A cell-permeable mycotoxin which binds to the barbed end of actin, reversibly inhibiting the elongation and shortening of actin filaments; blocks diverse cellular functions, including cell division, migration, phagocytosis, exocytosis, chemotaxis, and glucose transport.

A cell-permeable inhibitor that binds actin filaments, but not actin monomers, to inhibit polymerization at concentrations as low as 0.2 µM.

Inhibits actin polymerization; uniquely inhibits HIV-1 protease (IC50 = 3 μM); rapidly and reversibly inhibits glucose transport by competitively binding glucose transporters (Ki = 4.0 μM); induces the phosphorylation of the tyrosine phosphatase PTP3 of Dictyostelium, activating STATc.

A cell-permeable inhibitor of actin polymerization that has been shown to be 10 times less toxic in mice than cytochalasin D.