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.

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

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

In contrast with earlier conclusions, negative selection has a major role in cancer evolution.

Hydrogen-deuterium exchange, electron microscopy, and vesicle reconstitution show how binding of the autophagy adaptor NDP52 to the FIP200 subunit of the ULK1 complex triggers membrane binding in autophagy.

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

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.

LRH-1/NR5A2 responds to ER stress by inducing a novel pathway that is required for stress resolution in mice and can be targeted by LRH-1 agonists.

Genetic knockout of Hdac2 modifies molecular and cellular phenotypes in Huntington’s disease mice and has a prominent transcriptional regulatory role in adult medium spiny neurons.