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

Characterizing the initial encounter complex in cadherin adhesion.

Structure (London, England : 1993) - 12 Aug 2009

Sivasankar Sanjeevi, Zhang Yunxiang, Nelson W James, Chu Steven

Abstract excerpt

Cadherins are Ca(2+)-dependent cell-cell adhesion proteins with an extracellular region of five domains (EC1 to EC5). Adhesion is mediated by "strand swapping" of a conserved tryptophan residue in position 2 between EC1 domains of opposing cadherins, but the formation of this structure is not wel...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Cadherins
Share to Calcium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence Resonance Energy Transfer

Share to Microscopy, Atomic Force

Share to Protein Conformation

Share to Protein Multimerization

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 19646884
DOI: 10.1016/j.str.2009.06.012
PMCID: PMC4113602

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-19646884-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterizing the initial encounter complex in cadherin adhesion.PMID 19646884Read ↗

Calcium-induced strain in the monomer promotes dimerization in neural cadherin.Semantic proximity Read ↗

Two-step adhesive binding by classical cadherins.Semantic proximity Read ↗

Calcium site mutations in cadherin: impact on adhesion and evidence of cooperativity.Semantic proximity Read ↗

Characterizing interactions in E-cadherin assemblages.Semantic proximity Read ↗

Discrete interactions in cell adhesion measured by single-molecule force spectroscopy.Semantic proximity Read ↗

Arrhythmogenic cardiomyopathy-related cadherin variants affect desmosomal binding kinetics.Semantic proximity Read ↗

An analytical model for determining two-dimensional receptor-ligand kinetics.Semantic proximity Read ↗

Identification and characterization of the X-dimer of human P-cadherin: implications for homophilic cell adhesion.Semantic proximity Read ↗

Cadherin conformations associated with dimerization and adhesion.Semantic proximity Read ↗

Structural and energetic determinants of adhesive binding specificity in type I cadherins.Semantic proximity Read ↗

Functional analysis of the structural basis of homophilic cadherin adhesion.Semantic proximity Read ↗

Transmission of allostery through the lectin domain in selectin-mediated cell adhesion.Semantic proximity Read ↗

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