Poultry in commercial settings are exposed to a range of stressors. A growing body of
information clearly indicates that excess ROS/RNS production and oxidative stress are …

Cells are repeatedly exposed to environmental or endogenous stresses that can alter
normal cell behavior and increase cell vulnerability. In order to ensure tissue integrity and …

Molecular chaperones are highly conserved proteins that promote proper folding of other
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …

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

Heat shock protein 90 (Hsp90) is a molecular chaperone that folds and remodels proteins,
thereby regulating the activity of numerous substrate proteins. Hsp90 is widely conserved …

The prevailing current view of protein folding is the thermodynamic hypothesis, under which
the native folded conformation of a protein corresponds to the global minimum of Gibbs free …

Cells adapt to conditions that compromise protein conformational stability by activating
various stress response pathways, but the mechanisms used in sensing misfolded proteins …

From biosynthesis to assembly into nucleosomes, histones are handed through a cascade
of histone chaperones, which shield histones from non-specific interactions. Whether …

Various stimuli induce an unfolded protein response to endoplasmic reticulum stress,
accompanied by the expression of endoplasmic reticulum molecular chaperones. Hypoxia …

Heat shock protein 70 (Hsp70) chaperones bind many different sequences and discriminate
between incompletely folded and folded clients. Most research into the origins of this …