PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
8487265-4	1993	In terms of the parameter (turnover number)/Km, the bulky naphthyl analogs were invariably better substrates of MAO A than kynuramine, the reference substrate for this enzyme.	Kynuramine	123-133	monoamine oxidase A	Homo sapiens	112-117
3821373-1	1987	Type A monoamine oxidase (MAO-A) in human placental mitochondria was competitively inhibited by naturally occurring substances, quinoline and quinaldine, using kynuramine as substrate.	Kynuramine	160-170	monoamine oxidase A	Homo sapiens	7-24
8443155-4	1993	The second-order rate constant for the reoxidation was highest with monoamine oxidase A when kynuramine was the ligand (508 x 10(3) M-1 s-1) compared to 4 x 10(3) M-1 s-1 in its absence.	Kynuramine	93-103	monoamine oxidase A	Homo sapiens	68-87
3247497-4	1988	Inhibition of MAO-A of human placental mitochondria by L- and D-DOPA was non-competitive with the substrate kynuramine (Ki = 154 microM and 133 microM, respectively).	Kynuramine	108-118	monoamine oxidase A	Homo sapiens	14-19
2883261-4	1987	At the lower concentrations MPP+ inhibited MAO noncompetitively with respect to the substrate, kynuramine, and at the higher concentrations it increased both the Km and the Vmax values of MAO toward the substrate.	Kynuramine	95-105	monoamine oxidase A	Rattus norvegicus	43-46
2809594-3	1989	These values were similar to or even better than those of kynuramine and benzylamine, good substrates for MAO-A and MAO-B, respectively.	Kynuramine	58-68	monoamine oxidase A	Homo sapiens	106-111
2809594-3	1989	These values were similar to or even better than those of kynuramine and benzylamine, good substrates for MAO-A and MAO-B, respectively.	Kynuramine	58-68	monoamine oxidase B	Homo sapiens	116-121
2720850-2	1989	TL-1 showed mixed-type inhibition of MAO in mouse liver when kynuramine was used as a substrate, and the IC50 was 6.6 microM.	Kynuramine	61-71	tumor necrosis factor (ligand) superfamily, member 15	Mus musculus	0-4
20504500-5	1989	MAO was inhibited by NMIQ(+) in competition with a substrate, kynuramine, and the K(i) value was 20 ?M.	Kynuramine	62-72	monoamine oxidase A	Rattus norvegicus	0-3
3601232-2	1987	MAO-A was found to be markedly inhibited by BQ competitively with the substrate, kynuramine, while MAO-B was less sensitive to this inhibitor and the inhibition was non-competitive with the substrate.	Kynuramine	81-91	monoamine oxidase A	Rattus norvegicus	0-5
3821373-1	1987	Type A monoamine oxidase (MAO-A) in human placental mitochondria was competitively inhibited by naturally occurring substances, quinoline and quinaldine, using kynuramine as substrate.	Kynuramine	160-170	monoamine oxidase A	Homo sapiens	26-31
6335034-4	1984	Additionally, MAO A, isolated from human placenta, oxidizes MPTP to the same product at about 12% of the rate of kynuramine, again with a comparable Km value.	Kynuramine	113-123	monoamine oxidase A	Homo sapiens	14-19
2952905-2	1987	By kinetic analysis, the inhibition of MAO-B activity by QUIN was competitive with the substrate, kynuramine.	Kynuramine	98-108	monoamine oxidase B	Homo sapiens	39-44
2420928-1	1986	Monoamine oxidase (MAO) type A and type B were measured using kynuramine, 3,4-dihydroxyphenylethylamine (dopamine, DA), and 5-hydroxytryptamine (5-HT, serotonin) in 20 brain areas.	Kynuramine	62-72	monoamine oxidase A	Homo sapiens	0-41
3494215-3	1987	By kinetic analysis, MPP+ was found to inhibit MAO-A in competition with the substrate, kynuramine.	Kynuramine	88-98	monoamine oxidase A	Homo sapiens	47-52
