The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring
Collagen degradation in tuberculosis pathogenesis: the biochemical consequences of hosting an undesired guest
Revisiting the role of cholesterol in regulating the pore-formation mechanism of Vibrio cholerae cytolysin, a membrane-damaging β-barrel pore-forming toxin
Structure-guided identification of function: role of Capsicum annuum vicilin during oxidative stress
An Aβ42 variant that inhibits intra- and extracellular amyloid aggregation and enhances cell viability
In this issue, Keith Willison reviews of the structure and evolution of eukaryotic CCT (chaperonin-containing TCP-1) and how it effects actin folding. The cover image shows a space-fill model of the CCT3/γ apical domain with its solvent-accessible-binding surface highlighted in brown and a stretch of bound poly-Gln β-strand occupying the long stretch of anchoring sites. For further details, see pages 3009–3034. Image kindly provided by Miriam Eisenstein (Weizmann Institute for Science).