메뉴 건너뛰기




Volumn 135, Issue 4, 1996, Pages 1059-1069

Neurofascin induces neurites by heterophilic interactions with axonal NrCAM while NrCAM requires F11 on the axonal surface to extend neurites

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANE PROTEIN; CHIMERIC PROTEIN; FC RECEPTOR; IMMUNOGLOBULIN G; POLYLYSINE;

EID: 0029852196     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.135.4.1059     Document Type: Article
Times cited : (83)

References (55)
  • 1
    • 0022067755 scopus 로고
    • Fast and sensitive detection of protein and DNA bands by treatment with potassium permanganate
    • Ansorge, W. 1985. Fast and sensitive detection of protein and DNA bands by treatment with potassium permanganate. J. Biochem. Biophys. Methods. 11: 13-20.
    • (1985) J. Biochem. Biophys. Methods. , vol.11 , pp. 13-20
    • Ansorge, W.1
  • 2
    • 0024358833 scopus 로고
    • Drosophila neuroglian: A member of the immunoglobulin superfamily with extensive homology to the vertebrate neural adhesion molecule L1
    • Bieber, A.J., P.M. Snow, M. Hortsch, N.H. Patel, J.R. Jacobs, Z.R. Traquina, J. Schilling, and C.S. Goodman. 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    Traquina, Z.R.6    Schilling, J.7    Goodman, C.S.8
  • 3
    • 0029443827 scopus 로고
    • Cell adhesion molecules 1: Immunoglobulin superfamily
    • Brümmendorf, T., and F.G. Rathjen. 1995. Cell adhesion molecules 1: immunoglobulin superfamily. Protein Profile. 2: 963-1108.
    • (1995) Protein Profile , vol.2 , pp. 963-1108
    • Brümmendorf, T.1    Rathjen, F.G.2
  • 4
    • 0024644865 scopus 로고
    • Neural cell recognition molecule F11: Homology with fibronectin type III and immunoglobulin type C domains
    • Brümmendorf, T., J. M. Wolff, R. Frank, and F.G. Rathjen. 1989. Neural cell recognition molecule F11: homology with fibronectin type III and immunoglobulin type C domains. Neuron. 2:1351-1361.
    • (1989) Neuron. , vol.2 , pp. 1351-1361
    • Brümmendorf, T.1    Wolff, J.M.2    Frank, R.3    Rathjen, F.G.4
  • 5
    • 0027158056 scopus 로고
    • The axonal recognition molecule F11 is a multifunctional protein: Specific domains mediate interactions with Ng-CAM and restrictin
    • Brümmendorf, T., M. Hubert, U. Treubert, R. Leuschner, A. Tárnok, and F.G. Rathjen. 1993. The axonal recognition molecule F11 is a multifunctional protein: specific domains mediate interactions with Ng-CAM and restrictin. Neuron. 10:711-727.
    • (1993) Neuron. , vol.10 , pp. 711-727
    • Brümmendorf, T.1    Hubert, M.2    Treubert, U.3    Leuschner, R.4    Tárnok, A.5    Rathjen, F.G.6
  • 6
    • 0025977371 scopus 로고
    • Structure of the chicken neuron-glia cell adhesion molecule, Ng-CAM: Origin of the polypeptides and relation to the Ig superfamily
    • Burgoon, M.P., M. Grumet, V. Mauro, G.M. Edelman, and B.A. Cunningham. 1991. Structure of the chicken neuron-glia cell adhesion molecule, Ng-CAM: origin of the polypeptides and relation to the Ig superfamily. J. Cell Biol. 112:1017-1029.
    • (1991) J. Cell Biol. , vol.112 , pp. 1017-1029
    • Burgoon, M.P.1    Grumet, M.2    Mauro, V.3    Edelman, G.M.4    Cunningham, B.A.5
  • 7
    • 0029148550 scopus 로고
    • Functional analysis of posttranslational cleavage products of the neuron-glia cell adhesion molecule, Ng-CAM
    • Burgoon, M.P., R.B. Hazan, G.R. Phillips, K.L. Crossin, G.M. Edelman, and B.A. Cunningham. 1995. Functional analysis of posttranslational cleavage products of the neuron-glia cell adhesion molecule, Ng-CAM. J. Cell Biol. 130:733-744.
