메뉴 건너뛰기




Volumn 19, Issue 11, 1999, Pages 4245-4262

Mice deficient for tenascin-R display alterations of the extracellular matrix and decreased axonal conduction velocities in the CNS

Author keywords

Extracellular matrix glycoprotein; HNK 1 carbohydrate; Inhibitory interneurons; Knock out mutation; Node of Ranvier; Parvalbumin; Phosphacan; Sodium channel

Indexed keywords

GLYCOPROTEIN; IMMUNOGLOBULIN; PARVALBUMIN; SODIUM CHANNEL; TENASCIN;

EID: 0033153150     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.19-11-04245.1999     Document Type: Article
Times cited : (216)

References (94)
  • 1
    • 0019507223 scopus 로고
    • A differentiation antigen of human NK and K cells identified by a monoclonal antibody (HNK-1)
    • Abo T, Balch CM (1981) A differentiation antigen of human NK and K cells identified by a monoclonal antibody (HNK-1). J Immunol 127:1024-1029.
    • (1981) J Immunol , vol.127 , pp. 1024-1029
    • Abo, T.1    Balch, C.M.2
  • 2
    • 0028783449 scopus 로고
    • The versican C-type lectin domain recognizes the adhesion protein tenascin-R
    • Aspberg A, Binkert C, Ruoslahti E (1995) The versican C-type lectin domain recognizes the adhesion protein tenascin-R. Proc Natl Acad Sci USA 92:10590-10594.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10590-10594
    • Aspberg, A.1    Binkert, C.2    Ruoslahti, E.3
  • 3
    • 0026529925 scopus 로고
    • Immunohistological localization of tenascin in the developing and lesioned adult mouse optic nerve
    • Bartsch U, Bartsch S, Dörries U, Schachner M (1992a) Immunohistological localization of tenascin in the developing and lesioned adult mouse optic nerve. Eur J Neurosci 4:338-352.
    • (1992) Eur J Neurosci , vol.4 , pp. 338-352
    • Bartsch, U.1    Bartsch, S.2    Dörries, U.3    Schachner, M.4
  • 5
    • 0027669963 scopus 로고
    • Expression of janusin (J1-160/180) in the retina and optic nerve of the developing and adult mouse
    • Bartsch U, Pesheva P, Raff M, Schachner M (1993) Expression of janusin (J1-160/180) in the retina and optic nerve of the developing and adult mouse. Glia 9:57-69.
    • (1993) Glia , vol.9 , pp. 57-69
    • Bartsch, U.1    Pesheva, P.2    Raff, M.3    Schachner, M.4
  • 6
    • 0029382579 scopus 로고
    • Relationship between astrocytic processes and perineuronal nets in rat neocortex
    • Blümcke I, Eggli P, Celio MR (1995) Relationship between astrocytic processes and perineuronal nets in rat neocortex. Glia 15:131-140.
    • (1995) Glia , vol.15 , pp. 131-140
    • Blümcke, I.1    Eggli, P.2    Celio, M.R.3
  • 7
    • 0027231385 scopus 로고
    • Tenascin-X: A novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B
    • Bristow J, Kian Tee M, Gitelmann SE, Mellon SH, Miller WL (1993) Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B. J Cell Biol 122:265-278.
    • (1993) J Cell Biol , vol.122 , pp. 265-278
    • Bristow, J.1    Kian Tee, M.2    Gitelmann, S.E.3    Mellon, S.H.4    Miller, W.L.5
  • 9
    • 0027953823 scopus 로고
    • Cortical areas are revealed by distribution patterns of proteoglycan components and parvalbumin in the mongolian gerbil and rat
    • Brückner G, Seeger G, Brauer K, Härtig W, Kacza J, Bigl V (1994) Cortical areas are revealed by distribution patterns of proteoglycan components and parvalbumin in the mongolian gerbil and rat. Brain Res 658:67-86.
    • (1994) Brain Res , vol.658 , pp. 67-86
    • Brückner, G.1    Seeger, G.2    Brauer, K.3    Härtig, W.4    Kacza, J.5    Bigl, V.6
  • 10
    • 0024644865 scopus 로고
    • Neural cell adhesion molecule F11, homology with fibronectin type III and immunoglobulin type C domains
    • Brümmendorf T, Wolff JM, Frank R, Rathjen FG (1989) Neural cell adhesion 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
  • 11
    • 0027158056 scopus 로고
    • The axonal recognition molecule F11 is a multifunctional protein: Specific domains mediate interactions with Ng-CAM and restrictin
    • Brümmendorf T, Hubert M, Treubert U, Leuschner R, Tárnok A, Rathjen FG (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
  • 13
    • 0028158115 scopus 로고
    • Perineuronal nets: A specialized form of extracellular matrix in the adult nervous system
    • Celio MR, Blümcke I (1994) Perineuronal nets: a specialized form of extracellular matrix in the adult nervous system. Brain Res Rev 19:128-145.
