메뉴 건너뛰기




Volumn 584, Issue 9, 2010, Pages 1787-1792

GPI-anchored proteins at the node of Ranvier

Author keywords

Contactin; Myelin; Paranode; Raft; TAG 1

Indexed keywords

AXONIN 1; BETA1 INTEGRIN; CONTACTIN; CONTACTIN ASSOCIATED PROTEIN; FIBRONECTIN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; NERVE CELL ADHESION MOLECULE; POTASSIUM CHANNEL KCNQ; POTASSIUM CHANNEL KV1.1; POTASSIUM CHANNEL KV1.2; SODIUM CHANNEL NAV1.2; TENASCIN; UNCLASSIFIED DRUG; GLYCOSYLPHOSPHATIDYLINOSITOL; MEMBRANE PROTEIN;

EID: 77951930755     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.08.025     Document Type: Review
Times cited : (41)

References (79)
  • 1
    • 0030273292 scopus 로고    scopus 로고
    • Structure/function relationships of axon-associated adhesion receptors of the immunoglobulin superfamily
    • Brümmendorf T., Rathjen F. Structure/function relationships of axon-associated adhesion receptors of the immunoglobulin superfamily. Curr. Opin. Neurobiol. 1996, 6:584-592.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 584-592
    • Brümmendorf, T.1    Rathjen, F.2
  • 2
    • 0036814534 scopus 로고    scopus 로고
    • F3/contactin, a neuronal cell adhesion molecule implicated in axogenesis and myelination
    • Falk J., Bonnon C., Girault J.A., Faivre-Sarrailh C. F3/contactin, a neuronal cell adhesion molecule implicated in axogenesis and myelination. Biol. Cell 2002, 94:327-334.
    • (2002) Biol. Cell , vol.94 , pp. 327-334
    • Falk, J.1    Bonnon, C.2    Girault, J.A.3    Faivre-Sarrailh, C.4
  • 3
    • 3142772197 scopus 로고    scopus 로고
    • Neural GPI-anchored cell adhesion molecules
    • Karagogeos D. Neural GPI-anchored cell adhesion molecules. Front. Biosci. 2003, 8:s1304-1320.
    • (2003) Front. Biosci. , vol.8
    • Karagogeos, D.1
  • 4
    • 67049145076 scopus 로고    scopus 로고
    • Contactins. Emerging key roles in the development and function of the nervous system
    • Shimoda Y., Watanabe K. Contactins. Emerging key roles in the development and function of the nervous system. Cell Adhes. Migration 2009, 3:1-7.
    • (2009) Cell Adhes. Migration , vol.3 , pp. 1-7
    • Shimoda, Y.1    Watanabe, K.2
  • 6
    • 61549129037 scopus 로고    scopus 로고
    • Molecular domains of myelinated axons in the peripheral nervous system
    • Salzer J.L., Brophy P.J., Peles E. Molecular domains of myelinated axons in the peripheral nervous system. Glia 2008, 56:1532-1540.
    • (2008) Glia , vol.56 , pp. 1532-1540
    • Salzer, J.L.1    Brophy, P.J.2    Peles, E.3
  • 7
    • 56949103144 scopus 로고    scopus 로고
    • Molecular mechanisms of node of Ranvier formation
    • Susuki K., Rasband M.N. Molecular mechanisms of node of Ranvier formation. Curr. Opin. Cell Biol. 2008, 20:616-623.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 616-623
    • Susuki, K.1    Rasband, M.N.2
  • 8
    • 33847172262 scopus 로고    scopus 로고
    • Polarized targeting of ion channels in neurons
    • Arnold D.B. Polarized targeting of ion channels in neurons. Eur. J. Physiol. 2007, 453:763-769.
    • (2007) Eur. J. Physiol. , vol.453 , pp. 763-769
    • Arnold, D.B.1
  • 10
    • 0034993395 scopus 로고    scopus 로고
    • Contactin orchestrates assembly of the septate-like junctions at the paranode in myelinated peripheral nerve
    • Boyle M.E., Berglund E.O., Murai K.K., Weber L., Peles E., Ranscht B. Contactin orchestrates assembly of the septate-like junctions at the paranode in myelinated peripheral nerve. Neuron 2001, 30:385-397.
