymatic method for measurement of tyrosine in plasma, tyrosine is converted to tyramine by action of tyrosine decarboxylase (EC 4.1.1.25) and the tyramine produced is oxidized to p-hydroxybenzyl aldehyde and hydrogen peroxide by action of tyramine oxidase (EC 1.4.3.9).	Tyrosine	74-82	monoamine oxidase B	Homo sapiens	279-295	
2153484-1	1990	In this rapid, simple, and convenient enzymatic method for measurement of tyrosine in plasma, tyrosine is converted to tyramine by action of tyrosine decarboxylase (EC 4.1.1.25) and the tyramine produced is oxidized to p-hydroxybenzyl aldehyde and hydrogen peroxide by action of tyramine oxidase (EC 1.4.3.9).	Tyrosine	94-102	monoamine oxidase B	Homo sapiens	279-295	
7626622-0	1995	Mutagenesis at a highly conserved tyrosine in monoamine oxidase B affects FAD incorporation and catalytic activity.	Tyrosine	34-42	monoamine oxidase B	Homo sapiens	46-65	
19697948-5	2009	Increased nitration of Tyr-39 on endogenous alpha-synuclein via elevations in MAO-B levels could be abrogated by the addition of deprenyl, a specific MAO-B inhibitor.	Tyrosine	23-27	monoamine oxidase B	Homo sapiens	78-83	
26352677-4	2015	Our modeling study indicates that Tyr 326 of hMAO-B (or corresponded Ile 335 of hMAO-A) may be the determinant for the specificity of these compounds.	Tyrosine	34-37	monoamine oxidase B	Homo sapiens	45-51	
26593027-4	2012	Therefore, in order to investigate features essential for the modes of action of MAO, we have calculated pKa values of three relevant tyrosine residues in the MAO B active site, with and without dopamine bound as the substrate (as well as the pKa of the dopamine itself in the active site).	Tyrosine	134-142	monoamine oxidase B	Homo sapiens	159-164	
19697948-5	2009	Increased nitration of Tyr-39 on endogenous alpha-synuclein via elevations in MAO-B levels could be abrogated by the addition of deprenyl, a specific MAO-B inhibitor.	Tyrosine	23-27	monoamine oxidase B	Homo sapiens	150-155	
17256833-7	2007	The slightly different binding pose of 18 into the MAO-B active site seems to be forced by a bulkier Tyr residue, which replaces a smaller Ile residue present in MAO-A.	Tyrosine	101-104	monoamine oxidase B	Homo sapiens	51-56	
11134050-9	2001	Our results indicate that Ile-335 in MAO A and Tyr-326 in MAO B play a critical role in determining substrate and inhibitor specificities in human MAO A and B.	Tyrosine	47-50	monoamine oxidase B	Homo sapiens	58-63	
18391214-6	2008	The results confirm that the inhibitor selectivity of MAOA and MAOB is caused by the structural differences arising from Ile-335 in MAOA vs. Tyr-326 in MAOB.	Tyrosine	141-144	monoamine oxidase B	Homo sapiens	63-67	
18391214-6	2008	The results confirm that the inhibitor selectivity of MAOA and MAOB is caused by the structural differences arising from Ile-335 in MAOA vs. Tyr-326 in MAOB.	Tyrosine	141-144	monoamine oxidase B	Homo sapiens	152-156	
17401536-1	2007	Computational studies using the ONIOM methods have been performed to probe the catalytic roles of tyrosine residues 398 and 435 which constitute the "aromatic cage" in the active site of MAO-B.	Tyrosine	98-106	monoamine oxidase B	Homo sapiens	187-192	
11861643-3	2002	We have recently generated 14 site-directed mutants of human MAO A and B, and we found that four key amino acids, Lys-305, Trp-397, Tyr-407, and Tyr-444, in MAO A and their corresponding amino acids in MAO B, Lys-296, Trp-388, Tyr-398, and Tyr-435, play important roles in MAO catalytic activity.	Tyrosine	145-148	monoamine oxidase B	Homo sapiens	202-207	
11861643-3	2002	We have recently generated 14 site-directed mutants of human MAO A and B, and we found that four key amino acids, Lys-305, Trp-397, Tyr-407, and Tyr-444, in MAO A and their corresponding amino acids in MAO B, Lys-296, Trp-388, Tyr-398, and Tyr-435, play important roles in MAO catalytic activity.	Tyrosine	145-148	monoamine oxidase B	Homo sapiens	202-207	
11861643-3	2002	We have recently generated 14 site-directed mutants of human MAO A and B, and we found that four key amino acids, Lys-305, Trp-397, Tyr-407, and Tyr-444, in MAO A and their corresponding amino acids in MAO B, Lys-296, Trp-388, Tyr-398, and Tyr-435, play important roles in MAO catalytic activity.	Tyrosine	145-148	monoamine oxidase B	Homo sapiens	202-207	
11861643-4	2002	Based on the polyamine oxidase three-dimensional crystal structure, it is suggested that Lys-305, Trp-397, and Tyr-407 in MAO A and Lys-296, Trp-388, and Tyr-398 in MAO B may be involved in the non-covalent binding to FAD.	Tyrosine	111-114	monoamine oxidase B	Homo sapiens	165-170	
11861643-5	2002	Tyr-407 and Tyr-444 in MAO A (Tyr-398 and Tyr-435 in MAO B) may form an aromatic sandwich that stabilizes the substrate binding.	Tyrosine	0-3	monoamine oxidase B	Homo sapiens	53-58	
11861643-5	2002	Tyr-407 and Tyr-444 in MAO A (Tyr-398 and Tyr-435 in MAO B) may form an aromatic sandwich that stabilizes the substrate binding.	Tyrosine	12-15	monoamine oxidase B	Homo sapiens	53-58	
11861643-5	2002	Tyr-407 and Tyr-444 in MAO A (Tyr-398 and Tyr-435 in MAO B) may form an aromatic sandwich that stabilizes the substrate binding.	Tyrosine	12-15	monoamine oxidase B	Homo sapiens	53-58	
11861643-5	2002	Tyr-407 and Tyr-444 in MAO A (Tyr-398 and Tyr-435 in MAO B) may form an aromatic sandwich that stabilizes the substrate binding.	Tyrosine	12-15	monoamine oxidase B	Homo sapiens	53-58