메뉴 건너뛰기




Volumn 47, Issue 2, 2005, Pages 215-229

Gliomedin mediates Schwann cell-axon interaction and the molecular assembly of the nodes of Ranvier

Author keywords

[No Author keywords available]

Indexed keywords

FASCIN; GLIOMEDIN; LIGAND; NERVE CELL ADHESION MOLECULE; NEUROFASCIN; SODIUM CHANNEL; UNCLASSIFIED DRUG;

EID: 22544453872     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuron.2005.06.026     Document Type: Article
Times cited : (263)

References (70)
  • 1
    • 7544237295 scopus 로고    scopus 로고
    • Acute demyelination disrupts the molecular organization of peripheral nervous system nodes
    • E.J. Arroyo, E.E. Sirkowski, R. Chitale, and S.S. Scherer Acute demyelination disrupts the molecular organization of peripheral nervous system nodes J. Comp. Neurol. 479 2004 424 434
    • (2004) J. Comp. Neurol. , vol.479 , pp. 424-434
    • Arroyo, E.J.1    Sirkowski, E.E.2    Chitale, R.3    Scherer, S.S.4
  • 4
    • 0036894716 scopus 로고    scopus 로고
    • Identification of genes that are downregulated in the absence of the POU domain transcription factor pou3f1 (Oct-6, Tst-1, SCIP) in sciatic nerve
    • J.R. Bermingham Jr., S. Shumas, T. Whisenhunt, E.E. Sirkowski, S. O'Connell, S.S. Scherer, and M.G. Rosenfeld Identification of genes that are downregulated in the absence of the POU domain transcription factor pou3f1 (Oct-6, Tst-1, SCIP) in sciatic nerve J. Neurosci. 22 2002 10217 10231
    • (2002) J. Neurosci. , vol.22 , pp. 10217-10231
    • Bermingham Jr., J.R.1    Shumas, S.2    Whisenhunt, T.3    Sirkowski, E.E.4    O'Connell, S.5    Scherer, S.S.6    Rosenfeld, M.G.7
  • 5
    • 0020525489 scopus 로고
    • Electron microscopic serial section analysis of nodes of Ranvier in lumbosacral spinal roots of the cat: Ultrastructural organization of nodal compartments in fibres of different sizes
    • C.H. Berthold, and M. Rydmark Electron microscopic serial section analysis of nodes of Ranvier in lumbosacral spinal roots of the cat: ultrastructural organization of nodal compartments in fibres of different sizes J. Neurocytol. 12 1983 475 505
    • (1983) J. Neurocytol. , vol.12 , pp. 475-505
    • Berthold, C.H.1    Rydmark, M.2
  • 7
    • 0024256419 scopus 로고
    • The perinodal astrocyte
    • J.A. Black, and S.G. Waxman The perinodal astrocyte Glia 1 1988 169 183
    • (1988) Glia , vol.1 , pp. 169-183
    • Black, J.A.1    Waxman, S.G.2
  • 8
    • 0034993395 scopus 로고    scopus 로고
    • Contactin orchestrates assembly of the septate-like junctions at the paranode in myelinated peripheral nerve
    • M.E. Boyle, E.O. Berglund, K.K. Murai, L. Weber, E. Peles, and B. Ranscht Contactin orchestrates assembly of the septate-like junctions at the paranode in myelinated peripheral nerve Neuron 30 2001 385 397
    • (2001) Neuron , vol.30 , pp. 385-397
    • Boyle, M.E.1    Berglund, E.O.2    Murai, K.K.3    Weber, L.4    Peles, E.5    Ranscht, B.6
  • 9
    • 0036726313 scopus 로고    scopus 로고
    • Stable suppression of tumorigenicity by virus-mediated RNA interference
    • T.R. Brummelkamp, R. Bernards, and R. Agami Stable suppression of tumorigenicity by virus-mediated RNA interference Cancer Cell 2 2002 243 247
    • (2002) Cancer Cell , vol.2 , pp. 243-247
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 10
    • 0032031124 scopus 로고    scopus 로고
    • MAG-deficient Schwann cells myelinate dorsal root ganglion neurons in culture
    • S. Carenini, D. Montag, M. Schachner, and R. Martini MAG-deficient Schwann cells myelinate dorsal root ganglion neurons in culture Glia 22 1998 213 220
    • (1998) Glia , vol.22 , pp. 213-220
    • Carenini, S.1    Montag, D.2    Schachner, M.3    Martini, R.4
  • 11
    • 0033506221 scopus 로고    scopus 로고
