Results 1 to 10 of about 216,047 (380)

Heme oxygenase-1 deficiency alters erythroblastic island formation, steady-state erythropoiesis and red blood cell lifespan in mice

open access: yesHaematologica, 2015
Heme oxygenase-1 is critical for iron recycling during red blood cell turnover, whereas its impact on steady-state erythropoiesis and red blood cell lifespan is not known. We show here that in 8- to 14-week old mice, heme oxygenase-1 deficiency adversely
Stuart T. Fraser   +13 more
doaj   +2 more sources

Carnitine metabolism to trimethylamine by an unusual Rieske-type oxygenase from human microbiota [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2014
Dietary intake of L-carnitine can promote cardiovascular diseases in humans through microbial production of trimethylamine (TMA) and its subsequent oxidation to trimethylamine N-oxide (TMAO) by hepatic flavin-containing monooxygenases.
Bugg, Tim   +6 more
core   +2 more sources

STUDIES ON OXYGENASES

open access: hybridJournal of Biological Chemistry, 1957
Simon Rothberg   +2 more
openaire   +4 more sources

The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. [PDF]

open access: greenProceedings of the National Academy of Sciences of the United States of America, 1968
R Tenhunen, Harvey S. Marver, R. Schmid
openalex   +2 more sources

Hemin as a protective agent in an in vitro model of hypoxia/reoxygenation-induced injury. [PDF]

open access: yesSAGE Open Med
Objective: Ischemia-reperfusion injury exacerbates myocardial damage and affects the prognosis of patients with ST-elevation myocardial infarction. This study investigates the potential cytoprotective effects of hemin in an in vitro cardiomyocyte model ...
Wang Z, Liu W.
europepmc   +2 more sources

Heme Oxygenase-1 Signaling and Redox Homeostasis in Physiopathological Conditions

open access: yesBiomolecules, 2021
Heme-oxygenase is the enzyme responsible for degradation of endogenous iron protoporphyirin heme; it catalyzes the reaction’s rate-limiting step, resulting in the release of carbon monoxide (CO), ferrous ions, and biliverdin (BV), which is successively ...
Valeria Consoli   +3 more
semanticscholar   +1 more source

Structure and mutation of deoxypodophyllotoxin synthase (DPS) from Podophyllum hexandrum

open access: yesFrontiers in Catalysis, 2023
Deoxypodophyllotoxin synthase (DPS) is a 2-oxoglutarate (2-OG) dependent non-heme iron (II) dioxygenase that catalyzes the stereoselective ring-closing carbon-carbon bond formation of deoxypodophyllotoxin from the aryllignan (−)-yatein ...
Zoe Ingold   +3 more
doaj   +1 more source

Polystyrene Degradation by Exiguobacterium sp. RIT 594: Preliminary Evidence for a Pathway Containing an Atypical Oxygenase

open access: yesMicroorganisms, 2022
The widespread use of plastics has led to their increasing presence in the environment and subsequent pollution. Some microorganisms degrade plastics in natural ecosystems and the associated metabolic pathways can be studied to understand the degradation
Anutthaman Parthasarathy   +6 more
doaj   +1 more source

The Diverse Roles of Heme Oxygenase-1 in Tumor Progression

open access: yesFrontiers in Immunology, 2021
Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).
Kim Ngan Luu Hoang   +2 more
semanticscholar   +1 more source

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