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Volumn 54, Issue 1, 2007, Pages 1-18

The role of chondroitin sulfate proteoglycans in regeneration and plasticity in the central nervous system

Author keywords

Axon regeneration; Central nervous system injury; Chondroitin sulfate proteoglycans; Chondroitinase; Perineuronal nets; Plasticity

Indexed keywords

AGGRECAN; BREVICAN; GLYCOSAMINOGLYCAN; N ACETYLGALACTOSAMINE 4 SULFATASE; NEUROCAN; PROTEOCHONDROITIN SULFATE; VERSICAN;

EID: 33947645277     PISSN: 01650173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainresrev.2006.09.006     Document Type: Review
Times cited : (484)

References (212)
  • 3
    • 0032529346 scopus 로고    scopus 로고
    • Tenascin-R is antiadhesive for activated microglia that induce downregulation of the protein after peripheral nerve injury: a new role in neuronal protection
    • Angelov D.N., Walther M., Streppel M., Guntinas-Lichius O., Neiss W.F., Probstmeier R., and Pesheva P. Tenascin-R is antiadhesive for activated microglia that induce downregulation of the protein after peripheral nerve injury: a new role in neuronal protection. J. Neurosci. 18 (1998) 6218-6229
    • (1998) J. Neurosci. , vol.18 , pp. 6218-6229
    • Angelov, D.N.1    Walther, M.2    Streppel, M.3    Guntinas-Lichius, O.4    Neiss, W.F.5    Probstmeier, R.6    Pesheva, P.7
  • 4
    • 0032509720 scopus 로고    scopus 로고
    • Cortical distribution of neurofibrillary tangles in Alzheimer's disease matches the pattern of neurons that retain their capacity of plastic remodelling in the adult brain
    • Arendt T., Bruckner M.K., Gertz H.-J., and Marcova L. Cortical distribution of neurofibrillary tangles in Alzheimer's disease matches the pattern of neurons that retain their capacity of plastic remodelling in the adult brain. Neuroscience 83 (1998) 991-1002
    • (1998) Neuroscience , vol.83 , pp. 991-1002
    • Arendt, T.1    Bruckner, M.K.2    Gertz, H.-J.3    Marcova, L.4
  • 5
    • 0029278764 scopus 로고
    • On the existence of a cartilage-like proteoglycan and link proteins in the central nervous system
    • Asher R.A., Scheibe R.J., Keiser H.D., and Bignami A. On the existence of a cartilage-like proteoglycan and link proteins in the central nervous system. Glia 13 (1995) 294-308
    • (1995) Glia , vol.13 , pp. 294-308
    • Asher, R.A.1    Scheibe, R.J.2    Keiser, H.D.3    Bignami, A.4
  • 8
    • 0030963839 scopus 로고    scopus 로고
    • The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety
    • Aspberg A., Miura R., Bourdoulous S., Shimonaka M., Heinegard D., Schachner M., Ruoslahti E., and Yamaguchi Y. The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 10116-10121
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 10116-10121
    • Aspberg, A.1    Miura, R.2    Bourdoulous, S.3    Shimonaka, M.4    Heinegard, D.5    Schachner, M.6    Ruoslahti, E.7    Yamaguchi, Y.8
  • 9
    • 27944510242 scopus 로고    scopus 로고
    • Loss of perineuronal net N-acetylgalactosamine in Alzheimer's disease
    • Baig S., Wilcock G.K., and Love S. Loss of perineuronal net N-acetylgalactosamine in Alzheimer's disease. Acta Neuropathol. (Berl.) 110 (2005) 393-401
    • (2005) Acta Neuropathol. (Berl.) , vol.110 , pp. 393-401
    • Baig, S.1    Wilcock, G.K.2    Love, S.3
  • 10
    • 0033778942 scopus 로고    scopus 로고
    • Proteoglycans in the developing brain: new conceptual insights for old proteins
    • Bandtlow C.E., and Zimmermann D.R. Proteoglycans in the developing brain: new conceptual insights for old proteins. Physiol. Rev. 80 (2000) 1267-1290
    • (2000) Physiol. Rev. , vol.80 , pp. 1267-1290
    • Bandtlow, C.E.1    Zimmermann, D.R.2
  • 11
  • 13
    • 0030724057 scopus 로고    scopus 로고
    • HIV-I induced destruction of neocortical extracellular matrix components in AIDS victims
    • Belichenko P.V., Miklossy J., and Celio M.R. HIV-I induced destruction of neocortical extracellular matrix components in AIDS victims. Neurobiol. Dis. 4 (1997) 301-310
    • (1997) Neurobiol. Dis. , vol.4 , pp. 301-310
    • Belichenko, P.V.1    Miklossy, J.2    Celio, M.R.3
  • 14
    • 0032885694 scopus 로고    scopus 로고
    • Early destruction of the extracellular matrix around parvalbumin-immunoreactive interneurons in Creutzfeldt-Jakob disease
    • Belichenko P.V., Miklossy J., Belser B., Budka H., and Celio M.R. Early destruction of the extracellular matrix around parvalbumin-immunoreactive interneurons in Creutzfeldt-Jakob disease. Neurobiol. Dis. 6 (1999) 269-279
    • (1999) Neurobiol. Dis. , vol.6 , pp. 269-279
    • Belichenko, P.V.1    Miklossy, J.2    Belser, B.3    Budka, H.4    Celio, M.R.5
  • 17
    • 10444274980 scopus 로고    scopus 로고
    • Extracellular matrix and visual cortical plasticity: freeing the synapse
    • Berardi N., Pizzorusso T., and Maffei L. Extracellular matrix and visual cortical plasticity: freeing the synapse. Neuron 44 (2004) 905-908
    • (2004) Neuron , vol.44 , pp. 905-908
    • Berardi, N.1    Pizzorusso, T.2    Maffei, L.3
  • 18
    • 4544241046 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor controls functional differentiation and microcircuit formation of selectively isolated fast-spiking GABAergic interneurons
    • Berghuis P., Dobszay M.B., Sousa K.M., Schulte G., Mager P.P., Hartig W., Gorcs T.J., Zilberter Y., Ernfors P., and Harkany T. Brain-derived neurotrophic factor controls functional differentiation and microcircuit formation of selectively isolated fast-spiking GABAergic interneurons. Eur. J. Neurosci. 20 (2004) 1290-1306
    • (2004) Eur. J. Neurosci. , vol.20 , pp. 1290-1306
    • Berghuis, P.1    Dobszay, M.B.2    Sousa, K.M.3    Schulte, G.4    Mager, P.P.5    Hartig, W.6    Gorcs, T.J.7    Zilberter, Y.8    Ernfors, P.9    Harkany, T.10
  • 19
    • 0030065620 scopus 로고    scopus 로고
    • Immunohistochemical mapping of perineuronal nets containing chondroitin unsulfated proteoglycan in the rat central nervous system
    • Bertolotto A., Manzardo E., and Guglielmone R. Immunohistochemical mapping of perineuronal nets containing chondroitin unsulfated proteoglycan in the rat central nervous system. Cell Tissue Res. 283 (1996) 283-295
    • (1996) Cell Tissue Res. , vol.283 , pp. 283-295
    • Bertolotto, A.1    Manzardo, E.2    Guglielmone, R.3
  • 20
    • 0342684579 scopus 로고    scopus 로고
    • Structural alterations and changes in cytoskeletal proteins and proteoglycans after focal cortical ischemia
    • Bidmon H.-J., Jancsik V., Schleicher A., Hagemann G., Witte O.W., Woodhams P., and Zilles K. Structural alterations and changes in cytoskeletal proteins and proteoglycans after focal cortical ischemia. Neuroscience 82 (1997) 397-420
    • (1997) Neuroscience , vol.82 , pp. 397-420
    • Bidmon, H.-J.1    Jancsik, V.2    Schleicher, A.3    Hagemann, G.4    Witte, O.W.5    Woodhams, P.6    Zilles, K.7
  • 21
    • 0027389847 scopus 로고
    • Versican, a hyaluronate-binding proteoglycan of embryonal precartilaginous mesenchyma, is mainly expressed postnatally in rat brain
    • Bignami A., Perides G., and Rahemtulla F. Versican, a hyaluronate-binding proteoglycan of embryonal precartilaginous mesenchyma, is mainly expressed postnatally in rat brain. J. Neurosci. Res. 34 (1993) 97-106
    • (1993) J. Neurosci. Res. , vol.34 , pp. 97-106
    • Bignami, A.1    Perides, G.2    Rahemtulla, F.3
  • 22
    • 0028338551 scopus 로고
    • Link protein is ubiquitously expressed in non-cartilaginous tissues where it enhances and stabilizes the interaction of proteoglycans with hyaluronic acid
    • Binette F., Cravens J., Kahoussi B., Haudenschild D.R., and Goetinck P.F. Link protein is ubiquitously expressed in non-cartilaginous tissues where it enhances and stabilizes the interaction of proteoglycans with hyaluronic acid. J. Biol. Chem. 269 (1994) 19116-19122
    • (1994) J. Biol. Chem. , vol.269 , pp. 19116-19122
    • Binette, F.1    Cravens, J.2    Kahoussi, B.3    Haudenschild, D.R.4    Goetinck, P.F.5
  • 23
  • 25
    • 0030814682 scopus 로고    scopus 로고
    • Parvalbumin-immunoreactive neurons in the hippocampal formation of Alzheimer's diseased brain
    • Brady D.R., and Mufson E.J. Parvalbumin-immunoreactive neurons in the hippocampal formation of Alzheimer's diseased brain. Neuroscience 80 (1997) 1113-1125
    • (1997) Neuroscience , vol.80 , pp. 1113-1125
    • Brady, D.R.1    Mufson, E.J.2
  • 28
    • 0027953823 scopus 로고
    • Cortical areas are revealed by distribution patterns of proteoglycan components and parvalbumin in the Mongolian gerbil and rat
    • Bruckner G., Seeger G., Brauer K., Hartig W., Kacza J., and Bigl V. Cortical areas are revealed by distribution patterns of proteoglycan components and parvalbumin in the Mongolian gerbil and rat. Brain Res. 658 (1994) 67-86
    • (1994) Brain Res. , vol.658 , pp. 67-86
    • Bruckner, G.1    Seeger, G.2    Brauer, K.3    Hartig, W.4    Kacza, J.5    Bigl, V.6
  • 29
    • 0029973846 scopus 로고    scopus 로고
    • Extracellular matrix organization in various regions of rat brain grey matter
    • Bruckner G., Hartig W., Kacza J., Seeger J., Welt K., and Brauer K. Extracellular matrix organization in various regions of rat brain grey matter. J. Neurocytol. 25 (1996) 333-346
    • (1996) J. Neurocytol. , vol.25 , pp. 333-346
    • Bruckner, G.1    Hartig, W.2    Kacza, J.3    Seeger, J.4    Welt, K.5    Brauer, K.6
  • 30
    • 0031875189 scopus 로고    scopus 로고
    • Acute and long-lasting changes in extracellular-matrix chondroitin-sulphate proteoglycans induced by injection of chondroitinase ABC in the adult rat brain
    • Bruckner G., Bringmann A., Hartig W., Koppe G., Delpech B., and Brauer K. Acute and long-lasting changes in extracellular-matrix chondroitin-sulphate proteoglycans induced by injection of chondroitinase ABC in the adult rat brain. Exp. Brain Res. 121 (1998) 300-310
    • (1998) Exp. Brain Res. , vol.121 , pp. 300-310
    • Bruckner, G.1    Bringmann, A.2    Hartig, W.3    Koppe, G.4    Delpech, B.5    Brauer, K.6
  • 31
    • 0343939111 scopus 로고    scopus 로고
    • Cortical areas abundant in extracellular matrix chondroitin sulphate proteoglycans are less affected by cytoskeletal changes in Alzheimer's disease
    • Bruckner G., Hausen D., Hartig W., Drlicek M., Arendt T., and Brauer K. Cortical areas abundant in extracellular matrix chondroitin sulphate proteoglycans are less affected by cytoskeletal changes in Alzheimer's disease. Neuroscience 92 (1999) 791-805
    • (1999) Neuroscience , vol.92 , pp. 791-805
    • Bruckner, G.1    Hausen, D.2    Hartig, W.3    Drlicek, M.4    Arendt, T.5    Brauer, K.6
  • 33
    • 4944261474 scopus 로고    scopus 로고
    • Perineuronal nets characterized by vital labelling, confocal and electron microscopy in organotypic slice cultures of rat parietal cortex and hippocampus
    • Bruckner G., Kacza J., and Grosche J. Perineuronal nets characterized by vital labelling, confocal and electron microscopy in organotypic slice cultures of rat parietal cortex and hippocampus. J. Mol. Histol. 35 (2004) 115-122
    • (2004) J. Mol. Histol. , vol.35 , pp. 115-122
    • Bruckner, G.1    Kacza, J.2    Grosche, J.3
  • 34
    • 0035837290 scopus 로고    scopus 로고
    • Modification of extracellular matrix by enzymatic removal of chondroitin sulfate and by lack of tenascin-R differentially affects several forms of synaptic plasticity in the hippocampus
    • Bukalo O., Schachner M., and Dityatev A. Modification of extracellular matrix by enzymatic removal of chondroitin sulfate and by lack of tenascin-R differentially affects several forms of synaptic plasticity in the hippocampus. Neuroscience 104 (2001) 359-369
    • (2001) Neuroscience , vol.104 , pp. 359-369
    • Bukalo, O.1    Schachner, M.2    Dityatev, A.3
  • 35
    • 33947660639 scopus 로고    scopus 로고
    • Cafferty, W.B., Bradbury, E.J., Jones, M., Lidierth, M., McMahon, S.B. Chondroitinase ABC-mediated restitution of electrophysiological function after deafferentation. Program No. 619.3.[2004 Abstract Viewer/Itinerary Planner.]. 2004. Washington, DC: Society for Neuroscience, 2004. Online. Ref Type: Conference Proceeding.
