siRNA knockdown experiments reveal in detail the signaling pathway that controls cytoskeletal function during cell-in-cell invasion.

The rhoptry protein RhopH3 is crucial for the invasion and growth of the malaria parasite and disruption of it provides insight into the binding of the parasite to the host red blood cell and into the formation of new import pathways.

Gene knockdowns reveal that the conserved RhopH protein complex functions in both host cell invasion and channel-mediated nutrient uptake in malaria.

Genetic analysis identifies an enzyme of the malaria parasite that is required to seal its host red blood cell membrane upon invasion, a key requirement of this important intracellular pathogen.

Myristoylation of a secreted protein, identified in a global myristoylation analysis of the eukaryotic parasite Toxoplasma gondii, is important for host cell invasion.

The ATM kinase has an unanticipated role in tumor progression through the regulation of cell migration by oxidative stress.

p27Kip1 directly controls invadopodia turnover by promoting the interaction of PAK1 with Cortactin, which induces Cortactin phosphorylation, invadopodia disassembly and facilitates invasion through extracellular matrix.

The melanoma cell interaction with lymphatic endothelial cells promotes melanoma metastasis by inducing a reversible switch to invasively sprouting melanoma cells.

A high-resolution structure reveals how the RhopH complex traffics within Plasmodium-infected human erythrocytes to serve divergent, essential functions.

An aspartyl protease is essential for the lytic cycle of Toxoplasma gondii and is involved in the maturation of proteins critical for invasion and egress, and it can be targeted selectively with an ethylamine scaffold based peptidomimetic inhibitor.