Publisher Summary The goal of this chapter is to clarify the diversity within the heat shock
proteins (sHsps) family and to describe evidence indicating that sHsps have many different …

Small heat shock/α-crystallin proteins are defined by a conserved sequence of
approximately 90 amino acid residues, termed the α-crystallin domain, which is bounded by …

The 2.7 Å structure of wheat HSP16. 9, a member of the small heat shock proteins (sHSPs),
indicates how its α-crystallin domain and flanking extensions assemble into a dodecameric …

The small heat-shock proteins (sHSPs) form a diverse family of proteins that are produced in
all organisms. They function as chaperone-like proteins in that they bind unfolded …

A newly identified 22 kDa protein that interacts with Hsp27 (heat-shock protein 27) was
shown to possess the characteristic α-crystallin domain, hence named Hsp22, and …

α-Crystallin is a member of the small heat-shock protein family and functions like a
molecular chaperone, and may thus help in maintaining the transparency of the eye lens by …

Molecular chaperones are an essential part of the universal heat shock response that allows
organisms to survive stress conditions that cause intracellular protein unfolding. During the …

We examined the effect of heat stress on localization of two sHsps, αB-crystallin and Hsp25,
and of Hsc70, a member of a different class of heat shock proteins (Hsps), in both …

Encysted embryos of the primitive crustacean Artemia franciscana are among the most
resistant of all multicellular eukaryotes to environmental stress, in part due to massive …

Background The demonstration of chaperone-like activity in peptides (mini-chaperones)
derived from α-crystallin's chaperone region has generated significant interest in exploring …