The correct enzymatic activity of a previously misnamed enzyme is defined, placing the enzyme upstream of LARGE in building functional O-mannose structures on α-dystroglycan that are disrupted in multiple forms of congenital muscular dystrophy.

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

There is no such thing as a representative skeletal muscle tissue, as each member of this family of tissues expresses a specialized mRNA program.

Specific human mitofusin 2 mutations induce selective upper body obesity with suppressed leptin expression and severe adipose mitochondrial dysfunction.

Functional attachments between muscles and tendons require pentameric Thrombospondin-4, revealing novel roles both as an integrin ligand and extracellular matrix scaffold.

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

An agonist antibody to MuSK, delivered after disease onset, decreases the loss of neuromuscular synapses, improves motor function and extends the lifespan of ALS mice.

Post-phosphoryl modification of α-dystroglycan requires the glucuronyltransferase B4GAT1; this enzyme synthesizes the acceptor glycan that serves as a primer for the glycosyltransferase LARGE to synthesize the laminin-binding glycan.

Expression of the lamina-associated polypeptide α (LAP2α) prevents premature cellular ageing caused by expression of progerin in Hutchinson-Gilford progeria syndrome.

Genetic studies in the mouse provide a blueprint of the embryonic origins of neck muscles originating from cranial and somitic mesoderm, as well as associated connective tissue.