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rdf:type |
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lifeskim:mentions |
umls-concept:C0014257,
umls-concept:C0031715,
umls-concept:C0036720,
umls-concept:C0040005,
umls-concept:C0040669,
umls-concept:C0132555,
umls-concept:C0243044,
umls-concept:C0277785,
umls-concept:C0392756,
umls-concept:C1158884,
umls-concept:C1522564,
umls-concept:C1882911
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pubmed:issue |
8
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pubmed:dateCreated |
2004-8-6
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pubmed:abstractText |
The interaction of the heat shock protein 90 (Hsp90) with the endothelial NO synthase (eNOS) has been shown to account for a sustained production of NO in vitro. Here, we examined whether overexpression of Hsp90 in a pig model of cardiac infarct could preserve the myocardium from the deleterious effects of ischemia-reperfusion.
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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/AKT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Calcineurin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lactams, Macrocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/NG-Nitroarginine Methyl Ester,
http://linkedlifedata.com/resource/pubmed/chemical/NOS3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type III,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphothreonine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factor A,
http://linkedlifedata.com/resource/pubmed/chemical/geldanamycin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1524-4636
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1435-41
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15178564-Animals,
pubmed-meshheading:15178564-Benzoquinones,
pubmed-meshheading:15178564-Calcineurin,
pubmed-meshheading:15178564-Coronary Vessels,
pubmed-meshheading:15178564-Cyclic GMP,
pubmed-meshheading:15178564-Endothelium, Vascular,
pubmed-meshheading:15178564-Enzyme Inhibitors,
pubmed-meshheading:15178564-Gene Therapy,
pubmed-meshheading:15178564-Genetic Vectors,
pubmed-meshheading:15178564-HSP90 Heat-Shock Proteins,
pubmed-meshheading:15178564-Humans,
pubmed-meshheading:15178564-Lactams, Macrocyclic,
pubmed-meshheading:15178564-Liposomes,
pubmed-meshheading:15178564-Myocardial Infarction,
pubmed-meshheading:15178564-Myocardial Reperfusion Injury,
pubmed-meshheading:15178564-NG-Nitroarginine Methyl Ester,
pubmed-meshheading:15178564-Nitric Oxide,
pubmed-meshheading:15178564-Nitric Oxide Synthase,
pubmed-meshheading:15178564-Nitric Oxide Synthase Type III,
pubmed-meshheading:15178564-Phosphorylation,
pubmed-meshheading:15178564-Phosphoserine,
pubmed-meshheading:15178564-Phosphothreonine,
pubmed-meshheading:15178564-Protein Processing, Post-Translational,
pubmed-meshheading:15178564-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15178564-Proto-Oncogene Proteins,
pubmed-meshheading:15178564-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:15178564-Quinones,
pubmed-meshheading:15178564-Sus scrofa,
pubmed-meshheading:15178564-Transfection,
pubmed-meshheading:15178564-Umbilical Veins,
pubmed-meshheading:15178564-Vascular Endothelial Growth Factor A
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pubmed:year |
2004
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pubmed:articleTitle |
Heat shock protein 90 transfection reduces ischemia-reperfusion-induced myocardial dysfunction via reciprocal endothelial NO synthase serine 1177 phosphorylation and threonine 495 dephosphorylation.
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pubmed:affiliation |
Department of Medicine I, Klinikum Grosshadern, Ludwig-Maximilians-University of Munich, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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