PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29494209-5 2018 The antioxidant bilirubin and the enzyme that generates it, biliverdin reductase A (BVRA), are components of the heme catabolic pathway that have been shown to reduce hepatic steatosis. Heme 113-117 biliverdin reductase A Homo sapiens 84-88 25196843-0 2014 Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase. Heme 46-50 biliverdin reductase A Homo sapiens 121-141 28389660-10 2017 This was supported by an altered heme catabolism, indirectly reflecting in elevated unconjugated bilirubin (UCB; main phenotypic feature of GS) and iron, decreased hemopexin (Hpx) and Hpt and in up-regulated biliverdin reductase (BLVRA) gene expressions. Heme 33-37 biliverdin reductase A Homo sapiens 208-228 28389660-10 2017 This was supported by an altered heme catabolism, indirectly reflecting in elevated unconjugated bilirubin (UCB; main phenotypic feature of GS) and iron, decreased hemopexin (Hpx) and Hpt and in up-regulated biliverdin reductase (BLVRA) gene expressions. Heme 33-37 biliverdin reductase A Homo sapiens 230-235 25864768-1 2015 The heme oxygenase/biliverdin reductase (HO/BVR) pathway enhances cell stress response by degrading excess heme or producing antioxidant and cytoprotective molecules. Heme 4-8 biliverdin reductase A Homo sapiens 41-47 27316791-2 2016 Human biliverdin reductase (hBVR), an enzyme in the heme metabolism pathway, is involved in hypoxia-induced renal tubular EMT. Heme 52-56 biliverdin reductase A Homo sapiens 28-32 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. Heme 104-108 biliverdin reductase A Homo sapiens 28-32 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. Heme 59-63 biliverdin reductase A Homo sapiens 5-10 22408623-1 2012 Bilirubin-IX-alpha (BR) is the final product of heme metabolism through the heme oxygenase/biliverdin reductase (HO/BVR) system. Heme 48-52 biliverdin reductase A Homo sapiens 113-119 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. Heme 132-136 biliverdin reductase A Homo sapiens 6-34 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. Heme 132-136 biliverdin reductase A Homo sapiens 36-42 24813317-5 2013 Among the main components of the cell stress response is the heme oxygenase/biliverdin reductase (HO/BVR) axis, which catalyzes the degradation of heme which is toxic if produced in excess or under redox unbalanced conditions. Heme 61-65 biliverdin reductase A Homo sapiens 101-104 18395354-5 2008 BVR was known for a long time solely as an enzyme reducing biliverdin to bilirubin in the heme metabolic pathway. Heme 90-94 biliverdin reductase A Homo sapiens 0-3 19702533-1 2009 The heme oxygenase/biliverdin reductase (HO/BVR) axis catalyzes the degradation of heme, but this system and its by-products, carbon monoxide (CO) and bilirubin, have also been shown to exert cytoprotective effects by activating pro-survival pathways and scavenging free radicals. Heme 4-8 biliverdin reductase A Homo sapiens 41-47 19702533-4 2009 However, upregulation of the HO/BVR axis is not always beneficial for cells: the heme depletion and accumulation of CO and bilirubin it causes are potentially toxic. Heme 81-85 biliverdin reductase A Homo sapiens 29-35 19690164-1 2009 In mammalian cells, heme is degraded by heme oxygenase to biliverdin, which is then reduced to bilirubin by biliverdin reductase (BVR). Heme 20-24 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). Heme 20-24 biliverdin reductase A Homo sapiens 130-133 16287987-0 2005 New insights into biliverdin reductase functions: linking heme metabolism to cell signaling. Heme 58-62 biliverdin reductase A Homo sapiens 18-38 17919068-8 2007 Structural features of BVR and recent findings relevant to its function in cell-signaling pathways are reviewed here and are intended to complement a recent commentary on the role of BVR in linking heme metabolism and cell signaling. Heme 198-202 biliverdin reductase A Homo sapiens 23-26 12969425-5 2003 Together with the observation that Mg-porphyrin accumulation in dark-grown seedlings treated with