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rdf:type |
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lifeskim:mentions |
umls-concept:C0003402,
umls-concept:C0017337,
umls-concept:C0019425,
umls-concept:C0025936,
umls-concept:C0332453,
umls-concept:C0538674,
umls-concept:C0599894,
umls-concept:C0871261,
umls-concept:C1280500,
umls-concept:C1521840,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2603343,
umls-concept:C2911692
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pubmed:issue |
12
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pubmed:dateCreated |
2001-3-29
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pubmed:abstractText |
Heme oxygenase-1 (H(mox-1)) has been implicated in protection of cells against ischemia/reperfusion injury.
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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/1,3-dimethylthiourea,
http://linkedlifedata.com/resource/pubmed/chemical/6-hydroxy-2,5,7,8-tetramethylchroman...,
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Chromans,
http://linkedlifedata.com/resource/pubmed/chemical/Creatine Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase-1,
http://linkedlifedata.com/resource/pubmed/chemical/Hmox1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Malondialdehyde,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thiourea
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1524-4539
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
27
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pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1695-701
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11273999-Acetylcysteine,
pubmed-meshheading:11273999-Animals,
pubmed-meshheading:11273999-Antioxidants,
pubmed-meshheading:11273999-Chromans,
pubmed-meshheading:11273999-Creatine Kinase,
pubmed-meshheading:11273999-Disease Models, Animal,
pubmed-meshheading:11273999-Gene Targeting,
pubmed-meshheading:11273999-Heart,
pubmed-meshheading:11273999-Heart Rate,
pubmed-meshheading:11273999-Heme Oxygenase (Decyclizing),
pubmed-meshheading:11273999-Heme Oxygenase-1,
pubmed-meshheading:11273999-Heterozygote,
pubmed-meshheading:11273999-Ischemic Preconditioning, Myocardial,
pubmed-meshheading:11273999-Malondialdehyde,
pubmed-meshheading:11273999-Membrane Proteins,
pubmed-meshheading:11273999-Mice,
pubmed-meshheading:11273999-Mice, Transgenic,
pubmed-meshheading:11273999-Myocardial Contraction,
pubmed-meshheading:11273999-Myocardial Infarction,
pubmed-meshheading:11273999-Myocardial Ischemia,
pubmed-meshheading:11273999-Myocardium,
pubmed-meshheading:11273999-Reperfusion Injury,
pubmed-meshheading:11273999-Thiourea
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pubmed:year |
2001
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pubmed:articleTitle |
H(mox-1) constitutes an adaptive response to effect antioxidant cardioprotection: A study with transgenic mice heterozygous for targeted disruption of the Heme oxygenase-1 gene.
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pubmed:affiliation |
Cardiovascular Research Center, University of Connecticut School of Medicine, Farmington, CT 06030-1110, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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