Abnormally expanded polyglutamine (polyQ) tracts provide a gain of toxic functions to nine
otherwise unrelated human proteins and induce progressive neurodegenerative diseases …

Several neurodegenerative diseases are associated with the toxicity of misfolded proteins.
This toxicity must arise from a combination of the amino acid sequences of the misfolded …

Polyglutamine (polyQ) stretches exceeding a threshold length confer a toxic function to
proteins that contain them and cause at least nine neurological disorders. The basis for this …

Protein aggregation is a key mechanism involved in neurodegeneration associated with
Alzheimer's, Parkinson's and Huntington's diseases. Nine diseases (including Huntington's) …

Expanded polyglutamine (polyQ) repeats cause neurodegenerative disorders, but their
cytotoxic structures remain to be elucidated. Although soluble polyQ oligomers have been …

The nine polyglutamine (polyQ) neurodegenerative diseases are caused in part by a gain-of-
function mechanism involving protein misfolding, the deposition of β-sheet-rich aggregates …

Polyglutamine (polyQ) diseases are associated with a CAG/polyQ expansion mutation in
unrelated proteins. Upon elongation of the glutamine tract, disease proteins aggregate …

The polyglutamine (polyQ) diseases are a class of inherited neurodegenerative diseases
including Huntington's disease, caused by the expansion of a polyQ stretch within each …

Polyglutamine (polyQ) sequences of unknown normal function are present in a significant
number of proteins, and their repeat expansion is associated with a number of genetic …

Polyglutamine (polyQ) diseases are classified as conformational neurodegenerative
diseases, like Alzheimer and Parkinson diseases, and they are caused by proteins with an …