Apicomplexan-like parasites originated several times independently and many of them contain cryptic plastid organelles, which demonstrate that the parasites evolved from photosynthetic algae.

A phylum-specific ATP synthase subunit is needed for proper mitochondrial function and stability of the complex in Toxoplasma gondii.

A versatile acetylation-methylation switch at lysine 31 on the lateral surface of histone H4 contributes to chromatin structure in apicomplexan parasites.

The convergent evolution of unusually strict substrate specificity in apicomplexan LDHs arose by classic neofunctionalization of a duplicated MDH gene via few mutations of large effect.

In contrast to current knowledge that predicts that apicomplexan actin is unconventional, use of Chromobodies demonstrate that Toxoplasma F-actin forms a long, stable, highly dynamic tubular network that is required for material transfer and parasite maturation.

The proteins found in the mitochondria of apicomplexan parasites, including key proteins involved in energy generation, are very different from mitochondrial proteins of the animals these parasites infect.

An unbiased chemical screen identifies the AAA+ membrane metalloprotease FtsH1 as a novel apicoplast biogenesis factor and druggable antimalarial target.

A combination of high-resolution microscopy and reverse genetics identified key components of the alveolin network playing an essential role in the assembly of subpellicular microtubules and conoid in Toxoplasma gondii..

The structure, function and mechanism of the malaria vaccine candidate CelTOS reveal a unique pore-forming and membrane-disrupting protein with specificity for the inner leaflet of host and vector cells.

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.