메뉴 건너뛰기




Volumn 43, Issue 32, 2004, Pages 10364-10369

Backbone dynamics of the first, second, and third immunoglobulin modules of the neural cell adhesion molecule (NCAM)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

EID: 4043126001     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0495679     Document Type: Article
Times cited : (6)

References (32)
  • 1
  • 2
    • 0037312111 scopus 로고    scopus 로고
    • The role of phosphatidylinositol 3-kinase in neural cell adhesion molecule-mediated neuronal differentiation and survival
    • Ditlevsen, D. K., Kohler, L. B., Pedersen, M. V., Risell, M., Kolkova, K., Meyer, M., Berezin, V., and Bock, E. (2003) The role of phosphatidylinositol 3-kinase in neural cell adhesion molecule-mediated neuronal differentiation and survival, J. Neurochem. 84, 546-556.
    • (2003) J. Neurochem. , vol.84 , pp. 546-556
    • Ditlevsen, D.K.1    Kohler, L.B.2    Pedersen, M.V.3    Risell, M.4    Kolkova, K.5    Meyer, M.6    Berezin, V.7    Bock, E.8
  • 3
    • 0027185021 scopus 로고
    • Structural characterization of a homophilic binding site in the neural cell adhesion molecule
    • Rao, Y., Wu, X. F., Yip, P., Gariepy, J., and Siu, C. H. (1993) Structural characterization of a homophilic binding site in the neural cell adhesion molecule, J. Biol. Chem. 268, 20630-20638.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20630-20638
    • Rao, Y.1    Wu, X.F.2    Yip, P.3    Gariepy, J.4    Siu, C.H.5
  • 4
    • 0028036803 scopus 로고
    • Mechanisms of homophilic binding mediated by the neural cell adhesion molecule NCAM
    • Rao, Y., Zhao, X., and Siu, C. H. (1994) Mechanisms of homophilic binding mediated by the neural cell adhesion molecule NCAM, J. Biol. Chem. 269, 27540-27548.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27540-27548
    • Rao, Y.1    Zhao, X.2    Siu, C.H.3
  • 5
    • 0028236467 scopus 로고
    • The homophilic binding site of the neural cell adhesion molecule NCAM is directly involved in promoting neurite outgrowth from cultured neural retinal cells
    • Sandig, M., Rao, Y., and Siu, C. H. (1994) The homophilic 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) J. Biol. Chem. , vol.269 , pp. 14841-14848
    • Sandig, M.1    Rao, Y.2    Siu, C.H.3
  • 6
    • 0030338657 scopus 로고    scopus 로고
    • Integrity of the homophilic binding site is required for the preferential localization of NCAM in intercellular contacts
    • Sandig, M., Rao, Y., Kalnins, V. I., and Siu, C. H. (1996) Integrity of the homophilic binding site is required for the preferential localization of NCAM in intercellular contacts, Biochem. Cell Biol. 74, 373-381.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 373-381
    • Sandig, M.1    Rao, Y.2    Kalnins, V.I.3    Siu, C.H.4
  • 9
    • 0035800660 scopus 로고    scopus 로고
    • Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM: Can solution studies define the mechanism of homophilic binding?
    • Atkins, A. R., Chung, J., Deechongkit, S., Little, E. B., Edelman, G. M., Wright, P. E., Cunningham, B. A., and Dyson, H. J. (2001) Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM: Can solution studies define the mechanism of homophilic binding? J. Mol. Biol. 311, 161-172.
    • (2001) J. Mol. Biol. , vol.311 , pp. 161-172
    • Atkins, A.R.1    Chung, J.2    Deechongkit, S.3    Little, E.B.4    Edelman, G.M.5    Wright, P.E.6    Cunningham, B.A.7    Dyson, H.J.8
  • 12
    • 0033819054 scopus 로고    scopus 로고
    • Protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei
    • Ishima, R. and Torchia, D. A. (2000) Protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei, Nat. Struct. Biol. 7, 740-743.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 740-743
    • Ishima, R.1    Torchia, D.A.2
  • 13
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from NMR spectroscopy
    • Wand, A. J. (2001) Dynamic activation of protein function: A view emerging from NMR spectroscopy, Nat. Struct. Biol. 8,926-931.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 15
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6,277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 16
    • 0028673711 scopus 로고
    • Automated and semiautomated analysis of homo- and heteronuclear multi-dimensional nuclear magnetic resonance spectra of proteins; the program Pronto
    • Kjaer, M., Andersen, M. K., and Poulsen, F. M. (1994) Automated and semiautomated analysis of homo- and heteronuclear multi-dimensional nuclear magnetic resonance spectra of proteins; the program Pronto, Methods Enzymol. 239, 288-307.
    • (1994) Methods Enzymol. , vol.239 , pp. 288-307
    • Kjaer, M.1    Andersen, M.K.2    Poulsen, F.M.3
  • 17
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari and Szabo (1982) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity, J. Am. Chem. Soc. 104, 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari1    Szabo2
  • 18
    • 0028541223 scopus 로고
    • A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization
