Clusterin in disease pathology

Hydrophobic tails enable diverse functions of the extracellular chaperone clusterin

This study identifies hydrophobic peptide tails in clusterin as essential for its chaperone function and lipid binding, enabling diverse roles in protein clearance and lipoprotein formation.

Two sites in the C-terminal β-chain tail mediate interactions of the chaperone clusterin with amyloid beta and other misfolded client proteins

This study identifies two critical sites in the C-terminal β-chain tail of clusterin that mediate its interaction with misfolded proteins, including amyloid β, through experimental and computational approaches.