Structural basis for endothelial nitric oxide synthase binding to calmodulin
The enzyme nitric oxide synthase (NOS) is exquisitely regulated in vivo by the Ca(2+) sensor protein calmodulin (CaM) to control production of NO, a key signaling molecule and cytotoxin. The differential activation of NOS isozymes by CaM has remained enigmatic, despite extensive research. Here, the...
Tallennettuna:
| Julkaisussa: | EMBO J |
|---|---|
| Päätekijät: | , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Nature Publishing Group
2003
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC145438/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12574113/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/emboj/cdg078 |
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