Lentiviral transduction of mammalian cells for fast, scalable and high-level production of soluble and membrane proteins

Autor: A R Aricescu, R E Woolley, B. Bishop, E Y Jones, Jonathan Elegheert, E Behiels, David I. Stuart, S Scott, Veronica T. Chang, Byrne Efx., S.C. Griffiths, Christian Siebold

Publikováno v: Nature Protocols

Structural, biochemical and biophysical studies of eukaryotic soluble and membrane proteins require their production in milligram quantities. Although large-scale protein expression strategies based on transient or stable transfection of mammalian ce

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8fbefc15a622a2a727ddc9b82f30d05
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Structural basis for ion selectivity in potassium-selective channelrhodopsins.

Autor: Tajima S; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan., Kim YS; Department of Bioengineering, Stanford University, Stanford, CA, USA., Fukuda M; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan., Jo Y; Department of Bioengineering, Stanford University, Stanford, CA, USA., Wang PY; Department of Bioengineering, Stanford University, Stanford, CA, USA., Paggi JM; Department of Computer Science, Stanford University, Stanford, CA, USA., Inoue M; Department of Bioengineering, Stanford University, Stanford, CA, USA., Byrne EFX; Department of Bioengineering, Stanford University, Stanford, CA, USA., Kishi KE; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan., Nakamura S; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan., Ramakrishnan C; CNC Program, Stanford University, Stanford, CA, USA., Takaramoto S; The Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan., Nagata T; The Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan., Konno M; The Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan; PRESTO, Japan Science and Technology Agency, Kawaguchi, Saitama, Japan., Sugiura M; Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan., Katayama K; Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan., Matsui TE; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan., Yamashita K; MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge, UK., Kim S; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan., Ikeda H; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan., Kim J; Department of Bioengineering, Stanford University, Stanford, CA, USA., Kandori H; Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan; OptoBioTechnology Research Center, Nagoya Institute of Technology, Showa-ku, Japan., Dror RO; Department of Computer Science, Stanford University, Stanford, CA, USA; Institute for Computational and Mathematical Engineering, Stanford University, Stanford, CA, USA., Inoue K; The Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan., Deisseroth K; Department of Bioengineering, Stanford University, Stanford, CA, USA; CNC Program, Stanford University, Stanford, CA, USA; Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA; Department of Psychiatry and Behavioral Sciences, Stanford University, Stanford, CA, USA. Electronic address: deissero@stanford.edu., Kato HE; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo, Japan; FOREST, Japan Science and Technology Agency, Kawaguchi, Saitama, Japan. Electronic address: hekato@bio.c.u-tokyo.ac.jp.

Publikováno v: Cell [Cell] 2023 Sep 28; Vol. 186 (20), pp. 4325-4344.e26. Date of Electronic Publication: 2023 Aug 30.

Structural basis for channel conduction in the pump-like channelrhodopsin ChRmine.

Autor: Kishi KE; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan., Kim YS; Department of Bioengineering, Stanford University, Stanford, CA, USA., Fukuda M; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan., Inoue M; Department of Bioengineering, Stanford University, Stanford, CA, USA., Kusakizako T; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo, Japan., Wang PY; Department of Bioengineering, Stanford University, Stanford, CA, USA., Ramakrishnan C; CNC Program, Stanford University, Palo Alto, CA, USA., Byrne EFX; Department of Bioengineering, Stanford University, Stanford, CA, USA., Thadhani E; Department of Bioengineering, Stanford University, Stanford, CA, USA; Department of Computer Science, Stanford University, Stanford, CA, USA., Paggi JM; Department of Computer Science, Stanford University, Stanford, CA, USA., Matsui TE; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan., Yamashita K; MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge, UK., Nagata T; Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan; PRESTO, Japan Science and Technology Agency, Kawaguchi, Saitama, Japan., Konno M; Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan; PRESTO, Japan Science and Technology Agency, Kawaguchi, Saitama, Japan., Quirin S; Department of Bioengineering, Stanford University, Stanford, CA, USA., Lo M; Department of Bioengineering, Stanford University, Stanford, CA, USA., Benster T; Department of Bioengineering, Stanford University, Stanford, CA, USA., Uemura T; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Sakyo, Japan., Liu K; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Sakyo, Japan., Shibata M; WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma, Kanazawa, Japan; High-Speed AFM for Biological Application Unit, Institute for Frontier Science Initiative, Kanazawa University, Kakuma, Kanazawa, Japan., Nomura N; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Sakyo, Japan., Iwata S; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Sakyo, Japan; RIKEN SPring-8 Center, Kouto, Sayo-cho, Sayo-gun, Hyogo, Japan., Nureki O; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo, Japan., Dror RO; Department of Computer Science, Stanford University, Stanford, CA, USA; Institute for Computational and Mathematical Engineering, Stanford University, Stanford, CA, USA., Inoue K; Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan., Deisseroth K; Department of Bioengineering, Stanford University, Stanford, CA, USA; CNC Program, Stanford University, Palo Alto, CA, USA; Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA; Department of Psychiatry and Behavioral Sciences, Stanford University, Stanford, CA, USA. Electronic address: deissero@stanford.edu., Kato HE; Komaba Institute for Science, The University of Tokyo, Meguro, Tokyo, Japan; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo, Japan; PRESTO, Japan Science and Technology Agency, Kawaguchi, Saitama, Japan; FOREST, Japan Science and Technology Agency, Kawaguchi, Saitama, Japan. Electronic address: hekato@bio.c.u-tokyo.ac.jp.

