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Volumn 71, Issue 6, 1998, Pages 2615-2625

Structural analysis of the sixth immunoglobulin-like domain of mouse neural cell adhesion molecule L1 and its interactions with αv/β3, αIIb/β3, and α5/β1 integrins

Author keywords

Cell adhesion molecule L1; Immunoglobulin like domain; Integrins; RGD sites

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; GUANIDINE; IMMUNOGLOBULIN; INTEGRIN; LIGAND; NERVE CELL ADHESION MOLECULE; RECOMBINANT PROTEIN; RNA;

EID: 0031772345     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1998.71062615.x     Document Type: Article
Times cited : (33)

References (57)
  • 1
    • 0029957549 scopus 로고    scopus 로고
    • Outline structure of the human L1 cell adhesion molecule and the sites where mutations cause neurological disorders
    • Bateman A., Jouet M., MacFarlane J., Du J. S., Kenwrick S., and Cothia C. (1996) Outline structure of the human L1 cell adhesion molecule and the sites where mutations cause neurological disorders. EMBO J. 15, 6050-6059.
    • (1996) EMBO J. , vol.15 , pp. 6050-6059
    • Bateman, A.1    Jouet, M.2    MacFarlane, J.3    Du, J.S.4    Kenwrick, S.5    Cothia, C.6
  • 3
    • 0024358833 scopus 로고
    • Drosophila neuroglian: A member of the immunoglobulin superfamily with extensive homology to the vertebrate neural adhesion molecule L1
    • Bieber A. J., Snow P. M., Hortsch M., Patel N. H., Jacobs J. R., Tranquina Z. R., Schilling J., and Goodman C. S. (1989) Drosophila neuroglian: a member of the immunoglobulin superfamily with extensive homology to the vertebrate neural adhesion molecule L1. Cell 59, 447-460.
    • (1989) Cell , vol.59 , pp. 447-460
    • Bieber, A.J.1    Snow, P.M.2    Hortsch, M.3    Patel, N.H.4    Jacobs, J.R.5    Tranquina, Z.R.6    Schilling, J.7    Goodman, C.S.8
  • 4
    • 0022157779 scopus 로고
    • Demonstration of immunochemical identity between the nerve growth factor inducible large external (NILE) glycoprotein and the cell adhesion molecule L1
    • Bock E. C., Richter-Landsberg C., Faissner A., and Schachner M. (1985) Demonstration of immunochemical identity between the nerve growth factor inducible large external (NILE) glycoprotein and the cell adhesion molecule L1. EMBO J. 4, 2765-2768.
    • (1985) EMBO J. , vol.4 , pp. 2765-2768
    • Bock, E.C.1    Richter-Landsberg, C.2    Faissner, A.3    Schachner, M.4
  • 5
    • 0028170046 scopus 로고
    • Specific roles of the αvβ1, αvβ3 and αvβ5 integrins in avian neural crest cell adhesion and migration on vitronectin
    • Delannet M., Martin F., Bossy B., Cheresh D. A., Reichardt L. F., and Douband J. F. (1994) Specific roles of the αvβ1, αvβ3 and αvβ5 integrins in avian neural crest cell adhesion and migration on vitronectin. Development 120, 2687-2702.
    • (1994) Development , vol.120 , pp. 2687-2702
    • Delannet, M.1    Martin, F.2    Bossy, B.3    Cheresh, D.A.4    Reichardt, L.F.5    Douband, J.F.6
  • 6
    • 0345215170 scopus 로고    scopus 로고
    • Utilization of a soluble integrin-alkaline phosphatase chimera to characterize integrin α8β1 receptor interactions with tenascin: Murine α8β1 binds to the RGD site in tenascin-C fragments, but not to the native tenascin-C
    • Denda S., Müller U., Crossin K. L., Erickson H. P., and Reichardt L. F. (1998) Utilization of a soluble integrin-alkaline phosphatase chimera to characterize integrin α8β1 receptor interactions with tenascin: murine α8β1 binds to the RGD site in tenascin-C fragments, but not to the native tenascin-C. Biochemistry 37, 5464-5474.
    • (1998) Biochemistry , vol.37 , pp. 5464-5474
    • Denda, S.1    Müller, U.2    Crossin, K.L.3    Erickson, H.P.4    Reichardt, L.F.5
  • 9
    • 0023920778 scopus 로고
    • 2+: A possible role for unusual binding sites for divalent cations in receptors for proteins containing Arg-Gly-Asp
    • 2+: a possible role for unusual binding sites for divalent cations in receptors for proteins containing Arg-Gly-Asp. J. Cell Sci. 89, 507-513.
