The past 20 years have seen enormous progress in the understanding of the mechanisms
used by the enteric bacterium Escherichia coli to promote protein folding, support protein …

SUMMARY α-Crystallins were originally recognized as proteins contributing to the
transparency of the mammalian eye lens. Subsequently, they have been found in many, but …

We systematically analyzed the capability of the major cytosolic chaperones of Escherichia
coli to cope with protein misfolding and aggregation during heat stress in vivo and in cell …

Small heat shock proteins (sHsps) can efficiently prevent the aggregation of unfolded
proteins in vitro. However, how this in vitro activity translates to function in vivo is poorly …

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 …

The small heat shock proteins (sHSPs) are ubiquitous stress proteins proposed to act as
molecular chaperones to prevent irreversible protein denaturation. We characterized the …

Protein misfolding and aggregation are typically perceived as inevitable and detrimental
processes tied to a stress-or age-associated decline in cellular proteostasis. A careful …

The continuing expansion of interest in probiotic bacteria has led to an increase in
manufactured Functional Foods and medicines containing these bacteria. Given the …

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 …

Protein folding in the cell, long thought to be a spontaneous process, in fact often requires
the assistance of molecular chaperones. This is thought to be largely because of the danger …