N-terminal domain of dystroglycan enables like-acetylglucosaminyl transferase to elongate matriglycan on α-dystroglycan and prevent skeletal muscle pathophysiology.

Important mechanistic details on Duchenne Muscular Dystrophy arrhythmogenesis are revealed, providing a crucial lead for investigators interested in developing therapeutic solutions for this deadly disease.

Thrombospondin proteins regulate vesicular trafficking of integrins and other membrane attachment complex proteins to the plasma membrane of skeletal muscle, which provides greater stability and resistance to muscular dystrophy.

While Notch activation dedifferentiates newly differentiated muscle cells; it improves the function of muscle fiber as a niche-supporting cell of muscle stem cells.

Depending upon the parameters used, neuromuscular stimulation can have beneficial or deleterious impacts on muscle structure and function in an animal model of Duchenne muscular dystrophy.

Active site migration establishes kinase activity in protein O-mannose kinase.

A multidisciplinary approach was used to translate the mathematical analysis of Dystrophin movements inside muscle cells into the biology of how Dystrophin interacts with the cell membrane.

Bulk and single-cell RNA-seq data demonstrated that muscle stem cells express low levels of canonical endothelial cell markers, including VEGFA receptors, and VEGFA-FLT1 pathway has a drastic effect on muscle stem cell survival through AKT1 in vitro and in vivo.

Rescue of DUX4-induced muscle pathology by the RET inhibitor Sunitinib reveals the therapeutic potential for treatment of Facioscapulohumeral muscular dystrophy using tyrosine kinase inhibitors.

Disruption of the LG domain-binding phospho-ribitol-containing O-mannose structures on α-dystroglycan results in congenital muscular dystrophy.