  • 36
    • 14744306466 scopus 로고    scopus 로고
    • Chondroitinase ABCI improves locomotion and bladder function following contusion injury of the rat spinal cord
    • Caggiano A.O., Zimber M.P., Ganguly A., Blight A.R., and Gruskin E.A. Chondroitinase ABCI improves locomotion and bladder function following contusion injury of the rat spinal cord. J. Neurotrauma 22 (2005) 226-239
    • (2005) J. Neurotrauma , vol.22 , pp. 226-239
    • Caggiano, A.O.1    Zimber, M.P.2    Ganguly, A.3    Blight, A.R.4    Gruskin, E.A.5
  • 37
    • 0037307933 scopus 로고    scopus 로고
    • Plasticity of cortical projections after stroke
    • Carmichael S.T. Plasticity of cortical projections after stroke. Neuroscientist 9 (2003) 64-75
    • (2003) Neuroscientist , vol.9 , pp. 64-75
    • Carmichael, S.T.1
  • 38
    • 18144416945 scopus 로고    scopus 로고
    • Growth-associated gene expression after stroke: evidence for a growth-promoting region in peri-infarct cortex
    • Carmichael S.T., Archibeque I., Luke L., Nolan T., Momiy J., and Li S. Growth-associated gene expression after stroke: evidence for a growth-promoting region in peri-infarct cortex. Exp. Neurol. 193 (2005) 291-311
    • (2005) Exp. Neurol. , vol.193 , pp. 291-311
    • Carmichael, S.T.1    Archibeque, I.2    Luke, L.3    Nolan, T.4    Momiy, J.5    Li, S.6
  • 39
    • 13844275355 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycans in neural development and regeneration
    • Carulli D., Laabs T., Geller H.M., and Fawcett J.W. Chondroitin sulfate proteoglycans in neural development and regeneration. Curr. Opin. Neurobiol. 15 (2005) 252
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 252
    • Carulli, D.1    Laabs, T.2    Geller, H.M.3    Fawcett, J.W.4
  • 41
    • 0028158115 scopus 로고
    • Perineuronal nets-a specialized form of extracellular matrix in the adult nervous system
    • Celio M.R., and Blumcke I. Perineuronal nets-a specialized form of extracellular matrix in the adult nervous system. Brain Res. Brain Res. Rev. 19 (1994) 128-145
    • (1994) Brain Res. Brain Res. Rev. , vol.19 , pp. 128-145
    • Celio, M.R.1    Blumcke, I.2
  • 42
    • 0027331683 scopus 로고
    • 'Perineuronal nets' around cortical interneurons expressing parvalbumin are rich in tenascin
    • Celio M.R., and Chiquet-Ehrismann R. 'Perineuronal nets' around cortical interneurons expressing parvalbumin are rich in tenascin. Neurosci. Lett. 162 (1993) 137-140
    • (1993) Neurosci. Lett. , vol.162 , pp. 137-140
    • Celio, M.R.1    Chiquet-Ehrismann, R.2
  • 44
    • 1342268329 scopus 로고    scopus 로고
    • Chondroitinase ABC enhances axonal regrowth through Schwann cell-seeded guidance channels after spinal cord injury
    • Chau C.H., Shum D.K., Li H., Pei J., Lui Y.Y., Wirthlin L., Chan Y.S., and Xu X.M. Chondroitinase ABC enhances axonal regrowth through Schwann cell-seeded guidance channels after spinal cord injury. FASEB J. 18 (2004) 194-196
    • (2004) FASEB J. , vol.18 , pp. 194-196
    • Chau, C.H.1    Shum, D.K.2    Li, H.3    Pei, J.4    Lui, Y.Y.5    Wirthlin, L.6    Chan, Y.S.7    Xu, X.M.8
  • 45
    • 0037030726 scopus 로고    scopus 로고
    • Nervous system reorganization following injury
    • Chen R., Cohen L.G., and Hallett M. Nervous system reorganization following injury. Neuroscience 111 (2002) 761-773
    • (2002) Neuroscience , vol.111 , pp. 761-773
    • Chen, R.1    Cohen, L.G.2    Hallett, M.3
  • 46
    • 0032561202 scopus 로고    scopus 로고
    • The DSD-1 carbohydrate epitope depends on sulfation, correlates with chondroitin sulfate D motifs, and is sufficient to promote neurite outgrowth
    • Clement A.M., Nadanaka S., Masayama K., Mandl C., Sugahara K., and Faissner A. The DSD-1 carbohydrate epitope depends on sulfation, correlates with chondroitin sulfate D motifs, and is sufficient to promote neurite outgrowth. J. Biol. Chem. 273 (1998) 28444-28453
    • (1998) J. Biol. Chem. , vol.273 , pp. 28444-28453
    • Clement, A.M.1    Nadanaka, S.2    Masayama, K.3    Mandl, C.4    Sugahara, K.5    Faissner, A.6
  • 47
    • 0033575470 scopus 로고    scopus 로고
    • Chondroitin sulfate E promotes neurite outgrowth of rat embryonic day 18 hippocampal neurons
    • Clement A.M., Sugahara K., and Faissner A. Chondroitin sulfate E promotes neurite outgrowth of rat embryonic day 18 hippocampal neurons. Neurosci. Lett. 269 (1999) 125-128
    • (1999) Neurosci. Lett. , vol.269 , pp. 125-128
    • Clement, A.M.1    Sugahara, K.2    Faissner, A.3
  • 48
    • 23444436745 scopus 로고    scopus 로고
    • Degradation of chondroitin sulfate proteoglycans induces sprouting of intact Purkinje axons in the cerebellum of the adult rat
    • Corvetti L., and Rossi F. Degradation of chondroitin sulfate proteoglycans induces sprouting of intact Purkinje axons in the cerebellum of the adult rat. J. Neurosci. 25 (2005) 7150-7158
    • (2005) J. Neurosci. , vol.25 , pp. 7150-7158
    • Corvetti, L.1    Rossi, F.2
  • 50
    • 1642320994 scopus 로고    scopus 로고
    • Decorin suppresses neurocan, brevican, phosphacan and NG2 expression and promotes axon growth across adult rat spinal cord injuries
    • Davies J.E., Tang X., Denning J.W., Archibald S.J., and Davies S.J.A. Decorin suppresses neurocan, brevican, phosphacan and NG2 expression and promotes axon growth across adult rat spinal cord injuries. Eur. J. Neurosci. 19 (2004) 1226-1242
    • (2004) Eur. J. Neurosci. , vol.19 , pp. 1226-1242
    • Davies, J.E.1    Tang, X.2    Denning, J.W.3    Archibald, S.J.4    Davies, S.J.A.5
  • 51
    • 1842425011 scopus 로고    scopus 로고
    • Alternative splicing in the aggrecan G3 domain influences binding interactions with Tenascin-C and other extracellular matrix proteins
    • Day J.M., Olin A.I., Murdoch A.D., Canfield A., Sasaki T., Timpl R., Hardingham T.E., and Aspberg A. Alternative splicing in the aggrecan G3 domain influences binding interactions with Tenascin-C and other extracellular matrix proteins. J. Biol. Chem. 279 (2004) 12511-12518
    • (2004) J. Biol. Chem. , vol.279 , pp. 12511-12518
    • Day, J.M.1    Olin, A.I.2    Murdoch, A.D.3    Canfield, A.4    Sasaki, T.5    Timpl, R.6    Hardingham, T.E.7    Aspberg, A.8
  • 52
    • 0037113896 scopus 로고    scopus 로고
    • Specific molecular interactions of oversulfated chondroitin sulfate E with various heparin-binding growth factors. Implications as a physiological binding partner in the brain and other tissues
    • Deepa S.S., Umehara Y., Higashiyama S., Itoh N., and Sugahara K. Specific molecular interactions of oversulfated chondroitin sulfate E with various heparin-binding growth factors. Implications as a physiological binding partner in the brain and other tissues. J. Biol. Chem. 277 (2002) 43707-43716
    • (2002) J. Biol. Chem. , vol.277 , pp. 43707-43716
    • Deepa, S.S.1    Umehara, Y.2    Higashiyama, S.3    Itoh, N.4    Sugahara, K.5
  • 53
    • 4444347398 scopus 로고    scopus 로고
    • Chondroitin sulfate chains on Syndecan-1 and Syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct and cooperate with heparan sulfate chains to bind growth factors: a novel function to control binding of midkine, pleiotrophin and basic fibroblast growth factor
    • Deepa S.S., Yamada S., Zako M., Goldberger O., and Sugahara K. Chondroitin sulfate chains on Syndecan-1 and Syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct and cooperate with heparan sulfate chains to bind growth factors: a novel function to control binding of midkine, pleiotrophin and basic fibroblast growth factor. J. Biol. Chem. 279 (2004) 37368-37376
    • (2004) J. Biol. Chem. , vol.279 , pp. 37368-37376
    • Deepa, S.S.1    Yamada, S.2    Zako, M.3    Goldberger, O.4    Sugahara, K.5
  • 54
    • 33745860012 scopus 로고    scopus 로고
    • Composition of perineuronal net extracellular matrix in rat brain: a different disaccharide composition for the net-associated proteoglycans
    • Deepa S.S., Carulli D., Galtrey C., Rhodes K., Fukuda J., Mikami T., Sugahara K., and Fawcett J.W. Composition of perineuronal net extracellular matrix in rat brain: a different disaccharide composition for the net-associated proteoglycans. J. Biol. Chem. 281 (2006) 17789-17800
    • (2006) J. Biol. Chem. , vol.281 , pp. 17789-17800
    • Deepa, S.S.1    Carulli, D.2    Galtrey, C.3    Rhodes, K.4    Fukuda, J.5    Mikami, T.6    Sugahara, K.7    Fawcett, J.W.8
  • 56
    • 0036373890 scopus 로고    scopus 로고
    • Sprouting in the hippocampus after entorhinal cortex lesion is layer-specific but not translaminar: which molecules may be involved?
