PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10433694-6 1999 The FAD binding sites of QR1 and QR2 are very similar, but their hydride donor binding sites are considerably different. Flavin-Adenine Dinucleotide 4-7 NAD(P)H quinone dehydrogenase 1 Homo sapiens 25-28 22793692-1 2012 NAD(P)H:quinone-oxidoreductase-1 (NQO1) is a cytosolic enzyme that catalyzes the reduction of various quinones using flavin adenine dinucleotide (FAD) as a cofactor. Flavin-Adenine Dinucleotide 117-144 NAD(P)H quinone dehydrogenase 1 Homo sapiens 0-32 22793692-1 2012 NAD(P)H:quinone-oxidoreductase-1 (NQO1) is a cytosolic enzyme that catalyzes the reduction of various quinones using flavin adenine dinucleotide (FAD) as a cofactor. Flavin-Adenine Dinucleotide 117-144 NAD(P)H quinone dehydrogenase 1 Homo sapiens 34-38 22793692-1 2012 NAD(P)H:quinone-oxidoreductase-1 (NQO1) is a cytosolic enzyme that catalyzes the reduction of various quinones using flavin adenine dinucleotide (FAD) as a cofactor. Flavin-Adenine Dinucleotide 146-149 NAD(P)H quinone dehydrogenase 1 Homo sapiens 0-32 22793692-1 2012 NAD(P)H:quinone-oxidoreductase-1 (NQO1) is a cytosolic enzyme that catalyzes the reduction of various quinones using flavin adenine dinucleotide (FAD) as a cofactor. Flavin-Adenine Dinucleotide 146-149 NAD(P)H quinone dehydrogenase 1 Homo sapiens 34-38 10644008-1 1999 DT-diaphorase is an FAD-containing enzyme capable of a two-electron reduction of ortho- and paraquinones. Flavin-Adenine Dinucleotide 20-23 NAD(P)H quinone dehydrogenase 1 Homo sapiens 0-13 12590585-4 2003 The experimental and theoretical studies independently support a model in which quinones (with one to three fused aromatic rings) bind in the QR1 active site utilizing a pi-stacking interaction with the isoalloxazine ring of the FAD cofactor. Flavin-Adenine Dinucleotide 229-232 NAD(P)H quinone dehydrogenase 1 Homo sapiens 142-145 11340659-1 2001 NAD(P)H:quinone oxidoreductase type 1 (QR1, NQO1, formerly DT-diaphorase; EC 1.6.99.2) is an FAD-containing enzyme that catalyzes the nicotinamide nucleotide-dependent reduction of quinones, quinoneimines, azo dyes, and nitro groups. Flavin-Adenine Dinucleotide 93-96 NAD(P)H quinone dehydrogenase 1 Homo sapiens 0-42 11340659-1 2001 NAD(P)H:quinone oxidoreductase type 1 (QR1, NQO1, formerly DT-diaphorase; EC 1.6.99.2) is an FAD-containing enzyme that catalyzes the nicotinamide nucleotide-dependent reduction of quinones, quinoneimines, azo dyes, and nitro groups. Flavin-Adenine Dinucleotide 93-96 NAD(P)H quinone dehydrogenase 1 Homo sapiens 44-48 11340659-1 2001 NAD(P)H:quinone oxidoreductase type 1 (QR1, NQO1, formerly DT-diaphorase; EC 1.6.99.2) is an FAD-containing enzyme that catalyzes the nicotinamide nucleotide-dependent reduction of quinones, quinoneimines, azo dyes, and nitro groups. Flavin-Adenine Dinucleotide 93-96 NAD(P)H quinone dehydrogenase 1 Homo sapiens 59-72 9367528-3 1997 The present investigation has revealed that like DT-diaphorase, NQO2 is a dimer enzyme with one FAD prosthetic group per subunit. Flavin-Adenine Dinucleotide 96-99 NAD(P)H quinone dehydrogenase 1 Homo sapiens 49-62 9050836-0 1997 Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase) A mammalian cytosolic FAD-dependent enzyme that catalyzes the reduction of quinones by N-ribosyl- and N-alkyldihydronicotinamides, but not by NADH, NADPH, or NMNH (reduced nicotinamide mononucleotide), was isolated from bovine kidney more than 30 years ago [S. Liao, J. T. Dulaney and H. G. Williams-Ashman (1962) J. Biol. Flavin-Adenine Dinucleotide 147-150 NAD(P)H quinone dehydrogenase 1 Homo sapiens 110-123 7531691-1 1995 NAD(P)H:quinone oxidoreductase (EC 1.6.99.2) (DT-diaphorase) is an FAD-containing enzyme that catalyzes the 2-electron reduction of quinones to hydroquinones using either NADH or NADPH as the electron donor. Flavin-Adenine Dinucleotide 67-70 NAD(P)H quinone dehydrogenase 1 Homo sapiens 46-59 7531691-10 1995 The results suggest that DT-diaphorase shows the same properties as the C-C transhydrogenases, and the binding of dicumarol elicits a conformational change or an adjustment in the polarity of the FAD pocket. Flavin-Adenine Dinucleotide 196-199 NAD(P)H quinone dehydrogenase 1 Homo sapiens 25-38 2202258-6 1990 In seven isolates, a flavin compound (riboflavin, flavin