    • (1994) Brain Res Rev , vol.19 , pp. 128-145
    • Celio, M.R.1    Blümcke, I.2
  • 14
    • 0030012213 scopus 로고    scopus 로고
    • The GPI-anchored adhesion molecule F3 induces tyrosine phosphorylation: Involvement of the FNIII repeats
    • Cervello M, Matrange V, Durbec P, Rougon G, Gomez S (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    Matrange, V.2    Durbec, P.3    Rougon, G.4    Gomez, S.5
  • 15
    • 0024407119 scopus 로고
    • An improved culture medium supports development of random bred 1-cell mouse embryos in vitro
    • Chalot CL, Ziomek CA, Bavister BD, Lewis JL, Torres I (1989) An improved culture medium supports development of random bred 1-cell mouse embryos in vitro. J Reprod Fertil 86:679-688.
    • (1989) J Reprod Fertil , vol.86 , pp. 679-688
    • Chalot, C.L.1    Ziomek, C.A.2    Bavister, B.D.3    Lewis, J.L.4    Torres, I.5
  • 16
    • 0026099556 scopus 로고
    • In situ freezing of embryonic stem cells in multiwell plates
    • Chan SY, Evans MJ (1991) In situ freezing of embryonic stem cells in multiwell plates. Trends Genet 7:76.
    • (1991) Trends Genet , vol.7 , pp. 76
    • Chan, S.Y.1    Evans, M.J.2
  • 18
    • 0018333172 scopus 로고
    • A quantitative description of membrane currents in rabbit myelinated nerve
    • Chiu SY, Ritchie JM, Rogart RB, Stagg D (1979) A quantitative description of membrane currents in rabbit myelinated nerve. J Physiol (Lond) 292:149-166.
    • (1979) J Physiol (Lond) , vol.292 , pp. 149-166
    • Chiu, S.Y.1    Ritchie, J.M.2    Rogart, R.B.3    Stagg, D.4
  • 20
    • 0029859733 scopus 로고    scopus 로고
    • Spatial relationship of lectin-labeled extracellular matrix and glutamine synthetase-immunoreactive astrocytes in rat cortical forebrain regions
    • Derouiche A, Härtig W, Brauer K, Brückner G (1996) Spatial relationship of lectin-labeled extracellular matrix and glutamine synthetase-immunoreactive astrocytes in rat cortical forebrain regions. J Anat 189:363-372.
    • (1996) J Anat , vol.189 , pp. 363-372
    • Derouiche, A.1    Härtig, W.2    Brauer, K.3    Brückner, G.4
  • 21
    • 0027497951 scopus 로고
    • Adaptation of a non-radioactive in situ hybridization method to electron microscopy: Detection of tenascin messenger RNAs in mouse cerebellum with digoxygenin-labeled probes and gold-labeled antibodies
    • Dörries U, Bartsch U, Nolte C, Roth J, Schachner M (1993) Adaptation of a non-radioactive in situ hybridization method to electron microscopy: detection of tenascin messenger RNAs in mouse cerebellum with digoxygenin-labeled probes and gold-labeled antibodies. Histochemistry 99:251-262.
    • (1993) Histochemistry , vol.99 , pp. 251-262
    • Dörries, U.1    Bartsch, U.2    Nolte, C.3    Roth, J.4    Schachner, M.5
  • 22
    • 0028694581 scopus 로고
    • Evolution of the tenascin family: Implications for the function of the C-terminal fibrinogen-like domain
    • Erickson HP (1994) Evolution of the tenascin family: implications for the function of the C-terminal fibrinogen-like domain. Perspect Dev Neurobiol 2:9-19.
    • (1994) Perspect Dev Neurobiol , vol.2 , pp. 9-19
    • Erickson, H.P.1
  • 23
    • 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 C, Goridis C, Rougon G (1992) F3/F11 cell surface molecule expression in the developing mouse cerebellum is polarized at synaptic sites and within granule cells. J Neurosci 12:257-267.
    • (1992) J Neurosci , vol.12 , pp. 257-267
    • Faivre-Sarrailh, C.1    Gennarini, C.2    Goridis, C.3    Rougon, G.4
  • 24
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg AP, Vogelstein B (1983) A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem 132:6-13.
