PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11281991-2 1999 Phenylethylamine, however, is not stored in intra-neuronal vesicles and is rapidly degraded by monoamine oxidase-B. Phenethylamines 0-16 monoamine oxidase B Homo sapiens 95-114 7601156-5 1995 Whereas exchange of the ADP-binding sequence did not modify the catalytic properties of either MAO isoforms, chimeras with increasing length of the NH2-terminus of MAO-A (up to residue 256) showed a marked decrease in affinity towards the MAO-B substrate phenylethylamine and the inhibitor N-(2-aminoethyl)-5-chloro-2-pyridine carboxamide . Phenethylamines 255-271 monoamine oxidase B Homo sapiens 239-244 8573115-3 1996 Moreover the enzymatic activity of MAO-B towards phenylethylamine and tyramine is also suppressed after this immunoprecipitation, contrary to the MAO-A activity towards 5-hydroxy-tryptamine. Phenethylamines 49-65 monoamine oxidase B Homo sapiens 35-40 8613523-8 1996 In contrast, the only biochemical abnormalities detected in subjects with the MAO-B gene deletion are a complete absence of platelet MAO-B activity and an increased urinary excretion of phenylethylamine. Phenethylamines 186-202 monoamine oxidase B Homo sapiens 78-83 7896422-7 1994 MAO-B activity (pmol/10(8) cells/h) was measured in peripheral blood platelets, using phenylethylamine as substrate. Phenethylamines 86-102 monoamine oxidase B Homo sapiens 0-5 7711493-3 1995 The administration of PEA or of its precursor L-phenylalanine improves mood in depressed patients treated with a selective monoamine oxidase B inhibitor. Phenethylamines 22-25 monoamine oxidase B Homo sapiens 123-142 8044048-0 1994 Phenylethylamine relieves depression after selective MAO-B inhibition. Phenethylamines 0-16 monoamine oxidase B Homo sapiens 53-58 2041591-2 1991 Platelet monoamine oxidase-B activity is increased by the use of phenylethylamine but decreased by the use of dopamine as substrate. Phenethylamines 65-81 monoamine oxidase B Homo sapiens 9-28 8439389-1 1993 An increase in platelet monoamine oxidase (MAO) B activity in drug-free parkinsonians (n = 6) compared with healthy controls (n = 10) has been confirmed using both phenylethylamine (PEA) and dopamine as substrates, reaching statistical significance in the case of PEA oxidising activity (p < 0.05). Phenethylamines 164-180 monoamine oxidase B Homo sapiens 24-49 8439389-1 1993 An increase in platelet monoamine oxidase (MAO) B activity in drug-free parkinsonians (n = 6) compared with healthy controls (n = 10) has been confirmed using both phenylethylamine (PEA) and dopamine as substrates, reaching statistical significance in the case of PEA oxidising activity (p < 0.05). Phenethylamines 182-185 monoamine oxidase B Homo sapiens 24-49 2496202-6 1989 In contrast, the expressed MAO B prefers phenylethylamine as a substrate and is sensitive to the inhibitor deprenyl. Phenethylamines 41-57 monoamine oxidase B Homo sapiens 27-32 2018626-2 1991 This abnormality was associated with almost total (90%) reductions in the oxidatively deaminated urinary metabolites of the MAO-A substrate, norepinephrine, and with marked (100-fold) increases in an MAO-B substrate, phenylethylamine, confirming systemic functional consequences of the genetic enzyme deficiency. Phenethylamines 217-233 monoamine oxidase B Homo sapiens 200-205 3566791-6 1987 The photo-dependent incorporation could be protected by phenylethylamine, the substrate for MAO-B, in a concentration-dependent manner. Phenethylamines 56-72 monoamine oxidase B Homo sapiens 92-97 3083305-2 1986 This assay has been used to show that the rate of oxidation of MPTP parallels that of phenylethylamine in a range of human and rodent tissues, providing strong evidence that this reaction is predominantly catalysed by monoamine oxidase B (MAO-B). Phenethylamines 86-102 monoamine oxidase B Homo sapiens 218-237 20501066-6 1987 They could be protected by the presence of the substrate (phenylethylamine) or inhibitors (pargyline and trans-phenylcyclopropylamine) of MAO-B during photolysis. Phenethylamines 58-74 monoamine oxidase B Homo sapiens 138-143 3083305-2 1986 This assay has been used to show that the rate of oxidation of MPTP parallels that of phenylethylamine in a range of human and rodent tissues, providing strong evidence that this reaction is predominantly catalysed by monoamine oxidase B (MAO-B). Phenethylamines 86-102 monoamine oxidase B Homo sapiens 239-244 28738644-4 2017 Inhibition of hMAO B is evaluated by adding different concentrations of the inhibitor selegiline hydrochloride to the enzyme and applying a defined amount of the hMAO B substrate phenylethylamine (PEA). Phenethylamines 179-195 monoamine oxidase B Homo sapiens 14-20 28738644-4 2017 Inhibition of hMAO B is evaluated by adding different concentrations of the inhibitor selegiline hydrochloride to the enzyme and applying a defined amount of the hMAO B substrate phenylethylamine (PEA). Phenethylamines 179-195 monoamine oxidase B Homo sapiens 162-168 28738644-4 2017 Inhibition of hMAO B is evaluated by adding different concentrations of the inhibitor selegiline hydrochloride to the enzyme and applying a defined amount of the hMAO B substrate phenylethylamine (PEA). Phenethylamines 197-200 monoamine oxidase B Homo sapiens 14-20 28738644-4 2017 Inhibition of hMAO B is evaluated by adding different concentrations of the inhibitor selegiline hydrochloride to the enzyme and applying a defined amount of the hMAO B substrate phenylethylamine (PEA). Phenethylamines 197-200 monoamine oxidase B Homo sapiens 162-168 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. Phenethylamines 101-117 monoamine oxidase B Homo sapiens 131-136 16807522-1 2006 OBJECTIVES: The monoamine oxidase B (MAO-B) is an enzyme involved in metabolism of dopamine, benzylamine, phenylethylamine, tyramine and tryptamine. Phenethylamines 106-122 monoamine oxidase B Homo sapiens 16-35 16807522-1 2006 OBJECTIVES: The monoamine oxidase B (MAO-B) is an enzyme involved in metabolism of dopamine, benzylamine, phenylethylamine, tyramine and tryptamine. Phenethylamines 106-122 monoamine oxidase B Homo sapiens 37-42 15589121-2 2004 As phenylethylamine, a very toxic metabolite of phenylalanine, is rapidly degraded by monoamine oxydase type B, an enzyme that has a very low activity in neonates, these results are consistent with those of the hypothesis of MAO-B acting as a modifying gene in phenylketonuria. Phenethylamines 3-19 monoamine oxidase B Homo sapiens 225-230 11259630-1 2001 The human monoamine oxidase (MAO) B plays a major role in the degradation of biogenic and dietary amines such as phenylethylamine, benzylamine, dopamine, and tyramine. Phenethylamines 113-129 monoamine oxidase B Homo sapiens 10-35 29360121-2 2018 This work investigates the Y326I point mutation effect on the kinetics of oxidative deamination of phenylethylamine (PEA) catalyzed by the monoamine oxidase B (MAO B) enzyme. Phenethylamines 99-115 monoamine oxidase B Homo sapiens 139-158 29360121-2 2018 This work investigates the Y326I point mutation effect on the kinetics of oxidative deamination of phenylethylamine (PEA) catalyzed by the monoamine oxidase B (MAO B) enzyme. Phenethylamines 99-115 monoamine oxidase B Homo sapiens 160-165 29360121-2 2018 This work investigates the Y326I point mutation effect on the kinetics of oxidative deamination of phenylethylamine (PEA) catalyzed by the monoamine oxidase B (MAO B) enzyme. Phenethylamines 117-120 monoamine oxidase B Homo sapiens 139-158 29360121-2 2018 This work investigates the Y326I point mutation effect on the kinetics of