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.

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.

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.

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

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

A multi-scale integration of experimental and computational approaches shows how a non-linear dependence of T-type calcium channel gating on GABA_B receptor activity regulates thalamic network oscillations.

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

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

Metabolic switches between oxidative phosphorylation and aerobic glycolysis plus glutaminolysis direct T cell function by altering the flux of glucose and glutamine to N-glycosylation.

A critical role for glycosylation on viral entry and methods to use this knowledge to reduce SARS-CoV-2 infectivity has been demonstrated.