    • (1988) J. Cell Sci. , vol.89 , pp. 507-513
    • Edwards, J.1    Hameed, H.2    Campbell, G.3
  • 10
    • 0027439963 scopus 로고
    • The role of cell-cell and cell-matrix interactions in the morphogenesis of the neural crest
    • Erickson C. A. and Perris R. (1993) The role of cell-cell and cell-matrix interactions in the morphogenesis of the neural crest. Dev. Biol. 159, 60-74.
    • (1993) Dev. Biol. , vol.159 , pp. 60-74
    • Erickson, C.A.1    Perris, R.2
  • 11
    • 0023518623 scopus 로고
    • Monoclonal antibody detects microheterogeneity on the murine cell adhesion molecule L1
    • Faissner A. (1987) Monoclonal antibody detects microheterogeneity on the murine cell adhesion molecule L1. Neurosci. Lett. 83, 327-332.
    • (1987) Neurosci. Lett. , vol.83 , pp. 327-332
    • Faissner, A.1
  • 12
    • 0028238347 scopus 로고
    • Evidence for carbohydrate-mediated interactions between the neural cell adhesion molecules NCAM and L1
    • Feizi T. (1994) Evidence for carbohydrate-mediated interactions between the neural cell adhesion molecules NCAM and L1. Trends Biochem. Sci. 19, 233-234.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 233-234
    • Feizi, T.1
  • 13
    • 0028273033 scopus 로고
    • TAG-1 can mediate homophilic binding but neurite outgrowth on TAG-1 requires an L1-like molecule and beta 1 integrins
    • Felsenfeld D. P., Hynes M. A., Skoler K. M., Furley A. J., and Jessell T. M. (1994) TAG-1 can mediate homophilic binding but neurite outgrowth on TAG-1 requires an L1-like molecule and beta 1 integrins. Neuron 12, 675-690.
    • (1994) Neuron , vol.12 , pp. 675-690
    • Felsenfeld, D.P.1    Hynes, M.A.2    Skoler, K.M.3    Furley, A.J.4    Jessell, T.M.5
  • 15
    • 0028227022 scopus 로고
    • The neuronal chondroitin sulfate proteoglycan neurocan binds to the cell adhesion molecules Ng-CAM/L1/NILE and NCAM, and inhibits neuronal adhesion and neurite outgrowth
    • Friedlander D. R., Milev P., Karthikeyan L., Margolis R. K., Margolis R. U., and Grumet M. (1994) The neuronal chondroitin sulfate proteoglycan neurocan binds to the cell adhesion molecules Ng-CAM/L1/NILE and NCAM, and inhibits neuronal adhesion and neurite outgrowth. J. Cell Biol. 125, 669-680.
    • (1994) J. Cell Biol. , vol.125 , pp. 669-680
    • Friedlander, D.R.1    Milev, P.2    Karthikeyan, L.3    Margolis, R.K.4    Margolis, R.U.5    Grumet, M.6
  • 16
    • 0027492207 scopus 로고
    • Functional characterization of chondroitin sulfate proteoglycans of brain: Interactions with neurons and neural cell adhesion molecules
    • Grumet M., Flaccus A., and Margolis R. U. (1993) Functional characterization of chondroitin sulfate proteoglycans of brain: interactions with neurons and neural cell adhesion molecules. J. Cell Biol. 120, 815-824.
    • (1993) J. Cell Biol. , vol.120 , pp. 815-824
    • Grumet, M.1    Flaccus, A.2    Margolis, R.U.3
  • 17
    • 0031022865 scopus 로고    scopus 로고
    • L1/HNK-1 carbohydrate- And β1 integrin-dependent neural cell adhesion to laminin-1
    • Hall H., Carbonetto S., and Schachner M. (1997) L1/HNK-1 carbohydrate-and β1 integrin-dependent neural cell adhesion to laminin-1. J. Neurochem. 68, 544-553.
    • (1997) J. Neurochem. , vol.68 , pp. 544-553
    • Hall, H.1    Carbonetto, S.2    Schachner, M.3
  • 18
    • 0028361540 scopus 로고
    • 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
    • Harpaz Y, and Cothia C. (1994) 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) J. Mol. Biol. , vol.238 , pp. 528-539
    • Harpaz, Y.1    Cothia, C.2
  • 19
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S. N., Hunt H. D., Horton R. M., Pullen J. K., and Pease L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 20
    • 0026800671 scopus 로고
    • X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase at 2.8Å resolution
    • Holden H. M., Ito M., Hartshorne D. J., and Rayment I. (1992) X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase at 2.8Å resolution. J. Mol. Biol. 227, 840-851.
