The Hsp70 chaperone network
R Rosenzweig, NB Nillegoda, MP Mayer… - … reviews molecular cell …, 2019 - nature.com
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 …
large variety of cellular protein folding and remodelling processes. They function virtually at …
HSP70 multi-functionality in cancer
The 70-kDa heat shock proteins (HSP70s) are abundantly present in cancer, providing
malignant cells selective advantage by suppressing multiple apoptotic pathways, regulating …
malignant cells selective advantage by suppressing multiple apoptotic pathways, regulating …
Strain-release alkylation of Asp12 enables mutant selective targeting of K-Ras-G12D
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 …
non-small cell lung cancer drugs sotorasib and adagrasib covalently capture an acquired …
The Hydroxyquinoline Analogue YUM70 Inhibits GRP78 to Induce ER Stress–Mediated Apoptosis in Pancreatic Cancer
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 …
reticulum (ER) stress signaling. Cancer cells are highly proliferative and have high demand …
Rational design of allosteric modulators: Challenges and successes
Recent advances in structural biology and computational techniques have revealed
allosteric mechanisms for an abundance of targets leading to the establishment of rational …
allosteric mechanisms for an abundance of targets leading to the establishment of rational …
The Hsp70-chaperone machines in bacteria
MP Mayer - Frontiers in Molecular Biosciences, 2021 - frontiersin.org
The ATP-dependent Hsp70s are evolutionary conserved molecular chaperones that
constitute central hubs of the cellular protein quality surveillance network. None of the other …
constitute central hubs of the cellular protein quality surveillance network. None of the other …
Function, therapeutic potential, and inhibition of Hsp70 chaperones
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 …
binding and release of exposed hydrophobic residues on client proteins, Hsp70s can …
HSP70 family in cancer: signaling mechanisms and therapeutic advances
K Zhao, G Zhou, Y Liu, J Zhang, Y Chen, L Liu… - Biomolecules, 2023 - mdpi.com
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 …
heat shock proteins. One of the main functions of HSP70s is to act as molecular chaperones …
Allosteric modulators of HSP90 and HSP70: dynamics meets function through structure-based drug design
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 …
activation of a disparate ensemble of client proteins. They function through ATP hydrolysis …
Exploration of benzothiazole rhodacyanines as allosteric inhibitors of protein–protein interactions with heat shock protein 70 (Hsp70)
Cancer cells rely on the chaperone heat shock protein 70 (Hsp70) for survival and
proliferation. Recently, benzothiazole rhodacyanines have been shown to bind an allosteric …
proliferation. Recently, benzothiazole rhodacyanines have been shown to bind an allosteric …