    • Deller T., Haas C.A., and Frotscher M. Sprouting in the hippocampus after entorhinal cortex lesion is layer-specific but not translaminar: which molecules may be involved?. Restor. Neurol. Neurosci. 19 (2001) 159-167
    • (2001) Restor. Neurol. Neurosci. , vol.19 , pp. 159-167
    • Deller, T.1    Haas, C.A.2    Frotscher, M.3
  • 57
    • 18044383585 scopus 로고    scopus 로고
    • Semaphorin 3A displays a punctate distribution on the surface of neuronal cells and interacts with proteoglycans in the extracellular matrix
    • De Wit J., De Winter F., Klooster J., and Verhaagen J. Semaphorin 3A displays a punctate distribution on the surface of neuronal cells and interacts with proteoglycans in the extracellular matrix. Mol. Cell. Neurosci. 29 (2005) 40-55
    • (2005) Mol. Cell. Neurosci. , vol.29 , pp. 40-55
    • De Wit, J.1    De Winter, F.2    Klooster, J.3    Verhaagen, J.4
  • 58
    • 0030296714 scopus 로고    scopus 로고
    • Regenerative failure: a potential mechanism for neuritic dystrophy in Alzheimer's disease
    • DeWitt D.A., and Silver J. Regenerative failure: a potential mechanism for neuritic dystrophy in Alzheimer's disease. Exp. Neurol. 142 (1996) 103-110
    • (1996) Exp. Neurol. , vol.142 , pp. 103-110
    • DeWitt, D.A.1    Silver, J.2
  • 59
    • 0027209456 scopus 로고
    • Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease
    • DeWitt D.A., Silver J., Canning D.R., and Perry G. Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease. Exp. Neurol. 121 (1993) 149-152
    • (1993) Exp. Neurol. , vol.121 , pp. 149-152
    • DeWitt, D.A.1    Silver, J.2    Canning, D.R.3    Perry, G.4
  • 60
    • 0028068601 scopus 로고
    • Chondroitin sulfate proteoglycans are a common component of neuronal inclusions and astrocytic reaction in neurodegenerative diseases
    • DeWitt D.A., Richey P.L., Praprotnik D., Silver J., and Perry G. Chondroitin sulfate proteoglycans are a common component of neuronal inclusions and astrocytic reaction in neurodegenerative diseases. Brain Res. 656 (1994) 205-209
    • (1994) Brain Res. , vol.656 , pp. 205-209
    • DeWitt, D.A.1    Richey, P.L.2    Praprotnik, D.3    Silver, J.4    Perry, G.5
  • 61
    • 0035997236 scopus 로고    scopus 로고
    • Glycosaminoglycans and [beta]-amyloid, prion and tau peptides in neurodegenerative diseases
    • Diaz-Nido J., Wandosell F., and Avila J. Glycosaminoglycans and [beta]-amyloid, prion and tau peptides in neurodegenerative diseases. Peptides 23 (2002) 1323-1332
    • (2002) Peptides , vol.23 , pp. 1323-1332
    • Diaz-Nido, J.1    Wandosell, F.2    Avila, J.3
  • 62
    • 0037704306 scopus 로고    scopus 로고
    • Extracellular matrix molecules and synaptic plasticity
    • Dityatev A., and Schachner M. Extracellular matrix molecules and synaptic plasticity. Nat. Rev., Neurosci. 4 (2003) 456-468
    • (2003) Nat. Rev., Neurosci. , vol.4 , pp. 456-468
    • Dityatev, A.1    Schachner, M.2
  • 64
    • 0030452470 scopus 로고    scopus 로고
    • Inhibitors and promoters of thalamic neuron adhesion and outgrowth in embryonic neocortex: functional association with chondroitin sulfate
    • Emerling D.E., and Lander A.D. Inhibitors and promoters of thalamic neuron adhesion and outgrowth in embryonic neocortex: functional association with chondroitin sulfate. Neuron 17 (1996) 1089-1100
    • (1996) Neuron , vol.17 , pp. 1089-1100
    • Emerling, D.E.1    Lander, A.D.2
  • 65
    • 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., Maurel P., Margolis R.U., and Margolis R.K. Chondroitin sulfate proteoglycans in the developing central nervous system. I. cellular sites of synthesis of neurocan and phosphacan. J. Comp. Neurol. 366 (1996) 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
  • 67
    • 0029269650 scopus 로고
    • Disorders of the extracellular matrix and the pathogenesis of senile dementia of the Alzheimer's type
    • Fillit H., and Leveugle B. Disorders of the extracellular matrix and the pathogenesis of senile dementia of the Alzheimer's type. Lab. Invest. 72 (1995) 249-253
    • (1995) Lab. Invest. , vol.72 , pp. 249-253
    • Fillit, H.1    Leveugle, B.2
  • 68
    • 13944266687 scopus 로고    scopus 로고
    • Combining Schwann cell bridges and olfactory-ensheathing glia grafts with chondroitinase promotes locomotor recovery after complete transection of the spinal cord
    • Fouad K., Schnell L., Bunge M.B., Schwab M.E., Liebscher T., and Pearse D.D. Combining Schwann cell bridges and olfactory-ensheathing glia grafts with chondroitinase promotes locomotor recovery after complete transection of the spinal cord. J. Neurosci. 25 (2005) 1169-1178
    • (2005) J. Neurosci. , vol.25 , pp. 1169-1178
    • Fouad, K.1    Schnell, L.2    Bunge, M.B.3    Schwab, M.E.4    Liebscher, T.5    Pearse, D.D.6
  • 69
    • 0037443069 scopus 로고    scopus 로고
    • Rho kinase inhibition enhances axonal regeneration in the injured CNS
    • Fournier A.E., Takizawa B.T., and Strittmatter S.M. Rho kinase inhibition enhances axonal regeneration in the injured CNS. J. Neurosci. 23 (2003) 1416-1423
    • (2003) J. Neurosci. , vol.23 , pp. 1416-1423
    • Fournier, A.E.1    Takizawa, B.T.2    Strittmatter, S.M.3
  • 70
    • 0037044574 scopus 로고    scopus 로고
    • Neuroscience. Freeing the brain from the perineuronal net
    • Fox K., and Caterson B. Neuroscience. Freeing the brain from the perineuronal net. Science 298 (2002) 1187-1189
    • (2002) Science , vol.298 , pp. 1187-1189
    • Fox, K.1    Caterson, B.2
  • 71
    • 0141869012 scopus 로고    scopus 로고
    • Behavioral alterations in mice deficient for the extracellular matrix glycoprotein tenascin-R
    • Freitag S., Schachner M., and Morellini F. Behavioral alterations in mice deficient for the extracellular matrix glycoprotein tenascin-R. Behav. Brain Res. 145 (2003) 189-207
    • (2003) Behav. Brain Res. , vol.145 , pp. 189-207
    • Freitag, S.1    Schachner, M.2    Morellini, F.3
  • 72
    • 33947614432 scopus 로고    scopus 로고
    • Galtrey, C.M., Asher, R.A., Nothias F., Fawcett, J.W., in press. Promoting plasticity in the spinal cord with chondroitinase improves functional recovery after peripheral nerve repair. Brain.
  • 73
    • 0037929699 scopus 로고    scopus 로고
    • Phosphacan short isoform, a novel non-proteoglycan variant of phosphacan/receptor protein tyrosine phosphatase-{beta}, interacts with neuronal receptors and promotes neurite outgrowth
    • Garwood J., Heck N., Reichardt F., and Faissner A. Phosphacan short isoform, a novel non-proteoglycan variant of phosphacan/receptor protein tyrosine phosphatase-{beta}, interacts with neuronal receptors and promotes neurite outgrowth. J. Biol. Chem. 278 (2003) 24164-24173
    • (2003) J. Biol. Chem. , vol.278 , pp. 24164-24173
    • Garwood, J.1    Heck, N.2    Reichardt, F.3    Faissner, A.4
  • 75
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert M., Jakes R., Spillantini M.G., Hasegawa M., Smith M.J., and Crowther R.A. Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383 (1996) 550-553
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 76
    • 1242314200 scopus 로고    scopus 로고
    • A novel DNA enzyme reduces glycosaminoglycan chains in the glial scar and allows microtransplanted dorsal root ganglia axons to regenerate beyond lesions in the spinal cord
    • Grimpe B., and Silver J. A novel DNA enzyme reduces glycosaminoglycan chains in the glial scar and allows microtransplanted dorsal root ganglia axons to regenerate beyond lesions in the spinal cord. J. Neurosci. 24 (2004) 1393-1397
    • (2004) J. Neurosci. , vol.24 , pp. 1393-1397
    • Grimpe, B.1    Silver, J.2
  • 78
    • 0028978227 scopus 로고
    • Proteoglycan-mediated inhibition of A beta proteolysis. A potential cause of senile plaque accumulation
    • Gupta-Bansal R., Frederickson R.C., and Brunden K.R. Proteoglycan-mediated inhibition of A beta proteolysis. A potential cause of senile plaque accumulation. J. Biol. Chem. 270 (1995) 18666-18671
    • (1995) J. Biol. Chem. , vol.270 , pp. 18666-18671
    • Gupta-Bansal, R.1    Frederickson, R.C.2    Brunden, K.R.3
  • 79
    • 0034611771 scopus 로고    scopus 로고
    • Diversity and functions of glycosaminoglycan sulfotransferases
    • Habuchi O. Diversity and functions of glycosaminoglycan sulfotransferases. Biochim. Biophys. Acta (BBA)-Gen. Subj. 1474 (2000) 115-127
    • (2000) Biochim. Biophys. Acta (BBA)-Gen. Subj. , vol.1474 , pp. 115-127
    • Habuchi, O.1
  • 80
    • 0033606849 scopus 로고    scopus 로고
    • Immunohistochemical evidence for the brevican-tenascin-R interaction: colocalization in perineuronal nets suggests a physiological role for the interaction in the adult rat brain
    • Hagihara K., Miura R., Kosaki R., Berglund E., Ranscht B., and Yamaguchi Y. Immunohistochemical evidence for the brevican-tenascin-R interaction: colocalization in perineuronal nets suggests a physiological role for the interaction in the adult rat brain. J. Comp. Neurol. 410 (1999) 256-264
    • (1999) J. Comp. Neurol. , vol.410 , pp. 256-264
    • Hagihara, K.1    Miura, R.2    Kosaki, R.3    Berglund, E.4    Ranscht, B.5    Yamaguchi, Y.6
  • 81
    • 0026730633 scopus 로고
    • Wisteria floribunda agglutinin-labelled nets surround parvalbumin-containing neurons
    • Hartig W., Brauer K., and Bruckner G. Wisteria floribunda agglutinin-labelled nets surround parvalbumin-containing neurons. NeuroReport 3 (1992) 869-872
    • (1992) NeuroReport , vol.3 , pp. 869-872
    • Hartig, W.1    Brauer, K.2    Bruckner, G.3
  • 82
    • 18144441575 scopus 로고    scopus 로고
    • Cortical neurons immunoreactive for the potassium channel Kv3.1b subunit are predominantly surrounded by perineuronal nets presumed as a buffering system for cations
    • Hartig W., Derouiche A., Welt K., Brauer K., Grosche J., Mader M., Reichenbach A., and Bruckner G. Cortical neurons immunoreactive for the potassium channel Kv3.1b subunit are predominantly surrounded by perineuronal nets presumed as a buffering system for cations. Brain Res. 842 (1999) 15-29
    • (1999) Brain Res. , vol.842 , pp. 15-29
    • Hartig, W.1    Derouiche, A.2    Welt, K.3    Brauer, K.4    Grosche, J.5    Mader, M.6    Reichenbach, A.7    Bruckner, G.8
  • 83
    • 0035058042 scopus 로고    scopus 로고
    • Hyperphosphorylated protein tau is restricted to neurons devoid of perineuronal nets in the cortex of aged bison
    • Hartig W., Klein C., Brauer K., Schuppel K.F., Arendt T., Bigl V., and Bruckner G. Hyperphosphorylated protein tau is restricted to neurons devoid of perineuronal nets in the cortex of aged bison. Neurobiol. Aging 22 (2001) 25-33
    • (2001) Neurobiol. Aging , vol.22 , pp. 25-33
    • Hartig, W.1    Klein, C.2    Brauer, K.3    Schuppel, K.F.4    Arendt, T.5    Bigl, V.6    Bruckner, G.7
  • 84
    • 0035058042 scopus 로고    scopus 로고
    • Hyperphosphorylated protein tau is restricted to neurons devoid of perineuronal nets in the cortex of aged bison
    • Hartig W., Klein C., Brauer K., Schuppel K.F., Arendt T., Bigl V., and Bruckner G. Hyperphosphorylated protein tau is restricted to neurons devoid of perineuronal nets in the cortex of aged bison. Neurobiol. Aging 22 (2001) 25-33
    • (2001) Neurobiol. Aging , vol.22 , pp. 25-33
    • Hartig, W.1    Klein, C.2    Brauer, K.3    Schuppel, K.F.4    Arendt, T.5    Bigl, V.6    Bruckner, G.7
  • 85
    • 0035127422 scopus 로고    scopus 로고
    • Proteoglycans in the nervous system-the quest for functional roles in vivo
    • Hartmann U., and Maurer P. Proteoglycans in the nervous system-the quest for functional roles in vivo. Matrix Biol. 20 (2001) 23-35
    • (2001) Matrix Biol. , vol.20 , pp. 23-35
    • Hartmann, U.1    Maurer, P.2
  • 86
    • 0033542796 scopus 로고    scopus 로고
    • Phosphacan immunoreactivity is associated with perineuronal nets around parvalbumin-expressing neurones
    • Haunso A., Celio M.R., Margolis R.K., and Menoud P.A. Phosphacan immunoreactivity is associated with perineuronal nets around parvalbumin-expressing neurones. Brain Res. 834 (1999) 219-222
    • (1999) Brain Res. , vol.834 , pp. 219-222
    • Haunso, A.1    Celio, M.R.2    Margolis, R.K.3    Menoud, P.A.4
  • 87
    • 0029972298 scopus 로고    scopus 로고
    • Pyramidal cells ensheathed by perineuronal nets in human motor and somatosensory cortex
    • Hausen D., Bruckner G., Drlicek M., Hartig W., Brauer K., and Bigl V. Pyramidal cells ensheathed by perineuronal nets in human motor and somatosensory cortex. NeuroReport 7 (1996) 1725-1729
    • (1996) NeuroReport , vol.7 , pp. 1725-1729
    • Hausen, D.1    Bruckner, G.2    Drlicek, M.3    Hartig, W.4    Brauer, K.5    Bigl, V.6
  • 88
    • 13544259665 scopus 로고    scopus 로고
    • Neuronal expression of the chondroitin sulfate proteoglycans receptor-type protein-tyrosine phosphatase [beta] and phosphacan
    • Hayashi N., Miyata S., Yamada M., Kamei K., and Oohira A. Neuronal expression of the chondroitin sulfate proteoglycans receptor-type protein-tyrosine phosphatase [beta] and phosphacan. Neuroscience 131 (2005) 331-348
    • (2005) Neuroscience , vol.131 , pp. 331-348
    • Hayashi, N.1    Miyata, S.2    Yamada, M.3    Kamei, K.4    Oohira, A.5
