PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32425592-1 2020 Purpose: Biliverdin reductase A (BLVRA) is a pleiotropic enzyme that converts biliverdin-IX-alpha into the antioxidant and anti-nitrosative compound, bilirubin-IX-alpha. Biliverdine 78-97 biliverdin reductase A Homo sapiens 9-31 32425592-1 2020 Purpose: Biliverdin reductase A (BLVRA) is a pleiotropic enzyme that converts biliverdin-IX-alpha into the antioxidant and anti-nitrosative compound, bilirubin-IX-alpha. Biliverdine 78-97 biliverdin reductase A Homo sapiens 33-38 31704097-2 2019 Here, we report that inhibition of biliverdin reductase (BVR), the enzyme of the heme degradation pathway converting biliverdin to bilirubin, shifts endothelial phenotype of the primary human aortic endothelial cells (HAECs) to mesenchymal-like one. Biliverdine 35-45 biliverdin reductase A Homo sapiens 57-60 30954759-1 2019 In mammals, the green heme metabolite biliverdin is converted to a yellow anti-oxidant by NAD(P)H-dependent biliverdin reductase (BVR), whereas in O2-dependent photosynthetic organisms it is converted to photosynthetic or light-sensing pigments by ferredoxin-dependent bilin reductases (FDBRs). Biliverdine 38-48 biliverdin reductase A Homo sapiens 108-128 30954759-1 2019 In mammals, the green heme metabolite biliverdin is converted to a yellow anti-oxidant by NAD(P)H-dependent biliverdin reductase (BVR), whereas in O2-dependent photosynthetic organisms it is converted to photosynthetic or light-sensing pigments by ferredoxin-dependent bilin reductases (FDBRs). Biliverdine 38-48 biliverdin reductase A Homo sapiens 130-133 30954759-2 2019 In NADP+-bound and biliverdin-bound BVR-A, two biliverdins are stacked at the binding cleft; one is positioned to accept hydride from NADPH, and the other appears to donate a proton to the first biliverdin through a neighboring arginine residue. Biliverdine 19-29 biliverdin reductase A Homo sapiens 36-41 30954759-2 2019 In NADP+-bound and biliverdin-bound BVR-A, two biliverdins are stacked at the binding cleft; one is positioned to accept hydride from NADPH, and the other appears to donate a proton to the first biliverdin through a neighboring arginine residue. Biliverdine 47-58 biliverdin reductase A Homo sapiens 36-41 30954759-2 2019 In NADP+-bound and biliverdin-bound BVR-A, two biliverdins are stacked at the binding cleft; one is positioned to accept hydride from NADPH, and the other appears to donate a proton to the first biliverdin through a neighboring arginine residue. Biliverdine 47-57 biliverdin reductase A Homo sapiens 36-41 31065010-3 2019 Extending these previous findings, here we show that TLR4-SI expression post-CPB was associated with low serum bilirubin and reduced preoperative expression of biliverdin reductase A (BVRA), the enzyme that converts biliverdin to bilirubin, in patient"s leukocytes. Biliverdine 160-170 biliverdin reductase A Homo sapiens 184-188 31065010-4 2019 Biliverdin inhibited TLR4 signaling in leukocytes and triggered phosphorylation of mTORC2-specific targets, including Akt, PKCzeta, AMPKalpha-LKB1-TSC1/2, and their association with BVRA. Biliverdine 0-10 biliverdin reductase A Homo sapiens 182-186 28708313-1 2018 Human biliverdin reductase (hBVR), is an enzyme, that converts biliverdin to bilirubin, and has been implicated in epithelial-mesenchymal transition (EMT) in breast cancer. Biliverdine 6-16 biliverdin reductase A Homo sapiens 28-32 29249571-6 2018 The conversion of biliverdin to BR is catalyzed by biliverdin reductase-A (BVR-A). Biliverdine 18-28 biliverdin reductase A Homo sapiens 75-80 27166089-2 2016 Human BVR (hBVR) also reduces the hemeoxygenase activity product biliverdin to bilirubin and is directly activated by insulin receptor kinase (IRK). Biliverdine 65-75 biliverdin reductase A Homo sapiens 6-9 27166089-2 2016 Human BVR (hBVR) also reduces the hemeoxygenase activity product biliverdin to bilirubin and is directly activated by insulin receptor kinase (IRK). Biliverdine 65-75 biliverdin reductase A Homo sapiens 11-15 27387768-2 2016 Antioxidant defense is accepted to include biotransformation of biliverdin (BV) into bilirubin (BR) through BV reductase alpha (BVRalpha). Biliverdine 64-74 biliverdin reductase A Homo sapiens 128-136 27387768-2 2016 Antioxidant defense is accepted to include biotransformation of biliverdin (BV) into bilirubin (BR) through BV reductase alpha (BVRalpha). Biliverdine 76-78 biliverdin reductase A Homo sapiens 128-136 25196843-2 2014 Biliverdin reductase (BVR) then catalyzes conversion of biliverdin to bilirubin. Biliverdine 56-66 biliverdin reductase A Homo sapiens 0-20 25196843-2 2014 Biliverdin reductase (BVR) then catalyzes conversion of biliverdin to bilirubin. Biliverdine 56-66 biliverdin reductase A Homo sapiens 22-25 24095978-4 2014 HO-1/BVR-A reduces the intracellular levels of pro-oxidant heme and generates equimolar amounts of the free radical scavengers biliverdin-IX alpha (BV)/bilirubin-IX alpha (BR) as well as the pleiotropic gaseous neuromodulator carbon monoxide (CO) and ferrous iron. Biliverdine 127-140 biliverdin reductase A Homo sapiens 5-10 24113378-2 2013 Human biliverdin reductase (hBVR), an enzyme involved in the conversion of biliverdin into bilirubin in heme metabolism, was recently identified as an important cytoprotectant against oxidative stress and hypoxia. Biliverdine 6-16 biliverdin reductase A Homo sapiens 28-32 22823425-1 2012 Human biliverdin-IXalpha reductase (hBVR-A) catalyzes the conversion of biliverdin-IXalpha to bilirubin-IXalpha in the last step of heme degradation and is a key enzyme in regulating a wide range of cellular responses. Biliverdine 6-24 biliverdin reductase A Homo sapiens 36-42 22823425-3 2012 The present study employed induced fit docking (IFD) to study the substrate binding modes to hBVR-A of biliverdin-IXalpha and four analogues. Biliverdine 103-121 biliverdin reductase A Homo sapiens 93-99 22823425-6 2012 Furthermore, the ternary complex structure of hBVR-A binding with biliverdin-IXalpha and the electron donor cofactor NADPH obtained from MD simulations was exploited to investigate the catalytic mechanism, by calculating the reaction energy profile using the quantum mechanics/molecular mechanics (QM/MM) method. Biliverdine 66-84 biliverdin reductase A Homo sapiens 46-52 22584576-1 2012 Human biliverdin reductase (hBVR), a Ser/Thr/Tyr kinase, inhibits apoptosis by reducing biliverdin-IX to antioxidant bilirubin. Biliverdine 88-101 biliverdin reductase A Homo sapiens 28-32 22438843-10 2012 The BVR was reported to confer an antioxidant redox amplification cycle by which low, physiological bilirubin concentrations confer potent antioxidant protection via recycling of biliverdin from oxidized bilirubin by the BVR, linking this sink for oxidants to the NADPH pool. Biliverdine 179-189 biliverdin reductase A Homo sapiens 4-7 22438843-10 2012 The BVR was reported to confer an antioxidant redox amplification cycle by which low, physiological bilirubin concentrations confer potent antioxidant protection via recycling of biliverdin from oxidized bilirubin by the BVR, linking this sink for oxidants to the NADPH pool. Biliverdine 179-189 biliverdin reductase A Homo sapiens 221-224 22438844-2 