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Details on Person Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release
| Class:Id | LiteratureReference:202142 |
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| _displayName | Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release |
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| _timestamp | 2007-11-15 17:01:50 |
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| author | [Person:203772] Fontana, J
[Person:203582] Fulton, D
[Person:203661] Chen, Y
[Person:203627] Fairchild, TA
[Person:203571] McCabe, TJ
[Person:203570] Fujita, N
[Person:184055] Tsuruo, T
[Person:203549] Sessa, WC |
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| created | [InstanceEdit:202104] Hemish, J, 2007-10-19 18:00:42 |
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| journal | Circ Res |
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| modified | [InstanceEdit:203590] Hemish, J, 2007-11-15 17:00:52 |
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| pages | 866-73 |
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| pubMedIdentifier | 11988487 |
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| title | Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release |
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| volume | 90 |
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| year | 2002 |
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| (literatureReference) | [Summation:203744] HSP90 interacts with the amino terminus of eNOS (amino acids...
[CatalystActivityReference:9911172] enzyme-substrate adaptor activity of eNOS:CaM:HSP90 [plasma membrane] Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release
[Reaction:202137] AKT1 binds eNOS complex via HSP90 [Homo sapiens] |
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