    • (1992) J. Mol. Biol. , vol.227 , pp. 840-851
    • Holden, H.M.1    Ito, M.2    Hartshorne, D.J.3    Rayment, I.4
  • 21
    • 0030273263 scopus 로고    scopus 로고
    • The L1 family of cell adhesion molecules: Old proteins performing new tricks
    • Hortsch M. (1996) The L1 family of cell adhesion molecules: old proteins performing new tricks. Neuron 17, 587-593.
    • (1996) Neuron , vol.17 , pp. 587-593
    • Hortsch, M.1
  • 22
    • 0029066131 scopus 로고
    • Exon 2 of the gene for neural cell adhesion molecule L1 is alternatively spliced in B cells
    • Jouet M., Rosenthal A., and Kenwrick S. (1995) Exon 2 of the gene for neural cell adhesion molecule L1 is alternatively spliced in B cells. Brain Res. Mol. Brain Res. 30, 378-380.
    • (1995) Brain Res. Mol. Brain Res. , vol.30 , pp. 378-380
    • Jouet, M.1    Rosenthal, A.2    Kenwrick, S.3
  • 23
    • 0029061855 scopus 로고
    • Evidence for a cis interaction and cooperative signalling by the heat stable antigen nectadrin (murine CD24) and the cell adhesion molecule L1 in neurons
    • Kadmon G., von Bohlen und Halbach F., Horstkorte R., Eckert M., Altevogt P., and Schachner M. (1995) Evidence for a cis interaction and cooperative signalling by the heat stable antigen nectadrin (murine CD24) and the cell adhesion molecule L1 in neurons. Eur. J. Neurosci. 1, 993-1004.
    • (1995) Eur. J. Neurosci. , vol.1 , pp. 993-1004
    • Kadmon, G.1    Von Bohlen Halbach, F.2    Horstkorte, R.3    Eckert, M.4    Altevogt, P.5    Schachner, M.6
  • 24
    • 0032562663 scopus 로고    scopus 로고
    • Tenascin-C hexabrachion assembly is a two-step process initiated by coiled-coil alpha-helices
    • Kammerer R. A., Schulthess T., Landwehr R., Lustig A., Fischer D., and Engel J. (1998) Tenascin-C hexabrachion assembly is a two-step process initiated by coiled-coil alpha-helices. J. Biol. Chem. 273, 10602-10608.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10602-10608
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3    Lustig, A.4    Fischer, D.5    Engel, J.6
  • 26
    • 0026319551 scopus 로고
    • Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1 (G4)
    • Kuhn L. T., Stoeckli E. T., Condrau M. A., Rathjen F. G., and Sonderegger P. (1991) Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1 (G4). J. Cell Biol. 115, 1113-1126.
    • (1991) J. Cell Biol. , vol.115 , pp. 1113-1126
    • Kuhn, L.T.1    Stoeckli, E.T.2    Condrau, M.A.3    Rathjen, F.G.4    Sonderegger, P.5
  • 27
    • 0029036962 scopus 로고
    • Immunolocalization of the neural cell adhesion molecule L1 in non-proliferating epithelial cells of the male urogenital tract
    • Kujat R., Miragall F., Krause D., Dermietzel R., and Wrobel K. H. (1995) Immunolocalization of the neural cell adhesion molecule L1 in non-proliferating epithelial cells of the male urogenital tract. Histochem. Cell Biol. 103, 311-321.
    • (1995) Histochem. Cell Biol. , vol.103 , pp. 311-321
    • Kujat, R.1    Miragall, F.2    Krause, D.3    Dermietzel, R.4    Wrobel, K.H.5
  • 29
    • 0022891182 scopus 로고
    • The appearance of an L1-like molecule in the chick visual pathway
    • Lemmon V. and McLoon S. (1987) The appearance of an L1-like molecule in the chick visual pathway. J. Neurosci. 6, 2987-2994.
    • (1987) J. Neurosci. , vol.6 , pp. 2987-2994
    • Lemmon, V.1    McLoon, S.2
  • 30
    • 0024675417 scopus 로고
    • L1-mediated axon outgrowth occurs via homophilic binding mechanism
    • Lemmon V., Fair K. L., and Lagenaur C. (1989) L1-mediated axon outgrowth occurs via homophilic binding mechanism. Neuron 2, 1597-1603.
