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Article

ZZ domain is essentially required for the physiological binding of dystrophin and utrophin to beta-dystroglycan.

Human molecular genetics - 1 Apr 2004

Ishikawa-Sakurai Michiko, Yoshida Mikiharu, Imamura Michihiro, Davies Kay E, Ozawa Eijiro

Abstract excerpt

An intracellular protein, dystrophin, plays an important role in keeping muscle fibers intact by binding at its N-terminal end to the subsarcolemmal cytoskeletal actin network and via its C-terminal end to the transmembraneous protein beta-dystroglycan. Duchenne muscular dystrophy is caused by the loss of dystrophin, which can result from the loss of this binding. The N-terminal part of the latter binding site of...

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

Share to Dystroglycans

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Share to Mutation, Missense

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Source

Identifiers

PMID: 14962982
DOI: 10.1093/hmg/ddh087

Genes

DMD

Variants

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

ZZ domain is essentially required for the physiological binding of dystrophin and utrophin to beta-dystroglycan.PMID 14962982Read ↗

The ZZ domain of dystrophin in DMD: making sense of missense mutations.Semantic proximity Read ↗

Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins: potentials for protein-protein interactions.Semantic proximity Read ↗

The conserved WW-domain binding sites in Dystroglycan C-terminus are essential but partially redundant for Dystroglycan function.Semantic proximity Read ↗

Structure-function relationships in dystrophin and utrophin.Semantic proximity Read ↗

Dystrophin and utrophin: genetic analyses of their role in skeletal muscle.Semantic proximity Read ↗

Loss of sarcospan exacerbates pathology in mdx mice, but does not affect utrophin amelioration of disease.Semantic proximity Read ↗

Loss of a single amino acid from dystrophin resulting in Duchenne muscular dystrophy with retention of dystrophin protein.Semantic proximity Read ↗

Increasing complexity of the dystrophin-associated protein complex.Semantic proximity Read ↗

Is the carboxyl-terminus of dystrophin required for membrane association? A novel, severe case of Duchenne muscular dystrophy.Semantic proximity Read ↗

Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.Semantic proximity Read ↗

The utrophin and dystrophin genes share similarities in genomic structureSemantic proximity Read ↗

Is the maintainance of the C-terminus domain of dystrophin enough to ensure a milder Becker muscular dystrophy phenotype?Semantic proximity Read ↗

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