The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Structure and Biochemistry of Cadherins and Catenins
Open accessAbstract
Classical cadherins mediate specific adhesion at intercellular adherens junctions. Interactions between cadherin ectodomains from apposed cells mediate cell-cell contact, whereas the intracellular region functionally links cadherins to the underlying cytoskeleton. Structural, biophysical, and biochemical studies have provided important insights into the mechanism and specificity of cell-cell adhesion by classical cadherins and their interplay with the cytoskeleton. Adhesive binding arises through exchange of beta strands between the first extracellular cadherin domains (EC1) of partner cadherins from adjacent cells. This "strand-swap" binding mode is common to classical and desmosomal cadherins, but sequence alignments suggest that other cadherins will bind differently. The intracellular region of classical cadherins binds to p120 and beta-catenin, and beta-catenin binds to the F-actin binding protein alpha-catenin. Rather than stably bridging beta-catenin to actin, it appears that alpha-catenin actively regulates the actin cytoskeleton at cadherin-based cell-cell contacts.
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Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
The interplay between structure and function in intrinsically unstructured proteins
Tompa, P. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.072 · Cited by 717
3D domain swapping: As domains continue to swap
Liu, Y., & Eisenberg, D. (2002) · Protein Science · doi:10.1110/ps.0201402 · Cited by 684
Structural basis of calcium-induced E-cadherin rigidification and dimerization
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Regulation of motor neuron pool sorting by differential expression of type II cadherins
Price, S. R., De Marco Garcia, N. V., Ranscht, B., & Jessell, T. M. (2002) · Cell · doi:10.1016/s0092-8674(02)00695-5 · Cited by 304
Steinberg, M. S. (1975) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(75)80091-9 · Cited by 97
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Seong, E., Yuan, L., & Arikkath, J. (2015) · Cell Adhesion & Migration · doi:10.4161/19336918.2014.994919 · Cited by 105
New genomic data and analyses challenge the traditional vision of animal epithelium evolution
Belahbib, H., Renard, E., Santini, S., Jourda, C., Claverie, J.-M., Borchiellini, C., & Le Bivic, A. (2018) · BMC Genomics · doi:10.1186/s12864-018-4715-9 · Cited by 71
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Structural basis of coactivation of liver receptor homolog-1 by β-catenin
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Metadata
- Authors
- Shapiro, L., & Weis, W. I.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2009-08-19
- Volume
- 1
- Issue
- 3
- Pages
- a003053-a003053
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2097256807
- Cited by
- 462
- References
- 7
- Type
- posted content
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
