Biliverdin reductase: A major physiologic cytoprotectant
By D. Barañano, Mahil Rao, C. D. Ferris, S. Snyder. Proceedings of the National Academy of Sciences of the United States of America, 2002
1,121 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology, Pediatrics, Perinatology and Child Health
View Paper: https://www.semanticscholar.org/paper/e62600c88624f84f7f83f18db878c5e55adb4d19
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In Cell Biology
In Molecular Biology
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In Pediatrics, Perinatology and Child Health
Citations in the corpus
- Trends in oxidative aging theories. (2007, background): “New antioxidant genes are still being discovered, for example, heme oxygenase 1 and sulfiredoxin 1 [177,178].”
- Role of oxidative modifications in atherosclerosis. (2004, background): “Recently, biliverdin reductase has been proposed as a cellular protective agent via regeneration of bilirubin (32).”
- Carbon Monoxide: Endogenous Production, Physiological Functions, and Pharmacological Applications (2005, background): “Biliverdin and bilirubin are believed to be the most powerful endogenous antioxidants, efficiently scavenging peroxy radicals and inhibiting lipid peroxidation (Baranano et al., 2002; Stocker et al., 1987).”
- The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: a novel mechanism of human disease. (2005, background): “Carbon monoxide has vasodilatory, antiproliferative, antiinflammatory, and antioxidant properties,(30-33) while biliverdin is an antioxidant that is converted by biliverdin reductase to bilirubin.(34,35) Biliverdin reductase itself has catalytic antioxidant properties.”
- Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications. (2006, background): “BR also protected against H2O2-mediated cell death in HeLa cells at a 10,000-fold molar ratio of oxidant to antioxidant (48).”
- Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production (2008, neutral): “be the best physiological antioxidant (33).”
- Mechanisms of cell protection by heme oxygenase-1. (2010, background): “Heme is a protoporphyrin IX ring that contains in its center an Fe2+ atom that can act as a Fenton reactor to produce highly toxic hydroxyl radicals derived from hydrogen peroxide (H2O2) (4).”
- Reconstruction of Genome-Scale Active Metabolic Networks for 69 Human Cell Types and 16 Cancer Types Using INIT (2012, background): “Biliverdin reductase is known to be a major physiologic cytoprotectant against oxidative stress [39].”
- Pharmacological and Clinical Aspects of Heme Oxygenase (2008, positive): “However, recent studies by Snyder and colleagues (Baranano et al., 2002; Sedlak and Snyder, 2004) found that bilirubin was capable of protecting cells from a 10,000-fold increase in oxidative stress generated by hydrogen peroxide.”
- Heme oxygenase-1: from bench to bedside. (2005, background): “In neural cell culture for example, a minute amount of bilirubin is capable of protecting cells from 10,000-fold higher concentrations of the oxidant hydrogen peroxide (53).”