PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10858451-8 2000 The flavin reductase activity of biliverdin-IXbeta reductase is potently inhibited by mesobiliverdin-XIIIalpha and protohemin, which is consistent with the hypothesis that the tetrapyrrole and flavin substrate bind at a common site. 4,6-dinitro-o-cresol 4-10 biliverdin reductase B Homo sapiens 33-60 27207795-4 2016 BLVRB(S111L) encompassed within the substrate/cofactor [alpha/beta dinucleotide NAD(P)H] binding fold is a functionally defective redox coupler using flavin and biliverdin (BV) IXbeta tetrapyrrole(s) and results in exaggerated reactive oxygen species accumulation as a putative metabolic signal leading to differential hematopoietic lineage commitment and enhanced thrombopoiesis. 4,6-dinitro-o-cresol 150-156 biliverdin reductase B Homo sapiens 0-5 7400118-0 1980 Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. 4,6-dinitro-o-cresol 35-41 biliverdin reductase B Homo sapiens 80-102 29487133-5 2018 We found that the most potent BLVRB inhibitors contain a tricyclic hydrocarbon core structure similar to the isoalloxazine ring of flavin mononucleotide and that both xanthene- and acridine-based compounds inhibit BLVRB"s flavin and dichlorophenolindophenol (DCPIP) reductase functions. 4,6-dinitro-o-cresol 131-137 biliverdin reductase B Homo sapiens 30-35 34095235-1 2021 The biliverdin reductase B (BLVRB) class of enzymes catalyze the NADPH-dependent reduction of multiple flavin substrates and are emerging as critical players in cellular redox regulation. 4,6-dinitro-o-cresol 103-109 biliverdin reductase B Homo sapiens 4-26 34095235-1 2021 The biliverdin reductase B (BLVRB) class of enzymes catalyze the NADPH-dependent reduction of multiple flavin substrates and are emerging as critical players in cellular redox regulation. 4,6-dinitro-o-cresol 103-109 biliverdin reductase B Homo sapiens 28-33 7400118-5 1980 These results apparently suggest that the NADPH-flavin reductase system is able to reduce methemoglobin in erythrocytes at a moderate speed with about 1 microM flavin, and the reduction was estimated to vary from less than 1% to about 20% of that by the NADH-cytochrome b5 reductase system with 1 microM cytochrome b5, depending on the uptake of flavin by human erythrocytes. 4,6-dinitro-o-cresol 160-166 biliverdin reductase B Homo sapiens 42-64