Lysine residues in the N-terminal huntingtin amphipathicα-helix play a key role in peptide aggregation
Author:
Affiliation:
1. C. Eugene Bennett Department of Chemistry; West Virginia University; Morgantown WV 26506 USA
2. NanoSAFE Initiative; West Virginia University; Morgantown WV 26506 USA
3. Center for Neurosciences; West Virginia University; Morgantown WV 26506 USA
Funder
West Virginia University Eberly College of Arts & Sciences
WV Higher Education Policy Commission/Division of Science and Research
Publisher
Wiley
Subject
Spectroscopy
Reference65 articles.
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3. CAG repeat number governs the development rate of pathology in Huntington's disease;Penney;Ann. Neurol.,1997
4. Slow amyloid nucleation via alpha-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments;Jayaraman;J. Mol. Biol.,2012
5. Secondary structures of native and pathogenic huntingtin N-terminal fragments;Dlugosz;J. Phys. Chem. B,2011
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