The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Heat shock proteins (HSPs) constitute a large family of proteins involved in protein folding
and maturation whose expression is induced by heat shock or other stressors. The major …

Proteomic studies of human Alzheimer's disease brain tissue have potential to identify
protein changes that drive disease, and to identify new drug targets. Here, we analyse 38 …

All cells possess an internal stress response to cope with environmental and
pathophysiological challenges. Upon stress, cells reprogram their molecular functions to …

Misfolding, aggregation, and aberrant accumulation of proteins are central components in
the progression of neurodegenerative disease. Cellular molecular chaperone systems …

The accumulation of amyloid Tau aggregates is implicated in Alzheimer's disease (AD) and
other tauopathies. Molecular chaperones are known to maintain protein homeostasis. Here …

Aggregation of tau protein in the brain is associated with a class of neurodegenerative
diseases known as tauopathies. FK506 binding protein 51 kDa (FKBP51, encoded by …

Although the mechanisms of toxic activity of tau are not fully recognized, it is supposed that
the tau toxicity is related rather not to insoluble tau aggregates but to its intermediate forms. It …

Abstract Heat shock protein 27 (HSP27) is a multidimensional protein which acts as a
protein chaperone and an antioxidant and plays a role in the inhibition of apoptosis and …

In Alzheimer's disease (AD), the mechanisms of neuronal loss remain largely unknown.
Although tau pathology is closely correlated with neuronal loss, how its accumulation may …