Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion (2024)

1. Wagner, G. & Wyss, F. Cell surface adhesion receptors. Curr. Opin. Struct. Biol. 4, 841–851 (1994).

   Article CAS Google Scholar

2. Cremer, H. et al. Inactivation of the N-CAM gene in mice results in size reduction of the olfactory bulb and deficits in spatial learning. Nature 367, 455–459 ( 1994).

   Article CAS Google Scholar

3. Cunningham, B.A. et al. Neural cell adhesion molecule: structure, immunoglobulin-like domains, cell surface modulation, and alternative RNA splicing. Science 236, 799–806 ( 1987).

   Article CAS Google Scholar

4. Noble, M. et al. Glial cells express N-CAM/D2-CAM-like polypeptides in vitro. Nature 316, 725–728 (1985).

   Article CAS Google Scholar

5. Edelman, G.M. & Crossin, K.L. Cell adhesion molecules: implication for a molecular histology. Annu. Rev. Biochem. 60, 155–190 (1991).

   Article CAS Google Scholar

6. Moran, N. & Bock, E. Characterization of the kinetics of neural cell adhesion molecule hom*ophilic binding. FEBS Lett. 242, 121–124 (1988).

   Article CAS Google Scholar

   See Also

   Japanese mother and child stabbed in China in front of school bus | CNNThe ubiquitous neural cell adhesion molecule (N-CAM)N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signallingAnti-CD56 (NCAM) Antibodies | Invitrogen

7. Ranheim, T.S., Edelman, G.M. & Cunningham, B.A. hom*ophilic binding mediated by the neural cell adhesion molecule involves multiple immunoglobulin domains. Proc. Natl. Acad. Sci. USA 93, 4071–4075 (1996).

   Article CAS Google Scholar

8. Rao, Y., Wu, X.-F., Gariepy, J., Rutishauser, U. & Siu, C.-H. Identification of a peptide sequence involved in hom*ophilic binding in the neural cell adhesion molecule NCAM. J. Cell Biol. 118, 937–949 (1992).

   Article CAS Google Scholar

9. Rao, Y., Wu, X.-F., Yip, P., Gariepy, J. & Siu, C.-H. Structural characterization of a hom*ophilic binding site in the neural cell adhesion molecule. J. Biol. Chem. 268, 20630–20638 (1993).

   CAS PubMed Google Scholar

10. Rao, Y., Zhao, X. & Siu, C.-H. Mechanism of hom*ophilic binding mediated by the neural cell adhesion molecule NCAM. J. Mol. Biol. 269, 27540–27548 (1994).

    CAS Google Scholar

11. Sandig, M., Rao, Y. & Siu, C.-H. The hom*ophilic binding site of the neural cell adhesion molecule NCAM is directly involved in promoting neurite outgrowth from cultured neural retinal cells. J. Biol. Chem. 269, 14841– 14848 (1994).

    CAS PubMed Google Scholar

12. Kiselyov, V.K. et al. The first immunoglobulin-like neural cell adhesion molecule (NCAM) domain is involved in double-reciprocal interaction with the second immunoglobulin-like NCAM domain and in heparin binding. J. Biol. Chem. 272, 10125–10134 ( 1997).

    Article CAS Google Scholar

13. Becker, J.W., Erickson, H.P., Hoffman, S., Cunningham, B.A. & Edelman, G.M. Topology of cell adhesion molecules. Proc. Natl. Acad. Sci. USA 86, 1088 – 1092 (1989).

    Article CAS Google Scholar

14. Frei, T., von Bohlen und Halbach, F., Wille, W. & Schachner, M. Different extracellular domains of the neural cell adhesion molecule (NCAM) are involved in different functions. J. Cell Biol. 118, 177–194 (1992).

    See Also

    Inactivation of the N-CAM gene in mice results in size reduction of the olfactory bulb and deficits in spatial learning

    Article CAS Google Scholar

15. Harpaz, Y. & Chothia, C. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 238, 528–539 ( 1994).

    Article CAS Google Scholar

16. Hoffman, S. & Edelman, G.M. Kinetics of hom*ophilic binding by embryonic and adult forms of the neural cell adhesion molecule. Proc. Natl. Acad. Sci. USA 80, 5762– 5766 (1983).

    Article CAS Google Scholar

17. Baldwin, T.J., Fazli, M.S., Doherty, P. & Walsh, F.S. Elucidation of molecular actions of NCAM and structurally related adhesion molecules. J. Cell Biochem. 61, 501–513 (1994).

    Google Scholar

18. Thomsen, N.K. et al. The three-dimensional structure of the first domain of neural cell adhesion molecule. Nature Struct. Biol. 3, 581–585 (1996).

    Article CAS Google Scholar

19. Chothia, C. & Jones, E.Y. The molecular structure of cell adhesion molecules. Annu. Rev. Biochem. 66, 823–862 (1997).

    Article CAS Google Scholar

20. Bodenhausen, G. & Ruben, D.J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69, 185–189 ( 1980).

    Article CAS Google Scholar

21. Meissner, A., Schulte-Herbrüggen, T., Briand, J. & Sørensen, O.W. Double spin-state-selective coherence transfer. Application for two-dimensional selection of multiplet components with long transverse relaxation times. Molecular Physics 95, 1137–1142 (1998).

    CAS Google Scholar

22. Brünger, A.T. X-PLOR version 3.1: A system for X-ray crystallography and NMR (Yale University, New Haven Connecticut; 1992).

    Google Scholar

23. Braunsweiler, L. & Ernst, R.R. Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53, 521–528 (1983).

    Google Scholar

24. Kumar, A., Wagner, G., Ernst, R.R. & Wüthrich, K. Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation. J. Am. Chem. Soc. 103, 3654 – 3658 (1981).

    Article CAS Google Scholar

25. Piantini, U., Sørensen, O.W. & Ernst, R.R. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104, 6800– 6801 (1982).

    Article CAS Google Scholar

26. Zhang, O., Kay, L.E., Olivier, J.P. & Forman-Kay, J.D. Backbone ¹H and ¹⁵N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR. 4, 845–858 (1994).

    Article CAS Google Scholar

27. Kjær, M., Andersen, M.K. & Poulsen, F.M. Automated and semiautomated analysis of hom*o- and heteronuclear multidimensional nuclear magnetic resonance spectra of proteins: the program Pronto. Methods Enzymol. 239, 288–307 (1994).

    Article Google Scholar

28. Nicholls, A. GRASP: graphical representation and analysis of surface properties. (Columbia University Press, New York, NY; 1993).

    Google Scholar

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