José A. Gavira

This study investigates how Atg18 binds to phosphatidylinositol-3,4,5-triphosphate, showing it clusters membranes and tethers opposing membranes.

This study shows how a bacterial chemoreceptor evolved from a bimodular to a monomodular domain by losing one module, revealing that reducing complexity may be a common evolutionary trend in sensory domains.

The paper identifies a purine-binding motif in bacterial receptors and demonstrates its role in modulating second messenger signaling.

This study determines the structure of hNQO1 with NADH using serial crystallography and simulations, showing NADH binding stabilizes the protein and drives functional cooperativity through structural communication.

The paper identifies heme protection by polypeptides as a mechanism enhancing catalytic efficiency in ancestral proteins, suggesting it may have driven the evolution of enzymes.