Interactions were visualized between the nuclear egress complex from herpes simplex virus and a capsid protein that could promote nucleocytoplasmic translocation of the capsid in infected cells.

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.

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.

Comprehensive characterization of kinase-dependent phosphorylation in the human pathogen Toxoplasma gondii identifies a trafficking adaptor complex required for virulence factor secretion and infection.

Enterovirus D68, a pathogen associated with a rare child paralysis disease, depends on the cellular protein SIRT-1 for release of virus, indicating that SIRT-1 may be an important therapeutic target.

Ultrastructure expansion microscopy unlocks new fundamental cell biology of malaria parasites, providing new insights into processes including establishment of cell polarity, organelle biogenesis, and organelle fission.

Multi-omic analyses reveal that the chromatin-associated microrchidia protein, MORC (PF3D7_1468100), at the blood stage of the human malaria parasite, Plasmodium falciparum, interacts with a range of nuclear proteins.

A transient receptor channel in Toxoplasma gondii that conducts calcium represents the first molecular element that initiates upstream calcium signals that activate parasite pathogenic pathways.

Overexpression of interferon-stimulated genes revealed a role for RARRES3 in restricting growth of Toxoplasma gondii by inducing early egress from human cells.

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.