    • (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
  • 12
    • 46249114300 scopus 로고    scopus 로고
    • Glial and neuronal isoforms of Neurofascin have distinct roles in the assembly of nodes of Ranvier in the central nervous system
    • Zonta B., Tait S., Melrose S., Anderson H., Harroch S., Higginson J., Sherman D.L., Brophy P.J. Glial and neuronal isoforms of Neurofascin have distinct roles in the assembly of nodes of Ranvier in the central nervous system. J. Cell Biol. 2008, 181:1169-1177.
    • (2008) J. Cell Biol. , vol.181 , pp. 1169-1177
    • Zonta, B.1    Tait, S.2    Melrose, S.3    Anderson, H.4    Harroch, S.5    Higginson, J.6    Sherman, D.L.7    Brophy, P.J.8
  • 13
    • 66049088725 scopus 로고    scopus 로고
    • Spatiotemporal ablation of myelinating glia-specific neurofascin (NfascNF155) in mice reveals gradual loss of paranodal axoglial junctions and concomitant disorganization of axonal domains
    • Pillai A.M., Thaxton C., Pribisko A.L., Cheng J.G., Dupree J.L., Bhat M.A. Spatiotemporal ablation of myelinating glia-specific neurofascin (NfascNF155) in mice reveals gradual loss of paranodal axoglial junctions and concomitant disorganization of axonal domains. J. Neurosci. Res. 2009, 87:1773-1793.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 1773-1793
    • Pillai, A.M.1    Thaxton, C.2    Pribisko, A.L.3    Cheng, J.G.4    Dupree, J.L.5    Bhat, M.A.6
  • 15
    • 0034668775 scopus 로고    scopus 로고
    • Contactin-associated protein (Caspr) and contactin form a complex that is targeted to the paranodal junctions during myelination
    • Rios J.C., Melendez-Vasquez C.V., Einheber S., Lustig M., Grumet M., Hemperly J., Peles E., Salzer J.L. Contactin-associated protein (Caspr) and contactin form a complex that is targeted to the paranodal junctions during myelination. J. Neurosci. 2000, 20:8354-8364.
    • (2000) J. Neurosci. , vol.20 , pp. 8354-8364
    • Rios, J.C.1    Melendez-Vasquez, C.V.2    Einheber, S.3    Lustig, M.4    Grumet, M.5    Hemperly, J.6    Peles, E.7    Salzer, J.L.8
  • 19
    • 0027526588 scopus 로고
    • The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180
    • Pesheva P., Gennarini G., Goridis C., Schachner M. The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180. Neuron 1993, 10:69-82.
    • (1993) Neuron , vol.10 , pp. 69-82
    • Pesheva, P.1    Gennarini, G.2    Goridis, C.3    Schachner, M.4
  • 21
    • 10644241512 scopus 로고    scopus 로고
    • Heterophilic interactions of sodium channel beta1 subunits with axonal and glial cell adhesion molecules
    • McEwen D.P., Isom L.L. Heterophilic interactions of sodium channel beta1 subunits with axonal and glial cell adhesion molecules. J. Biol. Chem. 2004, 279:52744-52752.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52744-52752
    • McEwen, D.P.1    Isom, L.L.2
  • 22
    • 0028972374 scopus 로고
    • Structure and function of the beta 2 subunit of brain sodium channels, a transmembrane glycoprotein with CAM motif
    • Isom L.L., Ragsdale D.S., De Jongh K.S., Westenbroeck R.E., Reber B.F., Scheuer T., Catterall W.A. Structure and function of the beta 2 subunit of brain sodium channels, a transmembrane glycoprotein with CAM motif. Cell 1995, 83:433-442.