    • (1983) Anal Biochem , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 25
    • 0022448291 scopus 로고
    • Molecular specialization of astrocyte processes at nodes of Ranvier in rat optic nerve
    • Ffrench-Constant C, Miller RH, Kruse J, Schachner M, Raff MC (1986) Molecular specialization of astrocyte processes at nodes of Ranvier in rat optic nerve. J Cell Biol 102:844-852.
    • (1986) J Cell Biol , vol.102 , pp. 844-852
    • Ffrench-Constant, C.1    Miller, R.H.2    Kruse, J.3    Schachner, M.4    Raff, M.C.5
  • 28
    • 0024332007 scopus 로고
    • Glycosaminoglycan-related epitopes surrounding different subsets of mammalian central neurons
    • Fujita SC, Tada Y, Murakami F, Hayashi M, Matsumura M (1989) Glycosaminoglycan-related epitopes surrounding different subsets of mammalian central neurons. J Neurosci Res 7:117-130.
    • (1989) J Neurosci Res , vol.7 , pp. 117-130
    • Fujita, S.C.1    Tada, Y.2    Murakami, F.3    Hayashi, M.4    Matsumura, M.5
  • 29
    • 0030962459 scopus 로고    scopus 로고
    • Preprotachykinin A and cholecystokinin mRNAs in tenascin-gene knockout mouse brain
    • Fukamauchi F, Kusakabe M (1997) Preprotachykinin A and cholecystokinin mRNAs in tenascin-gene knockout mouse brain. Neuropeptides 31:199-201.
    • (1997) Neuropeptides , vol.31 , pp. 199-201
    • Fukamauchi, F.1    Kusakabe, M.2
  • 31
    • 0031566255 scopus 로고    scopus 로고
    • Tyrosine hydroxylase activity and its mRNA level in dopaminergic neurons of tenascin gene knockout mouse
    • Fukamauchi F, Mataga N, Wang YJ, Sato S, Yoshiki A, Kusakabe M (1997) Tyrosine hydroxylase activity and its mRNA level in dopaminergic neurons of tenascin gene knockout mouse. Biochem Biophys Res Commun 231:356-359.
    • (1997) Biochem Biophys Res Commun , vol.231 , pp. 356-359
    • Fukamauchi, F.1    Mataga, N.2    Wang, Y.J.3    Sato, S.4    Yoshiki, A.5    Kusakabe, M.6
  • 32
    • 0026075553 scopus 로고
    • Identification of a cDNA clone specific for the oligodendrocyte-derived repulsive extracellular matrix molecule J1-160/180
    • Fuss B, Pott U, Fischer P, Schwab ME, Schachner M (1991) Identification of a cDNA clone specific for the oligodendrocyte-derived repulsive extracellular matrix molecule J1-160/180. J Neurosci Res 29:299-307.
    • (1991) J Neurosci Res , vol.29 , pp. 299-307
    • Fuss, B.1    Pott, U.2    Fischer, P.3    Schwab, M.E.4    Schachner, M.5
  • 33
    • 0027397492 scopus 로고
    • Molecular characterization and in situ messenger RNA localization of the neural recognition molecule J1-160/180: A modular structure similar to tenascin
    • Fuss B, Wintergerst ES, Bartsch U, Schachner M (1993) Molecular characterization and in situ messenger RNA localization of the neural recognition molecule J1-160/180: a modular structure similar to tenascin. J Cell Biol 120:1237-1249.
    • (1993) J Cell Biol , vol.120 , pp. 1237-1249
    • Fuss, B.1    Wintergerst, E.S.2    Bartsch, U.3    Schachner, M.4
  • 34
    • 0024369647 scopus 로고
    • The mouse neuronal cell surface glycoprotein F3: A phosphatidylinositolanchored member of the immunoglobulin superfamily related to chicken contactin
    • Gennarini G, Cibelli G, Rougon G, Mattel MG, Goridis C (1989) The mouse neuronal cell surface glycoprotein F3: a phosphatidylinositolanchored member of the immunoglobulin superfamily related to chicken contactin. J Cell Biol 109:775-788.
    • (1989) J Cell Biol , vol.109 , pp. 775-788
    • Gennarini, G.1    Cibelli, G.2    Rougon, G.3    Mattel, M.G.4    Goridis, C.5
  • 35
    • 0024349202 scopus 로고
    • Presence of the HNK-1 epitope on poly (N-acetyllactosaminyl) oligosaccharides and identification of multiple core proteins in the chondroitin sulfate proteoglycans of the brain
    • Gowda DC, Margolis RU, Margolis RK (1989) Presence of the HNK-1 epitope on poly (N-acetyllactosaminyl) oligosaccharides and identification of multiple core proteins in the chondroitin sulfate proteoglycans of the brain. Biochemistry 28:4468-4474.
