Dystroglycan is a ubiquitously expressed heterodimeric adhesion receptor. The extracellular
α-subunit makes connections with a number of laminin G domain ligands including laminins …

The majority of proteins is modified with carbohydrate structures. This modification, called
glycosylation, was shown to be crucial for protein folding, stability and subcellular location …

During the last 15 years, following its identification and first detailed molecular
characterization, the dystroglycan (DG) complex has taken centre stage in biology and …

The Dystroglycan-Dystrophin (Dg-Dys) complex has a capacity to transmit information from
the extracellular matrix to the cytoskeleton inside the cell. It is proposed that this interaction …

Drosophila melanogaster provides a powerful platform with which researchers can dissect
complex genetic questions and biochemical pathways relevant to a vast array of human …

Background Dystroglycanopathies are a group of inherited disorders characterized by vast
clinical and genetic heterogeneity and caused by abnormal functioning of the ECM receptor …

Monolayers of astrocytes in culture respond to a scrape wound by orienting towards the
wound and extending processes that will repair it. We show here that they also upregulate …

In following up the experiments reported in this paper, we have discovered that the polarity
phenotypes of Dystroglycan and perlecan mutant clones under starvation conditions shown …

Protein O-glycosylation is the attachment of carbohydrate structures to the oxygen atom in
the hydroxyl group of Serine and Threonine residues. This post-translational modification is …

To assemble a brain, differentiating neurons must make proper connections and establish
specialized brain compartments. Abnormal levels of cell adhesion molecules disrupt these …