    • (1995) J. Cell Biol. , vol.130 , pp. 733-744
    • Burgoon, M.P.1    Hazan, R.B.2    Phillips, G.R.3    Crossin, K.L.4    Edelman, G.M.5    Cunningham, B.A.6
  • 8
    • 0030012213 scopus 로고    scopus 로고
    • The GPI-anchored adhesion molecule F3 induces tyrosine phosphorylation: Involvement of the FNIII repeats
    • Cervello, M., V. Matranga, P. Durbec, G. Rougon, and S. Gomez. 1996. The GPI-anchored adhesion molecule F3 induces tyrosine phosphorylation: involvement of the FNIII repeats. J. Cell Sci. 109:699-704.
    • (1996) J. Cell Sci. , vol.109 , pp. 699-704
    • Cervello, M.1    Matranga, V.2    Durbec, P.3    Rougon, G.4    Gomez, S.5
  • 9
    • 0029085733 scopus 로고
    • Cell adhesion molecules as morphoregulates
    • Cunningham, B.A. 1995. Cell adhesion molecules as morphoregulates. Curr. Opin. Cell Biol. 7:628-633.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 628-633
    • Cunningham, B.A.1
  • 10
    • 0023294574 scopus 로고
    • Extension of neuntes on axons is impaired by antibodies against specific neural cell surface glycoproteins
    • Chang, S., F.G. Rathjen, and J.A. Raper. 1987. Extension of neuntes on axons is impaired by antibodies against specific neural cell surface glycoproteins. J. Cell Biol. 104:355-362.
    • (1987) J. Cell Biol. , vol.104 , pp. 355-362
    • Chang, S.1    Rathjen, F.G.2    Raper, J.A.3
  • 11
    • 0027999616 scopus 로고
    • Ankyrin binding activity shared by the neurofascin/L1/NrCAM family of nervous system cell adhesion molecules
    • Davis, J., and V. Bennett. 1994. Ankyrin binding activity shared by the neurofascin/L1/NrCAM family of nervous system cell adhesion molecules. J. Biol. Chem. 269:27163-27166.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27163-27166
    • Davis, J.1    Bennett, V.2
  • 12
    • 0027532185 scopus 로고
    • Ankyrin-binding proteins related to nervous system cell adhesion molecules: Candidates to provide transmembrane and intercellular connections in adult brain
    • Davis, J., T. McLaughlin, and V. Bennett. 1993. Ankyrin-binding proteins related to nervous system cell adhesion molecules: candidates to provide transmembrane and intercellular connections in adult brain. J. Cell Biol. 121: 121-133.
    • (1993) J. Cell Biol. , vol.121 , pp. 121-133
    • Davis, J.1    McLaughlin, T.2    Bennett, V.3
  • 13
    • 0029953598 scopus 로고    scopus 로고
    • Heterophilic interactions of DM-GRASP: GRASP-NgCAM interactions involved in neurite extension
    • DeBernardo, A.P., and S. Chang. 1996. Heterophilic interactions of DM-GRASP: GRASP-NgCAM interactions involved in neurite extension. J. Cell Biol. 133:657-666.
    • (1996) J. Cell Biol. , vol.133 , pp. 657-666
    • DeBernardo, A.P.1    Chang, S.2
  • 14
    • 0025633403 scopus 로고
    • Topologically restricted appearance in the developing chick retino-tectal system of Bravo, a neural surface protein: Experimental modulation by environment cues
    • de la Rosa, E.J., J.F. Kayyem, J.M. Roman, Y.-D. Stierhof, W.J. Dreyer, and U. Schwarz. 1990. Topologically restricted appearance in the developing chick retino-tectal system of Bravo, a neural surface protein: experimental modulation by environment cues. J. Cell Biol. 111:3087-3096.
