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Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3.
Schoebel, Stefan; Mi, Wei; Stein, Alexander; Ovchinnikov, Sergey; Pavlovicz, Ryan; DiMaio, Frank; Baker, David; Chambers, Melissa G; Su, Huayou; Li, Dongsheng; Rapoport, Tom A; Liao, Maofu.
Afiliação
  • Schoebel S; Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
  • Mi W; Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
  • Stein A; Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
  • Ovchinnikov S; Institute for Protein Design, University of Washington, Seattle, Washington, USA.
  • Pavlovicz R; Institute for Protein Design, University of Washington, Seattle, Washington, USA.
  • DiMaio F; Institute for Protein Design, University of Washington, Seattle, Washington, USA.
  • Baker D; Institute for Protein Design, University of Washington, Seattle, Washington, USA.
  • Chambers MG; Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
  • Su H; National Lab for Parallel and Distributed Processing (PDL), School of Computer Science, National University of Defense Technology, Changsha, China.
  • Li D; National Lab for Parallel and Distributed Processing (PDL), School of Computer Science, National University of Defense Technology, Changsha, China.
  • Rapoport TA; Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
  • Liao M; Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Nature ; 548(7667): 352-355, 2017 08 17.
Article em En | MEDLINE | ID: mdl-28682307
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Glicoproteínas de Membrana / Microscopia Crioeletrônica / Proteínas de Saccharomyces cerevisiae / Ubiquitina-Proteína Ligases / Degradação Associada com o Retículo Endoplasmático Idioma: En Revista: Nature Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Estados Unidos
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Glicoproteínas de Membrana / Microscopia Crioeletrônica / Proteínas de Saccharomyces cerevisiae / Ubiquitina-Proteína Ligases / Degradação Associada com o Retículo Endoplasmático Idioma: En Revista: Nature Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Estados Unidos