Ariel Tennenhouse

The paper designs structurally diverse antibody repertoires with drug-like properties using a computational method called CADAbRe, demonstrating their utility in binding to challenging targets.

This study identifies structural features of HCV E2 glycoprotein recognized by germline B cell receptors and evaluates strategies to enhance germline antibody interactions.

The paper investigates how BMP and TGFβ pathways interact asymmetrically, showing that TGFβ inhibits BMP and BMP enhances TGFβ responses, reducing signaling ambiguity.

This paper introduces LAffAb, a method to co-optimize antibody affinity and stability through combinatorial mutation design, achieving significant affinity gains while maintaining developability.