PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
31964512-2	2020	Two novel mixed-mode chromatographic stationary phases, dicarboxyl cellulose-modified silica (DCC/SiO2) and (S)-alpha-phenylethylamine-bonded DCC/SiO2 ((S)-alpha-PEA/DCC/SiO2), were prepared by utilizing the easy functionalization characteristics of dialdehyde cellulose.	1-phenethylamine	108-134	DCC netrin 1 receptor	Homo sapiens	142-145
3747266-3	1986	The alpha-methylated substrate-analogue monoamines, dl-alpha-methyltryptamine, dl-alpha-methylbenzylamine and two optical isomers of alpha-methylbenzylamine, were shown to be inhibitors of rat lung semicarbazide-sensitive amine oxidase (SSAO), with dl-alpha-methyltryptamine being the most potent and d-alpha-methylbenzylamine, the least.	1-phenethylamine	79-105	amine oxidase, copper containing 3	Rattus norvegicus	198-235
3747266-3	1986	The alpha-methylated substrate-analogue monoamines, dl-alpha-methyltryptamine, dl-alpha-methylbenzylamine and two optical isomers of alpha-methylbenzylamine, were shown to be inhibitors of rat lung semicarbazide-sensitive amine oxidase (SSAO), with dl-alpha-methyltryptamine being the most potent and d-alpha-methylbenzylamine, the least.	1-phenethylamine	82-105	amine oxidase, copper containing 3	Rattus norvegicus	198-235
3747266-4	1986	The three compounds, dl-alpha-methyltryptamine and the two isomers of alpha-methylbenzylamine also inhibited rat brain monoamine oxidase (MAO)-A and -B with a greater selectivity towards MAO-A.	1-phenethylamine	70-93	monoamine oxidase A	Rattus norvegicus	119-144
3747266-4	1986	The three compounds, dl-alpha-methyltryptamine and the two isomers of alpha-methylbenzylamine also inhibited rat brain monoamine oxidase (MAO)-A and -B with a greater selectivity towards MAO-A.	1-phenethylamine	70-93	monoamine oxidase A	Rattus norvegicus	187-192
3336033-10	1988	These results, in conjunction with others from these laboratories, indicate that the PNMT active site beyond the zone that interacts with the central aromatic ring portion of phenylethanolamine substrates and alpha-methylbenzylamine inhibitors is essentially a flat, hydrophobic pocket.	1-phenethylamine	209-232	phenylethanolamine N-methyltransferase	Homo sapiens	85-89
7143356-3	1982	Some nonaromatic analogues of amphetamine and alpha-methylbenzylamine were prepared and evaluated as competitive inhibitors of norepinephrine N-methyltransferase (NMT).	1-phenethylamine	46-69	N-myristoyltransferase 1	Homo sapiens	163-166
7143356-5	1982	In order to determine if the aliphatic ring of these analogues bound to the same binding site as the phenyl ring of amphetamine and alpha-methylbenzylamine, the stereoselectivity of NMT toward the different compounds was determined.	1-phenethylamine	132-155	N-myristoyltransferase 1	Homo sapiens	182-185
7143357-1	1982	We investigated the directional nature of the bulk tolerance and hydrophobic binding in the aromatic ring binding region of the active site of norepinephrine N-methyltransferase (NMT) by comparing the substrate and inhibitor activities of m- and p-phenyl-substituted derivatives of amphetamine, phenylethanolamine, and alpha-methylbenzylamine.	1-phenethylamine	319-342	N-myristoyltransferase 1	Homo sapiens	179-182
7143366-1	1982	A series of omega-substituted analogues of amphetamine and alpha-methylbenzylamine were prepared and evaluated as inhibitors of norepinephrine N-methyltransferase (NMT).	1-phenethylamine	59-82	N-myristoyltransferase 1	Homo sapiens	164-167
31964512-2	2020	Two novel mixed-mode chromatographic stationary phases, dicarboxyl cellulose-modified silica (DCC/SiO2) and (S)-alpha-phenylethylamine-bonded DCC/SiO2 ((S)-alpha-PEA/DCC/SiO2), were prepared by utilizing the easy functionalization characteristics of dialdehyde cellulose.	1-phenethylamine	108-134	DCC netrin 1 receptor	Homo sapiens	142-145
28159615-5	2017	When the two immobilized enzymes were used together in one pot, the transformation of (R)-1-phenylethylamine was catalyzed by the immobilized ELP-RTA, and the co-product d-alanine was converted back to pyruvate under the catalysis of the immobilized ELP-DAAO, achieving the recycling of pyruvate in situ.	1-phenethylamine	86-108	nuclear receptor subfamily 5 group A member 1	Homo sapiens	142-145
