Chaperones/heat shock proteins (HSPs) of the HSP90 and HSP70 families show elevated
levels in proliferating mammalian cells and a cell cycle‐dependent expression. They …

Molecular chaperones are a functionally defined set of proteins which assist the structure
formation of proteins in vivo. Without certain protective mechanisms, such as binding …

Heat shock proteins (hsps) are versatile molecular chaperones that are responsiblefor many
cellular functions including proper folding, oligomeric assembly, activation, and transport of …

The Hsp90–Cdc37 chaperone pair has special responsibility for folding of protein kinases.
This function has made Hsp90 a target for new chemotherapeutic approaches, and several …

Cells respond to sudden changes in the environmental temperature with increased
synthesis of a distinct number of heat shock proteins (Hsps). Analysis of the function of these …

Hsp70 chaperone systems play an essential role in the life cycle of many proteins not only in
an hostile environment but also under normal growth conditions. In the course of evolution …

Molecular chaperones, many of them so-called heat-shock or stress proteins (hsps), have
emerged over recent years as an important topic in cell biology. The functions of these …

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The molecular chaperone Hsp90 (90 kDa heat-shock protein) is a remarkably versatile
protein involved in the stress response and in normal homoeostatic control mechanisms. It …

The molecular chaperone, Hsp90, facilitates the maturation and/or activation of over 100
'client proteins' involved in signal transduction and transcriptional regulation. Largely an …