    • (1990) J. Cell Biol. , vol.111 , pp. 3087-3096
    • De La Rosa, E.J.1    Kayyem, J.F.2    Roman, J.M.3    Stierhof, Y.-D.4    Dreyer, W.J.5    Schwarz, U.6
  • 15
    • 0023986284 scopus 로고
    • Spatial regulation of axonal glycoprotein expression on subsets of embryonic spinal neurons
    • Dodd, J., S.B. Morton, D. Karagogeos, M. Yamamoto, and T.M. Jessell. 1988. Spatial regulation of axonal glycoprotein expression on subsets of embryonic spinal neurons. Neuron. 1:105-116.
    • (1988) Neuron. , vol.1 , pp. 105-116
    • Dodd, J.1    Morton, S.B.2    Karagogeos, D.3    Yamamoto, M.4    Jessell, T.M.5
  • 16
    • 0028091350 scopus 로고
    • Signal transduction events underlying neurite outgrowth stimulated by cell adhesion molecules
    • Doherty, P., and F.S. Walsh. 1994. Signal transduction events underlying neurite outgrowth stimulated by cell adhesion molecules. Curr. Opin. Neurobiol. 4:49-55.
    • (1994) Curr. Opin. Neurobiol. , vol.4 , pp. 49-55
    • Doherty, P.1    Walsh, F.S.2
  • 17
    • 0028817332 scopus 로고
    • A soluble chimeric form of the L1 glycoprotein stimulates neurite outgrowth
    • Doherty, P., E. Williams, F.S. Walsh. 1995. A soluble chimeric form of the L1 glycoprotein stimulates neurite outgrowth. Neuron. 14:57-66.
    • (1995) Neuron. , vol.14 , pp. 57-66
    • Doherty, P.1    Williams, E.2    Walsh, F.S.3
  • 18
    • 0029899939 scopus 로고    scopus 로고
    • Neuroglian-mediated cell adhesion induces assembly of the membrane skeleton at cell contact sites
    • Dubreuil, R.R., G. MacVicar, S. Dissnayake, C. Liu, D. Homer, and M. Hortsch. 1996. Neuroglian-mediated cell adhesion induces assembly of the membrane skeleton at cell contact sites. J. Cell Biol. 133:647-655.
    • (1996) J. Cell Biol. , vol.133 , pp. 647-655
    • Dubreuil, R.R.1    MacVicar, G.2    Dissnayake, S.3    Liu, C.4    Homer, D.5    Hortsch, M.6
  • 19
    • 0030066547 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycans in the developing central nervous system. I. Cellular sites of synthesis of neurocan and phosphacan
    • Engel, M., P. Maurel, R.U. Margolis, and R.K. Margolis. 1996. Chondroitin sulfate proteoglycans in the developing central nervous system. I. Cellular sites of synthesis of neurocan and phosphacan. J. Comp. Neurol. 366:34-43.
    • (1996) J. Comp. Neurol. , vol.366 , pp. 34-43
    • Engel, M.1    Maurel, P.2    Margolis, R.U.3    Margolis, R.K.4
  • 20
    • 0028273033 scopus 로고
    • TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and β1 integrins
    • Felsenfeld, D.P., M.A. Hynes, K.M. Skoler, A.J. Furley, and T.M. Jessell. 1994. TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and β1 integrins. Neuron. 12:1-20.
    • (1994) Neuron. , vol.12 , pp. 1-20
    • Felsenfeld, D.P.1    Hynes, M.A.2    Skoler, K.M.3    Furley, A.J.4    Jessell, T.M.5
  • 21
    • 0029918439 scopus 로고    scopus 로고
    • Mechanisms and molecules that control growth cone guidance
    • Goodman, C.S. 1996. Mechanisms and molecules that control growth cone guidance. Annu. Rev. Neurosci. 19:341-377.
