{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nesbitt NM"],"funding":["Burroughs Wellcome Fund","NHLBI NIH HHS","American Society of Hematology","National Institutes of Health"],"pagination":["164-174"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8311568"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["164"],"pubmed_abstract":["Cytoprotective mechanisms of heme oxygenases function by derivatizing heme to generate carbon monoxide, ferrous iron, and isomeric biliverdins, followed by rapid NAD(P)H-dependent biliverdin reduction to the antioxidant bilirubin using two non-overlapping biliverdin reductases that display biliverdin isomer-restricted redox activity. Although cytoprotective functions of heme oxygenases are widely recognized, concomitant effects of downstream biliverdin reductases remain incomplete. A computational model predicated on murine hematopoietic single-cell transcriptomic data identified Blvrb as a biological driver linked to the tumor necrosis factor stress pathway as a predominant source of variation defining hematopoietic cell heterogeneity. In vivo studies using Blvrb-deficient mice establishe"],"journal":["Free radical biology & medicine"],"pubmed_title":["Divergent erythroid megakaryocyte fates in Blvrb-deficient mice establish non-overlapping cytoprotective functions during stress hematopoiesis."],"pmcid":["PMC8311568"],"funding_grant_id":["R01 HL153144","R44 HL150927","R01 HL119096","R01 HL091939"],"pubmed_authors":["Nesbitt NM","Liu Z","Jares A","Bahou WF","Malone LE","Gnatenko DV","Ma Y","Zhu W"],"additional_accession":[]},"is_claimable":false,"name":"Divergent erythroid megakaryocyte fates in Blvrb-deficient mice establish non-overlapping cytoprotective functions during stress hematopoiesis.","description":"Cytoprotective mechanisms of heme oxygenases function by derivatizing heme to generate carbon monoxide, ferrous iron, and isomeric biliverdins, followed by rapid NAD(P)H-dependent biliverdin reduction to the antioxidant bilirubin using two non-overlapping biliverdin reductases that display biliverdin isomer-restricted redox activity. Although cytoprotective functions of heme oxygenases are widely recognized, concomitant effects of downstream biliverdin reductases remain incomplete. A computational model predicated on murine hematopoietic single-cell transcriptomic data identified Blvrb as a biological driver linked to the tumor necrosis factor stress pathway as a predominant source of variation defining hematopoietic cell heterogeneity. In vivo studies using Blvrb-deficient mice establishe","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Feb","modification":"2026-05-31T08:56:20.153Z","creation":"2025-02-18T23:32:30.015Z"},"accession":"S-EPMC8311568","cross_references":{"pubmed":["33359909"],"doi":["10.1016/j.freeradbiomed.2020.12.015"]}}