    • (1995) Cell , vol.83 , pp. 433-442
    • Isom, L.L.1    Ragsdale, D.S.2    De Jongh, K.S.3    Westenbroeck, R.E.4    Reber, B.F.5    Scheuer, T.6    Catterall, W.A.7
  • 23
    • 0032418740 scopus 로고    scopus 로고
    • Interaction of voltage-gated sodium channels with the extracellular matrix molecules tenascin-C and tenascin-R
    • Srinivasan J., Schachner M., Catterall W.A. Interaction of voltage-gated sodium channels with the extracellular matrix molecules tenascin-C and tenascin-R. Proc. Natl. Acad. Sci. USA 1998, 95:15753-15757.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15753-15757
    • Srinivasan, J.1    Schachner, M.2    Catterall, W.A.3
  • 26
    • 0035939078 scopus 로고    scopus 로고
    • Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain
    • Ratcliffe C.F., Westenbroek R.E., Curtis R., Catterall W.A. Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain. J. Cell Biol. 2001, 154:427-434.
    • (2001) J. Cell Biol. , vol.154 , pp. 427-434
    • Ratcliffe, C.F.1    Westenbroek, R.E.2    Curtis, R.3    Catterall, W.A.4
  • 28
    • 0037092443 scopus 로고    scopus 로고
    • The neuronal adhesion protein TAG-1 is expressed by Schwann cells and oligodendrocytes and is localized to the juxtaparanodal region of myelinated fibers
    • Traka M., Dupree J.L., Popko B., Karagogeos D. The neuronal adhesion protein TAG-1 is expressed by Schwann cells and oligodendrocytes and is localized to the juxtaparanodal region of myelinated fibers. J. Neurosci. 2002, 22:3016-3024.
    • (2002) J. Neurosci. , vol.22 , pp. 3016-3024
    • Traka, M.1    Dupree, J.L.2    Popko, B.3    Karagogeos, D.4
  • 35
    • 34748840451 scopus 로고    scopus 로고
    • The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction
    • Mörtl M., Sonderegger P., Diederichs K., Welte W. The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction. Protein Sci. 2007, 16:2174-2183.
    • (2007) Protein Sci. , vol.16 , pp. 2174-2183
    • Mörtl, M.1    Sonderegger, P.2    Diederichs, K.3    Welte, W.4
  • 36
    • 0029825579 scopus 로고    scopus 로고
    • The fibronectin domains of the neural adhesion molecule TAX-1 are necessary and sufficient for homophilic binding
    • Tsiotra P.C., Theodorakis K., Papamatheakis J., Karagogeos D. The fibronectin domains of the neural adhesion molecule TAX-1 are necessary and sufficient for homophilic binding. J. Biol. Chem. 1996, 271:29216-29222.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29216-29222
    • Tsiotra, P.C.1    Theodorakis, K.2    Papamatheakis, J.3    Karagogeos, D.4
  • 38
    • 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., Jessell T.M. TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and beta 1 integrins. Neuron 1994, 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
  • 39
    • 0030455845 scopus 로고    scopus 로고
    • Cell adhesion molecules NgCAM and axonin-1 form heterodimers in the neuronal membrane and cooperate in neurite outgrowth promotion
    • Buchstaller A., Kunz S., Berger P., Kunz B., Ziegler U., Rader C., Sonderegger P. Cell adhesion molecules NgCAM and axonin-1 form heterodimers in the neuronal membrane and cooperate in neurite outgrowth promotion. J Cell Biol. 1996, 135:1593-1607.
