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) are present in all kingdoms of life and play fundamental
roles in cell biology. sHSPs are key components of the cellular protein quality control …

Crystallins are the predominant structural proteins in the lens that are evolutionarily related
to stress proteins. They were first discovered outside the vertebrate eye lens by Bhat and …

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

SUMMARY α-Crystallins were originally recognized as proteins contributing to the
transparency of the mammalian eye lens. Subsequently, they have been found in many, but …

The autosomal dominant mutation in the human αB-crystallin gene inducing a R120G amino
acid exchange causes a multisystem, protein aggregation disease including …

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 …

Myofibrillogenesis in striated muscles is a highly complex process that depends on the
coordinated assembly and integration of a large number of contractile, cytoskeletal, and …

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

Upregulation of αB-crystallin (CryAB), a small heat shock protein, is associated with a variety
of diseases, including the desmin-related myopathies. CryAB, which binds to both desmin …