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 341-377
    • Goodman, C.S.1
  • 22
    • 0025881186 scopus 로고
    • Structure of a new nervous system glycoprotein, NrCAM, and its relationship to subgroups of neural cell adhesion molecules
    • Grumet, M., V. Mauro, M.P. Burgoon, G.M. Edelman, and B.A. Cunningham. 1991. Structure of a new nervous system glycoprotein, NrCAM, and its relationship to subgroups of neural cell adhesion molecules. J. Cell Biol. 113: 1399-1412.
    • (1991) J. Cell Biol. , vol.113 , pp. 1399-1412
    • Grumet, M.1    Mauro, V.2    Burgoon, M.P.3    Edelman, G.M.4    Cunningham, B.A.5
  • 23
    • 0025297888 scopus 로고
    • Why are proteins O-glycosylated?
    • Jentoft, N. 1990. Why are proteins O-glycosylated? Trends Biochem. Sci. 15: 291-294.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 291-294
    • Jentoft, N.1
  • 24
    • 0026674084 scopus 로고
    • Bravo/Nr-CAM is closely related to the cell adhesion molecules L1 and Ng-CAM and has a similar heterodimer structure
    • Kayyem, J.F., J.M. Roman, E.J. de la Rosa, U. Schwarz, and W.J. Dreyer. 1992. Bravo/Nr-CAM is closely related to the cell adhesion molecules L1 and Ng-CAM and has a similar heterodimer structure. J. Cell Biol. 118:1259-1270.
    • (1992) J. Cell Biol. , vol.118 , pp. 1259-1270
    • Kayyem, J.F.1    Roman, J.M.2    De La Rosa, E.J.3    Schwarz, U.4    Dreyer, W.J.5
  • 25
    • 0025485402 scopus 로고
    • The avian tectobulbar tract: Development, explant culture, and effects of antibodies on the pattern of neurite outgrowth
    • Kröger, S., and U. Schwarz. 1990. The avian tectobulbar tract: development, explant culture, and effects of antibodies on the pattern of neurite outgrowth. J. Neurosci. 10:3118-3134.
    • (1990) J. Neurosci. , vol.10 , pp. 3118-3134
    • Kröger, S.1    Schwarz, U.2
  • 26
    • 0026319551 scopus 로고
    • Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1(G4)
    • Kuhn, T.B., E.T. Stoeckli, M.A. Condrau, F.G. Rathjen, and P. Sonderegger. 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, T.B.1    Stoeckli, E.T.2    Condrau, M.A.3    Rathjen, F.G.4    Sonderegger, P.5
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0024675417 scopus 로고
    • L1-mediated axon outgrowth occurs via a homophilic binding mechanism
    • Lemmon, V., K.L. Farr, and C. Lagenaur. 1989. L1-mediated axon outgrowth occurs via a homophilic binding mechanism. Neuron. 2:1597-1603.
    • (1989) Neuron. , vol.2 , pp. 1597-1603
    • Lemmon, V.1    Farr, K.L.2    Lagenaur, C.3
  • 29
    • 0026673974 scopus 로고
    • Homophilic and heterophilic binding activities of Nr-CAM, a nervous system cell adhesion molecule
    • Mauro, V.P., L.A. Krushel, B.A. Cunningham, and G.M. Edelman. 1992. Homophilic and heterophilic binding activities of Nr-CAM, a nervous system cell adhesion molecule. J. Cell Biol. 119:191-202.
    • (1992) J. Cell Biol. , vol.119 , pp. 191-202
    • Mauro, V.P.1    Krushel, L.A.2    Cunningham, B.A.3    Edelman, G.M.4
  • 30
    • 0023805739 scopus 로고
    • Neural adhesion molecule L1 as a member of the immunoglobulin superfamily with binding domains similar to fibronectin
    • Moos, M., R. Tacke, H. Scherer, D. Teplow, K. Früh, and M. Schachner. 1988. Neural adhesion molecule L1 as a member of the immunoglobulin superfamily with binding domains similar to fibronectin. Nature (Lond). 334:701-703.
