Results 291 to 300 of about 146,694 (331)
Bi-directional regulation of type I interferon signaling by heme oxygenase-1. [PDF]
iScienceWu M, Fan Y, Li L, Yuan J.
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Highly Selective Novel Heme Oxygenase-1 Hits Found by DNA-Encoded Library Machine Learning beyond the DEL Chemical Space. [PDF]
ACS Med Chem LettHan S +10 more
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Antioxidants & Redox Signaling, 2020
The special issue "Heme-Oxygenase-1" includes original research articles and reviews that are aimed at understanding the role of Heme Oxygenase-1 (HO-1) in several pathophysiological conditions, specially addressing those involving inflammation and ...
Mara Facchinetti
semanticscholar +6 more sources
The special issue "Heme-Oxygenase-1" includes original research articles and reviews that are aimed at understanding the role of Heme Oxygenase-1 (HO-1) in several pathophysiological conditions, specially addressing those involving inflammation and ...
Mara Facchinetti
semanticscholar +6 more sources
Heme oxygenase and heme degradation
Biochemical and Biophysical Research Communications, 2005The microsomal heme oxygenase system consists of heme oxygenase (HO) and NADPH-cytochrome P450 reductase, and plays a key role in the physiological catabolism of heme which yields biliverdin, carbon monoxide, and iron as the final products. Heme degradation proceeds essentially as a series of autocatalytic oxidation reactions involving heme bound to HO.
Masato Noguchi +2 more
openaire +3 more sources
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.
Anupam Agarwal +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.
Anupam Agarwal +2 more
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Chemical Reviews, 1996
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Masanori Sono +3 more
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AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Masanori Sono +3 more
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Mechanism of heme degradation by heme oxygenase
Journal of Inorganic Biochemistry, 2000Heme oxygenase catalyzes the three step-wise oxidation of hemin to alpha-biliverdin, via alpha-meso-hydroxyhemin, verdoheme, and ferric iron-biliverdin complex. This enzyme is a simple protein which does not have any prosthetic groups. However, heme and its two metabolites, alpha-meso-hydroxyhemin and verdoheme, combine with the enzyme and activate ...
Catharina T. Migita, Tadashi Yoshida
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Heme oxygenase-1 and heme oxygenase-2 expression in bruises
Forensic Science, Medicine, and Pathology, 2015The first step in catabolism of hemoglobin in a bruise is performed by the enzyme heme oxygenase, which produces biliverdin that is then reduced to bilirubin. The development of yellow coloration in bruises can be attributed to local accumulation of degradation products of hemoglobin, including bilirubin, but it is not clear why there is a delay before
Claire G. Ross +3 more
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The heme oxygenase system: a regulator of second messenger gases.
Annual Review of Pharmacology and Toxicology, 1997The heme oxygenase (HO) system consists of two forms identified to date: the oxidative stress-inducible protein HO-1 (HSP32) and the constitutive isozyme HO-2. These proteins, which are different gene products, have little in common in primary structure,
M. Maines
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Antioxidants & Redox Signaling, 2004
The importance of heme oxygenases in heme catabolism, iron utilization, and cellular signaling has been recognized for many years and is a well studied process in eukaryotes. Through the accessibility of an increasing number of bacterial genomes, it has become evident that heme oxygenases are also widespread in prokaryotes. In these organisms, the heme
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The importance of heme oxygenases in heme catabolism, iron utilization, and cellular signaling has been recognized for many years and is a well studied process in eukaryotes. Through the accessibility of an increasing number of bacterial genomes, it has become evident that heme oxygenases are also widespread in prokaryotes. In these organisms, the heme
openaire +3 more sources