an iron chelator was unaffected by BVR expression, these results indicate that BVR diverts tetrapyrrole metabolism toward heme synthesis while also reducing heme levels to de-repress ALA synthesis. Heme 220-224 biliverdin reductase A Homo sapiens 177-180 12969425-5 2003 Together with the observation that Mg-porphyrin accumulation in dark-grown seedlings treated with an iron chelator was unaffected by BVR expression, these results indicate that BVR diverts tetrapyrrole metabolism toward heme synthesis while also reducing heme levels to de-repress ALA synthesis. Heme 255-259 biliverdin reductase A Homo sapiens 177-180 11278740-14 2001 The results define a previously unknown mechanism for regulation of BVR activity and are discussed in the context of their relevance to heme metabolism. Heme 136-140 biliverdin reductase A Homo sapiens 68-71 11773068-10 2002 The potential significance of the AP-1 binding is suggested by the finding that the response of HO-1, in COS cells stably transfected with antisense hBVR, with 66% reduced BVR activity, to superoxide anion (O(2)()) formed by menadione is attenuated, whereas induction by heme is not affected. Heme 271-275 biliverdin reductase A Homo sapiens 149-153 11773068-10 2002 The potential significance of the AP-1 binding is suggested by the finding that the response of HO-1, in COS cells stably transfected with antisense hBVR, with 66% reduced BVR activity, to superoxide anion (O(2)()) formed by menadione is attenuated, whereas induction by heme is not affected. Heme 271-275 biliverdin reductase A Homo sapiens 150-153 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. Heme 56-60 biliverdin reductase A Homo sapiens 0-22 34453944-1 2021 AIM: Biliverdin reductase-A (BVR-A) other than its canonical role in the degradation pathway of heme as partner of heme oxygenase-1 (HO1), has recently drawn attention as a protein with pleiotropic functions involved in insulin-glucose homeostasis. Heme 96-100 biliverdin reductase A Homo sapiens 5-27 34453944-1 2021 AIM: Biliverdin reductase-A (BVR-A) other than its canonical role in the degradation pathway of heme as partner of heme oxygenase-1 (HO1), has recently drawn attention as a protein with pleiotropic functions involved in insulin-glucose homeostasis. Heme 96-100 biliverdin reductase A Homo sapiens 29-34 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. Heme 56-60 biliverdin reductase A Homo sapiens 24-27 35628384-4 2022 In the last decades, several studies have highlighted that biliverdin reductase-A (BVR-A), over its canonical role in the degradation of heme, acts as a regulator of insulin signaling. Heme 137-141 biliverdin reductase A Homo sapiens 59-81 35628384-4 2022 In the last decades, several studies have highlighted that biliverdin reductase-A (BVR-A), over its canonical role in the degradation of heme, acts as a regulator of insulin signaling. Heme 137-141 biliverdin reductase A Homo sapiens 83-88 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. Heme 81-85 biliverdin reductase A Homo sapiens 35-55 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. Heme 81-85 biliverdin reductase A Homo sapiens 57-60 31704097-4 2019 BVR-deficiency induces the activity of Nrf2 transcription factor and increases heme oxygenase-1 (HO-1) level, which is accompanied by the reduction of cellular heme content, increase in a free iron fraction and oxidative stress. Heme 79-83 biliverdin reductase A Homo sapiens 0-3 30556496-0 2020 Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures. Heme 72-76 biliverdin reductase A Homo sapiens 105-108 30556496-2 2020 Heme is first cleaved by the enzyme heme oxygenase (HO) to the linear tetrapyrrole biliverdin IXalpha (BV), and BV is then converted to bilirubin by biliverdin reductase (BVR). Heme 0-4 biliverdin reductase A Homo sapiens 149-169 30556496-2 2020 Heme is first cleaved by the enzyme heme oxygenase (HO) to the linear tetrapyrrole biliverdin IXalpha (BV), and BV is then converted to bilirubin by biliverdin reductase (BVR). Heme 0-4 biliverdin reductase A Homo sapiens 171-174