The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a
large variety of cellular protein folding and remodelling processes. They function virtually at …

This analytical review summarizes literature data and our own research on HSP70-
dependent mechanisms of neuroprotection and discusses potential pharmacological agents …

The ATP-dependent Hsp70s are evolutionary conserved molecular chaperones that
constitute central hubs of the cellular protein quality surveillance network. None of the other …

Protein misfolding and aggregation are pathological events that place a significant amount
of stress on the maintenance of protein homeostasis (proteostasis). For prevention and …

Iron–sulfur (Fe–S) clusters are ancient and ubiquitous cofactors and are involved in many
important biological processes. Unlike the non-photosynthetic bacteria, cyanobacteria have …

Obligate protozoan parasites of the kinetoplastids and apicomplexa infect human cells to
complete their life cycles. Some of the members of these groups of parasites develop in at …

Chaperones of the 70 kDa heat shock protein (Hsp70) superfamily are key components of
the cellular proteostasis system. Together with its co-chaperones, Hsp70 forms proteostasis …

Protein folding is a highly complex process proceeding through a number of disordered and
partially folded nonnative states with various degrees of structural organization. These …

The interaction between the Heat Shock Proteins 70 and 40 is at the core of the ATPase
regulation of the chaperone machinery that maintains protein homeostasis. However, the …

Sleep is a fundamental process essential for reparatory and restorative mechanisms in all
organisms. Recent research has linked sleep to various pathological conditions, including …