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 …

Small heat shock proteins are a diverse, ancient, and important family of proteins. All
organisms possess small heat shock proteins (sHSPs), indicating that these proteins …

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 …

TreeFam is a database of phylogenetic trees of gene families found in animals. It aims to
develop a curated resource that presents the accurate evolutionary history of all animal …

Small heat shock proteins (sHSPs) associate with nuclei, cytoskeleton and membranes, and
as molecular chaperones they bind partially denatured proteins, thereby preventing …

Small heat shock proteins (sHsps) are molecular chaperones involved in maintaining
protein homeostasis; they have also been implicated in protein folding diseases and in …

The crystallins were discovered more than 100 years ago by Mörner (1893. Untersuchungen
der Proteinsubstanzen in den lichtbrechenden Medien des Auges. Z. Physiol. Chem. 18, 61 …

Small heat shock proteins (sHSPs) function as molecular chaperones, preventing stress
induced aggregation of partially denatured proteins and promoting their return to native …

Heat shock proteins (HSPs) are molecular chaperones involved in a variety of life activities.
HSPs function in the refolding of misfolded proteins, thereby contributing to the maintenance …