Aggregation formation in the polyglutamine diseases: Protection at a cost?

Molecular Origin of Polyglutamine Aggregation in Neurodegenerative Diseases

Expansion of polyglutamine (polyQ) tracts in proteins results in protein aggregation and is associated with cell death in at least nine neurodegenerative diseases. Disease age of onset is correlated with the polyQ insert length above a critical value of 35-40 glutamines. The aggregation kinetics of isolated polyQ peptides in vitro also shows a similar critical-length dependence. While recent ex...

The Aggregation Inhibitor Peptide QBP1 as a Therapeutic Molecule for the Polyglutamine Neurodegenerative Diseases

Misfolding and abnormal aggregation of proteins in the brain are implicated in the pathogenesis of various neurodegenerative diseases including Alzheimer's, Parkinson's, and the polyglutamine (polyQ) diseases. In the polyQ diseases, an abnormally expanded polyQ stretch triggers misfolding and aggregation of the disease-causing proteins, eventually resulting in neurodegeneration. In this paper, ...

A Study of the Formation Status of Technical Protection and Health at Work’ Committee in Manufacturing Companies

Background and aims: Occupational Health and Safety (OHS) regulations have been developed with the aim of crating safe conditions at workplaces. Employers are required by OHS laws to provide a safe working environments for employees. A common method to manage OHS in many workplaces is to enforce the requirements of the OHS regulations from inside and outside the organizations. Implementation of...

Beyond the Qs in the polyglutamine diseases.

Are Polyglutamine Diseases Expanding?

It remains a matter of speculation as to whether the sense CUG-containing RNA and/or the antisense CAG-encoding polyglutamine peptide serves as the pathogenic moiety in Huntington's disease like-2 (HDL2). In this issue of Neuron, Wilburn et al. show that in a HDL2 mouse model, the polyglutamine peptide drives disease progression.