  • 90
    • 6344265574 scopus 로고    scopus 로고
    • Differential upregulation of extracellular matrix molecules associated with the appearance of granule cell dispersion and mossy fiber sprouting during epileptogenesis in a murine model of temporal lobe epilepsy
    • Heck N., Garwood J., Loeffler J.P., Larmet Y., and Faissner A. Differential upregulation of extracellular matrix molecules associated with the appearance of granule cell dispersion and mossy fiber sprouting during epileptogenesis in a murine model of temporal lobe epilepsy. Neuroscience 129 (2004) 309-324
    • (2004) Neuroscience , vol.129 , pp. 309-324
    • Heck, N.1    Garwood, J.2    Loeffler, J.P.3    Larmet, Y.4    Faissner, A.5
  • 91
    • 3943087045 scopus 로고    scopus 로고
    • Critical period regulation
    • Hensch T.K. Critical period regulation. Annu. Rev. Neurosci. 27 (2004) 549-579
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 549-579
    • Hensch, T.K.1
  • 92
    • 0034610059 scopus 로고    scopus 로고
    • The brain link protein-1 (BRAL1): cDNA cloning, genomic structure, and characterization as a novel link protein expressed in adult brain
    • Hirakawa S., Oohashi T., Su W.D., Yoshioka H., Murakami T., Arata J., and Ninomiya Y. The brain link protein-1 (BRAL1): cDNA cloning, genomic structure, and characterization as a novel link protein expressed in adult brain. Biochem. Biophys. Res. Commun. 276 (2000) 982-989
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 982-989
    • Hirakawa, S.1    Oohashi, T.2    Su, W.D.3    Yoshioka, H.4    Murakami, T.5    Arata, J.6    Ninomiya, Y.7
  • 93
    • 0035895930 scopus 로고    scopus 로고
    • Versican interacts with chemokines and modulates cellular responses
    • Hirose J., Kawashima H., Yoshie O., Tashiro K., and Miyasaka M. Versican interacts with chemokines and modulates cellular responses. J. Biol. Chem. 276 (2001) 5228-5234
    • (2001) J. Biol. Chem. , vol.276 , pp. 5228-5234
    • Hirose, J.1    Kawashima, H.2    Yoshie, O.3    Tashiro, K.4    Miyasaka, M.5
  • 94
    • 20344380725 scopus 로고    scopus 로고
    • Decomposition and long-lasting downregulation of extracellular matrix in perineuronal nets induced by focal cerebral ischemia in rats
    • Hobohm C., Gunther A., Grosche J., Rossner S., Schneider D., and Bruckner G. Decomposition and long-lasting downregulation of extracellular matrix in perineuronal nets induced by focal cerebral ischemia in rats. J. Neurosci. Res. 80 (2005) 539-548
    • (2005) J. Neurosci. Res. , vol.80 , pp. 539-548
    • Hobohm, C.1    Gunther, A.2    Grosche, J.3    Rossner, S.4    Schneider, D.5    Bruckner, G.6
  • 95
    • 0025553823 scopus 로고
    • Expression of neural proteoglycans correlates with the acquisition of mature neuronal properties in the mammalian brain
    • Hockfield S., Kalb R.G., Zaremba S., and Fryer H. Expression of neural proteoglycans correlates with the acquisition of mature neuronal properties in the mammalian brain. Cold Spring Harbor Symp. Quant. Biol. 55 (1990) 505-514
    • (1990) Cold Spring Harbor Symp. Quant. Biol. , vol.55 , pp. 505-514
    • Hockfield, S.1    Kalb, R.G.2    Zaremba, S.3    Fryer, H.4
  • 96
    • 0031902035 scopus 로고    scopus 로고
    • Leucine-rich repeat glycoproteins of the extracellular matrix
    • Hocking A.M., Shinomura T., and McQuillan D.J. Leucine-rich repeat glycoproteins of the extracellular matrix. Matrix Biol. 17 (1998) 1-19
    • (1998) Matrix Biol. , vol.17 , pp. 1-19
    • Hocking, A.M.1    Shinomura, T.2    McQuillan, D.J.3
  • 97
    • 33746094328 scopus 로고    scopus 로고
    • Combining an autologous peripheral nervous system "Bridge" and matrix modification by chondroitinase allows robust, functional regeneration beyond a hemisection lesion of the adult rat spinal cord
    • Houle J.D., Tom V.J., Mayes D., Wagoner G., Phillips N., and Silver J. Combining an autologous peripheral nervous system "Bridge" and matrix modification by chondroitinase allows robust, functional regeneration beyond a hemisection lesion of the adult rat spinal cord. J. Neurosci. 26 (2006) 7405-7415
    • (2006) J. Neurosci. , vol.26 , pp. 7405-7415
    • Houle, J.D.1    Tom, V.J.2    Mayes, D.3    Wagoner, G.4    Phillips, N.5    Silver, J.6
  • 98
    • 20544460672 scopus 로고    scopus 로고
    • Structural and functional aberrations in the cerebral cortex of tenascin-C deficient mice
    • Irintchev A., Rollenhagen A., Troncoso E., Kiss J.Z., and Schachner M. Structural and functional aberrations in the cerebral cortex of tenascin-C deficient mice. Cereb. Cortex 15 (2004) 950-962
    • (2004) Cereb. Cortex , vol.15 , pp. 950-962
    • Irintchev, A.1    Rollenhagen, A.2    Troncoso, E.3    Kiss, J.Z.4    Schachner, M.5
  • 99
    • 0042665641 scopus 로고    scopus 로고
    • The chondroitin sulfate proteoglycans neurocan, brevican, phosphacan, and versican are differentially regulated following spinal cord injury
    • Jones L.L., Margolis R.U., and Tuszynski M.H. The chondroitin sulfate proteoglycans neurocan, brevican, phosphacan, and versican are differentially regulated following spinal cord injury. Exp. Neurol. 182 (2003) 399-411
    • (2003) Exp. Neurol. , vol.182 , pp. 399-411
    • Jones, L.L.1    Margolis, R.U.2    Tuszynski, M.H.3
  • 100
    • 0023740395 scopus 로고
    • Molecular evidence for early activity-dependent development of hamster motor neurons
    • Kalb R.G., and Hockfield S. Molecular evidence for early activity-dependent development of hamster motor neurons. J. Neurosci. 8 (1988) 2350-2360
    • (1988) J. Neurosci. , vol.8 , pp. 2350-2360
    • Kalb, R.G.1    Hockfield, S.2
  • 101
    • 0025363556 scopus 로고
    • Large diameter primary afferent input is required for expression of the Cat-301 proteoglycan on the surface of motor neurons
    • Kalb R.G., and Hockfield S. Large diameter primary afferent input is required for expression of the Cat-301 proteoglycan on the surface of motor neurons. Neuroscience 34 (1990) 391-401
    • (1990) Neuroscience , vol.34 , pp. 391-401
    • Kalb, R.G.1    Hockfield, S.2
  • 103
    • 0037066693 scopus 로고    scopus 로고
    • Oversulfated chondroitin/dermatan sulfates containing GlcAbeta 1/IdoAalpha 1-3GalNAc(4,6-O-disulfate) interact with L- and P-selectin and chemokines
    • Kawashima H., Atarashi K., Hirose M., Hirose J., Yamada S., Sugahara K., and Miyasaka M. Oversulfated chondroitin/dermatan sulfates containing GlcAbeta 1/IdoAalpha 1-3GalNAc(4,6-O-disulfate) interact with L- and P-selectin and chemokines. J. Biol. Chem. 277 (2002) 12921-12930
    • (2002) J. Biol. Chem. , vol.277 , pp. 12921-12930
    • Kawashima, H.1    Atarashi, K.2    Hirose, M.3    Hirose, J.4    Yamada, S.5    Sugahara, K.6    Miyasaka, M.7
  • 104
    • 0035914310 scopus 로고    scopus 로고
    • Molecular cloning and expression of a human chondroitin synthase
    • Kitagawa H., Uyama T., and Sugahara K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721-38726
    • (2001) J. Biol. Chem. , vol.276 , pp. 38721-38726
    • Kitagawa, H.1    Uyama, T.2    Sugahara, K.3
  • 105
    • 0037478786 scopus 로고    scopus 로고
    • Molecular cloning of a chondroitin polymerizing factor that cooperates with chondroitin synthase for chondroitin polymerization
    • Kitagawa H., Izumikawa T., Uyama T., and Sugahara K. Molecular cloning of a chondroitin polymerizing factor that cooperates with chondroitin synthase for chondroitin polymerization. J. Biol. Chem. 278 (2003) 23666-23671
    • (2003) J. Biol. Chem. , vol.278 , pp. 23666-23671
    • Kitagawa, H.1    Izumikawa, T.2    Uyama, T.3    Sugahara, K.4
  • 107
    • 0032975510 scopus 로고    scopus 로고
    • The chondrocyte pericellular matrix: a model for hyaluronan-mediated cell-matrix interactions
    • Knudson C.B., Nofal G.A., Pamintuan L., and Aguiar D.J. The chondrocyte pericellular matrix: a model for hyaluronan-mediated cell-matrix interactions. Biochem. Soc. Trans. 27 (1999) 142-147
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 142-147
    • Knudson, C.B.1    Nofal, G.A.2    Pamintuan, L.3    Aguiar, D.J.4
  • 108
    • 0024414936 scopus 로고
    • Vicia villosa lectin-positive neurones in human cerebral cortex. Loss in Alzheimer-type dementia
    • Kobayashi K., Emson P.C., and Mountjoy C.Q. Vicia villosa lectin-positive neurones in human cerebral cortex. Loss in Alzheimer-type dementia. Brain Res. 498 (1989) 170-174
    • (1989) Brain Res. , vol.498 , pp. 170-174
    • Kobayashi, K.1    Emson, P.C.2    Mountjoy, C.Q.3
  • 109
    • 1642573173 scopus 로고    scopus 로고
    • Absence of mechanical allodynia and A[beta]-fiber sprouting after sciatic nerve injury in mice lacking membrane-type 5 matrix metalloproteinase
    • Komori K., Nonaka T., Okada A., Kinoh H., Hayashita-Kinoh H., Yoshida N., Yana I., and Seiki M. Absence of mechanical allodynia and A[beta]-fiber sprouting after sciatic nerve injury in mice lacking membrane-type 5 matrix metalloproteinase. FEBS Lett. 557 (2004) 125-128
    • (2004) FEBS Lett. , vol.557 , pp. 125-128
    • Komori, K.1    Nonaka, T.2    Okada, A.3    Kinoh, H.4    Hayashita-Kinoh, H.5    Yoshida, N.6    Yana, I.7    Seiki, M.8
  • 110
    • 0030907759 scopus 로고    scopus 로고
    • Developmental patterns of proteoglycan-containing extracellular matrix in perineuronal nets and neuropil of the postnatal rat brain
    • Koppe G., Bruckner G., Brauer K., Hartig W., and Bigl V. Developmental patterns of proteoglycan-containing extracellular matrix in perineuronal nets and neuropil of the postnatal rat brain. Cell Tissue Res. 288 (1997) 33-41
    • (1997) Cell Tissue Res. , vol.288 , pp. 33-41
    • Koppe, G.1    Bruckner, G.2    Brauer, K.3    Hartig, W.4    Bigl, V.5
  • 111
    • 0030905035 scopus 로고    scopus 로고
    • Characterization of proteoglycan-containing perineuronal nets by enzymatic treatments of rat brain sections
    • Koppe G., Bruckner G., Hartig W., Delpech B., and Bigl V. Characterization of proteoglycan-containing perineuronal nets by enzymatic treatments of rat brain sections. Histochem. J. 29 (1997) 11-20
    • (1997) Histochem. J. , vol.29 , pp. 11-20
    • Koppe, G.1    Bruckner, G.2    Hartig, W.3    Delpech, B.4    Bigl, V.5
  • 113
    • 33947612314 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycan glycosaminoglycan chain synthesis: a potential molecular target
    • Society for Neuroscience, Washington, DC Online. Ref Type: Conference Proceeding
    • Laabs T.L., Fawcett J.W., and Geller H.M. Chondroitin sulfate proteoglycan glycosaminoglycan chain synthesis: a potential molecular target. Program No. 386.4. 2005. 2005 Abstract Viewer/Itinerary Planner (2005), Society for Neuroscience, Washington, DC Online. Ref Type: Conference Proceeding
    • (2005) Program No. 386.4. 2005. 2005 Abstract Viewer/Itinerary Planner
    • Laabs, T.L.1    Fawcett, J.W.2    Geller, H.M.3
  • 114
    • 0031017794 scopus 로고    scopus 로고
    • A family of activity-dependent neuronal cell-surface chondroitin sulfate proteoglycans in cat visual cortex
    • Lander C., Kind P., Maleski M., and Hockfield S. A family of activity-dependent neuronal cell-surface chondroitin sulfate proteoglycans in cat visual cortex. J. Neurosci. 17 (1997) 1928-1939
    • (1997) J. Neurosci. , vol.17 , pp. 1928-1939
    • Lander, C.1    Kind, P.2    Maleski, M.3    Hockfield, S.4
  • 115
    • 0035400082 scopus 로고    scopus 로고
    • Intact aggrecan and fragments generated by both aggrecans and metalloproteinase-like activities are present in the developing and adult rat spinal cord and their relative abundance is altered by injury
    • Lemons M.L., Sandy J.D., Anderson D.K., and Howland D.R. Intact aggrecan and fragments generated by both aggrecans and metalloproteinase-like activities are present in the developing and adult rat spinal cord and their relative abundance is altered by injury. J. Neurosci. Off. J. Soc. Neurosci. 21 (2001) 4772-4781
    • (2001) J. Neurosci. Off. J. Soc. Neurosci. , vol.21 , pp. 4772-4781
    • Lemons, M.L.1    Sandy, J.D.2    Anderson, D.K.3    Howland, D.R.4
  • 116
    • 0032848943 scopus 로고    scopus 로고
    • Decorin attenuates gliotic scar formation in the rat cerebral hemisphere
    • Logan A., Baird A., and Berry M. Decorin attenuates gliotic scar formation in the rat cerebral hemisphere. Exp. Neurol. 159 (1999) 504-510
    • (1999) Exp. Neurol. , vol.159 , pp. 504-510
    • Logan, A.1    Baird, A.2    Berry, M.3
  • 117
    • 4143100146 scopus 로고    scopus 로고
    • Structural basis for interactions between tenascins and Lectican C-Type lectin domains; evidence for a crosslinking role for tenascins
    • Lundell A., Olin A.I., Morgelin M., Al Karadaghi S., Aspberg A., and Logan D.T. Structural basis for interactions between tenascins and Lectican C-Type lectin domains; evidence for a crosslinking role for tenascins. Structure (Cambridge) 12 (2004) 1495-1506
    • (2004) Structure (Cambridge) , vol.12 , pp. 1495-1506
    • Lundell, A.1    Olin, A.I.2    Morgelin, M.3    Al Karadaghi, S.4    Aspberg, A.5    Logan, D.T.6
  • 118
    • 0033578855 scopus 로고    scopus 로고
    • Long-term potentiation-a decade of progress?