    • Clustering of neuronal sodium channels requires contact with myelinating Schwann cells
    • W. Ching, G. Zanazzi, S.R. Levinson, and J.L. Salzer Clustering of neuronal sodium channels requires contact with myelinating Schwann cells J. Neurocytol. 28 1999 295 301
    • (1999) J. Neurocytol. , vol.28 , pp. 295-301
    • Ching, W.1    Zanazzi, G.2    Levinson, S.R.3    Salzer, J.L.4
  • 13
    • 0037819578 scopus 로고    scopus 로고
    • Abnormal sodium channel distribution in optic nerve axons in a model of inflammatory demyelination
    • M.J. Craner, A.C. Lo, J.A. Black, and S.G. Waxman Abnormal sodium channel distribution in optic nerve axons in a model of inflammatory demyelination Brain 126 2003 1552 1561
    • (2003) Brain , vol.126 , pp. 1552-1561
    • Craner, M.J.1    Lo, A.C.2    Black, J.A.3    Waxman, S.G.4
  • 15
    • 0030443956 scopus 로고    scopus 로고
    • Molecular composition of the node of Ranvier: Identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segments
    • J.Q. Davis, S. Lambert, and V. Bennett Molecular composition of the node of Ranvier: identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segments J. Cell Biol. 135 1996 1355 1367
    • (1996) J. Cell Biol. , vol.135 , pp. 1355-1367
    • Davis, J.Q.1    Lambert, S.2    Bennett, V.3
  • 17
    • 0033552610 scopus 로고    scopus 로고
    • Axo-glial interactions regulate the localization of axonal paranodal proteins
    • J.L. Dupree, J.A. Girault, and B. Popko Axo-glial interactions regulate the localization of axonal paranodal proteins J. Cell Biol. 147 1999 1145 1152
    • (1999) J. Cell Biol. , vol.147 , pp. 1145-1152
    • Dupree, J.L.1    Girault, J.A.2    Popko, B.3
  • 18
    • 0031453392 scopus 로고    scopus 로고
    • The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination
    • S. Einheber, G. Zanazzi, W. Ching, S. Scherer, T.A. Milner, E. Peles, and J.L. Salzer The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination J. Cell Biol. 139 1997 1495 1506
    • (1997) J. Cell Biol. , vol.139 , pp. 1495-1506
    • Einheber, S.1    Zanazzi, G.2    Ching, W.3    Scherer, S.4    Milner, T.A.5    Peles, E.6    Salzer, J.L.7
  • 19
    • 4143057045 scopus 로고    scopus 로고
    • Endocytotic elimination and domain-selective tethering constitute a potential mechanism of protein segregation at the axonal initial segment
    • M.P. Fache, A. Moussif, F. Fernandes, P. Giraud, J.J. Garrido, and B. Dargent Endocytotic elimination and domain-selective tethering constitute a potential mechanism of protein segregation at the axonal initial segment J. Cell Biol. 166 2004 571 578
    • (2004) J. Cell Biol. , vol.166 , pp. 571-578
    • Fache, M.P.1    Moussif, A.2    Fernandes, F.3    Giraud, P.4    Garrido, J.J.5    Dargent, B.6
  • 20
    • 0031006110 scopus 로고    scopus 로고
    • Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin
    • T.D. Garver, Q. Ren, S. Tuvia, and V. Bennett Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin J. Cell Biol. 137 1997 703 714
    • (1997) J. Cell Biol. , vol.137 , pp. 703-714
    • Garver, T.D.1    Ren, Q.2    Tuvia, S.3    Bennett, V.4
  • 21
    • 0042733242 scopus 로고    scopus 로고
    • Local ERM activation and dynamic growth cones at Schwann cell tips implicated in efficient formation of nodes of Ranvier
    • C.L. Gatto, B.J. Walker, and S. Lambert Local ERM activation and dynamic growth cones at Schwann cell tips implicated in efficient formation of nodes of Ranvier J. Cell Biol. 162 2003 489 498
    • (2003) J. Cell Biol. , vol.162 , pp. 489-498
    • Gatto, C.L.1    Walker, B.J.2    Lambert, S.3
  • 22
    • 0346732924 scopus 로고    scopus 로고
    • Caspr regulates the processing of contactin and inhibits its binding to neurofascin
