Related Experiment Video
Updated: Aug 24, 2026

Assays for the Degradation of Misfolded Proteins in Cells
Published on: August 28, 2016
Polyglutamine and neurodegeneration: structural aspects
1Division of Molecular Structure, National Institute for Medical Research, The Ridgeway, London NW7 1AA, UK. lmasino@nimr.mrc.ac.uk
Abstract:
Polyglutamine (polyQ) diseases are inherited neurodegenerative disorders caused by proteins with expanded polyQ regions. Although the pathological mechanisms of these diseases have not yet been elucidated, the processes of protein misfolding and aggregation seem to be a direct cause of neurodegeneration. Detailed structural information on polyQ proteins is therefore essential in order to understand the mechanisms underlying pathogenesis and to design therapeutic strategies. In the past decade, several studies have investigated the structural properties of polyQ proteins and the molecular basis of aggregation and fibre formation. The results obtained in these studies are reviewed here.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Alzheimer Disease ll: Pathophysiology
Parkinson Disease ll: Pathophysiology
Huntington Disease l: Introduction
Protein Folding Quality Check in the RER