    • Malenka R.C., and Nicoll R.A. Long-term potentiation-a decade of progress?. Science 285 (1999) 1870-1874
    • (1999) Science , vol.285 , pp. 1870-1874
    • Malenka, R.C.1    Nicoll, R.A.2
  • 119
    • 33646442052 scopus 로고    scopus 로고
    • Chondroitinase ABC digestion of the perineuronal net promotes functional collateral sprouting in the cuneate nucleus after cervical spinal cord injury
    • Massey J.M., Hubscher C.H., Wagoner M.R., Decker J.A., Amps J., Silver J., and Onifer S.M. Chondroitinase ABC digestion of the perineuronal net promotes functional collateral sprouting in the cuneate nucleus after cervical spinal cord injury. J. Neurosci. 26 (2006) 4406-4414
    • (2006) J. Neurosci. , vol.26 , pp. 4406-4414
    • Massey, J.M.1    Hubscher, C.H.2    Wagoner, M.R.3    Decker, J.A.4    Amps, J.5    Silver, J.6    Onifer, S.M.7
  • 120
    • 21644438258 scopus 로고    scopus 로고
    • Proteoglycans and injury of the central nervous system
    • Matsui F., and Oohira A. Proteoglycans and injury of the central nervous system. Congenit. Anom. 44 (2004) 181-188
    • (2004) Congenit. Anom. , vol.44 , pp. 181-188
    • Matsui, F.1    Oohira, A.2
  • 121
    • 0032550198 scopus 로고    scopus 로고
    • Occurrence of a N-terminal proteolytic fragment of neurocan, not a C-terminal half, in a perineuronal net in the adult rat cerebrum
    • Matsui F., Nishizuka M., Yasuda Y., Aono S., Watanabe E., and Oohira A. Occurrence of a N-terminal proteolytic fragment of neurocan, not a C-terminal half, in a perineuronal net in the adult rat cerebrum. Brain Res. 790 (1998) 45-51
    • (1998) Brain Res. , vol.790 , pp. 45-51
    • Matsui, F.1    Nishizuka, M.2    Yasuda, Y.3    Aono, S.4    Watanabe, E.5    Oohira, A.6
  • 123
  • 124
    • 0028298023 scopus 로고
    • Phosphacan, a chondroitin sulfate proteoglycan of brain that interacts with neurons and neural cell-adhesion molecules, is an extracellular variant of a receptor-type protein tyrosine phosphatase
    • Maurel P., Rauch U., Flad M., Margolis R.K., and Margolis R.U. Phosphacan, a chondroitin sulfate proteoglycan of brain that interacts with neurons and neural cell-adhesion molecules, is an extracellular variant of a receptor-type protein tyrosine phosphatase. Proc. Natl. Acad. Sci. 91 (1994) 2512-2516
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 2512-2516
    • Maurel, P.1    Rauch, U.2    Flad, M.3    Margolis, R.K.4    Margolis, R.U.5
  • 125
    • 0028841089 scopus 로고
    • Injury-induced proteoglycans inhibit the potential for laminin-mediated axon growth on astrocytic scars
    • McKeon R.J., Hoke A., and Silver J. Injury-induced proteoglycans inhibit the potential for laminin-mediated axon growth on astrocytic scars. Exp. Neurol. 136 (1995) 32-43
    • (1995) Exp. Neurol. , vol.136 , pp. 32-43
    • McKeon, R.J.1    Hoke, A.2    Silver, J.3
  • 126
    • 0033755865 scopus 로고    scopus 로고
    • Effect of amino-acid substitutions on Alzheimer's amyloid-{beta} peptide-glycosaminoglycan interactions
    • McLaurin J., and Fraser P.E. Effect of amino-acid substitutions on Alzheimer's amyloid-{beta} peptide-glycosaminoglycan interactions. Eur. J. Biochem. 267 (2000) 6353-6361
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6353-6361
    • McLaurin, J.1    Fraser, P.E.2
  • 127
    • 3242675370 scopus 로고    scopus 로고
    • Destruction of extracellular matrix proteoglycans is pervasive in simian retroviral neuroinfection
    • Medina-Flores R., Wang G., Bissel S.J., Murphey-Corb M., and Wiley C.A. Destruction of extracellular matrix proteoglycans is pervasive in simian retroviral neuroinfection. Neurobiol. Dis. 16 (2004) 604-616
    • (2004) Neurobiol. Dis. , vol.16 , pp. 604-616
    • Medina-Flores, R.1    Wang, G.2    Bissel, S.J.3    Murphey-Corb, M.4    Wiley, C.A.5
  • 128
    • 0030906999 scopus 로고    scopus 로고
    • The fibrinogen-like globe of tenascin-C mediates its interactions with neurocan and phosphacan/protein-tyrosine phosphatase-zeta/beta
    • Milev P., Fischer D., Haring M., Schulthess T., Margolis R.K., Chiquet-Ehrismann R., and Margolis R.U. The fibrinogen-like globe of tenascin-C mediates its interactions with neurocan and phosphacan/protein-tyrosine phosphatase-zeta/beta. J. Biol. Chem. 272 (1997) 15501-15509
    • (1997) J. Biol. Chem. , vol.272 , pp. 15501-15509
    • Milev, P.1    Fischer, D.2    Haring, M.3    Schulthess, T.4    Margolis, R.K.5    Chiquet-Ehrismann, R.6    Margolis, R.U.7
  • 129
    • 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., Haring M., Rauvala H., Schachner M., Ranscht B., Margolis R.K., and Margolis R.U. 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 (1998) 6998-7005
    • (1998) J. Biol. Chem. , vol.273 , pp. 6998-7005
    • Milev, P.1    Chiba, A.2    Haring, M.3    Rauvala, H.4    Schachner, M.5    Ranscht, B.6    Margolis, R.K.7    Margolis, R.U.8
  • 130
    • 3142751121 scopus 로고    scopus 로고
    • Activity-dependent regulation of a chondroitin sulfate proteoglycan 6B4 phosphacan/RPTPbeta in the hypothalamic supraoptic nucleus
    • Miyata S., Akagi A., Hayashi N., Watanabe K., and Oohira A. Activity-dependent regulation of a chondroitin sulfate proteoglycan 6B4 phosphacan/RPTPbeta in the hypothalamic supraoptic nucleus. Brain Res. 1017 (2004) 163-171
    • (2004) Brain Res. , vol.1017 , pp. 163-171
    • Miyata, S.1    Akagi, A.2    Hayashi, N.3    Watanabe, K.4    Oohira, A.5
  • 131
    • 26944433440 scopus 로고    scopus 로고
    • Construction of perineuronal net-like structure by cortical neurons in culture
    • Miyata S., Nishimura Y., Hayashi N., and Oohira A. Construction of perineuronal net-like structure by cortical neurons in culture. Neuroscience 136 (2005) 95-104
    • (2005) Neuroscience , vol.136 , pp. 95-104
    • Miyata, S.1    Nishimura, Y.2    Hayashi, N.3    Oohira, A.4
  • 132
    • 26244463171 scopus 로고    scopus 로고
    • Matrix-degrading enzymes tissue plasminogen activator and matrix metalloprotease-3 in the hypothalamo-neurohypophysial system
    • Miyata S., Nakatani Y., Hayashi N., and Nakashima T. Matrix-degrading enzymes tissue plasminogen activator and matrix metalloprotease-3 in the hypothalamo-neurohypophysial system. Brain Res. 1058 (2005) 1-9
    • (2005) Brain Res. , vol.1058 , pp. 1-9
    • Miyata, S.1    Nakatani, Y.2    Hayashi, N.3    Nakashima, T.4
  • 133
    • 24044525895 scopus 로고    scopus 로고
    • Expression of PrP(C) in the rat brain and characterization of a subset of cortical neurons
    • Moleres F.J., and Velayos J.L. Expression of PrP(C) in the rat brain and characterization of a subset of cortical neurons. Brain Res. 1056 (2005) 10-21
    • (2005) Brain Res. , vol.1056 , pp. 10-21
    • Moleres, F.J.1    Velayos, J.L.2
  • 134
    • 0037356722 scopus 로고    scopus 로고
    • The Rho/ROCK pathway mediates neurite growth-inhibitory activity associated with the chondroitin sulfate proteoglycans of the CNS glial scar
    • Monnier P.P., Sierra A., Schwab J.M., Henke-Fahle S., and Mueller B.K. The Rho/ROCK pathway mediates neurite growth-inhibitory activity associated with the chondroitin sulfate proteoglycans of the CNS glial scar. Mol. Cell. Neurosci. 22 (2003) 319-330
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 319-330
    • Monnier, P.P.1    Sierra, A.2    Schwab, J.M.3    Henke-Fahle, S.4    Mueller, B.K.5
  • 135
    • 0035784404 scopus 로고    scopus 로고
    • Reduction in CNS scar formation without concomitant increase in axon regeneration following treatment of adult rat brain with a combination of antibodies to TGF 1 and 2
    • Moon L.D.F., and Fawcett J.W. Reduction in CNS scar formation without concomitant increase in axon regeneration following treatment of adult rat brain with a combination of antibodies to TGF 1 and 2. Eur. J. Neurosci. 14 (2001) 1667-1677
    • (2001) Eur. J. Neurosci. , vol.14 , pp. 1667-1677
    • Moon, L.D.F.1    Fawcett, J.W.2
  • 136
    • 0035029305 scopus 로고    scopus 로고
    • Regeneration of CNS axons back to their target following treatment of adult rat brain with chondroitinase ABC
    • Moon L.D., Asher R.A., Rhodes K.E., and Fawcett J.W. Regeneration of CNS axons back to their target following treatment of adult rat brain with chondroitinase ABC. Nat. Neurosci. 4 (2001) 465-466
    • (2001) Nat. Neurosci. , vol.4 , pp. 465-466
    • Moon, L.D.1    Asher, R.A.2    Rhodes, K.E.3    Fawcett, J.W.4
  • 137
    • 0037127068 scopus 로고    scopus 로고
    • Relationship between sprouting axons, proteoglycans and glial cells following unilateral nigrostriatal axotomy in the adult rat
    • Moon L.D.F., Asher R.A., Rhodes K.E., and Fawcett J.W. Relationship between sprouting axons, proteoglycans and glial cells following unilateral nigrostriatal axotomy in the adult rat. Neuroscience 109 (2002) 101-117
    • (2002) Neuroscience , vol.109 , pp. 101-117
    • Moon, L.D.F.1    Asher, R.A.2    Rhodes, K.E.3    Fawcett, J.W.4
  • 139
    • 0036456428 scopus 로고    scopus 로고
    • Chondroitin sulphate proteoglycans in the CNS injury response
    • Morgenstern D.A., Asher R.A., and Fawcett J.W. Chondroitin sulphate proteoglycans in the CNS injury response. Prog. Brain Res. 137 (2002) 313-332
    • (2002) Prog. Brain Res. , vol.137 , pp. 313-332
    • Morgenstern, D.A.1    Asher, R.A.2    Fawcett, J.W.3
  • 140
    • 2942574539 scopus 로고    scopus 로고
    • Kindling and status epilepticus models of epilepsy: rewiring the brain
    • Morimoto K., Fahnestock M., and Racine R.J. Kindling and status epilepticus models of epilepsy: rewiring the brain. Prog. Neurobiol. 73 (2004) 1-60
    • (2004) Prog. Neurobiol. , vol.73 , pp. 1-60
    • Morimoto, K.1    Fahnestock, M.2    Racine, R.J.3
  • 141
    • 0034084881 scopus 로고    scopus 로고
    • Perineuronal nets ensheath fast spiking, parvalbumin-immunoreactive neurons in the medial septum/diagonal band complex
    • Morris N.P., and Henderson Z. Perineuronal nets ensheath fast spiking, parvalbumin-immunoreactive neurons in the medial septum/diagonal band complex. Eur. J. Neurosci. 12 (2000) 828-838
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 828-838
    • Morris, N.P.1    Henderson, Z.2
  • 142
    • 0032057384 scopus 로고    scopus 로고
    • Tissue plasminogen activator mediates reverse occlusion plasticity in visual cortex
    • Muller C.M., and Griesinger C.B. Tissue plasminogen activator mediates reverse occlusion plasticity in visual cortex. Nat. Neurosci. 1 (1998) 47-53
    • (1998) Nat. Neurosci. , vol.1 , pp. 47-53
    • Muller, C.M.1    Griesinger, C.B.2
