Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Dystrophic phenotype induced in vitro by antibody blockade of muscle alpha-dystroglycan-laminin interaction.

Journal of cell science - 1 Jan 1999

Brown S C, Fassati A, Popplewell L, Page A M, Henry M D, Campbell K P, Dickson G

Abstract excerpt

alpha-dystroglycan is a glycoprotein expressed on the surface of skeletal muscle fibres and other cell types. In muscle, alpha-dystroglycan provides a link between the myofibre cytoskeleton through its indirect binding to dystrophin, and the basal lamina through its binding to laminin-2, a protein of the extracellular matrix. The disruption of this linkage between the myofibre cytoskeleton and the extracellular...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antibodies, Monoclonal
Share to Cell Differentiation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cells, Cultured

Share to Membrane Glycoproteins

Share to Microscopy, Electron

Share to Phenotype

Share to Protein Binding

Source

Identifiers

PMID: 9858474
DOI: 10.1242/jcs.112.2.209

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dystrophic phenotype induced in vitro by antibody blockade of muscle alpha-dystroglycan-laminin interaction.PMID 9858474Read ↗

Cell–matrix interactions in muscle diseaseSemantic proximity Read ↗

Loss of dystrophin and β-sarcoglycan significantly exacerbates the phenotype of laminin α2 chain-deficient animals.Semantic proximity Read ↗

Removal of dystroglycan causes severe muscular dystrophy in zebrafish embryosSemantic proximity Read ↗

Adeno-Associated Virus-Mediated Mini-Agrin Delivery Is Unable to Rescue Disease Phenotype in a Mouse Model of Limb Girdle Muscular Dystrophy Type 2I.Semantic proximity Read ↗

Distinct Roles for Laminin Globular Domains in Laminin α1 Chain Mediated Rescue of Murine Laminin α2 Chain DeficiencySemantic proximity Read ↗

The genetic and molecular basis of muscular dystrophy: roles of cell-matrix linkage in the pathogenesis.Semantic proximity Read ↗

Chimaeric mice deficient in dystroglycans develop muscular dystrophy and have disrupted myoneural synapses.Semantic proximity Read ↗

Laminin-deficient muscular dystrophy: Molecular pathogenesis and structural repair strategies.Semantic proximity Read ↗

Muscular dystrophies, the cytoskeleton and cell adhesion.Semantic proximity Read ↗

Dystroglycan is not required for localization of dystrophin, syntrophin, and neuronal nitric-oxide synthase at the sarcolemma but regulates integrin alpha 7B expression and caveolin-3 distribution.Semantic proximity Read ↗

Laminin-111 Protein Therapy Reduces Muscle Pathology and Improves Viability of a Mouse Model of Merosin-Deficient Congenital Muscular DystrophySemantic proximity Read ↗

Linker molecules between laminins and dystroglycan ameliorate laminin-α2–deficient muscular dystrophy at all disease stagesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.