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

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

Trends in biochemical sciences - 1 Apr 1995

Blake D J, Tinsley J M, Davies K E, Knight A E, Winder S J, Kendrick-Jones J

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

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

Share to Cytoskeletal Proteins
Share to Dystrophin
Share to Membrane Proteins
Share to Muscular Dystrophies

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

Share to Protein Binding

Share to Protein Conformation

Share to Protein Structure, Tertiary

Share to Utrophin

Source

Identifiers

PMID: 7770909
DOI: 10.1016/s0968-0004(00)88986-0

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

Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins: potentials for protein-protein interactions.PMID 7770909Read ↗

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

Location of disorder in coiled coil proteins is influenced by its biological role and subcellular localization: a GO-based study on human proteome.Semantic proximity Read ↗

Distribution of disease-causing germline mutations in coiled-coils implies an important role of their N-terminal region.Semantic proximity Read ↗

The dystrophin-associated protein complex.Semantic proximity Read ↗

Distribution of disease-causing germline mutations in coiled-coils suggests essential role of their N-terminal regionSemantic proximity Read ↗

Dystrophins and dystrobrevins.Semantic proximity Read ↗

Flexibility in the N-terminal actin-binding domain: clues from in silico mutations and molecular dynamics.Semantic proximity Read ↗

Structure and misfolding of the flexible tripartite coiled coil domain of glaucoma-associated myocilinSemantic proximity Read ↗

The Structure of the N-Terminal Domain of the Fragile X Mental Retardation Protein: A Platform for Protein-Protein InteractionSemantic proximity Read ↗

Protein-protein interactions in the membrane: sequence, structural, and biological motifs.Semantic proximity Read ↗

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

Structural model of the TRPP2/PKD1 C-terminal coiled-coil complex produced by a combined computational and experimental approach.Semantic proximity Read ↗

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