    • (1996) J Cell Biol. , vol.135 , pp. 1593-1607
    • Buchstaller, A.1    Kunz, S.2    Berger, P.3    Kunz, B.4    Ziegler, U.5    Rader, C.6    Sonderegger, P.7
  • 40
    • 0029896991 scopus 로고    scopus 로고
    • TAG-1/axonin-1 is a high-affinity ligand of neurocan, phosphacan/protein-tyrosine phosphatasez/b, and N-CAM
    • Milev P., Maurel P., Häring M., Margolis R.K., Margolis R.U. TAG-1/axonin-1 is a high-affinity ligand of neurocan, phosphacan/protein-tyrosine phosphatasez/b, and N-CAM. J. Biol. Chem. 1996, 271:15716-15723.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15716-15723
    • Milev, P.1    Maurel, P.2    Häring, M.3    Margolis, R.K.4    Margolis, R.U.5
  • 41
    • 0033562362 scopus 로고    scopus 로고
    • Nr-CAM promotes neurite outgrowth from peripheral ganglia by a mechanism involving axonin-1 as a neuronal receptor
    • Lustig M., Sakurai T., Grumet M. Nr-CAM promotes neurite outgrowth from peripheral ganglia by a mechanism involving axonin-1 as a neuronal receptor. Dev. Biol. 1999, 209:340-351.
    • (1999) Dev. Biol. , vol.209 , pp. 340-351
    • Lustig, M.1    Sakurai, T.2    Grumet, M.3
  • 42
    • 0032827082 scopus 로고    scopus 로고
    • NrCAM, cerebellar granule cell receptor for the neuronal adhesion molecule F3, displays an actin-dependent mobility in growth cones
    • Faivre-Sarrailh C., Falk J., Pollerberg E., Schachner M., Rougon G. NrCAM, cerebellar granule cell receptor for the neuronal adhesion molecule F3, displays an actin-dependent mobility in growth cones. J. Cell Sci. 1999, 112:3015-3027.
    • (1999) J. Cell Sci. , vol.112 , pp. 3015-3027
    • Faivre-Sarrailh, C.1    Falk, J.2    Pollerberg, E.3    Schachner, M.4    Rougon, G.5
  • 43
    • 0036703489 scopus 로고    scopus 로고
    • Tenascin-C promotes neurite outgrowth of embryonic hippocampal neurons through the alternatively spliced fibronectin type III BD domains via activation of the cell adhesion molecule F3/contactin
    • Rigato F., Garwood J., Calco V., Heck N., Faivre-Sarrailh C., Faissner A. Tenascin-C promotes neurite outgrowth of embryonic hippocampal neurons through the alternatively spliced fibronectin type III BD domains via activation of the cell adhesion molecule F3/contactin. J. Neurosci. 2002, 22:6596-6609.
    • (2002) J. Neurosci. , vol.22 , pp. 6596-6609
    • Rigato, F.1    Garwood, J.2    Calco, V.3    Heck, N.4    Faivre-Sarrailh, C.5    Faissner, A.6
  • 45
    • 0032563627 scopus 로고    scopus 로고
    • Dissection of complex molecular interactions of neurofascin with axonin-1, F11, and tenascin-R, which promote attachment and neurite formation of tectal cells
    • Volkmer H., Zacharias U., Norenberg U., Rathjen F.G. Dissection of complex molecular interactions of neurofascin with axonin-1, F11, and tenascin-R, which promote attachment and neurite formation of tectal cells. J. Cell Biol. 1998, 142:1083-1093.
    • (1998) J. Cell Biol. , vol.142 , pp. 1083-1093
    • Volkmer, H.1    Zacharias, U.2    Norenberg, U.3    Rathjen, F.G.4
  • 46
    • 32244447756 scopus 로고    scopus 로고
    • A regulated switch of chick neurofascin isoforms modulates ligand recognition and neurite extension
    • Pruss T., Kranz E.U., Niere M., Volkmer H. A regulated switch of chick neurofascin isoforms modulates ligand recognition and neurite extension. Mol. Cell. Neurosci. 2006, 31:354-365.
