Anne K. Kenworthy

This study identifies how caveolin-1's hydrophobic residue patterning drives membrane bending through structural and computational analyses.

The paper identifies small-molecule modulators of lipid raft stability and protein-raft partitioning, revealing two classes of compounds with distinct mechanisms of action.

The paper shows that palmitoylated caveolin-1 facilitates endosome sorting of complex sphingolipids to the plasma membrane, independent of caveolae.

This paper investigates how the CAV1-8S caveolin complex interacts with lipid membranes through a novel leaflet replacement mechanism, revealing its role in membrane curvature and organization.

The paper investigates the membrane association of C99, finding it preferentially localizes to disordered domains rather than raft domains, challenging previous assumptions about its role in amyloidogenic processing.