  • 143
    • 0141644266 scopus 로고    scopus 로고
    • Perisynaptic barrier of proteoglycans in the mature brain and spinal cord
    • Murakami T., and Ohtsuka A. Perisynaptic barrier of proteoglycans in the mature brain and spinal cord. Arch. Histol. Cytol. 66 (2003) 195-207
    • (2003) Arch. Histol. Cytol. , vol.66 , pp. 195-207
    • Murakami, T.1    Ohtsuka, A.2
  • 144
    • 0141644266 scopus 로고    scopus 로고
    • Perisynaptic barrier of proteoglycans in the mature brain and spinal cord
    • Murakami T., and Ohtsuka A. Perisynaptic barrier of proteoglycans in the mature brain and spinal cord. Arch. Histol. Cytol. 66 (2003) 195-207
    • (2003) Arch. Histol. Cytol. , vol.66 , pp. 195-207
    • Murakami, T.1    Ohtsuka, A.2
  • 145
    • 0032918770 scopus 로고    scopus 로고
    • Perineuronal nets of proteoglycans in the adult mouse brain, with special reference to their reactions to Gomori's ammoniacal silver and Ehrlich's methylene blue
    • Murakami T., Murakami T., Sato H., Mubarak W.A., Ohtsuka A., and Abe K. Perineuronal nets of proteoglycans in the adult mouse brain, with special reference to their reactions to Gomori's ammoniacal silver and Ehrlich's methylene blue. Arch. Histol. Cytol. 62 (1999) 71-81
    • (1999) Arch. Histol. Cytol. , vol.62 , pp. 71-81
    • Murakami, T.1    Murakami, T.2    Sato, H.3    Mubarak, W.A.4    Ohtsuka, A.5    Abe, K.6
  • 146
    • 0032973657 scopus 로고    scopus 로고
    • Perineuronal nets of proteoglycans in the adult mouse brain are digested by collagenase
    • Murakami T., Murakami T., Su W.D., Ohtsuka A., Abe K., and Ninomiya Y. Perineuronal nets of proteoglycans in the adult mouse brain are digested by collagenase. Arch. Histol. Cytol. 62 (1999) 199-204
    • (1999) Arch. Histol. Cytol. , vol.62 , pp. 199-204
    • Murakami, T.1    Murakami, T.2    Su, W.D.3    Ohtsuka, A.4    Abe, K.5    Ninomiya, Y.6
  • 147
    • 24044462625 scopus 로고    scopus 로고
    • Focal cerebral ischemia induces changes in both MMP-13 and aggrecan around individual neurons
    • Nagel S., Sandy J.D., Meyding-Lamade U., Schwark C., Bartsch J.W., and Wagner S. Focal cerebral ischemia induces changes in both MMP-13 and aggrecan around individual neurons. Brain Res. 1056 (2005) 43-50
    • (2005) Brain Res. , vol.1056 , pp. 43-50
    • Nagel, S.1    Sandy, J.D.2    Meyding-Lamade, U.3    Schwark, C.4    Bartsch, J.W.5    Wagner, S.6
  • 148
    • 0027972772 scopus 로고
    • The link proteins
    • Neame P.J., and Barry F.P. The link proteins. EXS 70 (1994) 53-72
    • (1994) EXS , vol.70 , pp. 53-72
    • Neame, P.J.1    Barry, F.P.2
  • 149
    • 0033852395 scopus 로고    scopus 로고
    • Extracellular matrix and the brain: components and function
    • Novak U., and Kaye A.H. Extracellular matrix and the brain: components and function. J. Clin. Neurosci. 7 (2000) 280-290
    • (2000) J. Clin. Neurosci. , vol.7 , pp. 280-290
    • Novak, U.1    Kaye, A.H.2
  • 150
    • 0035832117 scopus 로고    scopus 로고
    • Brevican in the developing hippocampal fimbria: differential expression in myelinating oligodendrocytes and adult astrocytes suggests a dual role for brevican in central nervous system fiber tract development
    • Ogawa T., Hagihara K., Suzuki M., and Yamaguchi Y. Brevican in the developing hippocampal fimbria: differential expression in myelinating oligodendrocytes and adult astrocytes suggests a dual role for brevican in central nervous system fiber tract development. J. Comp. Neurol. 432 (2001) 285-295
    • (2001) J. Comp. Neurol. , vol.432 , pp. 285-295
    • Ogawa, T.1    Hagihara, K.2    Suzuki, M.3    Yamaguchi, Y.4
  • 151
    • 0032498938 scopus 로고    scopus 로고
    • Molecular heterogeneity of Vicia villosa-recognized perineuronal nets surrounding pyramidal and nonpyramidal neurons in the guinea pig cerebral cortex
    • Ojima H., Sakai M., and Ohyama J. Molecular heterogeneity of Vicia villosa-recognized perineuronal nets surrounding pyramidal and nonpyramidal neurons in the guinea pig cerebral cortex. Brain Res. 786 (1998) 274-280
    • (1998) Brain Res. , vol.786 , pp. 274-280
    • Ojima, H.1    Sakai, M.2    Ohyama, J.3
  • 152
    • 0028245678 scopus 로고
    • Chondroitin sulfate proteoglycans protect cultured rat's cortical and hippocampal neurons from delayed cell death induced by excitatory amino acids
    • Okamoto M., Mori S., Ichimura M., and Endo H. Chondroitin sulfate proteoglycans protect cultured rat's cortical and hippocampal neurons from delayed cell death induced by excitatory amino acids. Neurosci. Lett. 172 (1994) 51-54
    • (1994) Neurosci. Lett. , vol.172 , pp. 51-54
    • Okamoto, M.1    Mori, S.2    Ichimura, M.3    Endo, H.4
  • 153
    • 0345689359 scopus 로고    scopus 로고
    • Kainic acid-induced convulsions cause prolonged changes in the chondroitin sulfate proteoglycans neurocan and phosphacan in the limbic structures
    • Okamoto M., Sakiyama J., Mori S., Kurazono S., Usui S., Hasegawa M., and Oohira A. Kainic acid-induced convulsions cause prolonged changes in the chondroitin sulfate proteoglycans neurocan and phosphacan in the limbic structures. Exp. Neurol. 184 (2003) 179-195
    • (2003) Exp. Neurol. , vol.184 , pp. 179-195
    • Okamoto, M.1    Sakiyama, J.2    Mori, S.3    Kurazono, S.4    Usui, S.5    Hasegawa, M.6    Oohira, A.7
  • 154
    • 0035847046 scopus 로고    scopus 로고
    • The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding
    • Olin A.I., Morgelin M., Sasaki T., Timpl R., Heinegard D., and Aspberg A. The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding. J. Biol. Chem. 276 (2001) 1253-1261
    • (2001) J. Biol. Chem. , vol.276 , pp. 1253-1261
    • Olin, A.I.1    Morgelin, M.2    Sasaki, T.3    Timpl, R.4    Heinegard, D.5    Aspberg, A.6
  • 155
    • 0036152582 scopus 로고    scopus 로고
    • Bral1, a brain-specific link protein, colocalizing with the versican V2 isoform at the nodes of Ranvier in developing and adult mouse central nervous systems
    • Oohashi T., Hirakawa S., Bekku Y., Rauch U., Zimmermann D.R., Su W.D., Ohtsuka A., Murakami T., and Ninomiya Y. Bral1, a brain-specific link protein, colocalizing with the versican V2 isoform at the nodes of Ranvier in developing and adult mouse central nervous systems. Mol. Cell. Neurosci. 19 (2002) 43-57
    • (2002) Mol. Cell. Neurosci. , vol.19 , pp. 43-57
    • Oohashi, T.1    Hirakawa, S.2    Bekku, Y.3    Rauch, U.4    Zimmermann, D.R.5    Su, W.D.6    Ohtsuka, A.7    Murakami, T.8    Ninomiya, Y.9
  • 156
    • 0034141187 scopus 로고    scopus 로고
    • Molecular interactions of neural chondroitin sulfate proteoglycans in the brain development
    • Oohira A., Matsui F., Tokita Y., Yamauchi S., and Aono S. Molecular interactions of neural chondroitin sulfate proteoglycans in the brain development. Arch. Biochem. Biophys. 374 (2000) 24-34
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 24-34
    • Oohira, A.1    Matsui, F.2    Tokita, Y.3    Yamauchi, S.4    Aono, S.5
  • 157
    • 5444221720 scopus 로고    scopus 로고
    • Neuroglycan, C., a brain-specific part-time proteoglycan, with a particular multidomain structure
    • Oohira A., Shuo T., Tokita Y., Nakanishi K., and Aono S. Neuroglycan, C., a brain-specific part-time proteoglycan, with a particular multidomain structure. Glycoconj. J. 21 (2004) 53-57
    • (2004) Glycoconj. J. , vol.21 , pp. 53-57
    • Oohira, A.1    Shuo, T.2    Tokita, Y.3    Nakanishi, K.4    Aono, S.5
  • 158
    • 10444248793 scopus 로고    scopus 로고
    • Dendritic spine dynamics are regulated by monocular deprivation and extracellular matrix degradation
    • Oray S., Majewska A., and Sur M. Dendritic spine dynamics are regulated by monocular deprivation and extracellular matrix degradation. Neuron 44 (2004) 1021-1030
    • (2004) Neuron , vol.44 , pp. 1021-1030
    • Oray, S.1    Majewska, A.2    Sur, M.3
  • 161
    • 14244251041 scopus 로고    scopus 로고
    • Chondroitinase ABC I from Proteus vulgaris: cloning, recombinant expression and active site identification
    • Prabhakar V., Capila I., Bosques C.J., Pojasek K., and Sasisekharan R. Chondroitinase ABC I from Proteus vulgaris: cloning, recombinant expression and active site identification. Biochem. J. 386 (2005) 103-112
    • (2005) Biochem. J. , vol.386 , pp. 103-112
    • Prabhakar, V.1    Capila, I.2    Bosques, C.J.3    Pojasek, K.4    Sasisekharan, R.5
  • 162
    • 0037396474 scopus 로고    scopus 로고
    • Chondroitin sulphate proteoglycans in the central nervous system: changes and synthesis after injury
    • Properzi F., Asher R.A., and Fawcett J.W. Chondroitin sulphate proteoglycans in the central nervous system: changes and synthesis after injury. Biochem. Soc. Trans. 31 (2003) 335-336
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 335-336
    • Properzi, F.1    Asher, R.A.2    Fawcett, J.W.3
  • 164
    • 0033975514 scopus 로고    scopus 로고
    • Synthesis and sorting of proteoglycans
    • Prydz K., and Dalen K.T. Synthesis and sorting of proteoglycans. J. Cell Sci. 113 (2000) 193-205
    • (2000) J. Cell Sci. , vol.113 , pp. 193-205
    • Prydz, K.1    Dalen, K.T.2
  • 165
    • 4344702478 scopus 로고    scopus 로고
    • Extracellular matrix components associated with remodeling processes in brain
    • Rauch U. Extracellular matrix components associated with remodeling processes in brain. Cell. Mol. Life Sci. 61 (2004) 2031-2045
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2031-2045
    • Rauch, U.1
  • 167
    • 1942451831 scopus 로고    scopus 로고
    • Cartilage link protein interacts with neurocan, which shows hyaluronan binding characteristics different from CD44 and TSG-6
    • Rauch U., Hirakawa S., Oohashi T., Kappler J., and Roos G. Cartilage link protein interacts with neurocan, which shows hyaluronan binding characteristics different from CD44 and TSG-6. Matrix Biol. 22 (2004) 629-639
    • (2004) Matrix Biol. , vol.22 , pp. 629-639
    • Rauch, U.1    Hirakawa, S.2    Oohashi, T.3    Kappler, J.4    Roos, G.5
  • 168
    • 13444301122 scopus 로고    scopus 로고
    • Extracellular matrix alterations in brains lacking four of its components
    • Rauch U., Zhou X.H., and Roos G. Extracellular matrix alterations in brains lacking four of its components. Biochem. Biophys. Res. Commun. 328 (2005) 608-617
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 608-617
    • Rauch, U.1    Zhou, X.H.2    Roos, G.3
  • 169
    • 1442291888 scopus 로고    scopus 로고
    • Chondroitin sulphate proteoglycans: preventing plasticity or protecting the CNS?
