Converging evidence continues to point towards Tau aggregation and pathology formation
as central events in the pathogenesis of Alzheimer's disease and other Tauopathies …

One of the more transformative findings in human genetics was the discovery that the
expansion of unstable nucleotide repeats underlies a group of inherited neurological …

Amyloid proteins are widely studied, both for their unusual biophysical properties and their
association with disorders such as Alzheimer's and Parkinson's disease. Fluorescence …

Continuous assessment of transferable forcefields for molecular simulations is essential to
identify their weaknesses and direct improvement efforts. The latest efforts focused on better …

Huntington's disease (HD) is an autosomal dominant neurodegenerative disease caused by
a single mutation in the huntingtin gene (HTT). Normal HTT has a CAG trinucleotide repeat …

Protein aggregation into highly ordered, regularly repeated cross-β sheet structures called
amyloid fibrils is closely associated to human disorders such as neurodegenerative …

Posttranslational modifications play a crucial role in governing cellular functions and protein
behavior. Researchers have implicated dysregulated posttranslational modifications in …

Converging evidence points to the N-terminal domain comprising the first 17 amino acids of
the Huntingtin protein (Nt17) as a key regulator of its aggregation, cellular properties and …

Huntington's Disease (HD) is a devastating neurodegenerative disorder caused by a CAG
trinucleotide repeat expansion in the HTT gene, for which no disease modifying therapies …

Huntington's disease is a neurodegenerative disorder caused by the expansion of a
polyglutamine repeat (> 36Q) in the N-terminal domain of the huntingtin protein (Htt), which …