D. Velazquez-Carreras

The paper identifies amino acid substitutions in titin domains that increase hydrophilicity and cause dilated cardiomyopathy by destabilizing the protein structure.

The paper shows that substrate energy dissipation suppresses YAP mechanosensing more than stiffness cues in cell mechanotransduction.

This study investigates nanomechanical changes in cMyBP-C mutants linked to hypertrophic cardiomyopathy, finding that pathogenic mutations alter mechanical properties compared to non-pathogenic variants.

The paper identifies that mutations in conserved titin cysteines disrupt mechanoredox control, leading to dilated cardiomyopathy in humans.

The paper introduces a HaloTag-TEV genetic cassette to study protein mechanics in native tissues, showing titin's role in muscle contraction under mechanical forces.

This paper introduces concurrent AFM force measurements to improve the accuracy and throughput of mechanical property quantification in single-molecule studies.