Molecular chaperones are diverse families of multidomain proteins that have evolved to
assist nascent proteins to reach their native fold, protect subunits from heat shock during the …

Malaria parasites replicate within a parasitophorous vacuole in red blood cells (RBCs).
Progeny merozoites egress upon rupture of first the parasitophorous vacuole membrane (PVM), …

Under solution conditions where the native state is destabilized, the largely helical polypeptide
hormone insulin readily aggregates to form amyloid fibrils with a characteristic cross-β …

The small heat shock proteins (sHSPs) recently have been reported to have molecular
chaperone activity in vitro; however, the mechanism of this activity is poorly defined. We found …

The cross-β amyloid form of peptides and proteins represents an archetypal and widely
accessible structure consisting of ordered arrays of β-sheet filaments. These complex …

Small heat shock proteins (sHsps) are a conserved protein family, with members found in all
organisms analysed so far. Several sHsps have been shown to exhibit chaperone activity …

Amyloid fibrils are assemblies of misfolded proteins and are associated with pathological
conditions such as Alzheimer's disease and the spongiform encephalopathies. In the amyloid …

The bacterial toxin pneumolysin is released as a soluble monomer that kills target cells by
assembling into large oligomeric rings and forming pores in cholesterol-containing …

Natural killer cells and cytotoxic T lymphocytes accomplish the critically important function of
killing virus-infected and neoplastic cells. They do this by releasing the pore-forming protein …

The chaperonin GroEL is a large, double-ring structure that, together with ATP and the
cochaperonin GroES, assists protein folding in vivo. GroES forms an asymmetric complex with …