Conformational Switching in PolyGln Amyloid Fibrils Resulting from a Single Amino Acid Insertion

This publication has 41 references indexed in Scilit:

• Protein Homorepeats
  2010
• Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy
  Quarterly Reviews of Biophysics, 2008
• Trinucleotide Repeat Disorders
  Annual Review of Neuroscience, 2007
• Structural Models of Amyloid‐Like Fibrils
  2006
• Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils
  Proceedings of the National Academy of Sciences, 2000
• Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates
  Nature Genetics, 1998
• Intranuclear Neuronal Inclusions in Huntington's Disease and Dentatorubral and Pallidoluysian Atrophy: Correlation between the Density of Inclusions andIT15CAG Triplet Repeat Length
  Neurobiology of Disease, 1998
• Formation of Neuronal Intranuclear Inclusions Underlies the Neurological Dysfunction in Mice Transgenic for the HD Mutation
  Cell, 1997
• Huntingtin-Encoded Polyglutamine Expansions Form Amyloid-like Protein Aggregates In Vitro and In Vivo
  Cell, 1997
• Trinucleotide repeats and long homopeptides in genes and proteins associated with nervous system disease and development.
  Proceedings of the National Academy of Sciences, 1996