2012 Conversion of BV to bilirubin (BR) is catalyzed by biliverdin reductase (BVR) and is required for the downstream signaling and nuclear localization of BVR. Biliverdine 14-16 biliverdin reductase A Homo sapiens 51-71 22438844-2 2012 Conversion of BV to bilirubin (BR) is catalyzed by biliverdin reductase (BVR) and is required for the downstream signaling and nuclear localization of BVR. Biliverdine 14-16 biliverdin reductase A Homo sapiens 73-76 22438844-2 2012 Conversion of BV to bilirubin (BR) is catalyzed by biliverdin reductase (BVR) and is required for the downstream signaling and nuclear localization of BVR. Biliverdine 14-16 biliverdin reductase A Homo sapiens 151-154 22457648-6 2012 In this regard, the biliverdin to bilirubin conversion pathway, via biliverdin reductase (BVR), is suggested to be another major protective mechanism that scavenges lipophilic oxidants because of the lipophilic nature of bilirubin. Biliverdine 20-30 biliverdin reductase A Homo sapiens 68-88 22457648-6 2012 In this regard, the biliverdin to bilirubin conversion pathway, via biliverdin reductase (BVR), is suggested to be another major protective mechanism that scavenges lipophilic oxidants because of the lipophilic nature of bilirubin. Biliverdine 20-30 biliverdin reductase A Homo sapiens 90-93 21241799-1 2011 Biliverdin reductase-A is a pleiotropic enzyme involved not only in the reduction of biliverdin-IX-alpha into bilirubin-IX-alpha, but also in the regulation of glucose metabolism and cell growth secondary to its serine/threonine/tyrosine kinase activity. Biliverdine 85-95 biliverdin reductase A Homo sapiens 0-22 21278388-0 2011 A homozygous nonsense mutation (c.214C->A) in the biliverdin reductase alpha gene (BLVRA) results in accumulation of biliverdin during episodes of cholestasis. Biliverdine 53-63 biliverdin reductase A Homo sapiens 86-91 21099244-1 2011 Biliverdin reductase A (BLVRA), an enzyme that converts biliverdin to bilirubin, has recently emerged as a key regulator of the cellular redox cycle. Biliverdine 56-66 biliverdin reductase A Homo sapiens 0-22 21099244-1 2011 Biliverdin reductase A (BLVRA), an enzyme that converts biliverdin to bilirubin, has recently emerged as a key regulator of the cellular redox cycle. Biliverdine 56-66 biliverdin reductase A Homo sapiens 24-29 20704544-2 2010 BVR is the sole catalyst for the conversion of biliverdin-IXalpha the activity product of the stress-inducible HO-1 and the constitutive HO-2, to bilirubin-IXalpha. Biliverdine 47-57 biliverdin reductase A Homo sapiens 0-3 20679134-2 2010 Enzymatic studies with the purified 30-kDa form of HO-1 routinely use a coupled assay containing biliverdin reductase (BVR), which converts BV to bilirubin (BR). Biliverdine 119-121 biliverdin reductase A Homo sapiens 97-117 20410444-10 2010 Biliverdin, but not bilirubin, was as effective as TNF-alpha in inhibiting hBVR promoter activity. Biliverdine 0-10 biliverdin reductase A Homo sapiens 75-79 20410444-15 2010 Because hypoxia positively influences hBVR promoter and phosphorylation and TNF-alpha activated NF-kappaB inhibits the promoter, while biliverdin inhibits both NF-kappaB activity and hBVR promoter, we propose a regulatory mechanism for NF-kappaB by hypoxia and TNF-alpha centered on hBVR/biliverdin. Biliverdine 135-145 biliverdin reductase A Homo sapiens 183-187 20410444-15 2010 Because hypoxia positively influences hBVR promoter and phosphorylation and TNF-alpha activated NF-kappaB inhibits the promoter, while biliverdin inhibits both NF-kappaB activity and hBVR promoter, we propose a regulatory mechanism for NF-kappaB by hypoxia