Topic: Huntington disease

Deficits in sensory perception characterize Huntington disease (HD), alongside motor and cognitive impairments. This study investigates altered cortical network connectivity in HD, focusing on sensory spread, where sensory stimulation provokes more extensive cortical activity in HD model mice compared to wild-type (WT) controls.In vivo, we utilized widefield, mesoscale calcium imaging in the awake, head-fixed zQ175 mouse model of HD, crossed with Thy1-GCaMP mice, expressing GCaMP in cortical pyramidal neurons. In vivo, LED flashes induced visual responses imaged through an intact-skull cranial

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）

Huntington Disease (HD) originates from the expansion of a polyglutamine (PolyQ) tract in the Huntingtin protein (Htt), that can assume a Coiled coil fold (Cc). We previously found that Cc structures mediate the aggregation and toxicity of Htt and hypothesize they might be implicated in other aspects of Htt dysfunction. There is evidence that expanded and aggregated Htt can be released by sick cells and taken up by healthy ones. With a prion-like mechanism, aggregated Htt can then seed the misfolding of normal Htt spreading the disorder.We hypothesize that Cc also mediate the intercellular pro