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 …

What began as a molecular curiosity in fruit flies over 30 years ago (Ritossa 1962), the so-
called heat shock or stress response, now constitutes an active area of research in cell …

Functional proteins within cells are normally present in their native, completely folded form.
However, vital processes of protein biogenesis such as protein synthesis and translocation …

Over 400 participants attended the conference on the biology of heat shock proteins and
molecular chaperones held May 4-8, 1994, at Cold Spring Harbor Laboratory in Cold Spring …

The heat shock protein Hsp90 is a molecular chaperone which assists the refolding of
misfolded proteins, but also has highly selective functions in normal metabolism. These dual …

Molecular chaperones are a set of conserved protein families that share the remarkable
ability to recognize and selectively bind nonnative proteins under physiological and stress …

Virtually all organisms respond to up-shifts in temperature (heat shock) by synthesizing a set
of proteins called heat shock proteins (HSPs). The HSPs are induced not only by heat shock …

The term molecular chaperone includes a large family of unrelated proteins that comprise
both stress-inducible and constitutive molecules. In recent years, molecular chaperones or …

In response to either elevated temperatures or several other metabolic insults, cells from all
organisms respond by increasing the expression of so-called heat shock proteins (hsp or …

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 …