The heme synthesis and degradation pathways: role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties.
By S. Ryter, R. Tyrrell. Free Radical Biology & Medicine, 2000
850 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology, Pediatrics, Perinatology and Child Health
View Paper: https://www.semanticscholar.org/paper/64a6d1d3f1918d1fc3b982445909e1fb3e540a4b
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cell Biology
In Molecular Biology
In Pediatrics, Perinatology and Child Health
Citations in the corpus
- Iron metabolism and toxicity. (2005, background): “Interestingly, heme iron (either bfreeQ or within hemoproteins) may also catalyze the formation of radicals, mainly via formation of oxoferryl intermediates (Ryter and Tyrrell, 2000) (Fig.”
- Carbon Monoxide: Endogenous Production, Physiological Functions, and Pharmacological Applications (2005, background): “Normal cellular functions would be disturbed and pathological cellular injuries exacerbated (Dennery et al., 1998; Ryter and Tyrrell, 2000).”
- Oxidative stress in the pathogenesis of skin disease. (2006, background): “In addition, heme pathway intermediates may have prooxidant effects, whereas heme oxyge- nase, an enzyme that degrades heme, can function as both an antioxidant and a pro-oxidant (Ryter and Tyrrell, 2000).”