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Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics
The activity of endothelial NO synthase (eNOS) is triggered by calmodulin (CaM) binding and is often further regulated by phosphorylation at several positions in the enzyme. Phosphorylation at Ser(1179) occurs in response to diverse physiologic stimuli and increases the NO synthesis and cytochrome c...
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| I publikationen: | J Biol Chem |
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| Huvudupphovsmän: | , , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
American Society for Biochemistry and Molecular Biology
2016
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5087725/ https://ncbi.nlm.nih.gov/pubmed/27613870 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M116.737361 |
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