    • (1988) Nature (Lond) , vol.334 , pp. 701-703
    • Moos, M.1    Tacke, R.2    Scherer, H.3    Teplow, D.4    Früh, K.5    Schachner, M.6
  • 31
    • 0027723273 scopus 로고
    • Induction of axonal growth by heterophilic interactions between the cell surface recognition proteins F11 and Nr-CAM/ Bravo
    • Morales, G., M. Hubert, T. Brümmendorf, U. Treubert, A. Tárnok, U. Schwarz, and F.G. Rathjen. 1993. Induction of axonal growth by heterophilic interactions between the cell surface recognition proteins F11 and Nr-CAM/ Bravo. Neuron. 11:1113-1122.
    • (1993) Neuron. , vol.11 , pp. 1113-1122
    • Morales, G.1    Hubert, M.2    Brümmendorf, T.3    Treubert, U.4    Tárnok, A.5    Schwarz, U.6    Rathjen, F.G.7
  • 32
    • 0028927808 scopus 로고
    • Expression of four immunoglobulin superfamily adhesion molecules (L1, Nr-CAM/Bravo, Neurofascin/ABGP, and N-CAM) in the developing mouse spinal cord
    • Moscoso, L.M., and J.R. Sanes. 1995. Expression of four immunoglobulin superfamily adhesion molecules (L1, Nr-CAM/Bravo, Neurofascin/ABGP, and N-CAM) in the developing mouse spinal cord. J. Comp. Neurol. 352: 321-334.
    • (1995) J. Comp. Neurol. , vol.352 , pp. 321-334
    • Moscoso, L.M.1    Sanes, J.R.2
  • 33
    • 0029114404 scopus 로고
    • Characterization of functional domains of the Tenascin-R (Restrictin) polypeptide: Cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by Tenascin-R
    • Nörenberg, U., M. Hubert, T. Brümmendorf, A. Tárnok, and F.G. Rathjen. 1995. Characterization of functional domains of the Tenascin-R (Restrictin) polypeptide: cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by Tenascin-R. J. Cell Biol. 130:473-484.
    • (1995) J. Cell Biol. , vol.130 , pp. 473-484
    • Nörenberg, U.1    Hubert, M.2    Brümmendorf, T.3    Tárnok, A.4    Rathjen, F.G.5
  • 34
    • 0029096048 scopus 로고
    • The carbonic anhydrase domain of receptor tyrosine phosphatase β is a functional ligand for the axonal cell recognition molecule contactin
    • Peles, E., M. Nativ, P.L. Campbell, T. Sakurai, R. Martinez, S. Lev, D.O. Clary, J. Schilling, G. Barnea, G.D. Plowman et al. 1995. The carbonic anhydrase domain of receptor tyrosine phosphatase β is a functional ligand for the axonal cell recognition molecule contactin. Cell. 82:251-260.
    • (1995) Cell , vol.82 , pp. 251-260
    • Peles, E.1    Nativ, M.2    Campbell, P.L.3    Sakurai, T.4    Martinez, R.5    Lev, S.6    Clary, D.O.7    Schilling, J.8    Barnea, G.9    Plowman, G.D.10
  • 35
    • 0027526588 scopus 로고
    • The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180
    • Pesheva, P., G. Cennarini, C. Goridis, and M. Schachner. 1993. The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180. Neuron. 10:69-82.
    • (1993) Neuron. , vol.10 , pp. 69-82
    • Pesheva, P.1    Cennarini, G.2    Goridis, C.3    Schachner, M.4
  • 36
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G.L. 1977. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83:346-356.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 38
    • 0023931139 scopus 로고
    • Neurofascin: A novel chick cell-surface glycoprotein involved in neurite-neurite interactions
    • Rathjen, F.G., J.M. Wolff, S. Chang, F. Bonhoeffer, and J.A. Raper. 1987a. Neurofascin: a novel chick cell-surface glycoprotein involved in neurite-neurite interactions. Cell. 51:841-849.
