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.
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.
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.
An unbiased chemical screen identifies the AAA+ membrane metalloprotease FtsH1 as a novel apicoplast biogenesis factor and druggable antimalarial target.
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.
Partially overlapping functions of a limited subset of actin binding proteins allow the parasite Toxoplasma gondii to achieve actin regulation required for complex cellular processes.
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.
