Results 261 to 270 of about 60,693 (303)
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American Journal of Respiratory and Critical Care Medicine, 2005
As aspects of basic science come to play an increasingly prominent role in clinical medicine, heme oxygenase-1 is one of several molecules emerging as a central player in diseases of the lung and intensive care unit. Although the apparent raison d'être of this enzyme is to dispose of heme, its activity results in cytoprotection against oxidative injury
Danielle, Morse, Augustine M K, Choi
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As aspects of basic science come to play an increasingly prominent role in clinical medicine, heme oxygenase-1 is one of several molecules emerging as a central player in diseases of the lung and intensive care unit. Although the apparent raison d'être of this enzyme is to dispose of heme, its activity results in cytoprotection against oxidative injury
Danielle, Morse, Augustine M K, Choi
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Altered Expression of Heme Oxygenase 2 in Heme Oxygenase 1–deficient Mouse Embryos
Journal of Histochemistry & Cytochemistry, 2023Heme oxygenases (Hmoxs) are enzymes that catalyze the first and rate-limiting step in the degradation of heme to carbon monoxide, iron, and biliverdin. The two main isozymes, namely Hmox1 and Hmox2, are encoded by two different genes. Mutation of the Hmox1 gene in mice is known to cause extensive prenatal lethality, and limited information is ...
Meenakshi Rana +4 more
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Heme oxygenase and renal disease
Current Hypertension Reports, 2009The cellular content of heme, derived from the breakdown of heme proteins, is regulated via the heme oxygenase (HO) enzyme system. HO catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide, and biliverdin.
Tambi, Jarmi, Anupam, Agarwal
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DNA and Cell Biology, 2002
Heme plays a significant pathogenic role in several diseases involving the kidney. The cellular content of heme, derived either from the delivery of filtered heme proteins such as hemoglobin and myoglobin, or from the breakdown of ubiquitous intracellular heme proteins, is regulated via the heme oxygenase enzyme system.
Nathalie, Hill-Kapturczak +2 more
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Heme plays a significant pathogenic role in several diseases involving the kidney. The cellular content of heme, derived either from the delivery of filtered heme proteins such as hemoglobin and myoglobin, or from the breakdown of ubiquitous intracellular heme proteins, is regulated via the heme oxygenase enzyme system.
Nathalie, Hill-Kapturczak +2 more
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Current Pharmaceutical Design, 2008
Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin. In the recent years, HO-1 expression has been reported as an important protective endogenous mechanism against physical, chemical and biological stress.
FERRÁNDIZ, M.L., Devesa Giner, Isabel
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Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin. In the recent years, HO-1 expression has been reported as an important protective endogenous mechanism against physical, chemical and biological stress.
FERRÁNDIZ, M.L., Devesa Giner, Isabel
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2014
Many microbial pathogens are known to possess heme acquisition systems that allow the organisms to utilize heme or heme-bound proteins as sources of iron. These systems have been demonstrated to procure iron from heme, hemoglobin, haptoglobin, or hemopexin and are identified as nonsiderophore heme iron acquisition systems.
Melanie Ratliff-Griffin +2 more
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Many microbial pathogens are known to possess heme acquisition systems that allow the organisms to utilize heme or heme-bound proteins as sources of iron. These systems have been demonstrated to procure iron from heme, hemoglobin, haptoglobin, or hemopexin and are identified as nonsiderophore heme iron acquisition systems.
Melanie Ratliff-Griffin +2 more
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2005
The heme oxygenase (HO) system is the rate-limiting step in the conversion of heme into biliverdin, carbon monoxide (CO) and free iron (Fe). This oxidation reaction involves a sequence of transformations that consumes three molecules of O2 and seven electrons. In mammals, the electrons are provided by NADPH-cytochrome-P-450 reductase. Three HO isoforms
Sei-ichiro Tsuchihashi +2 more
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The heme oxygenase (HO) system is the rate-limiting step in the conversion of heme into biliverdin, carbon monoxide (CO) and free iron (Fe). This oxidation reaction involves a sequence of transformations that consumes three molecules of O2 and seven electrons. In mammals, the electrons are provided by NADPH-cytochrome-P-450 reductase. Three HO isoforms
Sei-ichiro Tsuchihashi +2 more
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Heme oxygenase, steering dioxygen activation toward heme hydroxylation
Journal of Inorganic Biochemistry, 2005The activation of dioxygen by heme oxygenase proceeds via formation of an obligatory ferric hydroperoxide intermediate (FeIII-OOH), as is the case in the activation of dioxygen by monooxygenase enzymes. This review summarizes current understanding of the structural and dynamic properties in heme oxygenase that channel the reactivity of the FeIII-OOH ...
Mario, Rivera, Yuhong, Zeng
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The mechanism of heme oxygenase
Current Opinion in Chemical Biology, 2000Major advances have been made in determining the structure of heme oxygenase and the relationship between its structure and catalytic activity. The nature of the first step in the reaction sequence, heme alpha-meso-hydroxylation, is now clear, although the mechanisms that control the alpha-regiospecificity remain elusive. Hypothetical mechanisms can be
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Proceedings of the Society for Experimental Biology and Medicine, 1999
Abstract.Heme is a molecule that is synthesized by the sequential actions of eight enzymes and is ubiquitous throughout nature. For many years it has been known that heme is also catabolized to yield biliverdin (which is subsequently reduced to bilirubin), one atom of iron, and one molecule of carbon monoxide.
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Abstract.Heme is a molecule that is synthesized by the sequential actions of eight enzymes and is ubiquitous throughout nature. For many years it has been known that heme is also catabolized to yield biliverdin (which is subsequently reduced to bilirubin), one atom of iron, and one molecule of carbon monoxide.
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