    • (2006) Mol. Cell. Neurosci. , vol.31 , pp. 354-365
    • Pruss, T.1    Kranz, E.U.2    Niere, M.3    Volkmer, H.4
  • 47
    • 0344081339 scopus 로고    scopus 로고
    • The paranodal complex of F3/contactin and caspr/paranodin traffics to the cell surface via a non-conventional pathway
    • Bonnon C., Goutebroze L., Denisenko-Nehrbass N., Girault J.A., Faivre-Sarrailh C. The paranodal complex of F3/contactin and caspr/paranodin traffics to the cell surface via a non-conventional pathway. J. Biol. Chem. 2003, 278:48339-48347.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48339-48347
    • Bonnon, C.1    Goutebroze, L.2    Denisenko-Nehrbass, N.3    Girault, J.A.4    Faivre-Sarrailh, C.5
  • 48
    • 0034678437 scopus 로고    scopus 로고
    • The glycosylphosphatidyl inositol-anchored adhesion molecule F3/contactin is required for surface transport of paranodin/contactin-associated protein (caspr)
    • Faivre-Sarrailh C., Gauthier F., Denisenko-Nehrbass N., Le Bivic A., Rougon G., Girault J.A. The glycosylphosphatidyl inositol-anchored adhesion molecule F3/contactin is required for surface transport of paranodin/contactin-associated protein (caspr). J. Cell Biol. 2000, 149:491-502.
    • (2000) J. Cell Biol. , vol.149 , pp. 491-502
    • Faivre-Sarrailh, C.1    Gauthier, F.2    Denisenko-Nehrbass, N.3    Le Bivic, A.4    Rougon, G.5    Girault, J.A.6
  • 49
    • 33846071958 scopus 로고    scopus 로고
    • PGY repeats and N-glycans govern the trafficking of paranodin and its selective association with contactin and neurofascin-155
    • Bonnon C., Bel C., Goutebroze L., Maigret B., Girault J.A., Faivre-Sarrailh C. PGY repeats and N-glycans govern the trafficking of paranodin and its selective association with contactin and neurofascin-155. Mol. Biol. Cell 2007, 18:229-241.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 229-241
    • Bonnon, C.1    Bel, C.2    Goutebroze, L.3    Maigret, B.4    Girault, J.A.5    Faivre-Sarrailh, C.6
  • 50
    • 0028845998 scopus 로고
    • Glycosyltransferase mutants: key to new insights in glycobiology
    • Stanley P., Ioffe E. Glycosyltransferase mutants: key to new insights in glycobiology. FASEB J. 1995, 9:1436-1444.
    • (1995) FASEB J. , vol.9 , pp. 1436-1444
    • Stanley, P.1    Ioffe, E.2
  • 51
    • 40749160804 scopus 로고    scopus 로고
    • Lipid remodeling of GPI-anchored proteins and its function
    • Fujita M., Jigami Y. Lipid remodeling of GPI-anchored proteins and its function. Biochim. Biophys. Acta 2008, 1780:410-420.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 410-420
    • Fujita, M.1    Jigami, Y.2
  • 52
    • 0036695441 scopus 로고    scopus 로고
    • Association of GPI-anchored protein TAG-1 with src-family kinase Lyn in lipid rafts of cerebellar granule cells
    • Kasahara K., Watanabe K., Kozutsumi Y., Oohira A., Yamamoto T., Sanai Y. Association of GPI-anchored protein TAG-1 with src-family kinase Lyn in lipid rafts of cerebellar granule cells. Neurochem. Res. 2002, 27:823-829.
    • (2002) Neurochem. Res. , vol.27 , pp. 823-829
    • Kasahara, K.1    Watanabe, K.2    Kozutsumi, Y.3    Oohira, A.4    Yamamoto, T.5    Sanai, Y.6
  • 53
    • 0037382309 scopus 로고    scopus 로고
    • The adhesion protein TAG-1 has a ganglioside environment in the sphingolipid-enriched membrane domains of neuronal cells in culture
    • Loberto N., Prioni S., Prinetti A., Ottico E., Chigorno V., Karagogeos D., Sonnino S. The adhesion protein TAG-1 has a ganglioside environment in the sphingolipid-enriched membrane domains of neuronal cells in culture. J. Neurochem. 2003, 85:224-233.
    • (2003) J. Neurochem. , vol.85 , pp. 224-233
    • Loberto, N.1    Prioni, S.2    Prinetti, A.3    Ottico, E.4    Chigorno, V.5    Karagogeos, D.6    Sonnino, S.7
  • 54
    • 0031978614 scopus 로고    scopus 로고
    • Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules
    • Ren Q., Bennett V. Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules. J. Neurochem. 1998, 70:1839-1849.
