Toby A. Dite

This paper presents cryo-EM structures of PORCN with inhibitors, revealing a conserved water-mediated binding mechanism for rational drug design.

The paper identifies an unconventional mechanism where Ca2+-CaM binds CHK2 kinase to inhibit its activity, contrasting with its typical role in promoting kinase activity.

The paper determines the cryo-EM structure of the Plasmodium falciparum Pfs230-Pfs48/45 fertilization complex and identifies domains critical for function and vaccine design.

This study shows NRBP1 and TSC22D proteins modulate WNK signaling in the kidney's distal convoluted tubule, affecting Na+ reabsorption through NCC phosphorylation.

This study identifies NRBP1 as an upstream activator of the WNK pathway by forming a multi-subunit complex with WNK1, SPAK, and TSC22D4 in response to osmotic stress.

This study characterizes MORC2 phosphorylation's role in DNA compaction and chromatin remodelling, showing it regulates ATP hydrolysis and DNA binding.

The paper identifies allosteric regulation of PSKH1 kinase activity by Ca2+ sensor proteins, showing both activation and suppression by different sensors.