Dissociation of Amyloid Fibrils of α-Synuclein and Transthyretin by Pressure Reveals Their Reversibl...
Dissociation of Amyloid Fibrils of α-Synuclein and Transthyretin by Pressure Reveals Their Reversible Nature and the Formation of Water-Excluded Cavities
About this item
Full title
Author / Creator
Publisher
United States: National Academy of Sciences
Journal title
Language
English
Formats
Publication information
Publisher
United States: National Academy of Sciences
Subjects
More information
Scope and Contents
Contents
Protein misfolding and aggregation have been linked to several human diseases, including Alzheimer's disease, Parkinson's disease, and systemic amyloidosis, by mechanisms that are not yet completely understood. The hallmark of most of these diseases is the formation of highly ordered and β-sheet-rich aggregates referred to as amyloid fibrils. Fibri...
Alternative Titles
Full title
Dissociation of Amyloid Fibrils of α-Synuclein and Transthyretin by Pressure Reveals Their Reversible Nature and the Formation of Water-Excluded Cavities
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_proquest_miscellaneous_19411954
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_19411954
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1734009100