    • (1989) Neuron , vol.2 , pp. 1597-1603
    • Lemmon, V.1    Fair, K.L.2    Lagenaur, C.3
  • 31
    • 0024605014 scopus 로고
    • Differential expression of cell adhesion molecules in variants of the K1735 melanoma cell differing in metastatic capacity
    • Linnemann D., Raz A., and Bock E. (1989) Differential expression of cell adhesion molecules in variants of the K1735 melanoma cell differing in metastatic capacity. Int. J. Cancer 43, 709-712.
    • (1989) Int. J. Cancer , vol.43 , pp. 709-712
    • Linnemann, D.1    Raz, A.2    Bock, E.3
  • 32
    • 0022976359 scopus 로고
    • Immunoelectron microscopic localization of neural cell adhesion molecules (L1, NCAM and MAG) and their shared carbohydrate epitope and myelin basic protein in developing sciatic nerve
    • Martini R. and Schachner M. (1986) Immunoelectron microscopic localization of neural cell adhesion molecules (L1, NCAM and MAG) and their shared carbohydrate epitope and myelin basic protein in developing sciatic nerve. J. Cell Biol. 103, 2439-2448.
    • (1986) J. Cell Biol. , vol.103 , pp. 2439-2448
    • Martini, R.1    Schachner, M.2
  • 33
    • 0025814772 scopus 로고
    • Molecular cloning of cDNA encoding the rat neural cell adhesion molecule L1. Two different isoforms in the cytoplasmic region are produced by differential splicing
    • Miura M., Kobayashi M., Asou H., and Uyemura H. (1991) Molecular cloning of cDNA encoding the rat neural cell adhesion molecule L1. Two different isoforms in the cytoplasmic region are produced by differential splicing. FEBS Lett. 89, 91-95.
    • (1991) FEBS Lett. , vol.89 , pp. 91-95
    • Miura, M.1    Kobayashi, M.2    Asou, H.3    Uyemura, H.4
  • 35
    • 0023805739 scopus 로고
    • Neural cell adhesion molecule L1 as a member of the immunoglobulin superfamily with binding domains similar to fibronectin
    • Moos A. T. R., Scherer H., Teplow D., Fruh K., and Schachner M. (1988) Neural cell adhesion molecule L1 as a member of the immunoglobulin superfamily with binding domains similar to fibronectin. Nature 334, 701-703.
    • (1988) Nature , vol.334 , pp. 701-703
    • Moos, A.T.R.1    Scherer, H.2    Teplow, D.3    Fruh, K.4    Schachner, M.5
  • 36
    • 0025907474 scopus 로고
    • The Cs5 peptide is a second site in the IICS region of fibronectin recognized by integrin α4β1. Inhibition of α4β1 function by RGD peptide homologues
    • Mould A. P., Komorya A., Yamada K. M., and Humphries M. J. (1991) The Cs5 peptide is a second site in the IICS region of fibronectin recognized by integrin α4β1. Inhibition of α4β1 function by RGD peptide homologues. J. Biol. Chem. 266, 3579-3585.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3579-3585
    • Mould, A.P.1    Komorya, A.2    Yamada, K.M.3    Humphries, M.J.4
  • 37
    • 0022827516 scopus 로고
    • Characterization of a unique glycoprotein antigen expressed on the surface of human neuroblastoma cells
    • Mujoo K., Spiro R. C., and Reisfeld R. A. (1986) Characterization of a unique glycoprotein antigen expressed on the surface of human neuroblastoma cells. J. Biol. Chem. 261, 10299-10309.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10299-10309
    • Mujoo, K.1    Spiro, R.C.2    Reisfeld, R.A.3
  • 38
    • 0027522533 scopus 로고
    • Diversity of primary structures of the carboxy-terminal regions of mammalian fibrinogen Aα-chains. Characterization of the partial nucleotide and deduced amino acid sequences in five mammalian species; rhesus monkey, pig, dog, mouse and Syrian hamster
    • Murakawa M., Okamura T., Kamura T., Shihuya T., Harada M., and Niho Y. (1993) Diversity of primary structures of the carboxy-terminal regions of mammalian fibrinogen Aα-chains. Characterization of the partial nucleotide and deduced amino acid sequences in five mammalian species; rhesus monkey, pig, dog, mouse and Syrian hamster. Thromb. Haemost. 69, 351-360.
