Calvin K. Yip

This study identifies phosphorylation of Y2090 in PI4KA as an inhibitory mechanism that suppresses its lipid kinase activity through conformational changes and reduced membrane recruitment.

The paper develops a nanobody that selectively blocks EFR3 recruitment of PI4KA by targeting TTC7B, reducing membrane recruitment and PI4P production.

The paper reports a cryo-EM structure of EFR3A bound to the PI4KA complex, revealing the molecular mechanism of PI4KA membrane recruitment and its regulation in human disease.

The paper reports a cryo-EM structure of Calcineurin bound to PI4KA, revealing direct interactions with both PI4KA and FAM126A and their conserved binding sequences.

The paper introduces a 3-track network for accurate protein structure and interaction prediction, achieving performance close to DeepMind's CASP14 results and enabling rapid modeling of protein complexes from sequence data.