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 conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

Small heat shock proteins (sHsps) constitute a diverse chaperone family that shares the α-
crystallin domain, which is flanked by variable, disordered N-and C-terminal extensions …

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 …

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 …

Hsp27, αB-crystallin and HSP22 are ubiquitous small heat shock proteins (sHsp) whose
expression is induced in response to a wide variety of unfavorable physiological and …

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

Mammalian small heat-shock proteins (sHSPs) are molecular chaperones that form
polydisperse and dynamic complexes with target proteins, serving as a first line of defense …

Small heat shock proteins (sHsps) are a ubiquitous family of molecular chaperones that
suppress the unspecific aggregation of miscellaneous proteins. Multicellular organisms …

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 …