Protein misfolding is associated with many human diseases, particularly neurodegenerative
diseases, such as Alzheimer's disease, Parkinson's disease, and Huntington's disease 1 …

Intracellular inclusions are a unifying feature of polyglutamine (polyQ) neurodegenerative
diseases, yet each polyQ disease displays a unique pattern of neuronal degeneration. This …

Polyglutamine expansions in certain proteins are the genetic determinants for nine distinct
progressive neurodegenerative disorders and resultant age-related dementia. In these …

Polyglutamine (polyQ) expansions cause neurodegeneration that is associated with protein
misfolding and influenced by functional properties of the host protein. The polyQ disease …

Proteins containing polyglutamine (polyQ) regions are found in almost all eukaryotes, albeit
with various frequencies. In humans, proteins such as huntingtin (Htt) with abnormally …

Ataxin-3 is a member of the polyglutamine family of proteins, which are associated with at
least nine different neurodegenerative diseases. In the disease state, expansion of the …

Spinocerebellar ataxia 1 (SCA1), one of the inherited polyglutamine neurodegenerative
diseases, is associated with intracellular aggregates. However, the process of aggregate …

Many neurodegenerative disorders are caused by abnormal accumulation of misfolded
proteins. In spinocerebellar ataxia type 1 (SCA1), accumulation of polyglutamine-expanded …

A network of chaperones and ubiquitin ligases sustain intracellular proteostasis and is
integral in preventing aggregation of misfolded proteins associated with various …

Polyglutamine (polyQ) expansion in many proteins, including huntingtin and ataxin‐3, is
pathogenic and responsible for neuronal dysfunction and degeneration. Although at least …