Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular...
Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport
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United States: Public Library of Science
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Language
English
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United States: Public Library of Science
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Contents
Aggregation of amyloidogenic proteins is associated with several neurodegenerative diseases. Sequestration of misfolded and aggregated proteins into specialized deposition sites may reduce their potentially detrimental properties. Yeast exhibits a distinct deposition site for amyloid aggregates termed "Insoluble PrOtein Deposit (IPOD)", but nothing...
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Full title
Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport
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TN_cdi_plos_journals_1829443646
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1829443646
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ISSN
1553-7404,1553-7390
E-ISSN
1553-7404
DOI
10.1371/journal.pgen.1006324