29453991-0	2018	Identification of branched-chain amino acid aminotransferases active towards (R)-(+)-1-phenylethylamine among PLP fold type IV transaminases.	1-phenethylamine	77-103	proteolipid protein 1	Homo sapiens	110-113
28650006-1	2017	A hierarchical yolk-shell@shell nanoreactor that spatially positioned Pd nanoparticles and the CALB enzyme in separated domains is constructed, and served as an efficient bifunctional catalyst for the one-pot dynamic kinetic resolution (DKR) reaction of 1-phenylethylamine with excellent activity and selectivity.	1-phenethylamine	254-272	calbindin 1	Homo sapiens	95-99
28159615-5	2017	When the two immobilized enzymes were used together in one pot, the transformation of (R)-1-phenylethylamine was catalyzed by the immobilized ELP-RTA, and the co-product d-alanine was converted back to pyruvate under the catalysis of the immobilized ELP-DAAO, achieving the recycling of pyruvate in situ.	1-phenethylamine	86-108	nuclear receptor subfamily 5 group A member 1	Homo sapiens	250-253
28159615-5	2017	When the two immobilized enzymes were used together in one pot, the transformation of (R)-1-phenylethylamine was catalyzed by the immobilized ELP-RTA, and the co-product d-alanine was converted back to pyruvate under the catalysis of the immobilized ELP-DAAO, achieving the recycling of pyruvate in situ.	1-phenethylamine	86-108	D-amino acid oxidase	Homo sapiens	254-258
24055435-9	2013	For the multi-step enzyme reaction, single IEMRs were cascaded in series, whereby the first enzyme, TK, catalyzed a model reaction of lithium-hydroxypyruvate (HPA) and glycolaldehyde (GA) to L-erythrulose (ERY), and the second unit of the IEMR with immobilized TAm converted ERY into ABT using (S)-alpha-methylbenzylamine (MBA) as amine donor.	1-phenethylamine	294-321	transketolase	Homo sapiens	100-102
24644036-0	2014	Tailoring D-amino acid oxidase from the pig kidney to R-stereoselective amine oxidase and its use in the deracemization of alpha-methylbenzylamine.	1-phenethylamine	123-146	D-amino acid oxidase	Sus scrofa	10-30
26601980-4	2016	For the single-enzyme system, in the reaction media, ELP-R-omega-TA self-assembled and formed enzyme clusters of micrometer size, and the substrate, (R)-1-phenylethylamine, also formed droplets of micrometer size.	1-phenethylamine	149-171	nuclear receptor subfamily 5 group A member 1	Homo sapiens	53-56
25679051-1	2015	Well-defined unnatural dipeptide-alcohols based on a cis-2,5-disubstitued pyrrolidine backbone were synthesized from commercially available starting materials meso-diethyl-2,5-dibromoadipate, (S)-(-)-1-phenylethylamine, and phenylalaninol.	1-phenethylamine	192-218	suppressor of cytokine signaling 2	Homo sapiens	53-58
24055435-9	2013	For the multi-step enzyme reaction, single IEMRs were cascaded in series, whereby the first enzyme, TK, catalyzed a model reaction of lithium-hydroxypyruvate (HPA) and glycolaldehyde (GA) to L-erythrulose (ERY), and the second unit of the IEMR with immobilized TAm converted ERY into ABT using (S)-alpha-methylbenzylamine (MBA) as amine donor.	1-phenethylamine	323-326	transketolase	Homo sapiens	100-102
24117430-1	2013	Diamine oxidase (DAO), the enzyme that is responsible for amine biodegradation in animals, plants and humans, catalyses the biotransformation of amines such as histamine (HA), putrescine, 1-phenylethylamine, tyrosine, tryptamine, serotonine and spermine.	1-phenethylamine	188-206	amine oxidase copper containing 1	Homo sapiens	0-15
24117430-1	2013	Diamine oxidase (DAO), the enzyme that is responsible for amine biodegradation in animals, plants and humans, catalyses the biotransformation of amines such as histamine (HA), putrescine, 1-phenylethylamine, tyrosine, tryptamine, serotonine and spermine.	1-phenethylamine	188-206	amine oxidase copper containing 1	Homo sapiens	17-20
22574648-1	2012	The enantiomeric lactams (-)-8, (+)-8, (+)-9, and (-)-9 were formed by the reaction of the dimeric phthalide rac-tokinolide B (rac-3) with (R)-(+)-alpha-methylbenzylamine and (S)-(-)-alpha-methylbenzylamine.	1-phenethylamine	139-170	Rac family small GTPase 3	Homo sapiens	127-132
22574648-1	2012	The enantiomeric lactams (-)-8, (+)-8, (+)-9, and (-)-9 were formed by the reaction of the dimeric phthalide rac-tokinolide B (rac-3) with (R)-(+)-alpha-methylbenzylamine and (S)-(-)-alpha-methylbenzylamine.	1-phenethylamine	175-206	Rac family small GTPase 3	Homo sapiens	127-132
