Impaired transport of intrinsically disordered proteins through the Sec61 and SecY translocon; implications for prion diseases
Author:
Affiliation:
1. Department Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, Germany
Funder
Deutsche Forschungsgemeinschaft
Publisher
Informa UK Limited
Subject
Infectious Diseases,Cell Biology,Cellular and Molecular Neuroscience,Biochemistry
Link
https://www.tandfonline.com/doi/pdf/10.1080/19336896.2018.1435936
Reference30 articles.
1. Asparagine-linked glycosylation of the scrapie and cellular prion proteins
2. Scrapie prion protein contains a phosphatidylinositol glycolipid
3. Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein
4. A Transmembrane Form of the Prion Protein in Neurodegenerative Disease
5. Neurotoxicity and Neurodegeneration When PrP Accumulates in the Cytosol
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1. Plastid chaperone HSP90C guides precursor proteins to the SEC translocase for thylakoid transport;Journal of Experimental Botany;2020-08-27
2. The Dynamic ATP-Driven Mechanism of Bacterial Protein Translocation and the Critical Role of Phospholipids;Frontiers in Microbiology;2019-06-19
3. The signal peptide plus a cluster of positive charges in prion protein dictate chaperone-mediated Sec61 channel gating;Biology Open;2019-01-01
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