José M. M. Caaveiro

This paper demonstrates that fusion-protein architecture determines site selectivity in proximity-directed enzymatic modification of antibodies, enabling site-specific functionalization.

The paper determines the Cryo-EM structure of the intestinal IMAC complex, revealing its heterotetrameric composition and structural features that enable microvilli adhesion and resilience to shear stress.

This study generates and characterizes monoclonal IgM and IgG antibodies against norovirus variants GII.4 and GII.17, revealing differences in binding mechanisms and affinity.

This study investigates the role of Pro230 in the hinge region of IgG by deleting it, revealing structural changes and functional effects on FcγRI-mediated activity.

This study identifies PfHO as essential for apicoplast biogenesis and gene expression in Plasmodium falciparum, revealing its role in maintaining apicoplast-encoded RNA levels.