In the Drosophila eye, proteins with an expanded polyglutamine (polyQ) tract form nuclear
and cytoplasmic inclusions and produce cytotoxicity, demonstrated as loss of eye …

The toxicity of an abnormally long polyglutamine [poly (Q)] tract within specific proteins is the
molecular lesion shared by Huntington's disease (HD) and several other hereditary …

Nuclear dysfunction is a key feature of the pathology of polyglutamine (polyQ) diseases. It
has been suggested that mutant polyQ proteins impair functions of nuclear factors by …

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 …

Protein misfolding, whether caused by aging, environmental factors, or genetic mutations, is
a common basis for neurodegenerative diseases. The misfolding of proteins with abnormally …

Polyglutamine (polyQ) diseases, resulting from a dynamic expansion of glutamine repeats in
a polypeptide, are a class of genetically inherited late onset neurodegenerative disorders …

Trinucleotide CAG repeat disorders are caused by expansion of polyglutamine (polyQ)
domains in certain proteins leading to fatal neurodegenerative disorders and are …

Polyglutamine (polyQ) repeat diseases are neurodegenerative ailments elicited by
glutamine-encoding CAG nucleotide expansions within endogenous human genes. Despite …

Age-related misfolding and aggregation of pathogenic proteins are responsible for several
neurodegenerative diseases. For example, Huntington's disease (HD) is principally driven …

We have successfully generated a Drosophila model of human polyglutamine (polyQ)
diseases by the targeted expression of expanded-polyQ (ex-polyQ) in the Drosophila …