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.

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.

Structurally dissimilar N-glycans can be functionally equivalent, and are produced via a self-correcting feature of the Golgi.

The maintenance of skeletal muscle function improves the quality of life, and therefore understanding how changes in the genome drive changes in the skeletal muscle proteome has revealed novel regulators of muscle physiology.

Neural crest cells differentiated from patient-derived cells with mutations in the chromatin remodeler CHD7 show defective delamination, migration and motility in vitro, and defective migration in chick embryos.

Loss of functional dystroglycan disrupts the formation and function of CCK⁺/CB₁R⁺ inhibitory synapses in hippocampal CA1, resulting in reduced seizure thresholds in mouse models of dystroglycanopathy.

Deep mining of GT-A fold sequences provides an evolutionary framework for investigating complex relationships connecting GT-A fold sequence, structure, function and regulation.

Dystroglycan interacts with multiple partners, including the transmembrane receptor Celsr3, to regulate axon tract formation throughout the developing nervous system.

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

ESRP1 is central to intestinal barrier integrity in mice and humans and alterations in ESRP1 function or expression contribute to intestinal pathology, partly through modified expression of ESRP1-specific GPR137 isoforms.