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Heme oxygenase 1 overexpression increases iron fluxes in Caco-2 cells
(Sociedad de Biología de Chile, 2006)
Heme oxygenase 1 overexpression increases iron fluxes in Caco-2 cells
(2006)
Heme oxygenase-1 is a microsomal enzyme that, when induced by stress, protects the cells from oxidative
injury. Heme oxygenase-1 participates in the cleavage of the heme ring producing biliverdin, CO and ferrous
Fe. The ...
Desaturation and heme elevation during COVID-19 infection: a potential prognostic factor of heme oxygenase-1
Increased heme levels, anemia, and desaturation occur during infection. We aimed to
compare the levels of heme, heme oxygenase-1 (HO-1), ferritin, and bilirubin in coronavirus
disease 2019 (COVID-19) patients at different ...
Heme-iron utilization by Leptospira interrogans requires a heme oxygenase and a plastidic-type ferredoxin-NADP+ reductase
(Elsevier Science, 2014-07)
Background: Heme oxygenase catalyzes the conversion of heme to iron, carbon monoxide and biliverdin employing oxygen and reducing equivalents. This enzyme is essential for heme-iron utilization and contributes to virulence ...
Adaptive Potential of the Heme Oxygenase/Carbon Monoxide Pathway During Hypoxia
(Frontiers Media, 2020)
Heme oxygenase (HO) enzymes catalyze heme into biliverdin, releasing carbon monoxide (CO) and iron into circulation. These byproducts of heme degradation can have potent cytoprotective effects in the face of stressors such ...
A heme-degradation pathway in a blood-sucking insect
(National Academy of Sciences, 2020)
HmuS and HmuQ of Ensifer/Sinorhizobium meliloti degrade heme in vitro and participate in heme metabolism in vivo
(Springer, 2016-04)
Ensifer meliloti is a nitrogen-fixing symbiont of the alfalfa legume able to use heme as an iron source. The transport mechanism involved in heme acquisition in E. meliloti has been identified and characterized, but the ...
Heme-oxygenases during erythropoiesis in K562 and human bone marrow cells
(Public Library of Science, 2018)
Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism
(Public Library of Science, 2017-08)
Heme oxygenase from Leptospira interrogans is an important virulence factor. During catalysis, redox equivalents are provided to this enzyme by the plastidic-type ferredoxin-NADP+ reductase also found in L. interrogans. ...