Publikováno v: Cell [Cell] 2022 Feb 17; Vol. 185 (4), pp. 672-689.e23. Date of Electronic Publication: 2022 Feb 02.

A serine in the first transmembrane domain of the human E3 ubiquitin ligase MARCH9 is critical for down-regulation of its protein substrates.

Autor: Tan C; From the Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 3052 Parkville, Victoria, Australia.; the Department of Medical Biology, University of Melbourne, 3052 Parkville, Victoria, Australia., Byrne EFX; the Department of Bioengineering, Stanford University, Stanford, California 94305, and., Ah-Cann C; the Department of Medical Biology, University of Melbourne, 3052 Parkville, Victoria, Australia.; the ACRF Stem Cells and Cancer Division, The Walter and Eliza Hall Institute of Medical Research, 3052 Parkville, Victoria, Australia., Call MJ; From the Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 3052 Parkville, Victoria, Australia, call@wehi.edu.au.; the Department of Medical Biology, University of Melbourne, 3052 Parkville, Victoria, Australia., Call ME; From the Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 3052 Parkville, Victoria, Australia, call@wehi.edu.au.; the Department of Medical Biology, University of Melbourne, 3052 Parkville, Victoria, Australia.

Publikováno v: The Journal of biological chemistry [J Biol Chem] 2019 Feb 15; Vol. 294 (7), pp. 2470-2485. Date of Electronic Publication: 2018 Dec 15.

Cilia-Associated Oxysterols Activate Smoothened.

Autor: Raleigh DR; Department of Radiation Oncology, University of California, San Francisco, San Francisco, CA, USA; Department of Neurological Surgery, University of California, San Francisco, San Francisco, CA, USA; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA., Sever N; Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, USA; Institute for Stem Cell Biology and Regenerative Medicine, Stanford University School of Medicine, Stanford, CA, USA., Choksi PK; Department of Radiation Oncology, University of California, San Francisco, San Francisco, CA, USA; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA., Sigg MA; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA., Hines KM; Department of Medicinal Chemistry, University of Washington, Seattle, WA, USA., Thompson BM; Center for Human Nutrition, University of Texas Southwestern Medical Center, Dallas, TX, USA., Elnatan D; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA., Jaishankar P; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA; Small Molecule Discovery Center, University of California, San Francisco, San Francisco, CA, USA., Bisignano P; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA; Cardiovascular Research Institute, University of California, San Francisco, San Francisco, CA, USA., Garcia-Gonzalo FR; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA., Krup AL; Department of Radiation Oncology, University of California, San Francisco, San Francisco, CA, USA; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA., Eberl M; Department of Dermatology, University of Michigan, Ann Arbor, MI, USA., Byrne EFX; Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK., Siebold C; Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK., Wong SY; Department of Dermatology, University of Michigan, Ann Arbor, MI, USA., Renslo AR; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA; Small Molecule Discovery Center, University of California, San Francisco, San Francisco, CA, USA., Grabe M; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, USA; Cardiovascular Research Institute, University of California, San Francisco, San Francisco, CA, USA., McDonald JG; Center for Human Nutrition, University of Texas Southwestern Medical Center, Dallas, TX, USA; Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX, USA., Xu L; Department of Medicinal Chemistry, University of Washington, Seattle, WA, USA., Beachy PA; Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, USA; Institute for Stem Cell Biology and Regenerative Medicine, Stanford University School of Medicine, Stanford, CA, USA; Department of Urology and Department of Developmental Biology, Stanford University School of Medicine, Stanford, CA, USA., Reiter JF; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA; Cardiovascular Research Institute, University of California, San Francisco, San Francisco, CA, USA. Electronic address: jeremy.reiter@ucsf.edu.

Publikováno v: Molecular cell [Mol Cell] 2018 Oct 18; Vol. 72 (2), pp. 316-327.e5.