rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2001-6-8
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pubmed:abstractText |
Three distinct antioxidant pathways are considered through which iron-catalyzed oxidative stress may be regulated by nitric oxide (NO). The first two pathways involve direct redox interactions of NO with iron catalytic sites and represent a fast response that may be considered an emergency mechanism to protect cells from the consequences of acute and intensive oxidative stress. These are (i) NO-induced nitrosylation at heme and non-heme iron catalytic sites that is capable of directly reducing oxoferryl-associated radicals, (ii) formation of nitrosyl complexes with intracellular "loosely" bound redox-active iron, and (iii) an indirect regulatory pathway that may function as an adaptive mechanism that becomes operational upon long-term exposure of cells to NO. In the latter pathway, NO down-regulates expression of iron-containing proteins to prevent their catalytic prooxidant reactions.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radical Scavengers,
http://linkedlifedata.com/resource/pubmed/chemical/Hemeproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Sulfur Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/tert-Butylhydroperoxide
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1523-0864
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
189-202
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11396475-Animals,
pubmed-meshheading:11396475-Antioxidants,
pubmed-meshheading:11396475-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:11396475-Free Radical Scavengers,
pubmed-meshheading:11396475-Hemeproteins,
pubmed-meshheading:11396475-Hemoglobins,
pubmed-meshheading:11396475-Humans,
pubmed-meshheading:11396475-Iron,
pubmed-meshheading:11396475-Iron-Regulatory Proteins,
pubmed-meshheading:11396475-Iron-Sulfur Proteins,
pubmed-meshheading:11396475-Nitric Oxide,
pubmed-meshheading:11396475-Oxidative Stress,
pubmed-meshheading:11396475-RNA-Binding Proteins,
pubmed-meshheading:11396475-Reactive Oxygen Species,
pubmed-meshheading:11396475-tert-Butylhydroperoxide
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pubmed:year |
2001
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pubmed:articleTitle |
Antioxidant mechanisms of nitric oxide against iron-catalyzed oxidative stress in cells.
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pubmed:affiliation |
Department of Environmental and Occupational Health, University of Pittsburgh, PA 15238, USA. kagan@pitt.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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