oxidative deamination of phenylethylamine (PEA) catalyzed by the monoamine oxidase B (MAO B) enzyme. Phenethylamines 117-120 monoamine oxidase B Homo sapiens 160-165 26091526-2 2015 The Quantum Chemical Cluster Approach was used to obtain transition states of MAO B complexed with phenylethylamine (PEA), benzylamine (BA), and p-nitrobenzylamine (NBA). Phenethylamines 99-115 monoamine oxidase B Homo sapiens 78-83 26091526-2 2015 The Quantum Chemical Cluster Approach was used to obtain transition states of MAO B complexed with phenylethylamine (PEA), benzylamine (BA), and p-nitrobenzylamine (NBA). Phenethylamines 117-120 monoamine oxidase B Homo sapiens 78-83 20123154-3 2010 Making the phenylethylamine scaffold rigid by fixing the amine chain in an extended six-membered ring conformation increased MAO-B (but not MAO-A) inhibitory activity relative to the more flexible alpha-methylated derivative. Phenethylamines 11-27 monoamine oxidase B Homo sapiens 125-130 15461973-4 2004 We suggest here that monoamine oxidase type B, MAOB, an enzyme degrading phenylethylamine, a very toxic metabolite of phenylalanine, could act as a modifying gene since a variant enzymatic activity of MAOB in PKU patients with similar phenylalanine levels would result in different phenylethylamine levels and different clinical outcomes. Phenethylamines 73-89 monoamine oxidase B Homo sapiens 21-45 15461973-4 2004 We suggest here that monoamine oxidase type B, MAOB, an enzyme degrading phenylethylamine, a very toxic metabolite of phenylalanine, could act as a modifying gene since a variant enzymatic activity of MAOB in PKU patients with similar phenylalanine levels would result in different phenylethylamine levels and different clinical outcomes. Phenethylamines 73-89 monoamine oxidase B Homo sapiens 47-51 15461973-4 2004 We suggest here that monoamine oxidase type B, MAOB, an enzyme degrading phenylethylamine, a very toxic metabolite of phenylalanine, could act as a modifying gene since a variant enzymatic activity of MAOB in PKU patients with similar phenylalanine levels would result in different phenylethylamine levels and different clinical outcomes. Phenethylamines 73-89 monoamine oxidase B Homo sapiens 201-205 15461973-4 2004 We suggest here that monoamine oxidase type B, MAOB, an enzyme degrading phenylethylamine, a very toxic metabolite of phenylalanine, could act as a modifying gene since a variant enzymatic activity of MAOB in PKU patients with similar phenylalanine levels would result in different phenylethylamine levels and different clinical outcomes. Phenethylamines 282-298 monoamine oxidase B Homo sapiens 21-45 15461973-4 2004 We suggest here that monoamine oxidase type B, MAOB, an enzyme degrading phenylethylamine, a very toxic metabolite of phenylalanine, could act as a modifying gene since a variant enzymatic activity of MAOB in PKU patients with similar phenylalanine levels would result in different phenylethylamine levels and different clinical outcomes. Phenethylamines 282-298 monoamine oxidase B Homo sapiens 47-51 15461973-4 2004 We suggest here that monoamine oxidase type B, MAOB, an enzyme degrading phenylethylamine, a very toxic metabolite of phenylalanine, could act as a modifying gene since a variant enzymatic activity of MAOB in PKU patients with similar phenylalanine levels would result in different phenylethylamine levels and different clinical outcomes. Phenethylamines 282-298 monoamine oxidase B Homo sapiens 201-205 15461973-5 2004 Finally the report of low MAOB, and consequently expectedly high phenylethylamine levels in neonates is consistent with a phenylethylamine-mediated brain injury possibly causing irreversible damages in PKU newborns prior to onset of the low protein diet. Phenethylamines 122-138 monoamine oxidase B Homo sapiens 26-30