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A flipped ion pair at the dynein–microtubule interface is critical for dynein motility and ATPase activation
Dynein is a motor protein that moves on microtubules (MTs) using the energy of adenosine triphosphate (ATP) hydrolysis. To understand its motility mechanism, it is crucial to know how the signal of MT binding is transmitted to the ATPase domain to enhance ATP hydrolysis. However, the molecular basis...
Autores principales: | Uchimura, Seiichi, Fujii, Takashi, Takazaki, Hiroko, Ayukawa, Rie, Nishikawa, Yosuke, Minoura, Itsushi, Hachikubo, You, Kurisu, Genji, Sutoh, Kazuo, Kon, Takahide, Namba, Keiichi, Muto, Etsuko |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4298687/ https://www.ncbi.nlm.nih.gov/pubmed/25583999 http://dx.doi.org/10.1083/jcb.201407039 |
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