Small heat shock proteins (sHsps) are conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

The primary function of the eye lens is to focus light on the retina. The major proteins in the
lens—α, β, and γ-crystallins—are constantly subjected to age-related changes such as …

The small heat shock proteins (sHSPs) recently have been reported to have molecular
chaperone activity in vitro; however, the mechanism of this activity is poorly defined. We …

Emphasizing effective, state-of-the art methodology and written by recognized experts in the
field, the Handbook of Food Analytical Chemistry is an indispensable reference for food …

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 proteins (sHsps) are a conserved protein family, with members found in all
organisms analysed so far. Several sHsps have been shown to exhibit chaperone activity …

The majority of active tuberculosis cases arise as a result of reactivation of latent organisms
which are quiescent within the host. The ability of mycobacteria to survive extended periods …

The role of α-crystallin as a molecular chaperone may explain how the lens stays
transparent for so long. α-Crystallin prevents the aggregation of other lens crystallins and …

Small heat shock proteins (sHSP) make up a remarkably diverse group of molecular
chaperones possessing a degree of structural plasticity unparalleled in other protein …

Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or
ordered (amyloid fibril) aggregates. The major lens protein, α-crystallin, is a member of the …