    • Rhodes K.E., and Fawcett J.W. Chondroitin sulphate proteoglycans: preventing plasticity or protecting the CNS?. J. Anat. 204 (2004) 33-48
    • (2004) J. Anat. , vol.204 , pp. 33-48
    • Rhodes, K.E.1    Fawcett, J.W.2
  • 170
    • 0035155083 scopus 로고    scopus 로고
    • Reduced perisomatic inhibition, increased excitatory transmission, and impaired long-term potentiation in mice deficient for the extracellular matrix glycoprotein tenascin-R
    • Saghatelyan A.K., Dityatev A., Schmidt S., Schuster T., Bartsch U., and Schachner M. Reduced perisomatic inhibition, increased excitatory transmission, and impaired long-term potentiation in mice deficient for the extracellular matrix glycoprotein tenascin-R. Mol. Cell. Neurosci. 17 (2001) 226-240
    • (2001) Mol. Cell. Neurosci. , vol.17 , pp. 226-240
    • Saghatelyan, A.K.1    Dityatev, A.2    Schmidt, S.3    Schuster, T.4    Bartsch, U.5    Schachner, M.6
  • 171
    • 0031149760 scopus 로고    scopus 로고
    • The cellular basis for the relative resistance of parvalbumin and calretinin immunoreactive neocortical neurons to the pathology of Alzheimer's disease
    • Sampson V.L., Morrison J.H., and Vickers J.C. The cellular basis for the relative resistance of parvalbumin and calretinin immunoreactive neocortical neurons to the pathology of Alzheimer's disease. Exp. Neurol. 145 (1997) 295-302
    • (1997) Exp. Neurol. , vol.145 , pp. 295-302
    • Sampson, V.L.1    Morrison, J.H.2    Vickers, J.C.3
  • 172
    • 0026035290 scopus 로고
    • Parvalbumin-immunoreactive neurons in the human central nervous system are decreased in Alzheimer's disease
    • Satoh J., Tabira T., Sano M., Nakayama H., and Tateishi J. Parvalbumin-immunoreactive neurons in the human central nervous system are decreased in Alzheimer's disease. Acta Neuropathol. (Berl.) 81 (1991) 388-395
    • (1991) Acta Neuropathol. (Berl.) , vol.81 , pp. 388-395
    • Satoh, J.1    Tabira, T.2    Sano, M.3    Nakayama, H.4    Tateishi, J.5
  • 174
    • 14044272769 scopus 로고    scopus 로고
    • Expression and purification of functionally active hyaluronan-binding domains from human cartilage link protein, aggrecan and versican: formation of ternary complexes with defined hyaluronan oligosaccharides
    • Seyfried N.T., McVey G.F., Almond A., Mahoney D.J., Dudhia J., and Day A.J. Expression and purification of functionally active hyaluronan-binding domains from human cartilage link protein, aggrecan and versican: formation of ternary complexes with defined hyaluronan oligosaccharides. J. Biol. Chem. 280 (2005) 5435-5448
    • (2005) J. Biol. Chem. , vol.280 , pp. 5435-5448
    • Seyfried, N.T.1    McVey, G.F.2    Almond, A.3    Mahoney, D.J.4    Dudhia, J.5    Day, A.J.6
  • 176
    • 27844581682 scopus 로고    scopus 로고
    • Developmental change and function of chondroitin sulfate deposited around cerebellar Purkinje cells
    • Shimazaki Y., Nagata I., Ishii M., Tanaka M., Marunouchi T., Hata T., and Maeda N. Developmental change and function of chondroitin sulfate deposited around cerebellar Purkinje cells. J. Neurosci. Res. 82 (2005) 172-183
    • (2005) J. Neurosci. Res. , vol.82 , pp. 172-183
    • Shimazaki, Y.1    Nagata, I.2    Ishii, M.3    Tanaka, M.4    Marunouchi, T.5    Hata, T.6    Maeda, N.7
  • 177
    • 0032524632 scopus 로고    scopus 로고
    • Neurons as well as astrocytes express proteoglycan-type protein tyrosine phosphatase zeta/RPTPbeta: analysis of mice in which the PTPzeta/RPTPbeta gene was replaced with the LacZ gene
    • Shintani T., Watanabe E., Maeda N., and Noda M. Neurons as well as astrocytes express proteoglycan-type protein tyrosine phosphatase zeta/RPTPbeta: analysis of mice in which the PTPzeta/RPTPbeta gene was replaced with the LacZ gene. Neurosci. Lett. 247 (1998) 135-138
    • (1998) Neurosci. Lett. , vol.247 , pp. 135-138
    • Shintani, T.1    Watanabe, E.2    Maeda, N.3    Noda, M.4
  • 178
    • 0034213582 scopus 로고    scopus 로고
    • Synaptic microenvironments-structural plasticity, adhesion molecules, proteases and their inhibitors
    • Shiosaka S., and Yoshida S. Synaptic microenvironments-structural plasticity, adhesion molecules, proteases and their inhibitors. Neurosci. Res. 37 (2000) 85-89
    • (2000) Neurosci. Res. , vol.37 , pp. 85-89
    • Shiosaka, S.1    Yoshida, S.2
  • 179
    • 0742288565 scopus 로고    scopus 로고
    • Regeneration beyond the glial scar
    • Silver J., and Miller J.H. Regeneration beyond the glial scar. Nat. Rev., Neurosci. 5 (2004) 146-156
    • (2004) Nat. Rev., Neurosci. , vol.5 , pp. 146-156
    • Silver, J.1    Miller, J.H.2
  • 180
    • 1442299897 scopus 로고    scopus 로고
    • PKC mediates inhibitory effects of myelin and chondroitin sulfate proteoglycans on axonal regeneration
    • Sivasankaran R., Pei J., Wang K.C., Zhang Y.P., Shields C.B., Xu X.M., and He Z. PKC mediates inhibitory effects of myelin and chondroitin sulfate proteoglycans on axonal regeneration. Nat. Neurosci. 7 (2004) 261-268
    • (2004) Nat. Neurosci. , vol.7 , pp. 261-268
    • Sivasankaran, R.1    Pei, J.2    Wang, K.C.3    Zhang, Y.P.4    Shields, C.B.5    Xu, X.M.6    He, Z.7
  • 181
    • 0028910601 scopus 로고
    • Increased axon regeneration in astrocytes grown in the presence of proteoglycan synthesis inhibitors
    • Smith-Thomas L.C., Stevens J., Fok-Seang J., Faissner A., Rogers J.H., and Fawcett J.W. Increased axon regeneration in astrocytes grown in the presence of proteoglycan synthesis inhibitors. J. Cell Sci. 108 (1995) 1307-1315
    • (1995) J. Cell Sci. , vol.108 , pp. 1307-1315
    • Smith-Thomas, L.C.1    Stevens, J.2    Fok-Seang, J.3    Faissner, A.4    Rogers, J.H.5    Fawcett, J.W.6
  • 182
    • 0025323095 scopus 로고
    • Sulfated proteoglycans in astroglial barriers inhibit neurite outgrowth in vitro
    • Snow D.M., Lemmon V., Carrino D.A., Caplan A.I., and Silver J. Sulfated proteoglycans in astroglial barriers inhibit neurite outgrowth in vitro. Exp. Neurol. 109 (1990) 111-130
    • (1990) Exp. Neurol. , vol.109 , pp. 111-130
    • Snow, D.M.1    Lemmon, V.2    Carrino, D.A.3    Caplan, A.I.4    Silver, J.5
  • 183
    • 0030175781 scopus 로고    scopus 로고
    • Growth cone behavior in the presence of soluble chondroitin sulfate proteoglycan (CSPG), compared to behavior on CSPG bound to laminin or fibronectin
    • Snow D.M., Brown E.M., and Letourneau P.C. Growth cone behavior in the presence of soluble chondroitin sulfate proteoglycan (CSPG), compared to behavior on CSPG bound to laminin or fibronectin. Int. J. Dev. Neurosci. 14 (1996) 331-349
    • (1996) Int. J. Dev. Neurosci. , vol.14 , pp. 331-349
    • Snow, D.M.1    Brown, E.M.2    Letourneau, P.C.3
  • 184
    • 1842510647 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-3 and agrin cleavage in cerebral ischemia/reperfusion
    • Sole S., Petegnief V., Gorina R., Chamorro A., and Planas A.M. Activation of matrix metalloproteinase-3 and agrin cleavage in cerebral ischemia/reperfusion. J Neuropathol Exp. Neurol. 63 (2004) 338-349
    • (2004) J Neuropathol Exp. Neurol. , vol.63 , pp. 338-349
    • Sole, S.1    Petegnief, V.2    Gorina, R.3    Chamorro, A.4    Planas, A.M.5
  • 185
    • 0029930270 scopus 로고    scopus 로고
    • Contingent vulnerability of entorhinal parvalbumin-containing neurons in Alzheimer's disease
    • Solodkin A., Veldhuizen S.D., and Van Hoesen G.W. Contingent vulnerability of entorhinal parvalbumin-containing neurons in Alzheimer's disease. J. Neurosci. 16 (1996) 3311-3321
    • (1996) J. Neurosci. , vol.16 , pp. 3311-3321
    • Solodkin, A.1    Veldhuizen, S.D.2    Van Hoesen, G.W.3
  • 186
    • 0038418630 scopus 로고    scopus 로고
    • A hyaluronan binding link protein gene family whose members are physically linked adjacent to chondroitin sulfate proteoglycan core protein genes: the missing links
    • Spicer A.P., Joo A., and Bowling Jr. R.A. A hyaluronan binding link protein gene family whose members are physically linked adjacent to chondroitin sulfate proteoglycan core protein genes: the missing links. J. Biol. Chem. 278 (2003) 21083-21091
    • (2003) J. Biol. Chem. , vol.278 , pp. 21083-21091
    • Spicer, A.P.1    Joo, A.2    Bowling Jr., R.A.3
  • 187
    • 0242552255 scopus 로고    scopus 로고
    • The NG2 proteoglycan: past insights and future prospects
    • Stallcup W.B. The NG2 proteoglycan: past insights and future prospects. J. Neurocytol. 31 (2002) 423-435
    • (2002) J. Neurocytol. , vol.31 , pp. 423-435
    • Stallcup, W.B.1
  • 189
    • 0023837510 scopus 로고
    • Expression of a surface-associated antigen on Y-cells in the cat lateral geniculate nucleus is regulated by visual experience
    • Sur M., Frost D.O., and Hockfield S. Expression of a surface-associated antigen on Y-cells in the cat lateral geniculate nucleus is regulated by visual experience. J. Neurosci. 8 (1988) 874-882
    • (1988) J. Neurosci. , vol.8 , pp. 874-882
    • Sur, M.1    Frost, D.O.2    Hockfield, S.3
  • 190
    • 0032322111 scopus 로고    scopus 로고
    • Three-dimensional microanatomy of perineuronal proteoglycan nets enveloping motor neurons in the rat spinal cord
    • Takahashi-Iwanaga H., Murakami T., and Abe K. Three-dimensional microanatomy of perineuronal proteoglycan nets enveloping motor neurons in the rat spinal cord. J. Neurocytol. 27 (1998) 817-827
    • (1998) J. Neurocytol. , vol.27 , pp. 817-827
    • Takahashi-Iwanaga, H.1    Murakami, T.2    Abe, K.3
  • 191
    • 0345354676 scopus 로고    scopus 로고
    • A chondroitin sulfate proteoglycan PTPzeta /RPTPbeta regulates the morphogenesis of Purkinje cell dendrites in the developing cerebellum
    • Tanaka M., Maeda N., Noda M., and Marunouchi T. A chondroitin sulfate proteoglycan PTPzeta /RPTPbeta regulates the morphogenesis of Purkinje cell dendrites in the developing cerebellum. J. Neurosci. 23 (2003) 2804-2814
