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

Calcium site mutations in cadherin: impact on adhesion and evidence of cooperativity.

Biochemistry - 6 Jun 2006

Prakasam A, Chien Y-H, Maruthamuthu V, Leckband D E

Abstract excerpt

This work describes quantitative force and bead aggregation measurements of the adhesion and binding mechanisms of canine E-cadherin mutants W2A, D134A, D103A, D216A, D325A, and D436A. The W2A mutation affects the formation of the N-terminal strand dimer, and the remaining mutations target calciu...

Read the complete abstract on PubMed

Topics

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

Share to Cadherins
Share to Calcium
Share to Cell Adhesion

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipid Bilayers

Share to Microspheres

Share to Staphylococcal Protein A

Share to Tryptophan

Source

Identifiers

PMID: 16734428
DOI: 10.1021/bi060213m

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Prepared record publication-16734428-2026-09-05.1. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Calcium site mutations in cadherin: impact on adhesion and evidence of cooperativity.PMID 16734428Read ↗

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

Sequential binding of calcium leads to dimerization in neural cadherin.Semantic proximity Read ↗

Mutations targeting intermodular interfaces or calcium binding destabilize the thrombospondin-2 signature domain.Semantic proximity Read ↗

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

T-cadherin structures reveal a novel adhesive binding mechanism.Semantic proximity Read ↗

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

Characterizing the initial encounter complex in cadherin adhesion.Semantic proximity Read ↗

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

Point mutations alter the mechanical stability of immunoglobulin modules.Semantic proximity Read ↗

Homophilic and Heterophilic Interactions of Type II Cadherins Identify Specificity Groups Underlying Cell-Adhesive Behavior.Semantic proximity Read ↗

Heterophilic recognition between E-cadherin and N-cadherin relies on same canonical binding interface as required for E-cadherin homodimerization.Semantic proximity Read ↗

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

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