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Changes in the free-energy landscape of p38α MAP kinase through its canonical activation and binding events as studied by enhanced molecular dynamics simulations
p38α is a Ser/Thr protein kinase involved in a variety of cellular processes and pathological conditions, which makes it a promising pharmacological target. Although the activity of the enzyme is highly regulated, its molecular mechanism of activation remains largely unexplained, even after decades...
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| Pubblicato in: | eLife |
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| Autori principali: | , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
eLife Sciences Publications, Ltd
2017
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5406204/ https://ncbi.nlm.nih.gov/pubmed/28445123 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7554/eLife.22175 |
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