    • (1987) Cell , vol.51 , pp. 841-849
    • Rathjen, F.G.1    Wolff, J.M.2    Chang, S.3    Bonhoeffer, F.4    Raper, J.A.5
  • 40
    • 0025744729 scopus 로고
    • Restrictin: A chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11
    • Rathjen F.G., J.M. Wolff, and R. Chiquet-Ehrismann. 1991. Restrictin: a chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11. Development (Camb.). 113:151-164.
    • (1991) Development (Camb.) , vol.113 , pp. 151-164
    • Rathjen, F.G.1    Wolff, J.M.2    Chiquet-Ehrismann, R.3
  • 41
    • 0027496214 scopus 로고
    • Adhesion molecules of the nervous system
    • Rutishauser, U. 1993. Adhesion molecules of the nervous system. Curr. Opin. Neurobiol. 3:709-715.
    • (1993) Curr. Opin. Neurobiol. , vol.3 , pp. 709-715
    • Rutishauser, U.1
  • 42
    • 0026018293 scopus 로고
    • Immunolocalization studies of putative guidance molecules used by axons and growth cones of intersegmental interneurons in the chick embryo spinal cord
    • Shiga, T., and R.W. Oppenheim. 1991. Immunolocalization studies of putative guidance molecules used by axons and growth cones of intersegmental interneurons in the chick embryo spinal cord. J. Comp. Neurol. 310:234-252.
    • (1991) J. Comp. Neurol. , vol.310 , pp. 234-252
    • Shiga, T.1    Oppenheim, R.W.2
  • 43
    • 0027893209 scopus 로고
    • Dissecting the modes of interactions amongst cell adhesion molecules
    • Simmons, D.L. 1993. Dissecting the modes of interactions amongst cell adhesion molecules. Dev. Suppl. 193-203.
    • (1993) Dev. Suppl. , pp. 193-203
    • Simmons, D.L.1
  • 44
    • 0027096397 scopus 로고
    • Regulation of axonal growth in the vertebrate nervous system by interactions between glycoproteins belonging to two subgroups of the immunoglobulin superfamily
    • Sonderegger, P., and F.G. Rathjen. 1992. Regulation of axonal growth in the vertebrate nervous system by interactions between glycoproteins belonging to two subgroups of the immunoglobulin superfamily. J. Cell Biol. 119:1387-1394.
    • (1992) J. Cell Biol. , vol.119 , pp. 1387-1394
    • Sonderegger, P.1    Rathjen, F.G.2
  • 45
    • 0029042874 scopus 로고
    • Axonin-1, Nr-CAM, and Ng-CAM play different roles in the in vivo guidance of chick commissural neurons
    • Stoeckli, E.T., and L.T. Landmesser. 1995. Axonin-1, Nr-CAM, and Ng-CAM play different roles in the in vivo guidance of chick commissural neurons. Neuron. 14:1165-1179.
    • (1995) Neuron. , vol.14 , pp. 1165-1179
    • Stoeckli, E.T.1    Landmesser, L.T.2
  • 46
    • 0028783746 scopus 로고
    • Binding between the neural cell adhesion molecules axonin-1 and Nr-CAM/Bravo is involved in neuron-glia interaction
    • Suter, D.M., G.E. Pollerberg, A. Buchstaller, R.J. Giger, W.J. Dreyer, and P. Sonderegger. 1995. Binding between the neural cell adhesion molecules axonin-1 and Nr-CAM/Bravo is involved in neuron-glia interaction. J. Cell Biol. 131:1067-1081.
    • (1995) J. Cell Biol. , vol.131 , pp. 1067-1081
    • Suter, D.M.1    Pollerberg, G.E.2    Buchstaller, A.3    Giger, R.J.4    Dreyer, W.J.5    Sonderegger, P.6
  • 47
    • 0026772491 scopus 로고
    • Polysialic acid influences specific pathfinding by avian motoneurons
    • Tang, J., L. Landmesser, and U. Rutishauser. 1992. Polysialic acid influences specific pathfinding by avian motoneurons. Neuron. 8:1031-1044.
