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 …

Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a
plethora of substrates (“clients”), including protein kinases, transcription factors, and E3 …

Hsp90 is a conserved and essential molecular chaperone responsible for the folding and
activation of hundreds of 'client'proteins,–. The glucocorticoid receptor (GR) is a model client …

INTRODUCTION Genetic interactions occur when mutations in two or more genes combine
to generate an unexpected phenotype. An extreme negative or synthetic lethal genetic …

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 …

Cells invest in an extensive network of factors to maintain protein homeostasis (proteostasis)
and prevent the accumulation of potentially toxic protein aggregates. This proteostasis …

Heat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of
disparate client proteins. This implicates Hsp90 in diverse biological processes that require …

Abstract Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that
facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched …

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 …

A common need for microbial cells is the ability to respond to potentially toxic environmental
insults. Here we review the progress in understanding the response of the yeast …