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Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism.
Yu, Qin; Ni, Dongchun; Kowal, Julia; Manolaridis, Ioannis; Jackson, Scott M; Stahlberg, Henning; Locher, Kaspar P.
Affiliation
  • Yu Q; Institute of Molecular Biology and Biophysics, Department of Biology, ETH Zürich, Zürich, Switzerland.
  • Ni D; Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel, Basel, Switzerland.
  • Kowal J; Laboratory of Biological Electron Microscopy, Institute of Physics, SB, EPFL, Lausanne, Switzerland.
  • Manolaridis I; Institute of Molecular Biology and Biophysics, Department of Biology, ETH Zürich, Zürich, Switzerland.
  • Jackson SM; Institute of Molecular Biology and Biophysics, Department of Biology, ETH Zürich, Zürich, Switzerland.
  • Stahlberg H; Institute of Molecular Biology and Biophysics, Department of Biology, ETH Zürich, Zürich, Switzerland.
  • Locher KP; Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel, Basel, Switzerland.
Nat Commun ; 12(1): 4376, 2021 07 19.
Article in En | MEDLINE | ID: mdl-34282134
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Pharmaceutical Preparations / ATP Binding Cassette Transporter, Subfamily G, Member 2 / Neoplasm Proteins Limits: Humans Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2021 Document type: Article Affiliation country: Suiza Country of publication: Reino Unido
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Pharmaceutical Preparations / ATP Binding Cassette Transporter, Subfamily G, Member 2 / Neoplasm Proteins Limits: Humans Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2021 Document type: Article Affiliation country: Suiza Country of publication: Reino Unido