Heat shock protein 90 transfection reduces ischemia-reperfusion-induced myocardial dysfunction via reciprocal endothelial NO synthase serine 1177 phosphorylation and threonine 495 dephosphorylation. [electronic resource]
Producer: 20050210Description: 1435-41 p. digitalISSN:- 1524-4636
- Animals
- Benzoquinones
- Calcineurin -- metabolism
- Coronary Vessels
- Cyclic GMP -- metabolism
- Endothelium, Vascular -- cytology
- Enzyme Inhibitors -- pharmacology
- Genetic Therapy
- Genetic Vectors -- administration & dosage
- HSP90 Heat-Shock Proteins -- genetics
- Humans
- Lactams, Macrocyclic
- Liposomes
- Myocardial Infarction -- enzymology
- Myocardial Reperfusion Injury -- enzymology
- NG-Nitroarginine Methyl Ester -- pharmacology
- Nitric Oxide -- metabolism
- Nitric Oxide Synthase -- metabolism
- Nitric Oxide Synthase Type III
- Phosphorylation -- drug effects
- Phosphoserine -- metabolism
- Phosphothreonine -- metabolism
- Protein Processing, Post-Translational -- drug effects
- Protein Serine-Threonine Kinases -- metabolism
- Proto-Oncogene Proteins -- metabolism
- Proto-Oncogene Proteins c-akt
- Quinones -- pharmacology
- Sus scrofa
- Transfection
- Umbilical Veins
- Vascular Endothelial Growth Factor A -- pharmacology
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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