adenine dinucleotide, or flavin mononucleotide) was required for azoreductase activity. Flavin-Adenine Dinucleotide 50-77 NAD(P)H quinone dehydrogenase 1 Homo sapiens 122-134 30615965-3 2019 In this work, binding of anions to the FAD binding pocket of human NAD(P)H:quinone oxidoreductase 1 (NQO1), a flavoprotein associated with cancer due to a common polymorphism causing a P187S amino acid substitution, was investigated. Flavin-Adenine Dinucleotide 39-42 NAD(P)H quinone dehydrogenase 1 Homo sapiens 67-99 31726777-4 2019 Herein, we have used hydrogen/deuterium exchange monitored by mass spectrometry (HDXMS) to investigate the structural dynamics of NQO1 in three ligation states: without ligands (NQO1apo), with FAD (NQO1holo) and with FAD and the inhibitor dicoumarol (NQO1dic). Flavin-Adenine Dinucleotide 193-196 NAD(P)H quinone dehydrogenase 1 Homo sapiens 130-134 31726777-4 2019 Herein, we have used hydrogen/deuterium exchange monitored by mass spectrometry (HDXMS) to investigate the structural dynamics of NQO1 in three ligation states: without ligands (NQO1apo), with FAD (NQO1holo) and with FAD and the inhibitor dicoumarol (NQO1dic). Flavin-Adenine Dinucleotide 217-220 NAD(P)H quinone dehydrogenase 1 Homo sapiens 130-134 31726777-5 2019 We show that NQO1apo has a minimally stable folded core holding the protein dimer, with FAD and dicoumarol binding sites populating binding non-competent conformations. Flavin-Adenine Dinucleotide 88-91 NAD(P)H quinone dehydrogenase 1 Homo sapiens 13-17 30615965-3 2019 In this work, binding of anions to the FAD binding pocket of human NAD(P)H:quinone oxidoreductase 1 (NQO1), a flavoprotein associated with cancer due to a common polymorphism causing a P187S amino acid substitution, was investigated. Flavin-Adenine Dinucleotide 39-42 NAD(P)H quinone dehydrogenase 1 Homo sapiens 101-105 30615965-5 2019 Herein, binding and protein stability analyses were carried out to show that anion binding to the apo-state of NQO1 P187S inhibits FAD binding with increasing strength following the chaotropic behavior of anions. Flavin-Adenine Dinucleotide 131-134 NAD(P)H quinone dehydrogenase 1 Homo sapiens 111-115 26822308-6 2016 Moreover, our studies reveal an extensive binding interface between E6a and the isoalloxazine ring of the flavin adenine dinucleotide (FAD) cofactor of NQO1 in addition to interactions with protein side chains in the active site. Flavin-Adenine Dinucleotide 106-133 NAD(P)H quinone dehydrogenase 1 Homo sapiens 152-156 28771686-1 2017 The cancer-associated P187S polymorphism in the NAD(P)H:quinone oxidoreductase 1 (NQO1) abolishes enzyme activity by strongly reducing FAD binding affinity. Flavin-Adenine Dinucleotide 135-138 NAD(P)H quinone dehydrogenase 1 Homo sapiens 48-80 28291250-4 2017 NQO1 is a FAD-dependent, two-domain multifunctional stress protein acting as a Phase II enzyme, activating cancer pro-drugs and stabilizing p53 and p73alpha oncosuppressors. Flavin-Adenine Dinucleotide 10-13 NAD(P)H quinone dehydrogenase 1 Homo sapiens 0-4 28771686-1 2017 The cancer-associated P187S polymorphism in the NAD(P)H:quinone oxidoreductase 1 (NQO1) abolishes enzyme activity by strongly reducing FAD binding affinity. Flavin-Adenine Dinucleotide 135-138 NAD(P)H quinone dehydrogenase 1 Homo sapiens 82-86 28771686-3 2017 To provide mechanistic insight into these effects, we report here a detailed structural and thermodynamic characterization of FAD binding to these NQO1 variants. Flavin-Adenine Dinucleotide 126-129 NAD(P)H quinone dehydrogenase 1 Homo sapiens 147-151 26838129-2 2016 Here, we use biochemical, biophysical, cell and computational biology tools to study two loss-of-function and cancer-associated polymorphisms (p.R139W and p.P187S) in human NAD(P)H quinone oxidoreductase 1 (NQO1), a FAD-dependent enzyme which activates cancer pro-drugs and stabilizes several oncosuppressors. Flavin-Adenine Dinucleotide 216-219 NAD(P)H quinone dehydrogenase 1 Homo sapiens 173-205 26822308-6 2016 Moreover, our studies reveal an extensive binding interface between E6a and the isoalloxazine ring of the flavin adenine dinucleotide (FAD) cofactor of NQO1 in addition to interactions with protein side chains in the active site. Flavin-Adenine Dinucleotide 135-138 NAD(P)H quinone dehydrogenase 1 Homo sapiens 152-156