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

Assuring a healthy proteome is indispensable for survival and organismal health. Proteome
disbalance and the loss of the proteostasis buffer are hallmarks of various diseases. The …

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 …

Allosteric drugs have been attracting increasing interest over the past few years. In this
context, it is common practice to use high-throughput screening for the discovery of non …

Allosteric regulation is a common mechanism employed by complex biomolecular systems
for regulation of activity and adaptability in the cellular environment, serving as an effective …

Molecular chaperones have recently emerged as fundamental regulators of salient
biological routines, including metabolic adaptations to environmental changes. Yet, many of …

Metabolic reprogramming, carried out by cancer cells to rapidly adapt to stress such as
hypoxia and limited nutrient conditions, is an emerging concepts in tumor biology, and is …

Molecular chaperones, a family of proteins of which Hsp90 and Hsp70 are integral
members, form an essential machinery to maintain healthy proteomes by controlling the …

The molecular chaperone HSP90 oversees the functional activation of a large number of
client proteins. Because of its role in multiple pathways linked to cancer and …

TRAP1, the mitochondrial isoform of heat shock protein (Hsp) 90 chaperones, is a key
regulator of metabolism and organelle homeostasis in diverse pathological states. While …