    • L. Gollan, D. Salomon, J.L. Salzer, and E. Peles Caspr regulates the processing of contactin and inhibits its binding to neurofascin J. Cell Biol. 163 2003 1213 1218
    • (2003) J. Cell Biol. , vol.163 , pp. 1213-1218
    • Gollan, L.1    Salomon, D.2    Salzer, J.L.3    Peles, E.4
  • 24
    • 11144352245 scopus 로고    scopus 로고
    • Neurexins Induce Differentiation of GABA and Glutamate Postsynaptic Specializations via Neuroligins
    • E.R. Graf, X. Zhang, S.X. Jin, M.W. Linhoff, and A.M. Craig Neurexins Induce Differentiation of GABA and Glutamate Postsynaptic Specializations via Neuroligins Cell 119 2004 1013 1026
    • (2004) Cell , vol.119 , pp. 1013-1026
    • Graf, E.R.1    Zhang, X.2    Jin, S.X.3    Linhoff, M.W.4    Craig, A.M.5
  • 25
    • 0037457020 scopus 로고    scopus 로고
    • Identification and characterization of CRG-L2, a new marker for liver tumor development
    • C.R. Graveel, S.R. Harkins-Perry, L.G. Acevedo, and P.J. Farnham Identification and characterization of CRG-L2, a new marker for liver tumor development Oncogene 22 2003 1730 1736
    • (2003) Oncogene , vol.22 , pp. 1730-1736
    • Graveel, C.R.1    Harkins-Perry, S.R.2    Acevedo, L.G.3    Farnham, P.J.4
  • 26
    • 0037450790 scopus 로고    scopus 로고
    • Amassin, an olfactomedin protein, mediates the massive intercellular adhesion of sea urchin coelomocytes
    • B.J. Hillier, and V.D. Vacquier Amassin, an olfactomedin protein, mediates the massive intercellular adhesion of sea urchin coelomocytes J. Cell Biol. 160 2003 597 604
    • (2003) J. Cell Biol. , vol.160 , pp. 597-604
    • Hillier, B.J.1    Vacquier, V.D.2
  • 27
    • 0025807797 scopus 로고
    • Three-dimensional fine structure of cytoskeletal-membrane interactions at nodes of Ranvier
    • T. Ichimura, and M.H. Ellisman Three-dimensional fine structure of cytoskeletal-membrane interactions at nodes of Ranvier J. Neurocytol. 20 1991 667 681
    • (1991) J. Neurocytol. , vol.20 , pp. 667-681
    • Ichimura, T.1    Ellisman, M.H.2
  • 29
    • 0035025620 scopus 로고    scopus 로고
    • Differential control of clustering of the sodium channels Na(v)1.2 and Na(v)1.6 at developing CNS nodes of Ranvier
    • M.R. Kaplan, M.H. Cho, E.M. Ullian, L.L. Isom, S.R. Levinson, and B.A. Barres Differential control of clustering of the sodium channels Na(v)1.2 and Na(v)1.6 at developing CNS nodes of Ranvier Neuron 30 2001 105 119
    • (2001) Neuron , vol.30 , pp. 105-119
    • Kaplan, M.R.1    Cho, M.H.2    Ullian, E.M.3    Isom, L.L.4    Levinson, S.R.5    Barres, B.A.6
  • 30
    • 0037148526 scopus 로고    scopus 로고
    • [Beta]IV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier
    • M. Komada, and P. Soriano [Beta]IV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier J. Cell Biol. 156 2002 337 348
    • (2002) J. Cell Biol. , vol.156 , pp. 337-348
    • Komada, M.1    Soriano, P.2
  • 31
    • 0025231649 scopus 로고
    • An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves
    • E. Kordeli, J. Davis, B. Trapp, and V. Bennett An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves J. Cell Biol. 110 1990 1341 1352
    • (1990) J. Cell Biol. , vol.110 , pp. 1341-1352
    • Kordeli, E.1    Davis, J.2    Trapp, B.3    Bennett, V.4
  • 32
    • 33044493298 scopus 로고    scopus 로고
    • Neurofascin interactions play a critical role in clustering sodium channels, ankyrinG and βiV spectrin at peripheral nodes of Ranvier
    • in press.
    • Koticha, D., Maurel, P., Zanazzi, G., Kane-Goldsmith, N., Basak, S., Babiarz, J., Salzer, J., and Grumet, M. (2005). Neurofascin interactions play a critical role in clustering sodium channels, ankyrinG and βIV spectrin at peripheral nodes of Ranvier. Dev. Biol., in press.
