ReviewGlycobiology2015
Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane.
Review in Glycobiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers.
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Who cites it
160 citing papers in PubMed, 260 citations in OpenAlex.
- Whole-blood RNA transcript-based models can predict clinical response in two large independent clinical studies of patients with advanced melanoma treated with the checkpoint inhibitor, tremelimumab.Journal for immunotherapy of cancer · 2017Trial
- Machine-Readable Database for Genotype-Phenotype Analyses in Rare Diseases Using FKTN-related Congenital Muscular Dystrophies as a Prototype.Research square · 2026Article
- Emerging Roles of Dystroglycan in Cardiac Remodeling, Fibrosis, and Heart Failure.International journal of molecular sciences · 2026Review
- Mitochondrial defects in the cAMP-PKA-DRP1 pathway in a Crppa deletion model of dystroglycanopathy.Disease models & mechanisms · 2026Article
- O-mannosylation and furin processing are critical maturation events for the KIAA1549 protein implicated in pediatric pilocytic astrocytomas.The Journal of biological chemistry · 2026Article
- Defining Haplosufficiency in Autosomal Recessive Limb-Girdle Muscular Dystrophy Using Molecular Markers in Disease Carriers.Neurology. Genetics · 2026Article
- Glycan-related genes and genetic disorders.Journal of human genetics · 2026Review
- Recent advances in the synthesis of α-dystroglycanRSC advances · 2026Review
- A homozygous variant in the beta-1,3-N-acetylglucosaminyltransferase 4 gene causes progressive brain atrophy and muscular dystrophy.European journal of human genetics : EJHG · 2026Article
- Regulation of Glycan Modification by Glycosyltransferases in the Golgi Apparatus.Sub-cellular biochemistry · 2026Review
- Biosynthesis and Regulation of Laminin-Binding O-Mannosyl Glycans Related to Muscular Dystrophy.Advances in experimental medicine and biology · 2026Review
- Impact of maternal compensation on developmental phenotypes in a zebrafish model of severe congenital muscular dystrophy.PLoS genetics · 2026Article
- Analysis of Dystrophin-Associated Glycoproteins: Focus on Expression and Glycosylation of Dystroglycan in Skeletal Muscle.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Alkyne-tagged ribitol-5-phosphate derivatives for metabolic labelling of alpha-dystroglycan.RSC chemical biology · 2025Article
- Expression of Dystroglycanopathy-Related Enzymes, POMGNT2 and POMGNT1, in the Mammalian Retina and 661W Cone-like Cell Line.Biomedicines · 2025Article
- Pathogenic mechanisms and clinical insights intoJournal of neuromuscular diseases · 2025Article
- Xylose phosphatase activity of dystroglycan self-regulates its receptor function.bioRxiv : the preprint server for biology · 2025Article
- LARGE1 processively polymerizes length-controlled matriglycan on prodystroglycan.Nature communications · 2025Article
- Article
- The diverse roles of complex glycans in synapse development and function.Current opinion in neurobiology · 2025Review
100 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Associations between cells and the basement membrane are critical for a variety of biological events including cell proliferation, cell migration, cell differentiation and the maintenance of tissue integrity. Dystroglycan is a highly glycosylated basement membrane receptor, and is involved in physiological processes that maintain integrity of the skeletal muscle, as well as development and function of the central nervous system. Aberrant O-glycosylation of the α subunit of this protein, and a concomitant loss of dystroglycan's ability to function as a receptor for extracellular matrix (ECM) ligands that bear laminin globular (LG) domains, occurs in several congenital/limb-girdle muscular dystrophies (also referred to as dystroglycanopathies). Recent genetic studies revealed that mutations in DAG1 (which encodes dystroglycan) and at least 17 other genes disrupt the ECM receptor function of dystroglycan and cause disease. Here, we summarize recent advances in our understanding of the enzymatic functions of two of these disease genes: the like-glycosyltransferase (LARGE) and protein O-mannose kinase (POMK, previously referred to as SGK196). In addition, we discuss the structure of the glycan that directly binds the ECM ligands and the mechanisms by which this functional motif is linked to dystroglycan. In light of the fact that dystroglycan functions as a matrix receptor and the polysaccharide synthesized by LARGE is the binding motif for matrix proteins, we propose to name this novel polysaccharide structure matriglycan.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.