M. J. Greenberg

This study shows that two point mutations at the same residue in beta-myosin heavy chain cause distinct cardiomyopathies through different molecular mechanisms.

This study investigates how thin filament regulatory proteins affect the mechanics and kinetics of cardiac myosin using single-molecule techniques, finding no significant impact at physiological ATP concentrations but some effects at low ATP.

This paper shows that the probability of cryptic pocket opening in myosin motor domains predicts drug specificity and affinity, using molecular dynamics simulations and Markov state models.

This study identifies myofilament glycation in diabetes as a cause of reduced cardiac contractility, showing that cMyBPC domains can rescue this dysfunction.

This study shows SARS-CoV-2 infects human engineered heart tissues, causing myocarditis-like features, and identifies ACE2 and proteases as entry factors.

The paper introduces a computational tool, SPASM, for ensemble averaging of single-molecule data to improve the accuracy of measuring mechanochemical coupling in molecular motors.

This study shows that a HCM mutation causes mechanical dysfunction, which drives cellular adaptation through altered force generation and signaling pathways.

The paper models conformational distributions of myosin motor domains using molecular dynamics simulations to predict mechanochemical properties better than sequence or structure alone.

This study investigates how a mutation in troponin-T affects cellular contractility and mechanosensing in familial dilated cardiomyopathy.

The paper introduces a computational tool to measure muscle activation equilibrium constants and analyze perturbations, applying it to study a mutation causing hypertrophic cardiomyopathy.

This study shows that omecamtiv mecarbil increases cardiac output by inhibiting myosin working stroke and enhancing thin filament activation through cooperative mechanisms.

The paper introduces a method to identify functionally-relevant conformational changes in proteins by analyzing cooperative solvent exposure changes, demonstrating its utility in discovering cryptic allosteric sites.