    • (1992) Neuron. , vol.8 , pp. 1031-1044
    • Tang, J.1    Landmesser, L.2    Rutishauser, U.3
  • 48
    • 0028133485 scopus 로고
    • Polysialic acid regulates growth cone behavior during sorting of motor axons in the plexus region
    • Tang, J., U. Rutishauser, and L. Landmesser. 1994. Polysialic acid regulates growth cone behavior during sorting of motor axons in the plexus region. Neuron. 13:405-414.
    • (1994) Neuron. , vol.13 , pp. 405-414
    • Tang, J.1    Rutishauser, U.2    Landmesser, L.3
  • 49
    • 0026718372 scopus 로고
    • Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily
    • Volkmer, H., B. Hassel, J.M. Wolff, R. Frank, and F.G. Rathjen. 1992. Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily. J. Cell Biol. 118:149-161.
    • (1992) J. Cell Biol. , vol.118 , pp. 149-161
    • Volkmer, H.1    Hassel, B.2    Wolff, J.M.3    Frank, R.4    Rathjen, F.G.5
  • 50
    • 44949279327 scopus 로고
    • Structure and function of the gene for neural cell adhesion molecule
    • Walsh, F.S., and P. Doherty. 1991. Structure and function of the gene for neural cell adhesion molecule. Semin. Neurosci. 3:271-284.
    • (1991) Semin. Neurosci. , vol.3 , pp. 271-284
    • Walsh, F.S.1    Doherty, P.2
  • 51
    • 0026452239 scopus 로고
    • Calcium influx into neurons can solely account for cell contactdependent neurite outgrowth stimulated by transfected L1
    • Williams, E.J., P. Doherty, G. Turner, R.A. Reid, J.J. Hemperley, and F.S. Walsh. 1992. Calcium influx into neurons can solely account for cell contactdependent neurite outgrowth stimulated by transfected L1. J. Cell Biol. 119: 883-892.
    • (1992) J. Cell Biol. , vol.119 , pp. 883-892
    • Williams, E.J.1    Doherty, P.2    Turner, G.3    Reid, R.A.4    Hemperley, J.J.5    Walsh, F.S.6
  • 52
    • 0023642605 scopus 로고
    • Biochemical characterization of polypeptide components involved in neurite fasciculation and elongation
    • Wolff, J.M., F.G. Rathjen, R. Frank, and S. Roth. 1987. Biochemical characterization of polypeptide components involved in neurite fasciculation and elongation. Eur. J. Biochem. 168:551-561.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 551-561
    • Wolff, J.M.1    Rathjen, F.G.2    Frank, R.3    Roth, S.4
  • 53
    • 0029038844 scopus 로고
    • Lamina-specific expression of adhesion molecules in developing chick optic tectum
    • Yamagata, M., J.P. Herman, and J.R. Sanes. 1995. Lamina-specific expression of adhesion molecules in developing chick optic tectum. J. Neurosci. 15: 4556-4571.
    • (1995) J. Neurosci. , vol.15 , pp. 4556-4571
    • Yamagata, M.1    Herman, J.P.2    Sanes, J.R.3
  • 54
  • 55
    • 0029165973 scopus 로고
    • The glypiated neuronal cell adhesion molecule contactin/ F11 complexes with src-family protein tyrosine kinase fyn
    • Zisch, A.H., L. D'Alessandri, K. Amrein, B. Ranscht, K.H. Winterhalter, and L. Vaughan. 1995. The glypiated neuronal cell adhesion molecule contactin/ F11 complexes with src-family protein tyrosine kinase fyn. Mol. Cell. Neurosci. 6:263-279.
    • (1995) Mol. Cell. Neurosci. , vol.6 , pp. 263-279
    • Zisch, A.H.1    D'Alessandri, L.2    Amrein, K.3    Ranscht, B.4    Winterhalter, K.H.5    Vaughan, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.