ArticleProceedings of the National Academy of Sciences of the United States of America2013
Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 40 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
40 citing papers in PubMed, 75 citations in OpenAlex.
- Bromodomain dimers: A case study of BRD4 and family-wide AlphaFold predictions.Structural dynamics (Melville, N.Y.) · 2026Article
- Paths to stability - actin regulation of adherens junction mechanics.Journal of cell science · 2025Review
- Observation of E-cadherin adherens junction dynamics with metal-induced energy transfer imaging and spectroscopy.Communications biology · 2024Article
- Study on the Interactions Between Cisplatin and Cadherin by Fluorescence Spectrometry and Atomic Force Microscopy.Journal of fluorescence · 2024Article
- Mesenchymal stromal cells with chimaeric antigen receptors for enhanced immunosuppression.Nature biomedical engineering · 2024Article
- Computational and experimental approaches to quantify protein binding interactions under confinement.Biophysical journal · 2024Review
- Strengthening E-cadherin adhesion via antibody-mediated binding stabilization.Structure (London, England : 1993) · 2024Article
- Mechanics of cell-cell junctions.Biophysical journal · 2023Article
- Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023Review
- Nucleation of cadherin clusters on cell-cell interfaces.Scientific reports · 2022Article
- Molecular mechanism for strengthening E-cadherin adhesion using a monoclonal antibody.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Multiple dimeric structures and strand-swap dimerization of E-cadherin in solution visualized by high-speed atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cadherins can dimerize via asymmetric interactions.FEBS letters · 2022Article
- Observation of Arginine Side-Chain Motions Coupled to the Global Conformational Exchange Process in Deubiquitinase A.ACS omega · 2022Article
- Computational model of E-cadherin clustering under force.Biophysical journal · 2021Article
- Inside-out regulation of E-cadherin conformation and adhesion.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Conformational Dynamics of Deubiquitinase A and Functional Implications.Biochemistry · 2021Article
- Homodimerization of a glycoside hydrolase family GH1 β-glucosidase suggests distinct activity of enzyme different states.Protein science : a publication of the Protein Society · 2020Article
- Interplay of Disorder and Sequence Specificity in the Formation of Stable Dynein-Dynactin Complexes.Biophysical journal · 2020Article
- Molecular Recognition between Cadherins Studied by a Coarse-Grained Model Interacting with a Coevolutionary Potential.The journal of physical chemistry. B · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Epithelial cadherin (E-cadherin), a member of the classical cadherin family, mediates calcium-dependent homophilic cell-cell adhesion. Crystal structures of classical cadherins reveal an adhesive dimer interface featuring reciprocal exchange of N-terminal β-strands between two protomers. Previous work has identified a putative intermediate (called the "X-dimer") in the dimerization pathway of wild-type E-cadherin EC1-EC2 domains, based on crystal structures of mutants not capable of strand swapping and on deceleration of binding kinetics by mutations at the X-dimer interface. In the present work, NMR relaxation dispersion spectroscopy is used to directly observe and characterize intermediate states without the need to disrupt the strand-swapped binding interface by mutagenesis. The results indicate that E-cadherin forms strand-swapped dimers predominantly by a mechanism in which formation of a weak and short-lived X-dimer-like state precedes the conformational changes required for formation of the mature strand-swapped dimeric structure. Disruption of this intermediate state through mutation reduces both association and dissociation rates by factors of ~10(4), while minimally perturbing affinity. The X-dimer interface lowers the energy barrier associated with strand swapping and enables E-cadherins to form strand-swapped dimers at a rate consistent with residence times in adherens junctions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.