    • (1989) Biochemistry , vol.28 , pp. 4468-4474
    • Gowda, D.C.1    Margolis, R.U.2    Margolis, R.K.3
  • 36
    • 0029822205 scopus 로고    scopus 로고
    • Tenascin-Y: A protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue
    • Hagios C, Koch M, Spring J, Chiquet M, Chiquel-Ehrismann R (1996) Tenascin-Y: a protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue. J Cell Biol 134:1499-1512.
    • (1996) J Cell Biol , vol.134 , pp. 1499-1512
    • Hagios, C.1    Koch, M.2    Spring, J.3    Chiquet, M.4    Chiquel-Ehrismann, R.5
  • 37
    • 0027516030 scopus 로고
    • The L2/HNK-1 carbohydrate mediates adhesion of neural cells to laminin
    • Hall H, Liu L, Schachner M, Schmitz B (1993) The L2/HNK-1 carbohydrate mediates adhesion of neural cells to laminin. Eur J Neurosci 5:3442.
    • (1993) Eur J Neurosci , vol.5 , pp. 3442
    • Hall, H.1    Liu, L.2    Schachner, M.3    Schmitz, B.4
  • 38
    • 0029063892 scopus 로고
    • Characterization of a 21 amino acid peptide sequence of the laminin G2 domain that is involved in HNK-1 carbohydrate binding and cell adhesion
    • Hall H, Vorherr T, Schachner M (1995) Characterization of a 21 amino acid peptide sequence of the laminin G2 domain that is involved in HNK-1 carbohydrate binding and cell adhesion. Glycobiology 5:435-441.
    • (1995) Glycobiology , vol.5 , pp. 435-441
    • Hall, H.1    Vorherr, T.2    Schachner, M.3
  • 39
    • 0026730633 scopus 로고
    • Wisteria floribunda agglutinin-labeled nets surround parvalbumin-containing neurons
    • Härtig W, Brauer K, Brückner G (1992) Wisteria floribunda agglutinin-labeled nets surround parvalbumin-containing neurons. NeuroReport 3:869-872.
    • (1992) NeuroReport , vol.3 , pp. 869-872
    • Härtig, W.1    Brauer, K.2    Brückner, G.3
  • 40
    • 0027979719 scopus 로고
    • Chondroitin sulfate proteoglycan-immunoreactivity of lectin-labeled perineuronal nets around parvalbumin-containing neurons
    • Härtig W, Brauer K, Bigl V, Brückner G (1994) Chondroitin sulfate proteoglycan-immunoreactivity of lectin-labeled perineuronal nets around parvalbumin-containing neurons. Brain Res 635:307-311.
    • (1994) Brain Res , vol.635 , pp. 307-311
    • Härtig, W.1    Brauer, K.2    Bigl, V.3    Brückner, G.4
  • 41
    • 0025836349 scopus 로고
    • A computational test of the requirements for conduction in demyelinated axons
    • Hines M, Shrager P (1991) A computational test of the requirements for conduction in demyelinated axons. Restor Neurol Neurosci 3:81-93.
    • (1991) Restor Neurol Neurosci , vol.3 , pp. 81-93
    • Hines, M.1    Shrager, P.2
  • 43
    • 0023150598 scopus 로고
    • HPRT-deficient (Lesch-Nyhan) mouse embryos derived from germline colonization by cultured cells
    • Hooper M, Hardy K, Handsyde A, Hunter S, Monk M (1987) HPRT-deficient (Lesch-Nyhan) mouse embryos derived from germline colonization by cultured cells. Nature 326:292-295.
    • (1987) Nature , vol.326 , pp. 292-295
    • Hooper, M.1    Hardy, K.2    Handsyde, A.3    Hunter, S.4    Monk, M.5
  • 45
    • 0030905035 scopus 로고    scopus 로고
    • Characterization of proteoglycan-containing perineuronal nets by enzymatic treatments of rat brain sections
    • Koppe G, Brückner G, Hartig W, Delpech B, Bigl V (1997) Characterization of proteoglycan-containing perineuronal nets by enzymatic treatments of rat brain sections. J Histochem Cytochem 29:11-20.
    • (1997) J Histochem Cytochem , vol.29 , pp. 11-20
    • Koppe, G.1    Brückner, G.2    Hartig, W.3    Delpech, B.4    Bigl, V.5
  • 46
    • 0021800963 scopus 로고
    • The J1 glycoprotein: A novel nervous system cell adhesion molecule of the L2/HNK-1 family
    • Kruse J, Keilhauer G, Faissner A, Timpl R, Schachner M (1985) The J1 glycoprotein: a novel nervous system cell adhesion molecule of the L2/HNK-1 family. Nature 316:146-148.
