John E. Burke

This study identifies how PIP3 activates an ancestral Tec kinase by displacing its PH domain from an inhibitory interaction with its kinase domain.

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.

This study identifies ARMH3 as a central scaffold at the Golgi/TGN by defining its interactions with Arl5, PI4KB, and GBF1 using HDX-MS and AI modeling.

This study develops domain-specific nanobodies that inhibit SARS-CoV-2 infection by disrupting N protein phase separation and replication.

This study investigates how different regulatory subunits modulate p110α activity and finds no significant differences in lipid kinase activity or conformational changes across subunit variants.

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

This study identifies how the SH2 domain sterically occludes the C2 domain to autoinhibit SHIP1, revealing structural and functional relationships critical for its membrane localization and phosphatase activity.

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.

This study develops a high-affinity anti-MR1 nanobody that selectively inhibits MR1-restricted T cell activation, providing insights into MR1 function and a tool for immunological research.

The paper reports the cryo-EM structure of human DET1 in complex with DDB1-DDA1 and Ube2e2, revealing how DET1 dynamics facilitate COP1 recruitment and ubiquitination.

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 describes a method using biolayer interferometry to measure nanobody binding kinetics and perform competition-based epitope mapping.

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.