Allan Haldane

The paper investigates how specific stalk-derived peptides can reactivate signaling in disease-associated PC1 mutants and uses computational simulations to support these findings.

This paper analyzes the binding of 50 type II inhibitors to 348 kinases, showing that protein reorganization significantly contributes to inhibitor selectivity with an AUC of ~0.8.

This paper introduces a method using molecular dynamics simulations to predict water positions in cryo-EM maps by analyzing excess chemical potential, showing high agreement with experimental data.

This study identifies the structural and sequence basis of epistatic interactions driving drug resistance in HIV by combining sequence models and molecular dynamics simulations.

This study evaluates ColabFold's ability to predict side chain conformations in proteins and shows how integrating it with a Potts model can explore mutation cooperativity.

The paper shows that protein evolution with epistasis and purifying selection does not lead to entrenchment, and that rate variation is due to epistasis, not historical contingency.

The paper investigates the structural basis for the distinct conformational landscapes of tyrosine and serine/threonine kinases using sequence and structure-based models.

This study identifies stalk-derived peptides that activate PC1 signaling by binding to specific regions, revealing structural dynamics and potential therapeutic applications for ADPKD.

The paper uses sequence coevolutionary analysis and structural contacts to reveal distinct residue interactions in GPCR classes A and B, providing insights for drug design.

The paper uses a Potts Hamiltonian model to infer epistatic effects in HIV-1 protease mutations, showing how these interactions influence drug resistance and fitness.