    • (1985) Nature , vol.316 , pp. 146-148
    • Kruse, J.1    Keilhauer, G.2    Faissner, A.3    Timpl, R.4    Schachner, M.5
  • 47
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 48
    • 0027235994 scopus 로고
    • Tenascin and extracellular matrix glycoproteins: From promotion to polarization of neurite outgrowth in vitro
    • Lochter A, Schachner M (1993) Tenascin and extracellular matrix glycoproteins: from promotion to polarization of neurite outgrowth in vitro. J Neurosci 13:3986-4000.
    • (1993) J Neurosci , vol.13 , pp. 3986-4000
    • Lochter, A.1    Schachner, M.2
  • 49
    • 0028353611 scopus 로고
    • The extracellular matrix molecule janusin regulates neuronal morphology in a substrate-and culture time-dependent manner
    • Lochter A, Taylor J, Fuss B, Schachner M (1994) The extracellular matrix molecule janusin regulates neuronal morphology in a substrate-and culture time-dependent manner. Eur J Neurosci 6:597-606.
    • (1994) Eur J Neurosci , vol.6 , pp. 597-606
    • Lochter, A.1    Taylor, J.2    Fuss, B.3    Schachner, M.4
  • 50
    • 0026582771 scopus 로고
    • Soybean lectin binding neurons in the visual cortex of the rat contain parvalbumin and are covered by glial nets
    • Luth HJ, Fischer J, Celio MR (1992) Soybean lectin binding neurons in the visual cortex of the rat contain parvalbumin and are covered by glial nets. J Neurocytol 21:211-221.
    • (1992) J Neurocytol , vol.21 , pp. 211-221
    • Luth, H.J.1    Fischer, J.2    Celio, M.R.3
  • 51
    • 0024296027 scopus 로고
    • Disruption of the proto-oncogene int-2 in mouse embryo-derived stem cells: A general strategy for targeting mutations to non-selectable genes
    • Mansour SL, Thomas KR, Capecchi MR (1988) Disruption of the proto-oncogene int-2 in mouse embryo-derived stem cells: a general strategy for targeting mutations to non-selectable genes. Nature 336:348-352.
    • (1988) Nature , vol.336 , pp. 348-352
    • Mansour, S.L.1    Thomas, K.R.2    Capecchi, M.R.3
  • 52
    • 0030339415 scopus 로고    scopus 로고
    • Neurocan and phosphacan, two major nervous tissue-specific chondroitin sulfate proteoglycans
    • Margolis RK, Rauch U, Maurel P, Margolis RU (1996) Neurocan and phosphacan, two major nervous tissue-specific chondroitin sulfate proteoglycans. Perspect Dev Neurobiol 3:273-290.
    • (1996) Perspect Dev Neurobiol , vol.3 , pp. 273-290
    • Margolis, R.K.1    Rauch, U.2    Maurel, P.3    Margolis, R.U.4
  • 53
    • 0025188130 scopus 로고
    • The Wnt-1 (int) proto-oncogene is required for the development of a large region of the mouse brain
    • McMahon AP, Bradley A (1990) The Wnt-1 (int) proto-oncogene is required for the development of a large region of the mouse brain. Cell 62:1073-1085.
    • (1990) Cell , vol.62 , pp. 1073-1085
    • McMahon, A.P.1    Bradley, A.2
  • 54
    • 0029015345 scopus 로고
    • Differential distribution of closely related potassium channels in rat Schwann cells
    • Mi H, Deerinck TJ, Ellisman MH, Schwarz TL (1995) Differential distribution of closely related potassium channels in rat Schwann cells. J Neurosci 15:3761-3774.
    • (1995) J Neurosci , vol.15 , pp. 3761-3774
    • Mi, H.1    Deerinck, T.J.2    Ellisman, M.H.3    Schwarz, T.L.4
  • 55
    • 0028091984 scopus 로고
    • Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules
    • Milev P, Friedlander DR, Sakurai T, Karthikeyan L, Flad M, Margolis RK, Grumet M, Margolis RU (1994) Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules. J Cell Biol 127:1703-1715.
    • (1994) J Cell Biol , vol.127 , pp. 1703-1715
    • Milev, P.1    Friedlander, D.R.2    Sakurai, T.3    Karthikeyan, L.4    Flad, M.5    Margolis, R.K.6    Grumet, M.7    Margolis, R.U.8
  • 56
    • 0032549591 scopus 로고    scopus 로고
    • High affinity binding and overlapping localization of neurocan and phosphacan/protein tyrosine phosphatase-zeta/beta with tenascin-R, amphoterin, and the heparin-binding growth-associated molecule
    • Milev P, Chiba A, Häring M, Rauvala H, Schachner M, Ranscht B, Margolis RK, Margolis RU (1998) High affinity binding and overlapping localization of neurocan and phosphacan/protein tyrosine phosphatase-zeta/beta with tenascin-R, amphoterin, and the heparin-binding growth-associated molecule. J Biol Chem 273:6998-7005.
