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

Localization and functional analysis of the LARGE family of glycosyltransferases: significance for muscular dystrophy.

Human molecular genetics - 1 Mar 2005

Brockington Martin, Torelli Silvia, Prandini Paola, Boito Chiara, Dolatshad Nazanin F, Longman Cheryl, Brown Susan C, Muntoni Francesco

Abstract excerpt

The dystroglycanopathies are a novel group of human muscular dystrophies due to mutations in known or putative glycosyltransferase enzymes. They share the common pathological feature of a hypoglycosylated form of alpha-dystroglycan, diminishing its ability to bind extracellular matrix ligands. The LARGE glycosyltransferase is mutated in both the myodystrophy mouse and congenital muscular dystrophy type 1D...

Read the complete abstract on PubMed

Topics

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

Share to Cricetinae
Share to Dystroglycans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosyltransferases

Share to Golgi Apparatus

Share to Laminin

Share to Multigene Family

Share to Muscular Dystrophies

Share to Myoblasts

Source

Identifiers

PMID: 15661757
DOI: 10.1093/hmg/ddi062

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Localization and functional analysis of the LARGE family of glycosyltransferases: significance for muscular dystrophy.PMID 15661757Read ↗

Mutation of Large, which encodes a putative glycosyltransferase, in an animal model of muscular dystrophy.Semantic proximity Read ↗

Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan.Semantic proximity Read ↗

Muscular dystrophies due to glycosylation defects.Semantic proximity Read ↗

Investigating the functions of LARGE: lessons from mutant mice.Semantic proximity Read ↗

Muscular dystrophies due to glycosylation defectsSemantic proximity Read ↗

Mutant glycosyltransferase and altered glycosylation of alpha-dystroglycan in the myodystrophy mouse.Semantic proximity Read ↗

Rewiring enervated: thinking LARGEr than myodystrophy.Semantic proximity Read ↗

The glucuronyltransferase B4GAT1 is required for initiation of LARGE-mediated α-dystroglycan functional glycosylation.Semantic proximity Read ↗

Muscle-specific expression of LARGE restores neuromuscular transmission deficits in dystrophic LARGEmyd miceSemantic proximity Read ↗

Protein glycosylation in disease: new insights into the congenital muscular dystrophies.Semantic proximity Read ↗

A rapid PCR method for genotyping the Large(myd) mouse, a model of glycosylation-deficient congenital muscular dystrophy.Semantic proximity Read ↗

Transgenic Overexpression of LARGE Induces α-Dystroglycan Hyperglycosylation in Skeletal and Cardiac MuscleSemantic proximity Read ↗

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