    • Schurr, J. M., Babcock, H. P. and Fujimoto, B. S. (1994) A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization, J. Magn. Reson., Ser. B 105, 211-224.
    • (1994) J. Magn. Reson., Ser. B , vol.105 , pp. 211-224
    • Schurr, J.M.1    Babcock, H.P.2    Fujimoto, B.S.3
  • 20
    • 0035072684 scopus 로고    scopus 로고
    • Anisotropic rotational diffusion in model-free analysis for a ternary DHFR complex
    • Osborne, M. J., and Wright, P. E. (2001) Anisotropic rotational diffusion in model-free analysis for a ternary DHFR complex, J. Biomol. NMR 19, 209-230.
    • (2001) J. Biomol. NMR , vol.19 , pp. 209-230
    • Osborne, M.J.1    Wright, P.E.2
  • 21
    • 0034328380 scopus 로고    scopus 로고
    • HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
    • Gacia de la Torre, J., Huertas, M. L., and Carrasco, B. (2000) HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations, J. Magn. Reson. 147, 138-146.
    • (2000) J. Magn. Reson. , vol.147 , pp. 138-146
    • Gacia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 22
    • 0034048847 scopus 로고    scopus 로고
    • Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data
    • Dosset, P., Hus, J. C., Blackledge, M., and Marion, D. (2000) Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data, J. Biomol. NMR 16, 23-28.
    • (2000) J. Biomol. NMR , vol.16 , pp. 23-28
    • Dosset, P.1    Hus, J.C.2    Blackledge, M.3    Marion, D.4
  • 24
    • 0001745136 scopus 로고    scopus 로고
    • (Krishna, N. R., and Berliner, L. J., Eds.), Kluwer Academic, New York
    • Engelke, J., and Rüterjans, H. (1999) in Biological Magnetic Resonance (Krishna, N. R., and Berliner, L. J., Eds.) pp 357-418, Kluwer Academic, New York.
    • (1999) Biological Magnetic Resonance , pp. 357-418
    • Engelke, J.1    Rüterjans, H.2
  • 25
    • 0031984752 scopus 로고    scopus 로고
    • Pervasive conformational fluctuations on micro-second time scales in a fibronectin type III domain
    • Akke, M., Liu, J., Cavanagh, J., Erickson, H. P., and Palmer, A. G., III (1998) Pervasive conformational fluctuations on micro-second time scales in a fibronectin type III domain, Nat. Struct. Biol. 5, 55-59.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 55-59
    • Akke, M.1    Liu, J.2    Cavanagh, J.3    Erickson, H.P.4    Palmer III, A.G.5
  • 26
    • 0030051783 scopus 로고    scopus 로고
    • The (Greek) key to structures of neural adhesion molecules
    • Vaughn, D. E., and Bjorkman, P. J. (1996) The (Greek) key to structures of neural adhesion molecules, Neuron 16, 261-273.
    • (1996) Neuron , vol.16 , pp. 261-273
    • Vaughn, D.E.1    Bjorkman, P.J.2
  • 27
    • 0026670583 scopus 로고
    • Identification of a peptide sequence involved in homophilic binding in the neural cell adhesion molecule NCAM
    • Rao, Y., Wu, X. F., Gariepy, J., Rutishauser, U., and Siu, C. H. (1992) Identification of a peptide sequence involved in homophilic binding in the neural cell adhesion molecule NCAM, J. Cell Biol. 118, 937-949.
    • (1992) J. Cell Biol. , vol.118 , pp. 937-949
    • Rao, Y.1    Wu, X.F.2    Gariepy, J.3    Rutishauser, U.4    Siu, C.H.5
  • 28
    • 0029867737 scopus 로고    scopus 로고
    • Homophilic adhesion mediated by the neural cell adhesion molecule involves multiple immumoglobulin domains
    • Ranheim, T. S., Edelman, G. M., and Cunningham, B. A. (1996) Homophilic adhesion mediated by the neural cell adhesion molecule involves multiple immumoglobulin domains, Proc. Natl. Acad. Sci. U.S.A. 93, 4071-4075.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 4071-4075
    • Ranheim, T.S.1    Edelman, G.M.2    Cunningham, B.A.3
  • 29
    • 0030899695 scopus 로고    scopus 로고
    • The first Ig-like NCAM domain is involved in both double reciprocal interaction with the second Ig-like NCAM domain and in heparin binding
    • Kiselyov, V. V., Berezin, V., Maar, T. E., Soroka, V., Edvardsen, K., Schousboe, A., and Bock, E. (1997) The first Ig-like NCAM domain is involved in both double reciprocal interaction with the second Ig-like NCAM domain and in heparin binding, J. Biol. Chem. 272, 10125-10134.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10125-10134
    • Kiselyov, V.V.1    Berezin, V.2    Maar, T.E.3    Soroka, V.4    Edvardsen, K.5    Schousboe, A.6    Bock, E.7
  • 30
    • 0032957672 scopus 로고    scopus 로고
    • Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM
    • Atkins, A. R., Osborne, M. J., Lashuel, H. A., Edelman, G. M., Wright, P. E., Cunningham, B. A., and Dyson, H. J. (1999) Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM, FEBS Lett. 451, 162-168.
    • (1999) FEBS Lett. , vol.451 , pp. 162-168
    • Atkins, A.R.1    Osborne, M.J.2    Lashuel, H.A.3    Edelman, G.M.4    Wright, P.E.5    Cunningham, B.A.6    Dyson, H.J.7
  • 31
    • 0033566242 scopus 로고    scopus 로고
    • Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F
    • Feher, V. A, and Cavanagh, J. (1999) Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F, Nature 400, 289-293.
    • (1999) Nature , vol.400 , pp. 289-293
    • Feher, V.A.1    Cavanagh, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.