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Cryo-ET and MD simulations reveal that dynein-2 is tuned for binding to the A-tubule of the ciliary doublet.

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Title: Cryo-ET and MD simulations reveal that dynein-2 is tuned for binding to the A-tubule of the ciliary doublet.
Authors: He HK; State Key Laboratory of Genetics and Development of Complex Phenotypes, Department of Biochemistry and Biophysics, School of Life Sciences, Fudan University, Shanghai, China., Kubo S; Department of Applied Chemistry, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan., Chen X; State Key Laboratory of Genetics and Development of Complex Phenotypes, Department of Biochemistry and Biophysics, School of Life Sciences, Fudan University, Shanghai, China., Lv QH; State Key Laboratory of Genetics and Development of Complex Phenotypes, Department of Biochemistry and Biophysics, School of Life Sciences, Fudan University, Shanghai, China., Kage A; Graduate School of Engineering, Muroran Institute of Technology, Muroran, Hokkaido, Japan., Ichikawa M; State Key Laboratory of Genetics and Development of Complex Phenotypes, Department of Biochemistry and Biophysics, School of Life Sciences, Fudan University, Shanghai, China. ichikawa_muneyoshi@fudan.edu.cn.
Source: The EMBO journal [EMBO J] 2025 Dec; Vol. 44 (24), pp. 7677-7701. Date of Electronic Publication: 2025 Nov 26.
Publication Type: Journal Article
Journal Info: Publisher: Nature Publishing Group Country of Publication: England NLM ID: 8208664 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1460-2075 (Electronic) Linking ISSN: 02614189 NLM ISO Abbreviation: EMBO J Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: Cryo-ET and MD simulations reveal that dynein-2 is tuned for binding to the A-tubule of the ciliary doublet.
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  Data: <searchLink fieldCode="AU" term="%22He+HK%22">He HK</searchLink>; State Key Laboratory of Genetics and Development of Complex Phenotypes, Department of Biochemistry and Biophysics, School of Life Sciences, Fudan University, Shanghai, China.<br /><searchLink fieldCode="AU" term="%22Kubo+S%22">Kubo S</searchLink>; Department of Applied Chemistry, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.<br /><searchLink fieldCode="AU" term="%22Chen+X%22">Chen X</searchLink>; State Key Laboratory of Genetics and Development of Complex Phenotypes, Department of Biochemistry and Biophysics, School of Life Sciences, Fudan University, Shanghai, China.<br /><searchLink fieldCode="AU" term="%22Lv+QH%22">Lv QH</searchLink>; State Key Laboratory of Genetics and Development of Complex Phenotypes, Department of Biochemistry and Biophysics, School of Life Sciences, Fudan University, Shanghai, China.<br /><searchLink fieldCode="AU" term="%22Kage+A%22">Kage A</searchLink>; Graduate School of Engineering, Muroran Institute of Technology, Muroran, Hokkaido, Japan.<br /><searchLink fieldCode="AU" term="%22Ichikawa+M%22">Ichikawa M</searchLink>; State Key Laboratory of Genetics and Development of Complex Phenotypes, Department of Biochemistry and Biophysics, School of Life Sciences, Fudan University, Shanghai, China. ichikawa_muneyoshi@fudan.edu.cn.
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  Data: <searchLink fieldCode="JN" term="%228208664%22">The EMBO journal</searchLink> [EMBO J] 2025 Dec; Vol. 44 (24), pp. 7677-7701. <i>Date of Electronic Publication: </i>2025 Nov 26.
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        Value: 10.1038/s44318-025-00648-1
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      – TitleFull: Cryo-ET and MD simulations reveal that dynein-2 is tuned for binding to the A-tubule of the ciliary doublet.
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              Text: 2025 Dec
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