    • (1993) Thromb. Haemost. , vol.69 , pp. 351-360
    • Murakawa, M.1    Okamura, T.2    Kamura, T.3    Shihuya, T.4    Harada, M.5    Niho, Y.6
  • 39
    • 0028805468 scopus 로고
    • The F3 neuronal glycophosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 fyn kinase in cerebellum
    • Olive S., Dubois C., Schachner M., and Rougon G. (1995) The F3 neuronal glycophosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 fyn kinase in cerebellum. J. Neurochem. 65, 2307-2317.
    • (1995) J. Neurochem. , vol.65 , pp. 2307-2317
    • Olive, S.1    Dubois, C.2    Schachner, M.3    Rougon, G.4
  • 40
    • 0031131885 scopus 로고    scopus 로고
    • Expression and regulation of the neural cell adhesion molecule L1 on human cells of myelomonocytic and lymphoid origin
    • Pancook J. D., Reisfeld R. A., Varki N., Vitello A., Fox R. I., and Montgomery A. M. P. (1997) Expression and regulation of the neural cell adhesion molecule L1 on human cells of myelomonocytic and lymphoid origin. J. Immunol. 158, 4413-4421.
    • (1997) J. Immunol. , vol.158 , pp. 4413-4421
    • Pancook, J.D.1    Reisfeld, R.A.2    Varki, N.3    Vitello, A.4    Fox, R.I.5    Montgomery, A.M.P.6
  • 41
    • 0027997413 scopus 로고
    • Selective recognition of cyclic RGD peptide of NMR defined conformation by αIIbβ3, αvβ3 and α5β1
    • Pfaff M., Tangemann K., Müller B., Gurrath M., Müller G., Kessler H., Timpl R., and Engel J. (1994) Selective recognition of cyclic RGD peptide of NMR defined conformation by αIIbβ3, αvβ3 and α5β1. J. Biol. Chem. 269, 20233-20238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20233-20238
    • Pfaff, M.1    Tangemann, K.2    Müller, B.3    Gurrath, M.4    Müller, G.5    Kessler, H.6    Timpl, R.7    Engel, J.8
  • 42
    • 0031575331 scopus 로고    scopus 로고
    • When a module is also a domain: The role of the N-terminus in the stability and the dynamics of immunoglobulin domains from titin
    • Pfuhl M., Improta S., Politou A. S., and Pastore A. (1997) When a module is also a domain: the role of the N-terminus in the stability and the dynamics of immunoglobulin domains from titin. J. Mol. Biol. 265, 242-256.
    • (1997) J. Mol. Biol. , vol.265 , pp. 242-256
    • Pfuhl, M.1    Improta, S.2    Politou, A.S.3    Pastore, A.4
  • 43
    • 0028058747 scopus 로고
    • Immunoglobulin-type domains of titin stabilized by amino-terminal extension
    • Politou A. S., Gautel M., Joseph C., and Pastore A. (1994) Immunoglobulin-type domains of titin stabilized by amino-terminal extension. FEBS Lett. 352, 27-31.
    • (1994) FEBS Lett. , vol.352 , pp. 27-31
    • Politou, A.S.1    Gautel, M.2    Joseph, C.3    Pastore, A.4
  • 44
    • 0030009318 scopus 로고    scopus 로고
    • The elastic I-band region of titin is assembled in a 'modular' fashion by weakly interacting Ig-like domains
    • Politou A. S., Gautel M., Improta S., Vangelista L., and Pastore A. (1996) The elastic I-band region of titin is assembled in a 'modular' fashion by weakly interacting Ig-like domains. J. Mol. Biol. 255, 604-616.
    • (1996) J. Mol. Biol. , vol.255 , pp. 604-616
    • Politou, A.S.1    Gautel, M.2    Improta, S.3    Vangelista, L.4    Pastore, A.5
  • 45
    • 0021298675 scopus 로고
    • Immunocytological and biochemical characterization of a new neuronal cell surface component (L1 antigen) which is involved in cell adhesion
    • Rathjen F. G. and Schachner M. (1984) Immunocytological and biochemical characterization of a new neuronal cell surface component (L1 antigen) which is involved in cell adhesion. EMBO J. 3, 1-10.
    • (1984) EMBO J. , vol.3 , pp. 1-10
    • Rathjen, F.G.1    Schachner, M.2
  • 46
    • 0026477126 scopus 로고
    • Variants of human L1 cell adhesion molecule arise through alternative splicing of RNA
    • Reid R. A. and Hemperly J. J. (1992) Variants of human L1 cell adhesion molecule arise through alternative splicing of RNA. J. Mol. Neurosci. 3, 127-135.