    • (2005) Dev. Biol.
    • Koticha, D.1    Maurel, P.2    Zanazzi, G.3    Kane-Goldsmith, N.4    Basak, S.5    Babiarz, J.6    Salzer, J.7    Grumet, M.8
  • 34
    • 0030824001 scopus 로고    scopus 로고
    • Morphogenesis of the node of Ranvier: Co-clusters of ankyrin and ankyrin-binding integral proteins define early developmental intermediates
    • S. Lambert, J.Q. Davis, and V. Bennett Morphogenesis of the node of Ranvier: co-clusters of ankyrin and ankyrin-binding integral proteins define early developmental intermediates J. Neurosci. 17 1997 7025 7036
    • (1997) J. Neurosci. , vol.17 , pp. 7025-7036
    • Lambert, S.1    Davis, J.Q.2    Bennett, V.3
  • 36
    • 0041345748 scopus 로고    scopus 로고
    • Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits
    • G. Lemaillet, B. Walker, and S. Lambert Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits J. Biol. Chem. 278 2003 27333 27339
    • (2003) J. Biol. Chem. , vol.278 , pp. 27333-27339
    • Lemaillet, G.1    Walker, B.2    Lambert, S.3
  • 37
    • 0442272486 scopus 로고    scopus 로고
    • A conserved postsynaptic transmembrane protein affecting neuromuscular signaling in Caenorhabditis elegans
    • P.M. Loria, J. Hodgkin, and O. Hobert A conserved postsynaptic transmembrane protein affecting neuromuscular signaling in Caenorhabditis elegans J. Neurosci. 24 2004 2191 2201
    • (2004) J. Neurosci. , vol.24 , pp. 2191-2201
    • Loria, P.M.1    Hodgkin, J.2    Hobert, O.3
  • 38
  • 39
    • 0034646634 scopus 로고    scopus 로고
    • Sodium channel beta subunits mediate homophilic cell adhesion and recruit ankyrin to points of cell-cell contact
    • J.D. Malhotra, K. Kazen-Gillespie, M. Hortsch, and L.L. Isom Sodium channel beta subunits mediate homophilic cell adhesion and recruit ankyrin to points of cell-cell contact J. Biol. Chem. 275 2000 11383 11388
    • (2000) J. Biol. Chem. , vol.275 , pp. 11383-11388
    • Malhotra, J.D.1    Kazen-Gillespie, K.2    Hortsch, M.3    Isom, L.L.4
  • 40
    • 0035207925 scopus 로고    scopus 로고
    • Essential role of oligodendrocytes in the formation and maintenance of central nervous system nodal regions
    • C. Mathis, N. Denisenko-Nehrbass, J.A. Girault, and E. Borrelli Essential role of oligodendrocytes in the formation and maintenance of central nervous system nodal regions Development 128 2001 4881 4890
    • (2001) Development , vol.128 , pp. 4881-4890
    • Mathis, C.1    Denisenko-Nehrbass, N.2    Girault, J.A.3    Borrelli, E.4
  • 41
    • 10644241512 scopus 로고    scopus 로고
    • Heterophilic interactions of sodium channel beta 1 subunits with axonal and glial cell adhesion molecules
    • D.P. McEwen, and L.L. Isom Heterophilic interactions of sodium channel beta 1 subunits with axonal and glial cell adhesion molecules J. Biol. Chem. 279 2004 52744 52752
    • (2004) J. Biol. Chem. , vol.279 , pp. 52744-52752
    • McEwen, D.P.1    Isom, L.L.2
  • 43
    • 2142707240 scopus 로고    scopus 로고
    • Rho kinase regulates schwann cell myelination and formation of associated axonal domains
    • C.V. Melendez-Vasquez, S. Einheber, and J.L. Salzer Rho kinase regulates schwann cell myelination and formation of associated axonal domains J. Neurosci. 24 2004 3953 3963
    • (2004) J. Neurosci. , vol.24 , pp. 3953-3963
    • Melendez-Vasquez, C.V.1    Einheber, S.2    Salzer, J.L.3
  • 45
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • J. Myllyharju, and K.I. Kivirikko Collagens, modifying enzymes and their mutations in humans, flies and worms Trends Genet. 20 2004 33 43
    • (2004) Trends Genet. , vol.20 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 46
    • 0042305307 scopus 로고    scopus 로고
    • Secreted glycoprotein myocilin is a component of the myelin sheath in peripheral nerves