12882012-1	2003	A simultaneous synthesis of (R)-1-phenylethanol and (R)-alpha-methylbenzylamine from racemic alpha-methylbenzylamine was achieved using an omega-transaminase, alcohol dehydrogenase, and glucose dehydrogenase in a coupled reaction.	1-phenethylamine	52-79	aldo-keto reductase family 1 member A1	Homo sapiens	159-180
22056424-5	2011	Although (S)-1-phenylethylamine was the best amino donor, beta-alanine and 4-aminobutyric acid, which are good substrates for typical omega-amino acid transaminase (EC 2.6.1.18) and GABA transaminase (2.6.1.19), were not reacted.	1-phenethylamine	9-31	4-aminobutyrate aminotransferase	Homo sapiens	182-199
20978623-1	2010	Candida antarctica lipase B (CALB) and racemization catalyst 4 were combined in the dynamic kinetic resolution (DKR) of (+-)-1-phenylethylamine (1).	1-phenethylamine	120-143	calbindin 1	Homo sapiens	0-27
20978623-1	2010	Candida antarctica lipase B (CALB) and racemization catalyst 4 were combined in the dynamic kinetic resolution (DKR) of (+-)-1-phenylethylamine (1).	1-phenethylamine	120-143	calbindin 1	Homo sapiens	29-33
17722015-1	2007	A new series of chiral cis-3-hydroxyazetidines have been prepared from (R)-1-phenylethylamine.	1-phenethylamine	71-93	suppressor of cytokine signaling 3	Homo sapiens	23-28
12882012-1	2003	A simultaneous synthesis of (R)-1-phenylethanol and (R)-alpha-methylbenzylamine from racemic alpha-methylbenzylamine was achieved using an omega-transaminase, alcohol dehydrogenase, and glucose dehydrogenase in a coupled reaction.	1-phenethylamine	52-79	hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase	Homo sapiens	186-207
12882012-1	2003	A simultaneous synthesis of (R)-1-phenylethanol and (R)-alpha-methylbenzylamine from racemic alpha-methylbenzylamine was achieved using an omega-transaminase, alcohol dehydrogenase, and glucose dehydrogenase in a coupled reaction.	1-phenethylamine	56-79	aldo-keto reductase family 1 member A1	Homo sapiens	159-180
12882012-1	2003	A simultaneous synthesis of (R)-1-phenylethanol and (R)-alpha-methylbenzylamine from racemic alpha-methylbenzylamine was achieved using an omega-transaminase, alcohol dehydrogenase, and glucose dehydrogenase in a coupled reaction.	1-phenethylamine	56-79	hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase	Homo sapiens	186-207
10705483-2	2000	The chiral centers at C-1 and C-3 were constructed by two routes starting from alaninol (3) and 1-phenylethylamine (4) as a chiral source.	1-phenethylamine	96-114	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	22-33
12882012-0	2003	Simultaneous synthesis of enantiomerically pure (R)-1-phenylethanol and (R)-alpha-methylbenzylamine from racemic alpha-methylbenzylamine using omega-transaminase/alcohol dehydrogenase/glucose dehydrogenase coupling reaction.	1-phenethylamine	72-99	aldo-keto reductase family 1 member A1	Homo sapiens	162-183
12882012-0	2003	Simultaneous synthesis of enantiomerically pure (R)-1-phenylethanol and (R)-alpha-methylbenzylamine from racemic alpha-methylbenzylamine using omega-transaminase/alcohol dehydrogenase/glucose dehydrogenase coupling reaction.	1-phenethylamine	76-99	aldo-keto reductase family 1 member A1	Homo sapiens	162-183
11004529-1	2000	The interaction of purified bovine liver MAO B with the benzylamine analogues N,N-dimethylbenzylamine and alpha-methylbenzylamine has been investigated.	1-phenethylamine	106-129	monoamine oxidase B	Bos taurus	41-46
11004529-6	2000	75+/-0.11)(0.1xV(w))-4.24+/-(0.16)alpha-Methyl benzylamine analogues are also found to be competitive inhibitors of MAO B-catalyzed benzylamine oxidation.	1-phenethylamine	34-58	monoamine oxidase B	Bos taurus	116-121
11004529-8	2000	Analysis of the binding affinities of five para-substituted alpha-methylbenzylamine analogues to MAO B shows the deprotonated form also to be preferentially bound and the affinity is marginally increased with increasing van der Waals volume of the para-substituent:Log K(i)=-0.71sigma-(0.32)(0.	1-phenethylamine	60-83	monoamine oxidase B	Bos taurus	97-102
12947681-2	2001	1H NMR chemical shift non-equivalence of the methyl doublet of alpha-phenylethylamine was 0.08 ppm(base-line separation) in solvent CDCl3, when the concentration of the sample was 0.051 mol.L-1, the molar ratio between chiral solvating agent and the sample was 0.33.	1-phenethylamine	63-85	immunoglobulin kappa variable 1-16	Homo sapiens	190-193