    • (1998) J Biol Chem , vol.273 , pp. 6998-7005
    • Milev, P.1    Chiba, A.2    Häring, M.3    Rauvala, H.4    Schachner, M.5    Ranscht, B.6    Margolis, R.K.7    Margolis, R.U.8
  • 57
    • 0028824199 scopus 로고
    • Detection of tenascin-C in the nervous system of the tenascin C-mutant mouse
    • Mitrovic N, Schachner M (1995) Detection of tenascin-C in the nervous system of the tenascin C-mutant mouse. J Neurosci Res 42:710-717.
    • (1995) J Neurosci Res , vol.42 , pp. 710-717
    • Mitrovic, N.1    Schachner, M.2
  • 59
    • 0025338819 scopus 로고
    • Oligodendrocyte-derived J1-160/180 extracellular matrix glycoproteins are adhesive or repulsive depending on the partner cell type and time of interaction
    • Morganti MC, Taylor J, Pesheva P, Schachner M (1990) Oligodendrocyte-derived J1-160/180 extracellular matrix glycoproteins are adhesive or repulsive depending on the partner cell type and time of interaction. Exp Neurol 109:98-110.
    • (1990) Exp Neurol , vol.109 , pp. 98-110
    • Morganti, M.C.1    Taylor, J.2    Pesheva, P.3    Schachner, M.4
  • 60
    • 0032519649 scopus 로고    scopus 로고
    • Organization and reorganization of neuromuscular junctions in mice lacking neural cell adhesion molecule, tenascin-C, or fibroblast growth factor-5
    • Moscoso LM, Cremer H, Sanes JR (1998) Organization and reorganization of neuromuscular junctions in mice lacking neural cell adhesion molecule, tenascin-C, or fibroblast growth factor-5. J Neurosci 18:1465-1477.
    • (1998) J Neurosci , vol.18 , pp. 1465-1477
    • Moscoso, L.M.1    Cremer, H.2    Sanes, J.R.3
  • 62
    • 0022657784 scopus 로고
    • Selective cytochemical demonstration of glycoconjugate-containing terminal N-acetylgalactosamine on some brain neurons
    • Nakagawa F, Schulte BA, Spicer SS (1986a) Selective cytochemical demonstration of glycoconjugate-containing terminal N-acetylgalactosamine on some brain neurons. J Comp Neurol 243:280-290.
    • (1986) J Comp Neurol , vol.243 , pp. 280-290
    • Nakagawa, F.1    Schulte, B.A.2    Spicer, S.S.3
  • 63
    • 0022538233 scopus 로고
    • GABAergic neurons of the rodent brain correspond partially with those staining for glycoconjugate with N-acetylgalactosamine
    • Nakagawa F, Schulte BA, Wu JY, Spicer SS (1986b) GABAergic neurons of the rodent brain correspond partially with those staining for glycoconjugate with N-acetylgalactosamine. J Neurocytol 15:389-396.
    • (1986) J Neurocytol , vol.15 , pp. 389-396
    • Nakagawa, F.1    Schulte, B.A.2    Wu, J.Y.3    Spicer, S.S.4
  • 64
    • 0023227016 scopus 로고
    • Postnatal appearance of glycoconjugate with terminal N-acetylgalactosamine on the surface of selected neurons in mouse brain
    • Nakagawa F, Schulte BA, Wu JY, Spicer SS (1987) Postnatal appearance of glycoconjugate with terminal N-acetylgalactosamine on the surface of selected neurons in mouse brain. Dev Neurosci 9:53-60.
    • (1987) Dev Neurosci , vol.9 , pp. 53-60
    • Nakagawa, F.1    Schulte, B.A.2    Wu, J.Y.3    Spicer, S.S.4
  • 65
    • 0026633247 scopus 로고
    • The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs
    • Nörenberg U, Wille H, Wolff JM, Frank R, Rathjen FG (1992) The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs. Neuron 8:849-863.
    • (1992) Neuron , vol.8 , pp. 849-863
    • Nörenberg, U.1    Wille, H.2    Wolff, J.M.3    Frank, R.4    Rathjen, F.G.5
  • 66
    • 0028805468 scopus 로고
    • The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum
    • Olive S, Dubois C, Schachner M, Rougon G (1995) The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and 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
  • 68
    • 0024424947 scopus 로고
    • J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates for cell adhesion
    • Pesheva P, Spiess E, Schachner M (1989) J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates for cell adhesion. J Cell Biol 109:1765-1778.
