Breast cancer is the most common cancer and the most frequent cause of cancer death
among women worldwide. Breast cancer is a complex, heterogeneous disease classified …

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 …

The 90-kDa heat-shock protein (Hsp90) is a molecular chaperone responsible for the
stability and function of a wide variety of client proteins that are critical for cell growth and …

TRAP1 is the mitochondrial paralog of the heat shock protein 90 (HSP90) chaperone family.
Its activity as an energy metabolism regulator has important implications in cancer …

Heat shock protein 90, also known as Hsp90, is an extensively preserved molecular
chaperone that performs a critical function in organizing various biological pathways and …

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 …

Heat shock proteins (HSPs) present as a double edged sword. While they play an important
role in maintaining protein homeostasis in a normal cell, cancer cells have evolved to co-opt …

The 90 kDa heat shock proteins (Hsp90) are responsible for the conformational maturation
of nascent polypeptides and the rematuration of denatured proteins. Proteins dependent …

Cells constantly need to adopt to changing environmental conditions, maintaining
homeostasis and proteostasis. Heat shock proteins are a diverse class of molecular …

ABSTRACT Introduction Heat shock protein 90 (Hsp90) is one of the most critical
chaperones amenable to mediating the folding and maturation of more than 300 client …