Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome.

Zhu, Yanan; Wang, Wei Li; Yu, Daqi; Ouyang, Qi; Lu, Ying; Mao, Youdong

Zhu, Yanan; Wang, Wei Li; Yu, Daqi; Ouyang, Qi; Lu, Ying; Mao, Youdong.

Affiliation

Zhu Y; Center for Quantitative Biology, Peking University, Beijing, 100871, China.
Wang WL; State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter and Material Physics, School of Physics, Peking University, Beijing, 100871, China.
Yu D; Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA, 02215, USA.
Ouyang Q; Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, 02115, USA.
Lu Y; State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter and Material Physics, School of Physics, Peking University, Beijing, 100871, China.
Mao Y; Center for Quantitative Biology, Peking University, Beijing, 100871, China.

Nat Commun ; 9(1): 1360, 2018 04 10.

Article de En | MEDLINE | ID: mdl-29636472

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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Adénosine triphosphate / Proteasome endopeptidase complex / ATPases associated with diverse cellular activities / Nucléotides Type d'étude: Prognostic_studies Langue: En Journal: Nat Commun Sujet du journal: BIOLOGIA / CIENCIA Année: 2018 Type de document: Article Pays d'affiliation: Chine

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