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Calmodulin-induced structural changes in endothelial nitric oxide synthase

We have derived structures of intact calmodulin(CaM)-free and CaM-bound endothelial nitric oxide synthase (eNOS) by reconstruction from cryo-electron micrographs. The CaM-free reconstruction is well fitted by the oxygenase domain dimer, but the reductase domains are not visible, suggesting they are...

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Autori principali: Persechini, Anthony, Tran, Quang-Kim, Black, D.J., Gogol, Edward P.
Natura: Artigo
Lingua:Inglês
Pubblicazione: 2012
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC3569036/
https://ncbi.nlm.nih.gov/pubmed/23266515
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.febslet.2012.12.012
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