Changes in the free-energy landscape of p38α MAP kinase through its canonical activation and binding...
Changes in the free-energy landscape of p38α MAP kinase through its canonical activation and binding events as studied by enhanced molecular dynamics simulations
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England: eLife Sciences Publications Ltd
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English
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England: eLife Sciences Publications Ltd
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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 of research. By using state-of-the-art molecular d...
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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
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TN_cdi_doaj_primary_oai_doaj_org_article_c79167d437ac42e5abc1ec4d6f61c530
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_c79167d437ac42e5abc1ec4d6f61c530
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2050-084X
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2050-084X
DOI
10.7554/eLife.22175
