Small heat shock proteins (sHsps) are a ubiquitous and ancient family of ATP-independent
molecular chaperones. A key characteristic of sHsps is that they exist in ensembles of iso …

Small heat shock proteins (sHsps) are virtually ubiquitous molecular chaperones that can
prevent the irreversible aggregation of denaturing proteins. sHsps complex with a variety of …

Previous studies have established that the folding, structure and function of membrane
proteins are influenced by their lipid environments,,,,,, and that lipids can bind to specific …

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 …

We demonstrate that it is feasible to determine high-resolution protein structures by electron
crystallography of three-dimensional crystals in an electron cryo-microscope (CryoEM) …

The small heat shock proteins (sHSPs) and the related α-crystallins (αCs) are virtually
ubiquitous proteins that are strongly induced by a variety of stresses, but that also function …

Amyloid diseases, including Alzheimer's, Parkinson's, and the prion conditions, are each
associated with a particular protein in fibrillar form. These amyloid fibrils were long …

The transparency of the eye lens depends on maintaining the native tertiary structures and
solubility of the lens crystallin proteins over a lifetime. Cataract, the leading cause of …

Misfolding, aggregation, and aberrant accumulation of proteins are central components in
the progression of neurodegenerative disease. Cellular molecular chaperone systems …

Modern classification of the family of human small heat shock proteins (the so-called HSPB)
is presented, and the structure and properties of three members of this family are analyzed …