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 …

The 70-kDa heat shock proteins (HSP70s) are abundantly present in cancer, providing
malignant cells selective advantage by suppressing multiple apoptotic pathways, regulating …

K-Ras is the most commonly mutated oncogene in human cancer. The recently approved
non-small cell lung cancer drugs sotorasib and adagrasib covalently capture an acquired …

Abstract GRP78 (glucose-regulated protein, 78 kDa) is a key regulator of endoplasmic
reticulum (ER) stress signaling. Cancer cells are highly proliferative and have high demand …

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

Recent advances in structural biology and computational techniques have revealed
allosteric mechanisms for an abundance of targets leading to the establishment of rational …

Hsp70s are among the most highly conserved proteins in all of biology. Through an iterative
binding and release of exposed hydrophobic residues on client proteins, Hsp70s can …

The 70 kDa heat shock proteins (HSP70s) are a group of highly conserved and inducible
heat shock proteins. One of the main functions of HSP70s is to act as molecular chaperones …

Binding of ATP to the N-terminal nucleotide-binding domain (NBD) of heat shock protein 70
(Hsp70) molecular chaperones reduces the affinity of their C-terminal substrate-binding …

Molecular chaperones HSP90 and HSP70 are essential regulators of the folding and
activation of a disparate ensemble of client proteins. They function through ATP hydrolysis …