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

Analysis of chromerid algal genomes reveals how apicomplexans have evolved from free-living algae into successful eukaryotic parasites via massive losses and re-inventing functional roles of genes.

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.

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

Time-resolved phosphoproteomics and thermal proteome profiling reveal the Ca²⁺-responsive proteome of the model apicomplexan Taxoplasma gondii, identifying PP1 as a Ca²⁺-responsive enzyme that regulates Ca²⁺ uptake to promote parasite motility.

Apicomplexan parasites secrete proteins to manipulate their hosts from sub-apical openings in their cell pellicle that are distinct from the apical complex from where invasion factors are secreted.

Formin-2 controls spatiotemporal polymerisation of actin filaments, a common mechanism used by apicomplexans for effective segregation of essential chloroplast-like organelles called apicoplasts, and additionally for daughter formation in Plasmodium falciparum.

Combined cutting-edge technologies discovered a pair of carboxylate transporters that appears evolutionarily different among novel transporters and that is essential for parasite physiology.

The epitranscriptomic-driven mRNA polyadenylation pathway protects transcriptome integrity by restricting transcriptional read-throughs and RNA chimera formation in apicomplexan parasites and plants.