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

A mechanism of gap junction docking revealed by functional rescue of a human-disease-linked connexin mutant.

Journal of cell science - 15 Jul 2013

Gong Xiang-Qun, Nakagawa So, Tsukihara Tomitake, Bai Donglin

Abstract excerpt

Gap junctions are unique intercellular channels formed by the proper docking of two hemichannels from adjacent cells. Each hemichannel is a hexamer of connexins (Cxs) - the gap junction subunits, which are encoded by 21 homologous genes in the human genome. The docking of two hemichannels to form a functional gap junction channel is only possible between compatible Cxs, but the underlying molecular mechanism is...

Read the complete abstract on PubMed

Topics

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

Share to Channelopathies
Share to Connexin 26
Share to Connexins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gap Junction beta-1 Protein

Share to Gap Junctions

Share to Genetic Engineering

Share to Ion Channels

Share to Models, Chemical

Source

Identifiers

PMID: 23687377
DOI: 10.1242/jcs.123430

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

A mechanism of gap junction docking revealed by functional rescue of a human-disease-linked connexin mutant.PMID 23687377Read ↗

Quantifying Electrostatic Control of Docking and Binding Energetics in Functional Cx36 Gap JunctionsSemantic proximity Read ↗

Crucial motifs and residues in the extracellular loops influence the formation and specificity of connexin docking.Semantic proximity Read ↗

Structural analysis of key gap junction domains--Lessons from genome data and disease-linked mutants.Semantic proximity Read ↗

Three-dimensional structure of a human connexin26 gap junction channel reveals a plug in the vestibule.Semantic proximity Read ↗

Engineered Cx40 variants increased docking and function of heterotypic Cx40/Cx43 gap junction channels.Semantic proximity Read ↗

Analysis of trafficking, stability and function of human connexin 26 gap junction channels with deafness-causing mutations in the fourth transmembrane helix.Semantic proximity Read ↗

Computer simulations reveal pathogenicity and inheritance modes of hearing loss-causing germinal variantsSemantic proximity Read ↗

Altered formation of hemichannels and gap junction channels caused by C-terminal connexin-32 mutations.Semantic proximity Read ↗

A fully atomistic model of the Cx32 connexon.Semantic proximity Read ↗

Asymmetric configurations and N-terminal rearrangements in connexin26 gap junction channels.Semantic proximity Read ↗

Gap junction channel structure in the early 21st century: facts and fantasies.Semantic proximity Read ↗

The structural context of disease-causing mutations in gap junctions.Semantic proximity Read ↗

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