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.

The combined use of NAD+ with ribitol or ribose potentiates the rescue of α-dystroglycan functional glycosylation in FKRP-mutant patient-specific iPSC-derived myotubes, representing potential novel treatments for FKRP muscular dystrophies.

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

An multi-species approach can be used to identify small molecules with properties that might prove useful for the treatment of some neuromuscular diseases.

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

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

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

Protein O-Mannose Kinase enables Like-acetyl-glucosaminyltransferase 1 to elongate matriglycan on α-dystroglycan, thereby allowing matriglycan to function as a scaffold for extracellular matrix proteins and prevent muscular dystrophy.

The LINC complex, that couples the interphase cytoskeleton to the nucleus, regulates the processing of a cluster of miRNAs required for muscle regeneration by recruiting and interacting directly with Drosha.