Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in
a myriad of biological processes, modulating polypeptide folding, degradation and …

Emerging evidence indicates that heat shock proteins (HSPs) are critical regulators in
normal neural physiological function as well as in cell stress responses. The functions of …

Misfolding and aggregation are associated with cytotoxicity in several protein folding
diseases. A large network of molecular chaperones ensures protein quality control. Here, we …

A small number of heat-shock proteins have previously been shown to act protectively on
aggregation of several proteins containing an extended polyglutamine (polyQ) stretch, which …

Protein aggregation is a hallmark of several neurodegenerative diseases including
Huntington's disease. We describe the use of the recently developed number and brightness …

Background Emerging evidence implicates altered gene expression within skeletal muscle
in the pathogenesis of Kennedy disease/spinal bulbar muscular atrophy (KD/SBMA). We …

The homeostasis of the protein synthesis and degradation is crucial for cell survival. Most
age-related neurodegenerative diseases are characterized by accumulation of aberrant …

Protein misfolding and aggregation are the causes of several neurodegenerative diseases
which affect an increasing number of people (ie, Alzheimer's, Parkinson's, Huntington's and …