PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30686752-7	2019	Docking simulations also implied that 6 interacted with hMAO-A at Phe208 and with hMAO-B at Ile199 by carbon hydrogen bondings.	Carbon	102-108	monoamine oxidase A	Homo sapiens	56-62	
24525204-5	2014	Pancreatic uptake of (11)C-5-HTP in nonhuman primates was markedly decreased by inhibition of the enzyme dopa decarboxylase, which converts (11)C-5-HTP to (11)C-serotonin and increased after inhibition of monoamine oxidase-A, the main enzyme responsible for serotonin degradation.	Carbon	25-26	monoamine oxidase A	Homo sapiens	205-224	
7931241-6	1994	In the case of the initial, non-covalent, inhibition all these compounds were competitive inhibitors of MAO-A, with respect to the amine substrate, and the affinity for inhibitor binding increased with carbon chain length.	Carbon	202-208	monoamine oxidase A	Homo sapiens	104-109	
23403377-1	2013	Positron emission tomography (PET) imaging of monoamine oxidases (MAO-A: [(11)C]harmine, [(11)C]clorgyline, and [(11)C]befloxatone; MAO-B: [(11)C]deprenyl-D2) has been actively pursued given clinical importance of MAOs in human neuropsychiatric disorders.	Carbon	77-79	monoamine oxidase A	Homo sapiens	66-71	
12188024-1	2002	The HOMO energies and the charges on the aromatic carbons of two sets of MAO-A-inhibiting phenylisopropylamines, one containing 4-amino substituents, were calculated by the AM1 method, in order to evaluate the importance of charge-transfer interactions between drug and enzyme.	Carbon	50-57	monoamine oxidase A	Homo sapiens	73-78	
21597803-1	1995	Operative specimens from 7 patients with urinary bladder cancer and with only inflammatory tissue in the operative sample from one patient, were used for frozen section autoradiography using [C-11]harmine to characterize the expression of the enzyme monoamine oxidase A (MAO-A).	Carbon	192-193	monoamine oxidase A	Homo sapiens	250-269	
9377092-1	1997	The monoamine oxidases A and B (MAO-A and MAO-B) catalyze the alpha-carbon oxidation of a variety of 4-substituted 1-methyl-1,2,3,6-tetrahydropyridine derivatives to yield the corresponding 2,3-dihydropyridinium species.	Carbon	68-74	monoamine oxidase A	Homo sapiens	4-30	
9377092-1	1997	The monoamine oxidases A and B (MAO-A and MAO-B) catalyze the alpha-carbon oxidation of a variety of 4-substituted 1-methyl-1,2,3,6-tetrahydropyridine derivatives to yield the corresponding 2,3-dihydropyridinium species.	Carbon	68-74	monoamine oxidase A	Homo sapiens	32-37	
7931241-10	1994	The time-dependent irreversible inhibition (measured as the IC50 values after 60 min enzyme-inhibitor preincubation) showed that the potency towards MAO-A increased when the side-chain length was increased from 2 to 3 carbons but that there was no significant difference between the 3 and 4 carbon-chain compounds.	Carbon	218-225	monoamine oxidase A	Homo sapiens	149-154	
7931241-10	1994	The time-dependent irreversible inhibition (measured as the IC50 values after 60 min enzyme-inhibitor preincubation) showed that the potency towards MAO-A increased when the side-chain length was increased from 2 to 3 carbons but that there was no significant difference between the 3 and 4 carbon-chain compounds.	Carbon	218-224	monoamine oxidase A	Homo sapiens	149-154	
3954792-0	1986	Stereospecific deuterium substitution at the alpha-carbon position of dopamine and its effect on oxidative deamination catalyzed by MAO-A and MAO-B from different tissues.	Carbon	51-57	monoamine oxidase A	Homo sapiens	132-137