    • A. Ohlmann, A. Goldwich, C. Flugel-Koch, A.V. Fuchs, K. Schwager, and E.R. Tamm Secreted glycoprotein myocilin is a component of the myelin sheath in peripheral nerves Glia 43 2003 128 140
    • (2003) Glia , vol.43 , pp. 128-140
    • Ohlmann, A.1    Goldwich, A.2    Flugel-Koch, C.3    Fuchs, A.V.4    Schwager, K.5    Tamm, E.R.6
  • 48
    • 0029096048 scopus 로고
    • The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin
    • E. Peles, M. Nativ, P.L. Campbell, T. Sakurai, R. Martinez, S. Lev, D.O. Clary, J. Schilling, G. Barnea, and G.D. Plowman The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin Cell 82 1995 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
  • 49
    • 0031041601 scopus 로고    scopus 로고
    • Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions
    • E. Peles, M. Nativ, M. Lustig, M. Grumet, J. Schilling, R. Martinez, G.D. Plowman, and J. Schlessinger Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions EMBO J. 16 1997 978 988
    • (1997) EMBO J. , vol.16 , pp. 978-988
    • Peles, E.1    Nativ, M.2    Lustig, M.3    Grumet, M.4    Schilling, J.5    Martinez, R.6    Plowman, G.D.7    Schlessinger, J.8
  • 50
    • 0345690096 scopus 로고    scopus 로고
    • The local differentiation of myelinated axons at nodes of Ranvier
    • S. Poliak, and E. Peles The local differentiation of myelinated axons at nodes of Ranvier Nat. Rev. Neurosci. 4 2003 968 980
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 968-980
    • Poliak, S.1    Peles, E.2
  • 51
    • 0033396331 scopus 로고    scopus 로고
    • Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with K+ channels
    • S. Poliak, L. Gollan, R. Martinez, A. Custer, S. Einheber, J.L. Salzer, J.S. Trimmer, P. Shrager, and E. Peles Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with K+ channels Neuron 24 1999 1037 1047
    • (1999) Neuron , vol.24 , pp. 1037-1047
    • Poliak, S.1    Gollan, L.2    Martinez, R.3    Custer, A.4    Einheber, S.5    Salzer, J.L.6    Trimmer, J.S.7    Shrager, P.8    Peles, E.9
  • 52
    • 0037191066 scopus 로고    scopus 로고
    • Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells
    • S. Poliak, S. Matlis, C. Ullmer, S.S. Scherer, and E. Peles Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells J. Cell Biol. 159 2002 361 372
    • (2002) J. Cell Biol. , vol.159 , pp. 361-372
    • Poliak, S.1    Matlis, S.2    Ullmer, C.3    Scherer, S.S.4    Peles, E.5
  • 54
    • 0020468098 scopus 로고
    • Differences between the nodes of Ranvier of large and small diameter fibres in the P.N.S
    • C.S. Raine Differences between the nodes of Ranvier of large and small diameter fibres in the P.N.S J. Neurocytol. 11 1982 935 947
    • (1982) J. Neurocytol. , vol.11 , pp. 935-947
    • Raine, C.S.1
  • 55
    • 0021355316 scopus 로고
    • On the association between perinodal astrocytic processes and the node of Ranvier in the C.N.S
    • C.S. Raine On the association between perinodal astrocytic processes and the node of Ranvier in the C.N.S J. Neurocytol. 13 1984 21 27
    • (1984) J. Neurocytol. , vol.13 , pp. 21-27
    • Raine, C.S.1
  • 56
    • 0035939078 scopus 로고    scopus 로고
    • Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain
    • C.F. Ratcliffe, R.E. Westenbroek, R. Curtis, and W.A. Catterall Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain J. Cell Biol. 154 2001 427 434
    • (2001) J. Cell Biol. , vol.154 , pp. 427-434
    • Ratcliffe, C.F.1    Westenbroek, R.E.2    Curtis, R.3    Catterall, W.A.4
  • 58
    • 0141987863 scopus 로고    scopus 로고
    • Polarized domains of myelinated axons
    • J.L. Salzer Polarized domains of myelinated axons Neuron 40 2003 297 318
    • (2003) Neuron , vol.40 , pp. 297-318
    • Salzer, J.L.1
  • 59
    • 1842610973 scopus 로고    scopus 로고
    • Does paranode formation and maintenance require partitioning of neurofascin 155 into lipid rafts?
