Kathleen M Ruppel

Mutations in the catalytic domain of human β-cardiac myosin that cause early onset hypertrophic cardiomyopathy significantly increase the fundamental parameters that determine ensemble force and velocity

This study examines two HCM-causing mutations in human β-cardiac myosin, finding significant increases in actin gliding velocity, intrinsic force, and ATPase activity, indicating a hyper-contractile phenotype.

Biophysical properties of human β-cardiac myosin with converter mutations that cause hypertrophic cardiomyopathy

The paper analyzes biophysical properties of human β-cardiac myosin with HCM-causing converter domain mutations, finding minimal changes or slightly hypo-contractile profiles, contrasting with clinical hyper-contractility.

Beyond the myosin mesa: a potential unifying hypothesis on the underlying molecular basis of hyper-contractility caused by a majority of hypertrophic cardiomyopathy mutations

This paper proposes a unifying hypothesis that hypertrophic cardiomyopathy mutations increase functionally accessible myosin heads in the sarcomere, leading to hyper-contractility.

Multi-dimensional structure function relationships in human β-cardiac myosin from population scale genetic variation.

This study combines structural models of myosin, exome sequencing, and phenotypic data to identify disease-associated variants in specific structural regions of β-cardiac myosin linked to HCM severity.