Integrative analysis of a Drosophila model of hypertrophic cardiomyopathy demonstrates that prolonged binding of the myosin cross-bridge to actin is a root cause of the disorder.

Mapping the locations of hypertrophic cardiomyopathy gene variants onto the three-dimensional structures of contractile proteins revealed that these disrupt protein interactions are critical for normal cardiac relaxation and efficient energy usage.

Cardiac-specific overexpression of a recently discovered micropeptide, DWORF, enhances calcium cycling and contractility in the heart and rescues the heart failure phenotype of a genetic mouse model of dilated cardiomyopathy.

The melanocortin-4 receptor knockout mouse exhibits a cardiomyopathy syndrome, which raises concerns about cardiovascular function in patients with the similar loss of function mutations, and perhaps even in the 1 in 1500 patients with heterozygous loss of the gene.

The newly discovered Titin internal promoter may explain why the severity of dilated cardiomyopathy in patients with truncating mutations in Titin varies dramatically depending on position of the mutation.

Mechanochemical defects of a β-cardiac myosin mutation that results in severe hypertrophic cardiomyopathy are reported and the heart failure drug omecamtiv mecarbil rescues these defects.

During heart maturation, embryonic ectoderm development as a chromatin remodeler triggers transcriptional silencing, while H3K27me3 is a passenger that is not sufficient for gene silencing.

A computer model of human cardiomyocyte was produced and validated on independent datasets, overcoming shortcomings of its predecessors, also yielding broadly relevant insights and results on major ionic currents.

A perspective of the energy-sparing super-relaxed state of myosin and its evolutionary role in modulating skeletal and cardiac muscle power under different physiological and pathophysiological perturbations.

lncEGFL7OS is a lncRNA located at the EGFL7/miR-126 locus that is critical for angiogenesis in humans.