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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.

Cellular NAD+ levels change during stage conversion and regulate function of a novel transcription factor that controls developmental switching in the human pathogen Entamoeba histolytica.

A small surface protein regulates gliding motility and host cell invasion by the sporozoite stage of the malaria parasite.

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.

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..

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.

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

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.

Secreted effector proteins of Toxoplasma gondii parasites create a supportive immune environment in mice, allowing individually less fit mutants to thrive and evade detection by in vivo CRISPR screens.