Results 11 to 20 of about 414,627 (398)
Gut microbiota facilitates dietary heme-induced epithelial hyperproliferation by opening the mucus barrier in colon [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2015 Colorectal cancer risk is associated with diets high in red meat. Heme, the pigment of red meat, induces cytotoxicity of colonic contents and elicits epithelial damage and compensatory hyperproliferation, leading to hyperplasia.
Clara Belzer +13 more
core +3 more sources
Role of Heme Oxygenase as a Modulator of Heme-Mediated Pathways [PDF]
Antioxidants, 2019 The heme oxygenase (HO) system is essential for heme and iron homeostasis and necessary for adaptation to cell stress. HO degrades heme to biliverdin (BV), carbon monoxide (CO) and ferrous iron.
J. Duvigneau +2 more
semanticscholar +5 more sources
From Synthesis to Utilization: The Ins and Outs of Mitochondrial Heme
Cells, 2020 Heme is a ubiquitous and essential iron containing metallo-organic cofactor required for virtually all aerobic life. Heme synthesis is initiated and completed in mitochondria, followed by certain covalent modifications and/or its delivery to apo ...
Samantha A. Swenson +5 more
doaj +2 more sources
Antioxidants, 2022 The heme oxygenase (HO) enzyme system catabolizes heme to carbon monoxide (CO), ferrous iron, and biliverdin-IXα (BV), which is reduced to bilirubin-IXα (BR) by biliverdin reductase (BVR).
S. Ryter
semanticscholar +1 more source
Molecular Mechanisms of Iron and Heme Metabolism.
Annual review of nutrition, 2022 An abundant metal in the human body, iron is essential for key biological pathways including oxygen transport, DNA metabolism, and mitochondrial function.
S. Dutt, I. Hamza, T. Bartnikas
semanticscholar +1 more source
Heme Oxygenase-1 Signaling and Redox Homeostasis in Physiopathological Conditions
Biomolecules, 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
Proceedings of the National Academy of Sciences of the United States of America, 2022 Significance Heme availability in the cell enables the proper folding and function of enzymes, which carry heme as a cofactor. Using genome-scale modeling, we identified metabolic fluxes and genes that limit heme production.
O. P. Ishchuk +6 more
semanticscholar +1 more source
Antimicrobial Agents and Chemotherapy, 2003 A recent Letter to the Editor (R. K. Haynes, D. Monti, D. Taramelli, N. Basilico, S. Parapini, and P. Olliaro, Letter, Antimicrob. Agents Chemother. 47:1175, 2003) presented cogent evidence that artemisinin and its derivatives do not inhibit hemozoin formation in vitro.
Haynes, Richard K. +5 more
openaire +6 more sources
Blood, 2021 Sickle cell disease (SCD) is characterized by increased hemolysis which results in plasma heme overload and ultimately cardiovascular complications. Here, we hypothesized that increased heme in SCD causes upregulation of heme oxygenase 1 (Hmox1) which ...
Archita V. Menon +6 more
semanticscholar +1 more source
Heme‐hemopexin: A ‘Chronosteric’ heme‐protein [PDF]
IUBMB Life, 2007 AbstractHemopexin (HPX) serves as scavenger and transporter of toxic plasma heme to the liver. HPX is formed by two four‐bladed β‐propeller domains, resembling two thick disks that lock together at a 90° angle. The heme is bound between the two β‐propeller domains in a pocket formed by the interdomain linker peptide.
ASCENZI P, FASANO, MAURO
openaire +5 more sources