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.

GnT1IP-L is a membrane bound glycoprotein that interacts with MGAT1 in the Golgi, but not in the endoplasmic reticulum, to regulate complex N-glycan synthesis.

The architecture of a gene regulatory network determines the effect of evolutionary changes in transcription factor binding.

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.

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

Inhibiting triglyceride storage in adipose tissue prevents obesity and improves metabolic health.

The molecular mechanisms by which midbrain dopamine neurons acquire the inhibitory neurotransmitter GABA for synaptic release are revealed.

MMnet is a conserved, trans-regulated gene network that controls skeletal homeostasis through osteoclast multinucleation and bone resorptive function.