Megan H. Wright

TL;DR: The chemistry and biology of N-myristoylation and NMT are introduced, and new developments in chemical proteomic technologies that are meeting the challenge of studying this important co-translational modification in living systems are discussed.

TL;DR: The presented data substantially expand the known repertoire of co- and post-translational N-myristoylation in addition to validating tools for the pharmacological inhibition of NMT in living cells.

TL;DR: It is demonstrated that N-myristoyltransferase is an essential and chemically tractable target in malaria parasites both in vitro and in vivo, and that selective inhibition of N- myristoylation leads to catastrophic and irreversible failure to assemble the inner membrane complex, a critical subcellular organelle in the parasite life cycle.

TL;DR: Systematic functional analyses of PPs in Plasmodium are provided to identify how phosphatases regulate parasite development and differentiation, and can inform the identification of drug targets for malaria.