The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins.

Autor: Shurtleff MJ; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States., Itzhak DN; Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany., Hussmann JA; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States., Schirle Oakdale NT; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States., Costa EA; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States., Jonikas M; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States., Weibezahn J; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States., Popova KD; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States., Jan CH; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States., Sinitcyn P; Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany., Vembar SS; Department of Biological Sciences, University of Pittsburgh, Pittsburgh, United States., Hernandez H; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, United States., Cox J; Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany., Burlingame AL; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, United States., Brodsky JL; Department of Biological Sciences, University of Pittsburgh, Pittsburgh, United States., Frost A; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.; Chan Zuckerberg Biohub, San Francisco, United States., Borner GH; Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany., Weissman JS; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States.; Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, United States.

Publikováno v: ELife [Elife] 2018 May 29; Vol. 7. Date of Electronic Publication: 2018 May 29.

Molecular Basis for the Interaction Between AP4 β4 and its Accessory Protein, Tepsin.

Autor: Frazier MN; Department of Biological Sciences, Vanderbilt University, Nashville, TN, USA.; Center for Structural Biology, Vanderbilt University, Nashville, TN, USA., Davies AK; Department of Clinical Biochemistry, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge, UK., Voehler M; Center for Structural Biology, Vanderbilt University, Nashville, TN, USA.; Department of Biochemistry and Chemistry, Vanderbilt University, Nashville, TN, USA., Kendall AK; Department of Biological Sciences, Vanderbilt University, Nashville, TN, USA.; Center for Structural Biology, Vanderbilt University, Nashville, TN, USA., Borner GH; Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany., Chazin WJ; Center for Structural Biology, Vanderbilt University, Nashville, TN, USA.; Department of Biochemistry and Chemistry, Vanderbilt University, Nashville, TN, USA., Robinson MS; Department of Clinical Biochemistry, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge, UK., Jackson LP; Department of Biological Sciences, Vanderbilt University, Nashville, TN, USA.; Center for Structural Biology, Vanderbilt University, Nashville, TN, USA.

Publikováno v: Traffic (Copenhagen, Denmark) [Traffic] 2016 Apr; Vol. 17 (4), pp. 400-15. Date of Electronic Publication: 2016 Mar 04.

A novel disorder reveals clathrin heavy chain-22 is essential for human pain and touch development.

Autor: Nahorski MS; 1 Cambridge Institute for Medical Research, University of Cambridge, Cambridge, CB2 0XY, UK msn27@cam.ac.uk cw347@cam.ac.uk., Al-Gazali L; 2 Department of Paediatrics, College of Medicine and Health Sciences, United Arab Emirates University, Al-Ain, UAE., Hertecant J; 3 Department of Paediatrics, Tawam Hospital, Al-Ain, UAE., Owen DJ; 1 Cambridge Institute for Medical Research, University of Cambridge, Cambridge, CB2 0XY, UK., Borner GH; 1 Cambridge Institute for Medical Research, University of Cambridge, Cambridge, CB2 0XY, UK 4 Max Planck Institute of Biochemistry, Department of Proteomics and Signal Transduction, Am Klopferspitz 18, 82152 Martinsried, Germany., Chen YC; 1 Cambridge Institute for Medical Research, University of Cambridge, Cambridge, CB2 0XY, UK., Benn CL; 5 Neusentis, The Portway Building, Granta Park, Cambridge. CB21 6GS, UK., Carvalho OP; 1 Cambridge Institute for Medical Research, University of Cambridge, Cambridge, CB2 0XY, UK., Shaikh SS; 1 Cambridge Institute for Medical Research, University of Cambridge, Cambridge, CB2 0XY, UK., Phelan A; 5 Neusentis, The Portway Building, Granta Park, Cambridge. CB21 6GS, UK., Robinson MS; 1 Cambridge Institute for Medical Research, University of Cambridge, Cambridge, CB2 0XY, UK., Royle SJ; 6 Division of Biomedical Cell Biology, Warwick Medical School, Gibbet Hill Road, Coventry CV4 7AL, UK., Woods CG; 1 Cambridge Institute for Medical Research, University of Cambridge, Cambridge, CB2 0XY, UK msn27@cam.ac.uk cw347@cam.ac.uk.

Publikováno v: Brain : a journal of neurology [Brain] 2015 Aug; Vol. 138 (Pt 8), pp. 2147-60. Date of Electronic Publication: 2015 Jun 11.

Using in-gel digestion and an Orbitrap mass spectrometer to analyze the proteome of clathrin-coated vesicles.

Autor: Borner GH; Department of Proteomics and Signal Transduction, Max Plank Institute of Biochemistry, 82152 Martinsried, Germany;, Fielding AB; Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool L69 3BX, United Kingdom.

Publikováno v: Cold Spring Harbor protocols [Cold Spring Harb Protoc] 2014 Nov 03; Vol. 2014 (11), pp. 1188-91. Date of Electronic Publication: 2014 Nov 03.

Using in-solution digestion, peptide fractionation, and a Q exactive mass spectrometer to analyze the proteome of clathrin-coated vesicles.

Autor: Borner GH; Department of Proteomics and Signal Transduction, Max Plank Institute of Biochemistry, 82152 Martinsried, Germany;, Fielding AB; Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool L69 3BX, United Kingdom.

Publikováno v: Cold Spring Harbor protocols [Cold Spring Harb Protoc] 2014 Nov 03; Vol. 2014 (11), pp. 1192-5. Date of Electronic Publication: 2014 Nov 03.