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ER-associated Protein Degradation at Atomic Resolution.
Eldeeb, Mohamed A; Fahlman, Richard P; Michalak, Marek.
Affiliation
  • Eldeeb MA; McGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, H3A 2B4, Canada. Electronic address: mohamed.eldeeb@mcgill.ca.
  • Fahlman RP; Department of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada. Electronic address: rfahlman@ualberta.ca.
  • Michalak M; Department of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada. Electronic address: marek.michalak@ualberta.ca.
Trends Biochem Sci ; 45(9): 723-725, 2020 09.
Article in En | MEDLINE | ID: mdl-32616332
ABSTRACT
The endoplasmic reticulum-associated degradation (ERAD) pathway eliminates misfolded proteins. The Hrd1 complex represents the main gate mediating retrotranslocation of ER luminal misfolded (ERAD-L) substrates to the cytosol. A recent cryo-electron microscopy (cryo-EM) study by Wu et al. unveils the structural features of active Hrd1, providing mechanistic insights into the movement of proteins directed for degradation across ER membranes.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cryoelectron Microscopy / Endoplasmic Reticulum-Associated Degradation Type of study: Risk_factors_studies Language: En Journal: Trends Biochem Sci Year: 2020 Type: Article
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cryoelectron Microscopy / Endoplasmic Reticulum-Associated Degradation Type of study: Risk_factors_studies Language: En Journal: Trends Biochem Sci Year: 2020 Type: Article