PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2023912-3 1991 Exon 12 codes for the covalent FAD-binding-site and is the most conserved exon; the MAOA and MAOB exon 12 products share 93.9% peptide identity. Flavin-Adenine Dinucleotide 31-34 monoamine oxidase A Homo sapiens 84-88 10482460-7 1999 As a result of this work, a model is proposed for the reversible inhibition of MAO A by befloxatone via long distance, reversible interactions with the flavin adenine dinucleotide (FAD) cofactor of the enzyme and with specific amino acids of the active site. Flavin-Adenine Dinucleotide 152-179 monoamine oxidase A Homo sapiens 79-84 10482460-7 1999 As a result of this work, a model is proposed for the reversible inhibition of MAO A by befloxatone via long distance, reversible interactions with the flavin adenine dinucleotide (FAD) cofactor of the enzyme and with specific amino acids of the active site. Flavin-Adenine Dinucleotide 181-184 monoamine oxidase A Homo sapiens 79-84 8428624-1 1993 Monoamine oxidase (MAO)-A and MAO-B are FAD-containing mitochondrial enzymes which catabolize biogenic and xenobiotic amines. Flavin-Adenine Dinucleotide 40-43 monoamine oxidase A Homo sapiens 0-25 2764901-0 1989 Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit. Flavin-Adenine Dinucleotide 96-99 monoamine oxidase A Homo sapiens 0-19 2125217-0 1990 Catalytically active monoamine oxidase type A from human liver expressed in Saccharomyces cerevisiae contains covalent FAD. Flavin-Adenine Dinucleotide 119-122 monoamine oxidase A Homo sapiens 21-45 33279529-1 2021 Monoamine oxidases (MAO-A and MAO-B) are the two flavin adenine dinucleotide (FAD) enzymes that play an important role in neurotransmitter homeostasis and in protection against biogenic amines. Flavin-Adenine Dinucleotide 49-76 monoamine oxidase A Homo sapiens 20-25 33279529-1 2021 Monoamine oxidases (MAO-A and MAO-B) are the two flavin adenine dinucleotide (FAD) enzymes that play an important role in neurotransmitter homeostasis and in protection against biogenic amines. Flavin-Adenine Dinucleotide 78-81 monoamine oxidase A Homo sapiens 20-25 29958841-9 2018 A molecular modeling study of virodhamine with MAO-B and its cofactor flavin adenine dinucleotide (FAD) predicted virodhamine"s terminal -NH2 group to be positioned near the N5 position of FAD, but for docking to MAO-A, virodhamine"s terminal -NH2 group was far away (~6.52 A) from the N5 position of FAD, and encountered bad contacts with nearby water molecules. Flavin-Adenine Dinucleotide 70-97 monoamine oxidase A Homo sapiens 213-218 29958841-9 2018 A molecular modeling study of virodhamine with MAO-B and its cofactor flavin adenine dinucleotide (FAD) predicted virodhamine"s terminal -NH2 group to be positioned near the N5 position of FAD, but for docking to MAO-A, virodhamine"s terminal -NH2 group was far away (~6.52 A) from the N5 position of FAD, and encountered bad contacts with nearby water molecules. Flavin-Adenine Dinucleotide 99-102 monoamine oxidase A Homo sapiens 213-218 29892597-2 2018 We characterized the covalent cyanine structure linking the multi-target propargylamine inhibitor ASS234 and the flavin adenine dinucleotide in MAO-A using a combination of ultra-high performance liquid chromatography, spectroscopy, mass spectrometry, and computational methods. Flavin-Adenine Dinucleotide 113-140 monoamine oxidase A Homo sapiens 144-149 24165164-7 2014 Furthermore, ability to inhibit both MAO-A and MAO-B can be potentialized by the formation of hydrogen bonds between these compounds and FAD and/or the residues in the active site. Flavin-Adenine Dinucleotide 137-140 monoamine oxidase A Homo sapiens 37-42 27734680-3 2016 In this work, we present atomistic empirical valence bond simulations of the rate-limiting step of the MAO-A-catalyzed NA (norepinephrine) degradation, involving hydride transfer from the substrate alpha-methylene group to the flavin moiety of the flavin