Small heat shock proteins (sHSPs) are ATP-independent chaperones that delay formation of
harmful protein aggregates. sHSPs' role in protein homeostasis has been appreciated for …

α-Crystallins are small heat-shock proteins that act as holdase chaperones. In humans, αA-
crystallin is expressed only in the eye lens, while αB-crystallin is found in many tissues. α …

Small heat shock proteins function as chaperones by binding unfolding substrate proteins in
an ATP-independent manner to keep them in a folding-competent state and to prevent …

Neuropathological hallmarks of Alzheimer's disease (AD) include pathogenic accumulation
of amyloid-β (Aβ) peptides and age-dependent formation of amyloid plaques in the brain …

Exposure to solar UV irradiation damages γ-crystallin, leading to cataract formation via
aggregation. α-Crystallin, as a small heat shock protein, efficiently suppresses this …

Mycobacterium leprae uptakes various bivalent metal ions via different transporters in host
species. Uptake of Cu 2+ and Zn 2+ are essential for generation of superoxide dismutases …

Background: αA-and αB-crystallin are members of small heat shock protein family with
chaperone property. Their interactions with Cu2+ ions are reported in neurodegenerative …

The G98R mutation in αA-crystallin is associated with the onset of presenile cataract and is
characterized biochemically by an increased oligomeric mass, altered chaperone function …

Exposure to solar UV irradiation damages g-crystallin, leading to cataract formation via
aggregation. a-Crystallin, as a small heat shock protein, efficiently suppresses this …

For the eye lens to function correctly, it must be transparent and refract visible light strongly
enough to form an image on the retina. The bulk of this unique tissue is made of layers of …