M. J. Blackman

Activation loop phosphorylation and cGMP saturation of PKG regulate egress of malaria parasites.

This study shows that PKG regulation in malaria parasites involves cGMP saturation and activation loop phosphorylation, with phosphorylation being essential for in vivo function.

A malaria parasite phospholipase facilitates efficient asexual blood stage egress

This study identifies LCAT as a key enzyme required for efficient egress of malaria parasites from red blood cells during the asexual blood stage.

Global analysis of putative phospholipases in the malaria parasite Plasmodium falciparum reveals critical factors for parasite proliferation

The paper identifies essential phospholipases in Plasmodium falciparum, showing PF3D7_1013500 is critical for parasite maturation and PF3D7_1358000 is vital for mitochondrial function and growth.

Synchrony between daily rhythms of malaria parasites and hosts is driven by an essential amino acid

This study shows malaria parasites synchronize their asexual replication with host daily rhythms via the essential amino acid isoleucine, which is periodically supplied through host feeding.

A multipass membrane protein interacts with the cGMP-dependent protein kinase to regulate critical calcium signals in malaria parasites

This study identifies ICM1, a multipass membrane protein interacting with PKG in malaria parasites, and shows it regulates calcium signals critical for gametogenesis and parasite survival.

The malaria parasite sheddase SUB2 governs host red blood cell membrane sealing at invasion

This study shows that the malaria parasite's SUB2 protease is essential for shedding surface proteins during RBC invasion and for sealing the host cell membrane.

A lipocalin mediates unidirectional haem biomineralization in malaria parasites

This study identifies PV5, a lipocalin-like protein, as critical for controlling haem crystallization into haemozoin in malaria parasites, with implications for drug development.