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Hrd1 forms the retrotranslocation pore regulated by auto-ubiquitination and binding of misfolded proteins.
Vasic, Vedran; Denkert, Niels; Schmidt, Claudia C; Riedel, Dietmar; Stein, Alexander; Meinecke, Michael.
Affiliation
  • Vasic V; Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
  • Denkert N; Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
  • Schmidt CC; Department of Cellular Biochemistry, University Medical Centre Göttingen, Göttingen, Germany.
  • Riedel D; Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
  • Stein A; Department of Structural Dynamics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
  • Meinecke M; Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. alexander.stein@mpibpc.mpg.de.
Nat Cell Biol ; 22(3): 274-281, 2020 03.
Article in En | MEDLINE | ID: mdl-32094691
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Folding / Saccharomyces cerevisiae Proteins / Ubiquitin-Protein Ligases / Ubiquitination / Endoplasmic Reticulum-Associated Degradation Language: En Journal: Nat Cell Biol Year: 2020 Document type: Article Affiliation country: Alemania Country of publication: Reino Unido
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Folding / Saccharomyces cerevisiae Proteins / Ubiquitin-Protein Ligases / Ubiquitination / Endoplasmic Reticulum-Associated Degradation Language: En Journal: Nat Cell Biol Year: 2020 Document type: Article Affiliation country: Alemania Country of publication: Reino Unido