    • (1998) J. Neurochem. , vol.70 , pp. 1839-1849
    • Ren, Q.1    Bennett, V.2
  • 55
    • 1842610973 scopus 로고    scopus 로고
    • Does paranode formation and maintenance require partitioning of neurofascin 155 into lipid rafts?
    • Schafer D.P., Bansal R., Hedstrom K.L., Pfeiffer S.E., Rasband M.N. Does paranode formation and maintenance require partitioning of neurofascin 155 into lipid rafts?. J. Neurosci. 2004, 24:3176-3185.
    • (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
  • 56
    • 0001619084 scopus 로고    scopus 로고
    • VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells
    • Cheong K.H., Zacchetti D., Schneeberger E.E., Simons K. VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells. Proc. Natl. Acad. Sci. USA 1999, 96:6241-6248.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6241-6248
    • Cheong, K.H.1    Zacchetti, D.2    Schneeberger, E.E.3    Simons, K.4
  • 57
    • 4444270899 scopus 로고    scopus 로고
    • The raft-associated protein MAL is required for maintenance of proper axon-glia interactions in the central nervous system
    • Schaeren-Wiemers N., Bonnet A., Erb M., Erne B., Bartsch U., Kern F., Mantei N., Sherman D., Suter U. The raft-associated protein MAL is required for maintenance of proper axon-glia interactions in the central nervous system. J. Cell Biol. 2004, 166:731-742.
    • (2004) J. Cell Biol. , vol.166 , pp. 731-742
    • Schaeren-Wiemers, N.1    Bonnet, A.2    Erb, M.3    Erne, B.4    Bartsch, U.5    Kern, F.6    Mantei, N.7    Sherman, D.8    Suter, U.9
  • 58
    • 0032420901 scopus 로고    scopus 로고
    • Myelin abnormalities in mice deficient in galactocerebroside and sulfatide
    • Dupree J.L., Coetzee T., Suzuki K., Popko B. Myelin abnormalities in mice deficient in galactocerebroside and sulfatide. J. Neurocytol. 1998, 27:649-659.
    • (1998) J. Neurocytol. , vol.27 , pp. 649-659
    • Dupree, J.L.1    Coetzee, T.2    Suzuki, K.3    Popko, B.4
  • 59
    • 0034651041 scopus 로고    scopus 로고
    • Myelin galactolipids: mediators of axon-glia interactions?
    • Popko B. Myelin galactolipids: mediators of axon-glia interactions?. Glia 2000, 29:149-153.
    • (2000) Glia , vol.29 , pp. 149-153
    • Popko, B.1
  • 60
    • 27644558148 scopus 로고    scopus 로고
    • Guillain-Barré syndrome
    • Hughes R.A., Cornblath D.R. Guillain-Barré syndrome. Lancet 2005, 366:1653-1666.
    • (2005) Lancet , vol.366 , pp. 1653-1666
    • Hughes, R.A.1    Cornblath, D.R.2
  • 62
    • 65549163117 scopus 로고    scopus 로고
    • Defects in myelination, paranode organization and Purkinje cell innervation in the ether lipid-deficient mouse cerebellum
    • Teigler A., Komljenovic D., Draguhn A., Gorgas K., Just W.W. Defects in myelination, paranode organization and Purkinje cell innervation in the ether lipid-deficient mouse cerebellum. Hum. Mol. Genet. 2009, 18:1897-1908.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1897-1908
    • Teigler, A.1    Komljenovic, D.2    Draguhn, A.3    Gorgas, K.4    Just, W.W.5
  • 63
    • 33845339567 scopus 로고    scopus 로고
    • The ether lipid-deficient mouse: tracking down plasmalogen functions
    • Gorgas K., Teigler A., Komljenovic D., Just W.W. The ether lipid-deficient mouse: tracking down plasmalogen functions. Biochim. Biophys. Acta 2006, 1763:1511-1526.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1511-1526
    • Gorgas, K.1    Teigler, A.2    Komljenovic, D.3    Just, W.W.4
  • 64
    • 0026579471 scopus 로고
    • F3/F11 cell surface molecule expression in the developing mouse cerebellum is polarized at synaptic sites and within granule cells
    • Faivre-Sarrailh C., Gennarini G., Goridis C., Rougon G. F3/F11 cell surface molecule expression in the developing mouse cerebellum is polarized at synaptic sites and within granule cells. J. Neurosci. 1992, 12:257-267.