    • (1992) J. Mol. Neurosci. , vol.3 , pp. 127-135
    • Reid, R.A.1    Hemperly, J.J.2
  • 47
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. (1996) RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 12, 697-715.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 50
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa
    • Schägger H. and von Jagow G. (1987) Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 51
    • 0030021514 scopus 로고    scopus 로고
    • CD9 of mouse brain is implicated in neunte outgrowth and cell migration in vitro and is associated with the α6β1 integrin and the neural cell adhesion molecule L1
    • Schmidt C., Künemund V., Wintergerst E. S., Schmitz B., and Schachner M. (1996) CD9 of mouse brain is implicated in neunte outgrowth and cell migration in vitro and is associated with the α6β1 integrin and the neural cell adhesion molecule L1. J. Neurosci. Res. 43, 12-31.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 12-31
    • Schmidt, C.1    Künemund, V.2    Wintergerst, E.S.3    Schmitz, B.4    Schachner, M.5
  • 52
    • 0029984696 scopus 로고    scopus 로고
    • Structural and functional analysis of the globular domain IVa of the laminin α1 chain and its impact on the adjacent RGD site
    • Schulze B., Mann K., Pöschl E., Yamada Y., and Timpl R. (1996) Structural and functional analysis of the globular domain IVa of the laminin α1 chain and its impact on the adjacent RGD site. Biochem. J. 314, 847-851.
    • (1996) Biochem. J. , vol.314 , pp. 847-851
    • Schulze, B.1    Mann, K.2    Pöschl, E.3    Yamada, Y.4    Timpl, R.5
  • 53
    • 0027156648 scopus 로고
    • The energetics and cooperativity of protein folding: A simple experimental analysis based upon the solvation of internal residues
    • Staniforth R. A., Burston S. G., Smith C. J., Jackson G. S., Badcoe I. G., Atkinson T., Holbrook J. J., and Anthony R. C. (1993) The energetics and cooperativity of protein folding: a simple experimental analysis based upon the solvation of internal residues. Biochemistry 32, 3842-3851.
    • (1993) Biochemistry , vol.32 , pp. 3842-3851
    • Staniforth, R.A.1    Burston, S.G.2    Smith, C.J.3    Jackson, G.S.4    Badcoe, I.G.5    Atkinson, T.6    Holbrook, J.J.7    Anthony, R.C.8
  • 54
    • 0023409795 scopus 로고
    • Characterization of the cell adhesion molecule L1, NCAM and J1 in the intestine
    • Thor G., Probstmeier R., and Schachner M. (1987) Characterization of the cell adhesion molecule L1, NCAM and J1 in the intestine. EMBO J. 6, 2581-2586.
    • (1987) EMBO J. , vol.6 , pp. 2581-2586
    • Thor, G.1    Probstmeier, R.2    Schachner, M.3
  • 55
    • 0028789329 scopus 로고
    • Zebrafish neurons express two L1-related molecules during early axonogenesis
    • Tongiorgi E., Bernhardt R. R., and Schachner M. (1995) Zebrafish neurons express two L1-related molecules during early axonogenesis. J. Neurosci. Res. 42, 547-561.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 547-561
    • Tongiorgi, E.1    Bernhardt, R.R.2    Schachner, M.3
  • 56
    • 0031439129 scopus 로고    scopus 로고
    • Neural cell adhesion molecules of the immunoglobulin superfamily: Role in axon growth and guidance
    • Walsh F. S. and Doherty P. (1997) Neural cell adhesion molecules of the immunoglobulin superfamily: role in axon growth and guidance. Annu. Rev. Cell Biol. 13, 425-456.
    • (1997) Annu. Rev. Cell Biol. , vol.13 , pp. 425-456
    • Walsh, F.S.1    Doherty, P.2
  • 57
    • 0031882047 scopus 로고    scopus 로고
    • The Arg-Gly-Asp motif in the cell adhesion molecule L1 promotes neurite outgrowth via interaction with the alphavbeta3 integrin
    • Yip P. M., Zhao X., Montgomery A. M., and Siu C. H. (1998) The Arg-Gly-Asp motif in the cell adhesion molecule L1 promotes neurite outgrowth via interaction with the alphavbeta3 integrin. Mol. Biol. Cell 9, 277-290.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 277-290
    • Yip, P.M.1    Zhao, X.2    Montgomery, A.M.3    Siu, C.H.4


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