The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends
The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends
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Author / Creator
Schneider, Matthias M. , Gautam, Saurabh , Herling, Therese W. , Andrzejewska, Ewa , Krainer, Georg , Miller, Alyssa M. , Trinkaus, Victoria A. , Peter, Quentin A. E. , Ruggeri, Francesco Simone , Vendruscolo, Michele , Bracher, Andreas , Dobson, Christopher M. , Hartl, F. Ulrich and Knowles, Tuomas P. J.
Publisher
London: Nature Publishing Group UK
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Language
English
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Publisher
London: Nature Publishing Group UK
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Contents
Molecular chaperones contribute to the maintenance of cellular protein homoeostasis through assisting de novo protein folding and preventing amyloid formation. Chaperones of the Hsp70 family can further disaggregate otherwise irreversible aggregate species such as α-synuclein fibrils, which accumulate in Parkinson’s disease. However, the mechanisms...
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Full title
The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends
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TN_cdi_doaj_primary_oai_doaj_org_article_9d156d4ff127467f8d1a03fe03aed8f5
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_9d156d4ff127467f8d1a03fe03aed8f5
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-021-25966-w