    • (1992) J. Neurosci. , vol.12 , pp. 257-267
    • Faivre-Sarrailh, C.1    Gennarini, G.2    Goridis, C.3    Rougon, G.4
  • 65
    • 0030200165 scopus 로고    scopus 로고
    • F3 neuronal adhesion molecule controls outgrowth and fasciculation of cerebellar granule cell neurites: a cell-type specific effect mediated by the Ig-like domains
    • Buttiglione M., Revest J.M., Rougon G., Faivre-Sarrailh C. F3 neuronal adhesion molecule controls outgrowth and fasciculation of cerebellar granule cell neurites: a cell-type specific effect mediated by the Ig-like domains. Mol. Cell. Neurosci. 1996, 8:53-69.
    • (1996) Mol. Cell. Neurosci. , vol.8 , pp. 53-69
    • Buttiglione, M.1    Revest, J.M.2    Rougon, G.3    Faivre-Sarrailh, C.4
  • 66
    • 17344368338 scopus 로고    scopus 로고
    • A functional interaction between the neuronal adhesion molecules TAG-1 and F3 modulates neurite outgrowth and fasciculation of cerebellar granule cells
    • Buttiglione M., Revest J.M., Pavlou O., Karagogeos D., Furley A., Rougon G., Faivre-Sarrailh C. A functional interaction between the neuronal adhesion molecules TAG-1 and F3 modulates neurite outgrowth and fasciculation of cerebellar granule cells. J. Neurosci. 1998, 18:6853-6870.
    • (1998) J. Neurosci. , vol.18 , pp. 6853-6870
    • Buttiglione, M.1    Revest, J.M.2    Pavlou, O.3    Karagogeos, D.4    Furley, A.5    Rougon, G.6    Faivre-Sarrailh, C.7
  • 68
    • 0037022128 scopus 로고    scopus 로고
    • Contactin supports synaptic plasticity associated with hippocampal long-term depression but not potentiation
    • Murai K.K., Misner D., Ranscht B. Contactin supports synaptic plasticity associated with hippocampal long-term depression but not potentiation. Curr. Biol. 2002, 12:181-190.
    • (2002) Curr. Biol. , vol.12 , pp. 181-190
    • Murai, K.K.1    Misner, D.2    Ranscht, B.3
  • 70
    • 33845312662 scopus 로고    scopus 로고
    • Disruption of neurofascin localization reveals early changes preceding demyelination and remyelination in multiple sclerosis
    • Howell O.W., Palser A., Polito A., Melrose S., Zonta B., Scheiermann C., Vora A.J., Brophy P.J., Reynolds R. Disruption of neurofascin localization reveals early changes preceding demyelination and remyelination in multiple sclerosis. Brain 2006, 129:3147-3149.
    • (2006) Brain , vol.129 , pp. 3147-3149
    • Howell, O.W.1    Palser, A.2    Polito, A.3    Melrose, S.4    Zonta, B.5    Scheiermann, C.6    Vora, A.J.7    Brophy, P.J.8    Reynolds, R.9
  • 71
    • 13444274593 scopus 로고    scopus 로고
    • Alteration of the extracellular matrix interferes with raft association of neurofascin in oligodendrocytes. Potential significance for multiple sclerosis?
    • Maier O., van der Heide T., van Dam A.M., Baron W., de Vries H., Hoekstra D. Alteration of the extracellular matrix interferes with raft association of neurofascin in oligodendrocytes. Potential significance for multiple sclerosis?. Mol. Cell. Neurosci. 2005, 28:390-401.
