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 …

Heat shock proteins (HSPs) are a large family of chaperones that are involved in protein
folding and maturation of a variety of “client” proteins protecting them from degradation …

New drug discovery has been acknowledged as a complicated, expensive, time-consuming,
and challenging project. It has been estimated that around 12 years and 2.7 billion USD, on …

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 …

Heat shock protein (Hsp) 90 is an ATP-dependent molecular chaperone that is exploited by
malignant cells to support activated oncoproteins, including many cancer-associated …

Abstract The phosphoinositide 3-kinase (PI3K) pathway is a key signal transduction system
that links oncogenes and multiple receptor classes to many essential cellular functions, and …

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 …

Extracellular heat shock proteins (ex-HSPs) have been found in exosomes, oncosomes,
membrane surfaces, as well as free HSP in cancer and various pathological conditions, also …

Hsp90 is one of the most important chaperones involved in regulating the maturation of
more than 300 client proteins, many of which are closely associated with refractory diseases …

This review summarizes recent evidence concerning molecular changes in the commonest
type of lymphoma, diffuse large-B-cell lymphoma. Detailed studies have revealed three …