The herpesvirus nuclear export protein BFRF1 attenuates polyQ-expanded Ataxin 3 induced toxicity in a Drosophila model of SCA3
Ming-Tsan Su, Yu-Hsuan Hsu, Chung-pei Lee · FENS Forum 2024
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）
ePoster · Neuroscience