6877035-0	1983	Localization of rat striatal monoamine oxidase activities towards dopamine, serotonin and kynuramine by gradient centrifugation and nigro-striatal lesions.	Kynuramine	90-100	monoamine oxidase A	Rattus norvegicus	29-46
6877035-3	1983	As 5HT is specifically deaminated by MAO-A while KYN is a common MAO substrate, this supports earlier suggestions that in rat striatal preparations DA is deaminated preferentially by MAO-A.	Kynuramine	49-52	monoamine oxidase A	Rattus norvegicus	183-188
6877035-2	1983	The distribution pattern of monoamine oxidase (MAO) activity towards dopamine (DA) was very similar to the pattern of MAO activity towards serotonin (5HT), but differed from the pattern of MAO activity towards kynuramine (KYN).	Kynuramine	222-225	monoamine oxidase A	Rattus norvegicus	47-50
510362-6	1979	Differences in rat heart MAO seem to be exposed by some substrates but not others, such as kynuramine.	Kynuramine	91-101	monoamine oxidase A	Rattus norvegicus	25-28
7098495-2	1982	Kynuramine, a substrate for both types of MAO, was used and the sources of enzyme were rat heart (type A) and mouse heart (type B).	Kynuramine	0-10	monoamine oxidase A	Rattus norvegicus	42-45
476201-5	1979	Both in the PS and PF rats, hepatic MAO activity was strongly decreased when assayed with kynuramine.	Kynuramine	90-100	monoamine oxidase A	Rattus norvegicus	36-39
476201-6	1979	In U rats, hepatic MAO activity was highly increased when assayed with kynuramine but the other tissues responded differently.	Kynuramine	71-81	monoamine oxidase A	Rattus norvegicus	19-22
1262860-3	1976	When the activity of MAO was plotted as % of the highest specific activity towards tyramine, kynuramine oxidation remained fairly constant in fractions 10 to 30 but tyramine and dopamine showed separate peaks of activity in fractions 21 and 32 respectively.	Kynuramine	93-103	monoamine oxidase A	Rattus norvegicus	21-24
877399-1	1977	Monoamine oxidase (MAO) activity was characterized using whole tissue homogenates and kynuramine as the substrate.	Kynuramine	86-96	monoamine oxidase A	Rattus norvegicus	0-17
877399-1	1977	Monoamine oxidase (MAO) activity was characterized using whole tissue homogenates and kynuramine as the substrate.	Kynuramine	86-96	monoamine oxidase A	Rattus norvegicus	19-22
877399-3	1977	These studies, and mixed substrate experiments with tryptamine, proved that kynuramine is a substrate for MAO types A and B.	Kynuramine	76-86	monoamine oxidase A	Rattus norvegicus	106-109
938797-6	1976	3 MAO activity towards kynuramine, tyramine and dopamine increased after birth in all brain regions and also in the liver, to reach maximal values between days 40 and 80.	Kynuramine	23-33	monoamine oxidase A	Rattus norvegicus	2-5
26810928-13	2016	The MAO-A and -B activities were evaluated in vitro by an end-point method using kynuramine as the substrate and mitochondrial suspension or human recombinant enzymes as the enzymatic source.	Kynuramine	81-91	monoamine oxidase A	Homo sapiens	4-16
30809547-5	2019	Kynuramine metabolism by human recombinant MAO-A and MAO-B leads to formation of 4-hydroxyquinoline, with Vmax values of 10.2+-0.2 and 7.35+-0.69 nmol/mg/min, respectively, and Km values of 23.1+-0.8 muM and 18.0+-2.3 muM, respectively.	Kynuramine	0-10	monoamine oxidase A	Homo sapiens	43-48
30809547-5	2019	Kynuramine metabolism by human recombinant MAO-A and MAO-B leads to formation of 4-hydroxyquinoline, with Vmax values of 10.2+-0.2 and 7.35+-0.69 nmol/mg/min, respectively, and Km values of 23.1+-0.8 muM and 18.0+-2.3 muM, respectively.	Kynuramine	0-10	monoamine oxidase B	Homo sapiens	53-58