adenine dinucleotide prosthetic group, employing the full dimensionality and thermal fluctuations of the hydrated enzyme, with extensive configurational sampling. Flavin-Adenine Dinucleotide 248-275 monoamine oxidase A Homo sapiens 103-108 20410615-4 2010 Docking studies show that the imine moiety is located in hydrophobic pocket, bringing the propargyl group close to FAD which indicates that the different inhibitory potency toward MAO-A may be ascribable to both the distance between alkynyl group and N5 of FAD, and hydrogen bonding interactions between inhibitors and enzymes. Flavin-Adenine Dinucleotide 115-118 monoamine oxidase A Homo sapiens 180-185 20843688-3 2010 Docking study was carried out to demonstrate the binding mode between a9 and MAO-A/B, and the result reveals that a9 localized in the "aromatic cage" and oriented to establish pi-pi stacking interactions with Tyr407, Tyr444 and FAD in MAO-A rather than in MAO-B. Flavin-Adenine Dinucleotide 228-231 monoamine oxidase A Homo sapiens 77-84 20843688-3 2010 Docking study was carried out to demonstrate the binding mode between a9 and MAO-A/B, and the result reveals that a9 localized in the "aromatic cage" and oriented to establish pi-pi stacking interactions with Tyr407, Tyr444 and FAD in MAO-A rather than in MAO-B. Flavin-Adenine Dinucleotide 228-231 monoamine oxidase A Homo sapiens 77-82 23242744-1 2013 Monoamine oxidases (MAO) A and B are flavin adenine dinucleotides containing enzymes bound to the mitochondrial outer membranes of the cells of the brain, liver, intestine, and placenta, as well as platelets. Flavin-Adenine Dinucleotide 37-65 monoamine oxidase A Homo sapiens 0-32 20410615-4 2010 Docking studies show that the imine moiety is located in hydrophobic pocket, bringing the propargyl group close to FAD which indicates that the different inhibitory potency toward MAO-A may be ascribable to both the distance between alkynyl group and N5 of FAD, and hydrogen bonding interactions between inhibitors and enzymes. Flavin-Adenine Dinucleotide 257-260 monoamine oxidase A Homo sapiens 180-185 18951803-5 2008 However, only compound 22 was able to form hydrogen bonds with FAD, a finding which was in accordance with its potent anti-MAO-A activity. Flavin-Adenine Dinucleotide 63-66 monoamine oxidase A Homo sapiens 123-128 19091581-11 2009 The very high MAO-B selectivity for 4i can be also explained in terms of the distance between the FAD and the compound, which was greater in the complex of MAO-A-4i as compared to the corresponding MAO-B complex. Flavin-Adenine Dinucleotide 98-101 monoamine oxidase A Homo sapiens 156-161 12445480-6 2002 D-Amphetamine, harmine, and tetrindole stabilise the semiquinone form of FAD during reduction of MAO A by dithionite and no further reduction of these inhibitor-MAO A complexes has been observed. Flavin-Adenine Dinucleotide 73-76 monoamine oxidase A Homo sapiens 97-102 14697881-0 2004 The FAD binding sites of human monoamine oxidases A and B. Flavin-Adenine Dinucleotide 4-7 monoamine oxidase A Homo sapiens 31-57 14697881-3 2004 Since those amino acids interacting with the FAD are conserved in monoamine oxidase A (MAO A), it is proposed that the FAD binding site in MAO A is quite similar to that in MAO B. Flavin-Adenine Dinucleotide 45-48 monoamine oxidase A Homo sapiens 66-85 14697881-3 2004 Since those amino acids interacting with the FAD are conserved in monoamine oxidase A (MAO A), it is proposed that the FAD binding site in MAO A is quite similar to that in MAO B. Flavin-Adenine Dinucleotide 45-48 monoamine oxidase A Homo sapiens 87-92 14697881-3 2004 Since those amino acids interacting with the FAD are conserved in monoamine oxidase A (MAO A), it is proposed that the FAD binding site in MAO A is quite similar to that in MAO B. Flavin-Adenine Dinucleotide 45-48 monoamine oxidase A Homo sapiens 139-144 14697881-3 2004 Since those amino acids interacting with the FAD are conserved in