    • (2005) Mol. Cell. Neurosci. , vol.28 , pp. 390-401
    • Maier, O.1    van der Heide, T.2    van Dam, A.M.3    Baron, W.4    de Vries, H.5    Hoekstra, D.6
  • 72
    • 34249079967 scopus 로고    scopus 로고
    • Reduced raft-association of NF155 in active MS-lesions is accompanied by the disruption of the paranodal junction
    • Maier O., Baron W., Hoekstra D. Reduced raft-association of NF155 in active MS-lesions is accompanied by the disruption of the paranodal junction. Glia 2007, 55:885-895.
    • (2007) Glia , vol.55 , pp. 885-895
    • Maier, O.1    Baron, W.2    Hoekstra, D.3
  • 74
    • 66249138823 scopus 로고    scopus 로고
    • The gray aspects of white matter disease in multiple sclerosis
    • Steinman L. The gray aspects of white matter disease in multiple sclerosis. Proc. Natl. Acad. Sci. USA 2009, 106:8302-8307.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8302-8307
    • Steinman, L.1
  • 75
    • 8444247453 scopus 로고    scopus 로고
    • Drosophila contactin, a homolog of vertebrate contactin, is required for septate junction organization and paracellular barrier function
    • Faivre-Sarrailh C., Banerjee S., Li J., Hortsch M., Laval M., Bhat M.A. Drosophila contactin, a homolog of vertebrate contactin, is required for septate junction organization and paracellular barrier function. Development 2004, 131:4931-4942.
    • (2004) Development , vol.131 , pp. 4931-4942
    • Faivre-Sarrailh, C.1    Banerjee, S.2    Li, J.3    Hortsch, M.4    Laval, M.5    Bhat, M.A.6
  • 76
    • 49249124939 scopus 로고    scopus 로고
    • The lateral mobility of cell adhesion molecules is highly restricted at septate junctions in Drosophila
    • Laval M., Bel C., Faivre-Sarrailh C. The lateral mobility of cell adhesion molecules is highly restricted at septate junctions in Drosophila. BMC Cell Biol. 2008, 9:38.
    • (2008) BMC Cell Biol. , vol.9 , pp. 38
    • Laval, M.1    Bel, C.2    Faivre-Sarrailh, C.3
  • 77
    • 0142188562 scopus 로고    scopus 로고
    • Septate and paranodal junctions: kissing cousins
    • Hortsch M., Margolis B. Septate and paranodal junctions: kissing cousins. Trends Cell Biol. 2003, 13:557-561.
    • (2003) Trends Cell Biol. , vol.13 , pp. 557-561
    • Hortsch, M.1    Margolis, B.2
  • 78
    • 0033597141 scopus 로고    scopus 로고
    • Association of sterol- and glycosylphosphatidylinositol-linked proteins with Drosophila raft lipid microdomains
    • Rietveld A., Neutz S., Simons K., Eaton S. Association of sterol- and glycosylphosphatidylinositol-linked proteins with Drosophila raft lipid microdomains. J. Biol. Chem. 1999, 274:12049-12054.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12049-12054
    • Rietveld, A.1    Neutz, S.2    Simons, K.3    Eaton, S.4
  • 79
    • 34548480704 scopus 로고    scopus 로고
    • Light-induced recruitment of INAD-signaling complexes to detergent-resistant lipid rafts in Drosophila photoreceptors
    • Sanxaridis P.D., Cronin M.A., Rawat S.S., Waro G., Acharya U., Tsunoda S. Light-induced recruitment of INAD-signaling complexes to detergent-resistant lipid rafts in Drosophila photoreceptors. Mol. Cell. Neurosci. 2007, 36:36-46.
    • (2007) Mol. Cell. Neurosci. , vol.36 , pp. 36-46
    • Sanxaridis, P.D.1    Cronin, M.A.2    Rawat, S.S.3    Waro, G.4    Acharya, U.5    Tsunoda, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.