Topic: polyglutamine

Spinocerebellar ataxia type 2 (SCA2) is an autosomal dominant disorder caused by an abnormal expansion of the trinucleotide CAG in the coding region of the ATXN2 gene. This is translated into an expanded polyglutamine tract in the ataxin-2 protein, leading to a gain of toxic function affecting especially the neurons. Besides the pathogenic mechanisms triggered by ataxin-2 dysfunction, previous studies showed that abnormally expanded CAG repeats display toxicity already at the RNA level, contributing to disease pathogenesis. Considering these data, it is important to develop therapeutic approac

The aberrant formation and accumulation of the misfolded polyglutamine （polyQ） containing proteins in the nuclei are considered to be the major hallmark and cause of many neurodegenerative diseases, including Spinocerebellar ataxias （SCAs）, Huntington Disease （HD）, Spinal and Bulbar Muscular Atrophy （SBMA）, and Dentatorubro pallidoluysian atrophy （DRPLA）. It is, therefore, believed that intervening biosynthesis, resolution, and clearance of the misfolded proteins, may represent potential therapeutic approaches. Previous studies have found that the BFRF1 protein of the Epstein-Barr virus （EBV）