Results 21 to 30 of about 107,951 (150)

Biliverdin Reductase inhibitors did not improve severe unconjugated hyperbilirubinemia in vivo

open access: yesScientific Reports, 2017
We aimed to identify potent biliverdin reductase (BVRA) inhibitors as a novel concept for the treatment of severe unconjugated hyperbilirubinemia. 1280 FDA-approved compounds were screened in vitro for their ability to inhibit human and rat BVRA activity
Remco van Dijk   +8 more
doaj   +2 more sources

The Heme Oxygenase/Biliverdin Reductase System and Its Genetic Variants in Physiology and Diseases [PDF]

open access: yesAntioxidants
Heme oxygenase (HO) metabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin-IXα (BV), the latter being reduced into bilirubin-IXα (BR) by the biliverdin reductase-A (BVR).
Cesare Mancuso
doaj   +2 more sources

Biliverdin reductase in cardiovascular inflammation [PDF]

open access: yes, 2011
Biliverdin Reductase (BVR) functions downstream of Heme Oxygenase 1 (HO-1) in the process of heme degradation and catalyses the reduction of biliverdin to bilirubin.
Sangha, Jason
core   +7 more sources

Cycling the Wagons for Biliverdin Reductase [PDF]

open access: yesJournal of Biological Chemistry, 2009
This letter was prompted by our reading of the article by Maghzal et al. (1). Bilirubin (BR) is a major physiologic antioxidant cytoprotectant. Tissue levels are only in nanomolar concentrations, because high levels are neurotoxic, yet BR protects against micromolar levels of oxidants because of a cycle wherein biliverdin (BV) generated by BR ...
Thomas W, Sedlak, Solomon H, Snyder
openaire   +2 more sources

Biliverdin reductase: A major physiologic cytoprotectant [PDF]

open access: yesProceedings of the National Academy of Sciences, 2002
Bilirubin, an abundant pigment that causes jaundice, has long lacked any clear physiologic role. It arises from enzymatic reduction by biliverdin reductase of biliverdin, a product of heme oxygenase activity. Bilirubin is a potent antioxidant that we show can protect cells from a 10,000-fold excess of H 2
David E, Baranano   +3 more
openaire   +2 more sources

Abnormal modulation of cell protective systems in response to ischemic/reperfusion injury is important in the development of mouse sickle cell hepatopathy

open access: yesHaematologica, 2011
Background Sickle cell disease, a genetic red cell disorder inherited in an autosomal recessive manner, occurs throughout the world. Hepatic dysfunction and liver damage may be present in sickle cell disease, but the pathogenesis of these conditions is ...
Angela Siciliano   +10 more
doaj   +1 more source

A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity

open access: yesNature Communications, 2017
Biliverdin reductase (BVR) catalyses the last step in haem degradation. Here the authors present the crystal structure of cyanobacterial BVR bound to its substrate biliverdin and oxidised cofactor NADP+, which was used to propose the catalytic mechanism ...
Haruna Takao   +16 more
doaj   +1 more source

The Nuclear Translocation of Heme Oxygenase-1 in Human Diseases

open access: yesFrontiers in Cell and Developmental Biology, 2022
Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), free iron and biliverdin, which could then be converted to bilirubin by biliverdin reductase.
Qing Yang, Wenqian Wang
doaj   +1 more source

The Role of Bilirubin and the Other “Yellow Players” in Neurodegenerative Diseases

open access: yesAntioxidants, 2020
Bilirubin is a yellow endogenous derivate of the heme catabolism. Since the 1980s, it has been recognized as one of the most potent antioxidants in nature, able to counteract 10,000× higher intracellular concentrations of H2O2.
Sri Jayanti   +3 more
doaj   +1 more source

Identifying structural and dynamic changes during the Biliverdin Reductase B catalytic cycle

open access: yesFrontiers in Molecular Biosciences, 2023
Biliverdin Reductase B (BLVRB) is an NADPH-dependent reductase that catalyzes the reduction of multiple substrates and is therefore considered a critical cellular redox regulator.
Eunjeong Lee   +6 more
doaj   +1 more source

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