Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core

Proceedings of the National Academy of Sciences of the United States of America

Volumn 113, Issue 6, 2016, Pages 1546-1551

  Hoop, Cody L ^a,d   Lin, Hsiang Kai ^a   Kar, Karunakar ^a,e   Magyarfalvi, Gábor ^b   Lamley, Jonathan M ^c   Boatz, Jennifer C ^a   Mandal, Abhishek ^a   Lewandowski, Józef R ^c   Wetzel, Ronald ^a   Van Der Wel, Patrick C A ^a  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

^b EÖTVÖS LORÁND UNIVERSITY   (Hungary)

^c UNIVERSITY OF WARWICK   (United Kingdom)

^d RUTGERS UNIVERSITY   (United States)

^e INDIAN INSTITUTE OF TECHNOLOGY JODHPUR   (India)

Author keywords

Amyloid; Amyloid disease; Huntington's disease; Protein aggregation; Solid state NMR

Indexed keywords

AMYLOID; HUNTINGTIN; POLYGLUTAMINE; NERVE PROTEIN; PEPTIDE;

ARTICLE; BETA SHEET; CAG REPEAT; CHEMICAL STRUCTURE; EXON; HUNTINGTON CHOREA; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; SOLID STATE; SOLID STATE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; X RAY POWDER DIFFRACTION; AMINO ACID SEQUENCE; CHEMISTRY; GENETICS; MARKOV CHAIN; MOLECULAR GENETICS; MOLECULAR MODEL; PROTEIN SECONDARY STRUCTURE; ULTRASTRUCTURE;

AMINO ACID SEQUENCE; AMYLOID; EXONS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; STOCHASTIC PROCESSES;

EID: 84957824317     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1521933113     Document Type: Article

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