and TNF-alpha centered on hBVR/biliverdin. Biliverdine 135-145 biliverdin reductase A Homo sapiens 183-187 20430037-0 2010 Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1-evidence for direct and indirect antioxidant actions of bilirubin. Biliverdine 14-24 biliverdin reductase A Homo sapiens 41-61 20430037-8 2010 Moreover, protection by hemin-induced HO-1 expression or biliverdin-triggered bilirubin formation was impaired upon silencing of the HO-1 or BVR gene, respectively. Biliverdine 57-67 biliverdin reductase A Homo sapiens 141-144 19690164-1 2009 In mammalian cells, heme is degraded by heme oxygenase to biliverdin, which is then reduced to bilirubin by biliverdin reductase (BVR). Biliverdine 58-68 biliverdin reductase A Homo sapiens 108-128 19690164-1 2009 In mammalian cells, heme is degraded by heme oxygenase to biliverdin, which is then reduced to bilirubin by biliverdin reductase (BVR). Biliverdine 58-68 biliverdin reductase A Homo sapiens 130-133 19509285-1 2009 Biliverdin reductase A (BVR) catalyzes the reduction of biliverdin (BV) to bilirubin (BR) in all cells. Biliverdine 56-66 biliverdin reductase A Homo sapiens 24-27 19509285-4 2009 The enzymatic conversion of BV to BR on the surface by BVR initiates a signaling cascade through tyrosine phosphorylation of BVR on the cytoplasmic tail. Biliverdine 28-30 biliverdin reductase A Homo sapiens 55-58 19509285-4 2009 The enzymatic conversion of BV to BR on the surface by BVR initiates a signaling cascade through tyrosine phosphorylation of BVR on the cytoplasmic tail. Biliverdine 28-30 biliverdin reductase A Homo sapiens 125-128 19614742-2 2009 Biliverdin-IXalpha reductase (BVR-A) is most active with its physiological substrate biliverdin-IXalpha, but can also reduce the three other biliverdin isomers IXbeta, IXdelta and IXgamma. Biliverdine 85-103 biliverdin reductase A Homo sapiens 0-28 19614742-2 2009 Biliverdin-IXalpha reductase (BVR-A) is most active with its physiological substrate biliverdin-IXalpha, but can also reduce the three other biliverdin isomers IXbeta, IXdelta and IXgamma. Biliverdine 85-103 biliverdin reductase A Homo sapiens 30-35 19614742-2 2009 Biliverdin-IXalpha reductase (BVR-A) is most active with its physiological substrate biliverdin-IXalpha, but can also reduce the three other biliverdin isomers IXbeta, IXdelta and IXgamma. Biliverdine 85-95 biliverdin reductase A Homo sapiens 0-28 19614742-2 2009 Biliverdin-IXalpha reductase (BVR-A) is most active with its physiological substrate biliverdin-IXalpha, but can also reduce the three other biliverdin isomers IXbeta, IXdelta and IXgamma. Biliverdine 85-95 biliverdin reductase A Homo sapiens 30-35 19614742-4 2009 Therefore, the activity of BVR-A can be measured using biliverdin-IXalpha as a specific substrate. Biliverdine 55-73 biliverdin reductase A Homo sapiens 27-32 19614742-9 2009 In the present study, we report that a number of sterically locked conformers of 18-ethylbiliverdin-IXalpha are substrates for human BVR-A, and discuss the implications for the biliverdin binding site. Biliverdine 89-99 biliverdin reductase A Homo sapiens 133-138 18412543-1 2008 hBVR (human biliverdin reductase) is an enzyme that reduces biliverdin (the product of haem oxygenases HO-1 and HO-2 activity) to the antioxidant bilirubin. Biliverdine 12-22 biliverdin reductase A Homo sapiens 0-4 18241201-2 2008 Mechanistically it is a good model for BVR-A (biliverdin-IXalpha reductase), a potential pharmacological target for neonatal jaundice and also a potential target for adjunct therapy to maintain protective levels of biliverdin-IXalpha during organ transplantation. Biliverdine 46-64 biliverdin reductase A Homo sapiens 39-44 18395354-5 2008 BVR was known for a long time solely as an enzyme reducing biliverdin to bilirubin in the heme metabolic pathway. Biliverdine 59-69 biliverdin reductase A Homo sapiens 0-3 18276984-1 2008 Biliverdin reductase (BVR) was known for a long time solely as an enzyme converting biliverdin to bilirubin, the major physiological antioxidant. Biliverdine 84-94 biliverdin reductase A Homo sapiens 0-20 18276984-1 2008 Biliverdin reductase (BVR) was known for a long time solely as an enzyme converting biliverdin to bilirubin, the major physiological antioxidant. Biliverdine 84-94 biliverdin reductase A Homo sapiens 22-25 18276984-8 2008 In conclusion, BVR together with its substrate, biliverdin, and product, bilirubin, are revealed to be important players in cellular signal transduction pathways, gene expression and oxidative response. Biliverdine 48-58 biliverdin reductase A Homo sapiens 15-18 17919068-7 2007 The emergence of biliverdin and bilirubin as a newly defined category of modulators of cell signaling and kinase activity further underscores the critical input of hBVR in the response of intracellular pathways into the external environment. Biliverdine 17-27 biliverdin reductase A Homo sapiens 164-168 16287987-1 2005 Biliverdin reductase (BVR) functions in cell signaling through three distinct tracks: a dual-specificity kinase that functions in the insulin receptor/MAPK pathways (25, 29, 51); a bzip-type transcription factor for ATF-2/CREB and HO-1 regulation (1, 25); and a reductase that catalyzes the conversion of biliverdin to bilirubin (27). Biliverdine 305-315 biliverdin reductase A Homo sapiens 0-20 16287987-1 2005 Biliverdin reductase (BVR) functions in cell signaling through three distinct tracks: a dual-specificity kinase that functions in the insulin receptor/MAPK pathways (25, 29, 51); a bzip-type transcription factor for ATF-2/CREB and HO-1 regulation (1, 25); and a reductase that catalyzes the conversion of biliverdin to bilirubin (27). Biliverdine 305-315 biliverdin reductase A Homo sapiens 22-25 15665804-1 2004 OBJECTIVES: The purpose of this study was to localize in cranial ganglia of man the occurrence of the putative gaseous neural messenger carbon monoxide (CO) and the biliverdin degrading enzyme biliverdin reductase (BVR). Biliverdine 165-175 biliverdin reductase A Homo sapiens 193-213 14988408-1 2004 Biliverdin IXalpha reductase (BVR) catalyzes reduction of the HO activity product, biliverdin, to bilirubin. Biliverdine 83-93 biliverdin reductase A Homo sapiens 0-28 14988408-1 2004 Biliverdin IXalpha reductase (BVR) catalyzes reduction of the HO activity product, biliverdin, to bilirubin. Biliverdine 83-93 biliverdin reductase A Homo sapiens 30-33 11909697-2 2002 Several studies have been published on the localization of the carbon monoxide producing enzyme heme oxygenase-2 (HO-2), which concomitantly generates biliverdin; histochemical data on the distribution of biliverdin reductase (BVR), converting biliverdin to bilirubin, are still very scarce in large mammals including humans. Biliverdine 205-215 biliverdin reductase A Homo sapiens 227-230 11773068-1 2002 Human biliverdin reductase (hBVR) is a serine/threonine kinase that catalyzes reduction of the heme oxygenase (HO) activity product, biliverdin, to bilirubin. Biliverdine 6-16 biliverdin reductase A Homo sapiens 28-32 11278740-1 2001 Biliverdin reductase (BVR) reduces heme oxygenase (HO) activity product, biliverdin, to bilirubin. Biliverdine 73-83 biliverdin reductase A Homo sapiens 0-20 11278740-1 2001 