27028260-4	2016	The inhibitory activity of the compounds against MAO-A and MAO-B enzymes was evaluated by using in vitro flurometric method in which kynuramine was used as a substrate.	Kynuramine	133-143	monoamine oxidase A	Homo sapiens	49-54
27028260-4	2016	The inhibitory activity of the compounds against MAO-A and MAO-B enzymes was evaluated by using in vitro flurometric method in which kynuramine was used as a substrate.	Kynuramine	133-143	monoamine oxidase B	Homo sapiens	59-64
1164597-1	1975	6-Hydroxydopamine (6-OHDA) inhibits rat brain mitochondrial monoamine oxidase (MAO) when kynuramine or dopamine are used as substrates.	Kynuramine	89-99	monoamine oxidase A	Rattus norvegicus	60-77
1164597-1	1975	6-Hydroxydopamine (6-OHDA) inhibits rat brain mitochondrial monoamine oxidase (MAO) when kynuramine or dopamine are used as substrates.	Kynuramine	89-99	monoamine oxidase A	Rattus norvegicus	79-82
5420143-11	1970	Tyrosine in the brain showed a 30 to 96% increase in concentration and MAO activity, using kynuramine as substrate, showed an approximately 5% increase 0.5 to 2 h after the subcutaneous administration of 500 mg/kg sodium diethyldithiocarbamate.6.	Kynuramine	91-101	monoamine oxidase A	Rattus norvegicus	71-74
31714755-6	2019	The PcncAAAD-catalyzed decarboxylation products, kynuramine and 3-hydroxykynuramine, could further be converted to quinoline scaffolds through the addition of H. sapiens monoamine oxidase A (HsMAO-A).	Kynuramine	49-59	monoamine oxidase A	Homo sapiens	170-189
26579577-0	2015	Kynuramines induce overexpression of heat shock proteins in pancreatic cancer cells via 5-hydroxytryptamine and MT1/MT2 receptors.	Kynuramine	0-11	metallothionein 1I, pseudogene	Homo sapiens	112-129
19883764-8	2010	Compared with human MAO A, rat MAO A oxidizes serotonin or kynuramine with twofold higher k(cat)/K(m) values, oxidizes phenethylamine with a 6.7-fold higher catalytic efficiency and benzylamine with a approximately 40-fold higher catalytic efficiency.	Kynuramine	59-69	monoamine oxidase A	Rattus norvegicus	31-36
25857233-3	2015	In the present study, we found eight active compounds isolated from V. cinerea that comprise inhibitory activity toward CYP2A6 and MAO-A and MAO-B enzymes using activity-guided assays, with coumarin as substrate of CYP2A6 and kynuramine of MAOs.	Kynuramine	226-236	cytochrome P450 family 2 subfamily A member 6	Homo sapiens	120-126
25857233-3	2015	In the present study, we found eight active compounds isolated from V. cinerea that comprise inhibitory activity toward CYP2A6 and MAO-A and MAO-B enzymes using activity-guided assays, with coumarin as substrate of CYP2A6 and kynuramine of MAOs.	Kynuramine	226-236	monoamine oxidase A	Homo sapiens	131-136
18036149-5	2008	Double immunofluorescent labeling and spectrofluorimetric assay via kynuramine oxidation showed MAO-B expression and activity in SC neurons.	Kynuramine	68-78	monoamine oxidase B	Mus musculus	96-101
9675034-5	1998	17beta-Estradiol treatment for 2 weeks significantly increased (P < 0.01) MAO activity in the hamster kidney (76.7 +/- 10.0 and 113.0 +/- 10.8% over controls for the substrates tyramine and kynuramine, respectively).	Kynuramine	193-203	monoamine oxidase A	Rattus norvegicus	77-80
17401535-2	2007	The pH dependence of the kinetic parameters for kynuramine oxidation by purified human MAO-A and for phenylethylamine oxidation by MAO-B in granulocytes at pH values from 5 to 10 was consistent with the protonated amine being used.	Kynuramine	48-58	monoamine oxidase A	Homo sapiens	87-92