    • (1989) J Cell Biol , vol.109 , pp. 1765-1778
    • Pesheva, P.1    Spiess, E.2    Schachner, M.3
  • 69
    • 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 (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    Gennarini, G.2    Goridis, C.3    Schachner, M.4
  • 70
    • 0030919911 scopus 로고    scopus 로고
    • Tenascin-R is an intrinsic autocrine factor for oligodendrocyte differentiation and promotes cell adhesion by sulfatide-mediated mechanism
    • Pesheva P, Gloor S, Schachner M, Probstmeier R (1997) Tenascin-R is an intrinsic autocrine factor for oligodendrocyte differentiation and promotes cell adhesion by sulfatide-mediated mechanism. J Neurosci 17:4642-4651.
    • (1997) J Neurosci , vol.17 , pp. 4642-4651
    • Pesheva, P.1    Gloor, S.2    Schachner, M.3    Probstmeier, R.4
  • 72
    • 0023424909 scopus 로고
    • Myelin-associated glycoprotein, a member of the L2/HNK-1 family of neural cell adhesion molecules, is involved in neuronoligodendrocyte and oligodendrocyte-oligodendrocyte interaction
    • Poltorak M, Sadoul R, Keilhauer G, Landa C, Fahrig T, Schachner M (1987) Myelin-associated glycoprotein, a member of the L2/HNK-1 family of neural cell adhesion molecules, is involved in neuronoligodendrocyte and oligodendrocyte-oligodendrocyte interaction. J Cell Biol 105:1893-1899.
    • (1987) J Cell Biol , vol.105 , pp. 1893-1899
    • Poltorak, M.1    Sadoul, R.2    Keilhauer, G.3    Landa, C.4    Fahrig, T.5    Schachner, M.6
  • 77
    • 0028704499 scopus 로고
    • The perplexing multifunctionality of janusin, a tenascin-related molecule
    • Schachner M, Taylor J, Bartsch U, Pesheva P (1994) The perplexing multifunctionality of janusin, a tenascin-related molecule. Perspect Dev Neurobiol 2:33-41.
    • (1994) Perspect Dev Neurobiol , vol.2 , pp. 33-41
    • Schachner, M.1    Taylor, J.2    Bartsch, U.3    Pesheva, P.4
  • 78
    • 0028156815 scopus 로고
    • Mapping of perineuronal nets in the rat brain stained by colloidal iron hydroxide histochemistry and lectin cytochemistry
    • Seeger G, Brauer K, Härtig W, Brückner G (1994) Mapping of perineuronal nets in the rat brain stained by colloidal iron hydroxide histochemistry and lectin cytochemistry. Neuroscience 58:371-388.
    • (1994) Neuroscience , vol.58 , pp. 371-388
    • Seeger, G.1    Brauer, K.2    Härtig, W.3    Brückner, G.4
  • 80
    • 0026023289 scopus 로고
    • Targeted disruption of the c-scr proto-oncogene leads to osteopetrosis in mice
    • Soriano P, Montgomery C, Geske R, Bradley A (1991) Targeted disruption of the c-scr proto-oncogene leads to osteopetrosis in mice. Cell 64:693-702.
    • (1991) Cell , vol.64 , pp. 693-702
    • Soriano, P.1    Montgomery, C.2    Geske, R.3    Bradley, A.4
  • 81
    • 7344259971 scopus 로고    scopus 로고
    • Interaction between neuronal voltage gated sodium channels and the extracellular matrix protein tenascin
    • Srinivasan J, Laeng P, Schachner M, Catterall WA (1997) Interaction between neuronal voltage gated sodium channels and the extracellular matrix protein tenascin. Soc Neurosci Abstr 23:909.
    • (1997) Soc Neurosci Abstr , vol.23 , pp. 909
    • Srinivasan, J.1    Laeng, P.2    Schachner, M.3    Catterall, W.A.4
  • 82
    • 0025728907 scopus 로고
    • Compound action potential of nerve recorded by suction electrode: A theoretical and experimental analysis
    • Stys PK, Ransom BR, Waxman SG (1991) Compound action potential of nerve recorded by suction electrode: a theoretical and experimental analysis. Brain Res 546:18-32.
    • (1991) Brain Res , vol.546 , pp. 18-32
    • Stys, P.K.1    Ransom, B.R.2    Waxman, S.G.3
  • 83
    • 0027190321 scopus 로고
    • Influence of janusin and tenascin on growth cone behaviour in vitro. 3
    • Taylor J, Pesheva P, Schachner M (1993) Influence of janusin and tenascin on growth cone behaviour in vitro. 3 Neurosci Res 35:347-362.