monoamine oxidase A (MAO A), it is proposed that the FAD binding site in MAO A is quite similar to that in MAO B. Flavin-Adenine Dinucleotide 119-122 monoamine oxidase A Homo sapiens 66-85 14697881-3 2004 Since those amino acids interacting with the FAD are conserved in monoamine oxidase A (MAO A), it is proposed that the FAD binding site in MAO A is quite similar to that in MAO B. Flavin-Adenine Dinucleotide 119-122 monoamine oxidase A Homo sapiens 87-92 14697881-3 2004 Since those amino acids interacting with the FAD are conserved in monoamine oxidase A (MAO A), it is proposed that the FAD binding site in MAO A is quite similar to that in MAO B. Flavin-Adenine Dinucleotide 119-122 monoamine oxidase A Homo sapiens 139-144 11911838-6 2002 Difference absorption spectral studies showed similar perturbations of the covalent FAD moieties of both human MAO A and MAO B, which suggests a similar mode of binding in both enzymes. Flavin-Adenine Dinucleotide 84-87 monoamine oxidase A Homo sapiens 111-116 11263670-8 2001 Cu2+ dose-dependently reduced flavin adenine dinucleotide (FAD)-dependent monoamine oxidase A (MAO-A) activity in a time-independent manner, with an IC50 value approximately 20 microM, whereas Mn2+ had no effect. Flavin-Adenine Dinucleotide 30-57 monoamine oxidase A Homo sapiens 74-93 11331009-4 2001 Use of the fungal enzyme, MAO N, which lacks the covalent attachment to the flavin adenine dinucleotide (FAD) cofactor present in the mammalian forms MAO A and MAO B, has allowed for the isolation and further structural identification of the flavin-inactivator adduct. Flavin-Adenine Dinucleotide 105-108 monoamine oxidase A Homo sapiens 150-155 11761322-1 2001 The midpoint potentials for the reduction of the cysteinyl-flavin adenine dinucleotide (FAD) in monoamine oxidases (MAO) A and B in the absence and presence of ligands have been determined. Flavin-Adenine Dinucleotide 88-91 monoamine oxidase A Homo sapiens 96-128 11263670-8 2001 Cu2+ dose-dependently reduced flavin adenine dinucleotide (FAD)-dependent monoamine oxidase A (MAO-A) activity in a time-independent manner, with an IC50 value approximately 20 microM, whereas Mn2+ had no effect. Flavin-Adenine Dinucleotide 30-57 monoamine oxidase A Homo sapiens 95-100 11263670-8 2001 Cu2+ dose-dependently reduced flavin adenine dinucleotide (FAD)-dependent monoamine oxidase A (MAO-A) activity in a time-independent manner, with an IC50 value approximately 20 microM, whereas Mn2+ had no effect. Flavin-Adenine Dinucleotide 59-62 monoamine oxidase A Homo sapiens 74-93 11263670-8 2001 Cu2+ dose-dependently reduced flavin adenine dinucleotide (FAD)-dependent monoamine oxidase A (MAO-A) activity in a time-independent manner, with an IC50 value approximately 20 microM, whereas Mn2+ had no effect. Flavin-Adenine Dinucleotide 59-62 monoamine oxidase A Homo sapiens 95-100 10877844-1 2000 The FAD binding site of human liver monoamine oxidase A (MAO A) has been investigated by mutagenesis of the amino acid site of covalent FAD attachment (Cys-406) to an alanyl residue. Flavin-Adenine Dinucleotide 4-7 monoamine oxidase A Homo sapiens 36-55 10877844-1 2000 The FAD binding site of human liver monoamine oxidase A (MAO A) has been investigated by mutagenesis of the amino acid site of covalent FAD attachment (Cys-406) to an alanyl residue. Flavin-Adenine Dinucleotide 4-7 monoamine oxidase A Homo sapiens 57-62 10877844-1 2000 The FAD binding site of human liver monoamine oxidase A (MAO A) has been investigated by mutagenesis of the amino acid site of covalent FAD attachment (Cys-406) to an alanyl residue. Flavin-Adenine Dinucleotide 136-139 monoamine oxidase A Homo sapiens 36-55 10877844-1 2000 The FAD binding site of human liver monoamine oxidase A (MAO A) has been investigated by mutagenesis of the amino acid site of covalent FAD attachment (Cys-406) to an alanyl residue. Flavin-Adenine Dinucleotide 136-139 monoamine oxidase A Homo sapiens 57-62