16139309-3	2006	In this paper, "ready to drink" coffee brews exhibited inhibitory properties on recombinant human MAO A and B isozymes catalyzing the oxidative deamination of kynuramine, suggesting that coffee contains compounds acting as MAO inhibitors.	Kynuramine	159-169	monoamine oxidase A	Homo sapiens	98-103
11812236-7	2002	The steady-state kinetic properties of P. pastoris-expressed MAO-A are similar to those of S. cerevisiae-expressed MAO-A using the following substrates: phenethylamine, p-CF(3)-benzylamine, dopamine, serotonin, and kynuramine.	Kynuramine	215-225	monoamine oxidase A	Homo sapiens	61-66
11812236-7	2002	The steady-state kinetic properties of P. pastoris-expressed MAO-A are similar to those of S. cerevisiae-expressed MAO-A using the following substrates: phenethylamine, p-CF(3)-benzylamine, dopamine, serotonin, and kynuramine.	Kynuramine	215-225	monoamine oxidase A	Homo sapiens	115-120
9874092-5	1998	Kynuramine inhibited the metabolism of benzylamine by SSAO with high affinity in a non-competitive manner.	Kynuramine	0-10	amine oxidase copper containing 2	Homo sapiens	54-58
17480205-3	2007	When purified human monoamine oxidase A was used to examine the interaction with the active site, inhibition by guanabenz, 2-(2-benzofuranyl)-2-imidazoline and idazoxan was competitive with kynuramine as substrate, giving K(i) values of 3 microM, 26 microM and 125 microM, respectively.	Kynuramine	190-200	monoamine oxidase A	Homo sapiens	20-39
15694196-6	2005	The platelet MAO-B activity was determined fluorimetrically using kynuramine as a substrate.	Kynuramine	66-76	monoamine oxidase B	Homo sapiens	13-18
15095350-2	2004	The method used kynuramine as a common substrate for both MAO-A and MAO-B in incubations, and the 4-hydroxyquinoline (4-HQ) resulting from deamination of kynuramine followed by intramolecular condensation was analyzed using LC/MS/MS; formation of 4-HQ was used as the marker of MAO activity to evaluate the effects of test compounds.	Kynuramine	16-26	monoamine oxidase A	Homo sapiens	58-63
11833714-2	2001	Coptisine showed an inhibitory effect on MAO-A activity in a concentration-dependent manner using a substrate kynuramine, but coptisine did not inhibit MAO-B activity.	Kynuramine	110-120	monoamine oxidase A	Mus musculus	41-46
11833714-5	2001	Coptisine competitively inhibited MAO-A activity with kynuramine.	Kynuramine	54-64	monoamine oxidase A	Mus musculus	34-39
11732903-2	2001	All mutant enzymes were expressed and exhibited lower specific activities as compared to WT MAO A using kynuramine as substrate.	Kynuramine	104-114	monoamine oxidase A	Homo sapiens	92-97
11732903-6	2001	Y444F MAO A oxidizes kynuramine with a k(cat) <2% of WT enzyme and is greater than 100-fold slower in catalyzing the oxidation of phenylethylamine or of serotonin.	Kynuramine	21-31	monoamine oxidase A	Homo sapiens	6-11
10606764-4	2000	Catalytic activities, as monitored by kynuramine oxidation, are equivalent to (MAO A) or 2-fold greater (MAO B) than control preparations expressed in the presence of riboflavin.	Kynuramine	38-48	monoamine oxidase A	Homo sapiens	79-84
7498967-6	1995	The tryptophan metabolite kynuramine, which possesses significant contractile activity at the 5-HT2B receptor, contracted hypertensive arteries significantly (50% of 5-HT maximum) but not sham arteries.	Kynuramine	26-36	5-hydroxytryptamine receptor 2B	Rattus norvegicus	94-100
8990278-4	1997	The oxidation of kynuramine by MAO A in the presence of the more effective inhibitors showed a lag period before reaching the steady state.	Kynuramine	17-27	monoamine oxidase A	Homo sapiens	31-36