    • (1993) Neurosci Res , vol.35 , pp. 347-362
    • Taylor, J.1    Pesheva, P.2    Schachner, M.3
  • 84
    • 0028820205 scopus 로고
    • Tenascin-C mRNA is expressed in cranial neural crest cells, in some placodal derivatives, and in discrete domains of the embryonic zebrafish brain
    • Tongiorgi E, Bernhardt RR, Zinn K, Schachner M (1995) Tenascin-C mRNA is expressed in cranial neural crest cells, in some placodal derivatives, and in discrete domains of the embryonic zebrafish brain. J Neurobiol 28:391-407.
    • (1995) J Neurobiol , vol.28 , pp. 391-407
    • Tongiorgi, E.1    Bernhardt, R.R.2    Zinn, K.3    Schachner, M.4
  • 85
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 87
  • 88
    • 0027401599 scopus 로고
    • Localization of janusin mRNA in the central nervous system of the developing and adult mouse
    • Wintergerst ES, Fuss B, Bartsch U (1993) Localization of janusin mRNA in the central nervous system of the developing and adult mouse. Eur J Neurosci 5:299-310.
    • (1993) Eur J Neurosci , vol.5 , pp. 299-310
    • Wintergerst, E.S.1    Fuss, B.2    Bartsch, U.3
  • 89
    • 0029978087 scopus 로고    scopus 로고
    • Distinct functions of recombinant tenascin-R domains on neuronal cell adhesion, growth cone guidance, neuronal polarity, and interaction with the neuronal immunoglobulin superfamily adhesion molecule F3/11
    • Xiao ZC, Taylor J, Montag D, Rougon G, Schachner M (1996) Distinct functions of recombinant tenascin-R domains on neuronal cell adhesion, growth cone guidance, neuronal polarity, and interaction with the neuronal immunoglobulin superfamily adhesion molecule F3/11. Eur J Neurosci 8:766-782.
    • (1996) Eur J Neurosci , vol.8 , pp. 766-782
    • Xiao, Z.C.1    Taylor, J.2    Montag, D.3    Rougon, G.4    Schachner, M.5
  • 90
    • 0031449805 scopus 로고    scopus 로고
    • Isolation of a tenascin-R receptor from mouse brain membranes: A phosphacan-related chondroitin sulfate glycoproteoglycan
    • Xiao ZC, Bartsch U, Margolis RK, Margolis RU, Rougon G, Montag D, Schachner M (1997) Isolation of a tenascin-R receptor from mouse brain membranes: a phosphacan-related chondroitin sulfate glycoproteoglycan. J Biol Chem 272:32092-32101.
    • (1997) J Biol Chem , vol.272 , pp. 32092-32101
    • Xiao, Z.C.1    Bartsch, U.2    Margolis, R.K.3    Margolis, R.U.4    Rougon, G.5    Montag, D.6    Schachner, M.7
  • 91
    • 0032524781 scopus 로고    scopus 로고
    • Defasciculation of neurites is mediated by tenascin-R and its neuronal receptor F3/11
    • Xiao ZC, Revest JM, Laeng P, Rougon G, Schachner M, Montag D (1998) Defasciculation of neurites is mediated by tenascin-R and its neuronal receptor F3/11. J Neurosci Res 52:390-404.
    • (1998) J Neurosci Res , vol.52 , pp. 390-404
    • Xiao, Z.C.1    Revest, J.M.2    Laeng, P.3    Rougon, G.4    Schachner, M.5    Montag, D.6
  • 92
    • 0023615165 scopus 로고
    • Distribution of glucuronic acid-and-sulfate-containing glycoproteins in the central nervous system of the adult mouse
    • Yamamoto M, Marshall P, Hemmendinger LM, Boyer AB, Caviness VS (1988) Distribution of glucuronic acid-and-sulfate-containing glycoproteins in the central nervous system of the adult mouse. J Neurosci Res 5:273-298.
    • (1988) J Neurosci Res , vol.5 , pp. 273-298
    • Yamamoto, M.1    Marshall, P.2    Hemmendinger, L.M.3    Boyer, A.B.4    Caviness, V.S.5
  • 93
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Vanish-Perron C, Vieira J, Messing J (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Vanish-Perron, C.1    Vieira, J.2    Messing, J.3
  • 94
    • 0029165973 scopus 로고
    • The glypiated neuronal cell adhesion molecule contactin/F11 complexes with src-family protein tyrosine kinase Fyn
    • Zisch AH, D'Alessandri L, Amrein K, Ranscht B, Winterhalter K, Vaughan L (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.5    Vaughan, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.