    • D.P. Schafer, R. Bansal, K.L. Hedstrom, S.E. Pfeiffer, and M.N. Rasband Does paranode formation and maintenance require partitioning of neurofascin 155 into lipid rafts? J. Neurosci. 24 2004 3176 3185
    • (2004) J. Neurosci. , vol.24 , pp. 3176-3185
    • Schafer, D.P.1    Bansal, R.2    Hedstrom, K.L.3    Pfeiffer, S.E.4    Rasband, M.N.5
  • 60
  • 61
    • 0036311467 scopus 로고    scopus 로고
    • Caspr3 and caspr4, two novel members of the caspr family are expressed in the nervous system and interact with PDZ domains
    • I. Spiegel, D. Salomon, B. Erne, N. Schaeren-Wiemers, and E. Peles Caspr3 and caspr4, two novel members of the caspr family are expressed in the nervous system and interact with PDZ domains Mol. Cell. Neurosci. 20 2002 283 297
    • (2002) Mol. Cell. Neurosci. , vol.20 , pp. 283-297
    • Spiegel, I.1    Salomon, D.2    Erne, B.3    Schaeren-Wiemers, N.4    Peles, E.5
  • 64
    • 48749147247 scopus 로고
    • Axolemmal differentiation in myelinated fibers of rat peripheral nerves
    • J.H. Tao-Cheng, and J. Rosenbluth Axolemmal differentiation in myelinated fibers of rat peripheral nerves Brain Res. 285 1983 251 263
    • (1983) Brain Res. , vol.285 , pp. 251-263
    • Tao-Cheng, J.H.1    Rosenbluth, J.2
  • 65
    • 0037075179 scopus 로고    scopus 로고
    • Dorsalization of the neural tube by Xenopus tiarin, a novel patterning factor secreted by the flanking nonneural head ectoderm
    • H. Tsuda, N. Sasai, M. Matsuo-Takasaki, M. Sakuragi, Y. Murakami, and Y. Sasai Dorsalization of the neural tube by Xenopus tiarin, a novel patterning factor secreted by the flanking nonneural head ectoderm Neuron 33 2002 515 528
    • (2002) Neuron , vol.33 , pp. 515-528
    • Tsuda, H.1    Sasai, N.2    Matsuo-Takasaki, M.3    Sakuragi, M.4    Murakami, Y.5    Sasai, Y.6
  • 66
    • 0029781360 scopus 로고    scopus 로고
    • The clustering of axonal sodium channels during development of the peripheral nervous system
    • I. Vabnick, S.D. Novakovic, S.R. Levinson, M. Schachner, and P. Shrager The clustering of axonal sodium channels during development of the peripheral nervous system J. Neurosci. 16 1996 4914 4922
    • (1996) J. Neurosci. , vol.16 , pp. 4914-4922
    • Vabnick, I.1    Novakovic, S.D.2    Levinson, S.R.3    Schachner, M.4    Shrager, P.5
  • 68
    • 0027398432 scopus 로고
    • Molecular dissection of the myelinated axon
    • S.G. Waxman, and J.M. Ritchie Molecular dissection of the myelinated axon Ann. Neurol. 33 1993 121 136
    • (1993) Ann. Neurol. , vol.33 , pp. 121-136
    • Waxman, S.G.1    Ritchie, J.M.2
  • 69
    • 7244258884 scopus 로고    scopus 로고
    • BetaIV spectrins are essential for membrane stability and the molecular organization of nodes of Ranvier
    • Y. Yang, S. Lacas-Gervais, D.K. Morest, M. Solimena, and M.N. Rasband BetaIV spectrins are essential for membrane stability and the molecular organization of nodes of Ranvier J. Neurosci. 24 2004 7230 7240
    • (2004) J. Neurosci. , vol.24 , pp. 7230-7240
    • Yang, Y.1    Lacas-Gervais, S.2    Morest, D.K.3    Solimena, M.4    Rasband, M.N.5
  • 70
    • 0027287406 scopus 로고
    • Molecular cloning of olfactomedin, an extracellular matrix protein specific to olfactory neuroepithelium
    • H. Yokoe, and R.R. Anholt Molecular cloning of olfactomedin, an extracellular matrix protein specific to olfactory neuroepithelium Proc. Natl. Acad. Sci. USA 90 1993 4655 4659
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4655-4659
    • Yokoe, H.1    Anholt, R.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.