Daniel Kaganovich

Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the alpha-rings.

Protein quality control: chaperones culling corrupt conformations.

Misfolded proteins partition between two distinct quality control compartments.

Equivalent mutations in the eight subunits of the chaperonin CCT produce dramatically different cellular and gene expression phenotypes.

Polyglutamine shows a urea-like affinity for unfolded cytosolic protein.

Cyclosporin-A-induced prion protein aggresomes are dynamic quality-control cellular compartments.

Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity.

Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast.