Matthew Carter Childers

This study shows that the E525K β-myosin mutation reduces cardiomyocyte contraction without altering crossbridge cycling, through structural and computational analysis.

This study investigates how the E525K mutation in cardiac myosin affects its structure and function by analyzing conformational changes using cryo-EM and MD simulations.

This paper studies the G768R mutation in cardiac myosin, showing it increases the duty ratio to >60%, leading to hypercontractility and impaired relaxation.

The paper uses molecular dynamics simulations to show how conformational changes in loop 2 of myosin affect actomyosin association strength through electrostatic interactions.

The paper identifies a dynamic gene regulatory network in Duchenne muscular dystrophy that controls cell fate decisions and shows how disease mutations disrupt this network.

This study investigates the R403Q mutation in beta-myosin heavy chain using porcine and human stem cell models, revealing altered contractile properties and mechanisms of hypercontractility and impaired relaxation.

This study investigates how HCM mutations Y115H and E497D disrupt the folded-back state of human beta-cardiac myosin, leading to hypercontractility by destabilizing the OFF-state.

This study investigates how the G256E HCM mutation affects myosin function by altering nucleotide handling, leading to prolonged relaxation and contributing to hypertrophic cardiomyopathy.

This study uses molecular dynamics simulations to investigate how 2-deoxy-ATP modifies the structure and dynamics of myosin in the interacting heads motif state.

The paper identifies heterozygous missense variants in ACTC1 as the cause of distal arthrogryposis with congenital heart defects in five families.

This study investigates the effects of the MYH7 G256E mutation on myosin function across multiple scales, finding increased hypercontractility and mitochondrial respiration.