Alan F. Cowman

This paper identifies MMV006833 as an inhibitor of PfSTART1 in P. falciparum but shows it is ineffective against P. berghei due to structural differences and other factors.

This study evaluates resistance development to PMX-selective and dual PMIX/X inhibitors in Plasmodium falciparum, finding that dual inhibitors have a higher resistance barrier.

This study shows that targeting PTRAMP-CSS inhibits Plasmodium falciparum across liver, blood, and mosquito stages, supporting its potential as a multistage vaccine target.

This study identifies EGF7 in PfRipr as a critical domain for inhibiting Plasmodium falciparum erythrocyte invasion and provides a basis for vaccine design.

This study investigates how Plasmodium falciparum bypasses the erythrocyte cytoskeleton during invasion by analyzing the timing of cytoskeletal disassembly and apical organelle release using lattice light sheet microscopy.

This study identifies MMV687794 as an inhibitor of Plasmodium falciparum RBC invasion by targeting PfSLIRP, a rhoptry protein involved in lipid metabolism and vacuole formation.

The paper identifies a conserved complex formed by PTRAMP, CSS, and Ripr in Plasmodium species that facilitates merozoite invasion of erythrocytes and shows its structural and functional conservation across species.

This study identifies CD44 as a host factor promoting Plasmodium falciparum invasion through cross-linking, which alters RBC membrane structure and enhances ligand-receptor interactions.

This study evaluates the cross-species neutralization potential of monoclonal antibodies against PfCyRPA and PfRIPR against P. knowlesi, finding minimal inhibition despite partial epitope conservation.

This study investigates the on-target activity of plasmepsin V peptidomimetics in Plasmodium falciparum by combining chemoproteomic methods and genetic validation.

The paper identifies LSA3 as an exported protein essential for Plasmodium falciparum liver-stage development and presents it as a potential vaccine candidate.

The paper identifies aryl amino acetamides that inhibit Plasmodium falciparum ring development by targeting PfSTART1, a lipid transfer protein, and shows these inhibitors block parasite transmission.