Biliverdin reductase (BVR) reduces heme oxygenase (HO) activity product, biliverdin, to bilirubin. Biliverdine 73-83 biliverdin reductase A Homo sapiens 22-25 11224564-2 2001 BVR-B displays a preference for biliverdin isomers without propionates straddling the C10 position, in contrast to biliverdin IXalpha reductase (BVR-A), the major form of BVR in adult human liver. Biliverdine 32-42 biliverdin reductase A Homo sapiens 0-3 11224565-1 2001 Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Biliverdine 92-102 biliverdin reductase A Homo sapiens 0-20 11224565-1 2001 Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Biliverdine 92-102 biliverdin reductase A Homo sapiens 22-25 10957639-1 2000 Biliverdin reductase (BVR) catalyzes the final step of haem degradation and converts biliverdin to bilirubin using NAD(P)H as an electron donor. Biliverdine 85-95 biliverdin reductase A Homo sapiens 0-20 10957639-1 2000 Biliverdin reductase (BVR) catalyzes the final step of haem degradation and converts biliverdin to bilirubin using NAD(P)H as an electron donor. Biliverdine 85-95 biliverdin reductase A Homo sapiens 22-25 8631357-2 1996 Biliverdin IXalpha reductase (BVR) catalyzes the conversion of the heme b degradation product, biliverdin, to bilirubin. Biliverdine 95-105 biliverdin reductase A Homo sapiens 0-28 8631357-2 1996 Biliverdin IXalpha reductase (BVR) catalyzes the conversion of the heme b degradation product, biliverdin, to bilirubin. Biliverdine 95-105 biliverdin reductase A Homo sapiens 30-33 1417867-1 1992 Biliverdins with extended conformations are reduced by biliverdin reductase (BvR) at higher rates than biliverdins with helical conformations. Biliverdine 0-11 biliverdin reductase A Homo sapiens 55-75 1417867-1 1992 Biliverdins with extended conformations are reduced by biliverdin reductase (BvR) at higher rates than biliverdins with helical conformations. Biliverdine 0-11 biliverdin reductase A Homo sapiens 77-80 1417867-1 1992 Biliverdins with extended conformations are reduced by biliverdin reductase (BvR) at higher rates than biliverdins with helical conformations. Biliverdine 103-114 biliverdin reductase A Homo sapiens 55-75 1417867-1 1992 Biliverdins with extended conformations are reduced by biliverdin reductase (BvR) at higher rates than biliverdins with helical conformations. Biliverdine 103-114 biliverdin reductase A Homo sapiens 77-80 1417867-2 1992 To find out the molecular basis for this important feature of BvR mechanism, helical and extended biliverdins were titrated for their acid-base equilibria in a protic solvent (methanol). Biliverdine 98-109 biliverdin reductase A Homo sapiens 62-65 34924900-9 2021 Treatment of both cell lines with biliverdin plus DTNB, a BVR-A inhibitor, increased the cell death significantly when compared with biliverdin alone. Biliverdine 34-44 biliverdin reductase A Homo sapiens 58-63 34224815-1 2021 Biliverdin reductase-A (BVR) catalyzes the reduction of heme-derived biliverdin into bilirubin, this latter being a powerful endogenous free radical scavenger. Biliverdine 69-79 biliverdin reductase A Homo sapiens 0-22 34224815-1 2021 Biliverdin reductase-A (BVR) catalyzes the reduction of heme-derived biliverdin into bilirubin, this latter being a powerful endogenous free radical scavenger. Biliverdine 69-79 biliverdin reductase A Homo sapiens 24-27 2759328-15 1989 The finding of a very low, but measurable BVR activity in lapine liver and spleen may explain, in part, why rabbits, unlike rats, cattle and sheep, excrete primarily biliverdin (70%) into bile. Biliverdine 166-176 biliverdin reductase A Homo sapiens 42-45