Heat shock protein 90 (HSP90) is a vital chaperone protein, regulating signaling pathways
and correcting misfolded proteins in cancer cells by interacting with oncogenic client …

HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein,
it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits …

The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are
involved in myriad cellular processes. Their distribution in various cellular compartments …

The heat shock response is an evolutionarily conserved mechanism that protects cells or
organisms from the harmful effects of various stressors such as heat, chemicals toxins, UV …

The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …

Simple Summary Here we present a comprehensive review of the current literature
describing mechanisms of damage incurred by cryopreservation, and we highlight several …

Cells have a remarkable ability to synthesize large amounts of protein in a very short period
of time. Under these conditions, many hydrophobic surfaces on proteins may be transiently …

Heat shock proteins (HSPs) are a large group of chaperones found in most eukaryotes and
bacteria. They are responsible for the correct protein folding, protection of the cell against …

The molecular chaperone heat shock protein 90 (HSP90) has been used by cancer cells to
facilitate the function of numerous oncoproteins, and it can be argued that cancer cells …

Abstract Structure-based drug design has often been restricted by the rather static picture of
protein–ligand complexes presented by crystal structures, despite the widely accepted …