    • (2003) J. Neurosci. , vol.23 , pp. 2804-2814
    • Tanaka, M.1    Maeda, N.2    Noda, M.3    Marunouchi, T.4
  • 192
    • 0037310986 scopus 로고    scopus 로고
    • Changes in distribution, cell associations, and protein expression levels of NG2, neurocan, phosphacan, brevican, versican V2, and tenascin-C during acute to chronic maturation of spinal cord scar tissue
    • Tang X., Davies J.E., and Davies S.J. Changes in distribution, cell associations, and protein expression levels of NG2, neurocan, phosphacan, brevican, versican V2, and tenascin-C during acute to chronic maturation of spinal cord scar tissue. J. Neurosci. Res. 71 (2003) 427-444
    • (2003) J. Neurosci. Res. , vol.71 , pp. 427-444
    • Tang, X.1    Davies, J.E.2    Davies, S.J.3
  • 193
    • 2942592251 scopus 로고    scopus 로고
    • Neuronal, glial and synaptic remodeling in the adult hypothalamus: functional consequences and role of cell surface and extracellular matrix adhesion molecules
    • Theodosis D.T., Piet R., Poulain D.A., and Oliet S.H. Neuronal, glial and synaptic remodeling in the adult hypothalamus: functional consequences and role of cell surface and extracellular matrix adhesion molecules. Neurochem. Int. 45 (2004) 491-501
    • (2004) Neurochem. Int. , vol.45 , pp. 491-501
    • Theodosis, D.T.1    Piet, R.2    Poulain, D.A.3    Oliet, S.H.4
  • 194
    • 0033931910 scopus 로고    scopus 로고
    • The chondroitin sulphate proteoglycan brevican is upregulated by astrocytes after entorhinal cortex lesions in adult rats
    • Thon N., Haas C.A., Rauch U., Merten T., Fassler R., Frotscher M., and Deller T. The chondroitin sulphate proteoglycan brevican is upregulated by astrocytes after entorhinal cortex lesions in adult rats. Eur. J. Neurosci. 12 (2000) 2547-2558
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 2547-2558
    • Thon, N.1    Haas, C.A.2    Rauch, U.3    Merten, T.4    Fassler, R.5    Frotscher, M.6    Deller, T.7
  • 195
    • 3042697038 scopus 로고    scopus 로고
    • Hyaluronan: from extracellular glue to pericellular cue
    • Toole B.P. Hyaluronan: from extracellular glue to pericellular cue. Nat. Rev., Cancer 4 (2004) 528-539
    • (2004) Nat. Rev., Cancer , vol.4 , pp. 528-539
    • Toole, B.P.1
  • 196
    • 0043127460 scopus 로고    scopus 로고
    • Synergistic effects of brain-derived neurotrophic factor and chondroitinase ABC on retinal fiber sprouting after denervation of the superior colliculus in adult rats
    • Tropea D., Caleo M., and Maffei L. Synergistic effects of brain-derived neurotrophic factor and chondroitinase ABC on retinal fiber sprouting after denervation of the superior colliculus in adult rats. J. Neurosci. 23 (2003) 7034-7044
    • (2003) J. Neurosci. , vol.23 , pp. 7034-7044
    • Tropea, D.1    Caleo, M.2    Maffei, L.3
  • 197
    • 0033564779 scopus 로고    scopus 로고
    • Spatiotemporal expression patterns of metalloproteinases and their inhibitors in the postnatal developing rat cerebellum
    • Vaillant C., Didier-Bazes M., Hutter A., Belin M.F., and Thomasset N. Spatiotemporal expression patterns of metalloproteinases and their inhibitors in the postnatal developing rat cerebellum. J. Neurosci. 19 (1999) 4994-5004
    • (1999) J. Neurosci. , vol.19 , pp. 4994-5004
    • Vaillant, C.1    Didier-Bazes, M.2    Hutter, A.3    Belin, M.F.4    Thomasset, N.5
  • 198
    • 0034803060 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycans in the rat thalamus: expression during postnatal development and correlation with calcium-binding proteins in adults
    • Vitellaro-Zuccarello L., Meroni A., Amadeo A., and De Biasi S. Chondroitin sulfate proteoglycans in the rat thalamus: expression during postnatal development and correlation with calcium-binding proteins in adults. Cell Tissue Res. 306 (2001) 15-26
    • (2001) Cell Tissue Res. , vol.306 , pp. 15-26
    • Vitellaro-Zuccarello, L.1    Meroni, A.2    Amadeo, A.3    De Biasi, S.4
  • 199
    • 0036756745 scopus 로고    scopus 로고
    • Human brain plasticity: an emerging view of the multiple substrates and mechanisms that cause cortical changes and related sensory dysfunctions after injuries of sensory inputs from the body
    • Wall J.T., Xu J., and Wang X. Human brain plasticity: an emerging view of the multiple substrates and mechanisms that cause cortical changes and related sensory dysfunctions after injuries of sensory inputs from the body. Brain Res. Brain Res. Rev. 39 (2002) 181-215
    • (2002) Brain Res. Brain Res. Rev. , vol.39 , pp. 181-215
    • Wall, J.T.1    Xu, J.2    Wang, X.3
  • 200
    • 0032931819 scopus 로고    scopus 로고
    • Mice lacking link protein develop dwarfism and craniofacial abnormalities
    • Watanabe H., and Yamada Y. Mice lacking link protein develop dwarfism and craniofacial abnormalities. Nat. Genet. 21 (1999) 225-229
    • (1999) Nat. Genet. , vol.21 , pp. 225-229
    • Watanabe, H.1    Yamada, Y.2
  • 202
    • 0842320841 scopus 로고    scopus 로고
    • Diffuse perineuronal nets and modified pyramidal cells immunoreactive for glutamate and the GABA(A) receptor alpha1 subunit form a unique entity in rat cerebral cortex
    • Wegner F., Hartig W., Bringmann A., Grosche J., Wohlfarth K., Zuschratter W., and Bruckner G. Diffuse perineuronal nets and modified pyramidal cells immunoreactive for glutamate and the GABA(A) receptor alpha1 subunit form a unique entity in rat cerebral cortex. Exp. Neurol. 184 (2003) 705-714
    • (2003) Exp. Neurol. , vol.184 , pp. 705-714
    • Wegner, F.1    Hartig, W.2    Bringmann, A.3    Grosche, J.4    Wohlfarth, K.5    Zuschratter, W.6    Bruckner, G.7
  • 203
    • 0030175383 scopus 로고    scopus 로고
    • The proteoglycan DSD-1-PG occurs in perineuronal nets around parvalbumin-immunoreactive interneurons of the rat cerebral cortex
    • Wintergerst E.S., Faissner A., and Celio M.R. The proteoglycan DSD-1-PG occurs in perineuronal nets around parvalbumin-immunoreactive interneurons of the rat cerebral cortex. Int. J. Dev. Neurosci. 14 (1996) 249-255
    • (1996) Int. J. Dev. Neurosci. , vol.14 , pp. 249-255
    • Wintergerst, E.S.1    Faissner, A.2    Celio, M.R.3
  • 204
    • 0035144802 scopus 로고    scopus 로고
    • Glucocorticoid receptor-mediated suppression of activator protein-1 activation and matrix metalloproteinase expression after spinal cord injury
    • Xu J., Kim G.M., Ahmed S.H., Xu J., Yan P., Xu X.M., and Hsu C.Y. Glucocorticoid receptor-mediated suppression of activator protein-1 activation and matrix metalloproteinase expression after spinal cord injury. J. Neurosci. 21 (2001) 92-97
    • (2001) J. Neurosci. , vol.21 , pp. 92-97
    • Xu, J.1    Kim, G.M.2    Ahmed, S.H.3    Xu, J.4    Yan, P.5    Xu, X.M.6    Hsu, C.Y.7
  • 205
    • 0034024027 scopus 로고    scopus 로고
    • Lecticans: organizers of the brain extracellular matrix
    • Yamaguchi Y. Lecticans: organizers of the brain extracellular matrix. Cell. Mol. Life Sci. 57 (2000) 276-289
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 276-289
    • Yamaguchi, Y.1
  • 206
    • 0028069336 scopus 로고
    • Immunohistochemical localization of hyaluronic acid in rat and human brain
    • Yasuhara O., Akiyama H., McGeer E.G., and McGeer P.L. Immunohistochemical localization of hyaluronic acid in rat and human brain. Brain Res. 635 (1994) 269-282
    • (1994) Brain Res. , vol.635 , pp. 269-282
    • Yasuhara, O.1    Akiyama, H.2    McGeer, E.G.3    McGeer, P.L.4
  • 207
    • 0037757588 scopus 로고    scopus 로고
    • Axonal regeneration of Clarke's neurons beyond the spinal cord injury scar after treatment with chondroitinase ABC
    • Yick L.W., Cheung P.T., So K.F., and Wu W. Axonal regeneration of Clarke's neurons beyond the spinal cord injury scar after treatment with chondroitinase ABC. Exp. Neurol. 182 (2003) 160-168
    • (2003) Exp. Neurol. , vol.182 , pp. 160-168
    • Yick, L.W.1    Cheung, P.T.2    So, K.F.3    Wu, W.4
  • 208
    • 3242879990 scopus 로고    scopus 로고
    • Lithium chloride reinforces the regeneration-promoting effect of chondroitinase ABC on rubrospinal neurons after spinal cord injury
    • Yick L.W., So K.F., Cheung P.T., and Wu W.T. Lithium chloride reinforces the regeneration-promoting effect of chondroitinase ABC on rubrospinal neurons after spinal cord injury. J. Neurotrauma 21 (2004) 932-943
    • (2004) J. Neurotrauma , vol.21 , pp. 932-943
    • Yick, L.W.1    So, K.F.2    Cheung, P.T.3    Wu, W.T.4
  • 209
    • 0033950591 scopus 로고    scopus 로고
    • Selective distribution of matrix metalloproteinase-3 (MMP-3) in Alzheimer's disease brain
    • Yoshiyama Y., Asahina M., and Hattori T. Selective distribution of matrix metalloproteinase-3 (MMP-3) in Alzheimer's disease brain. Acta Neuropathol. 99 (2000) 91-95
    • (2000) Acta Neuropathol. , vol.99 , pp. 91-95
    • Yoshiyama, Y.1    Asahina, M.2    Hattori, T.3
  • 210
    • 0036837361 scopus 로고    scopus 로고
    • Association between protease-specific proteolytic cleavage of brevican and synaptic loss in the dentate gyrus of kainate-treated rats
    • Yuan W., Matthews R.T., Sandy J.D., and Gottschall P.E. Association between protease-specific proteolytic cleavage of brevican and synaptic loss in the dentate gyrus of kainate-treated rats. Neuroscience 114 (2002) 1091-1101
    • (2002) Neuroscience , vol.114 , pp. 1091-1101
    • Yuan, W.1    Matthews, R.T.2    Sandy, J.D.3    Gottschall, P.E.4
  • 211
    • 0024624639 scopus 로고
    • Characterization of an activity-dependent, neuronal surface proteoglycan identified with monoclonal antibody Cat-301
    • Zaremba S., Guimaraes A., Kalb R.G., and Hockfield S. Characterization of an activity-dependent, neuronal surface proteoglycan identified with monoclonal antibody Cat-301. Neuron 2 (1989) 1207-1219
    • (1989) Neuron , vol.2 , pp. 1207-1219
    • Zaremba, S.1    Guimaraes, A.2    Kalb, R.G.3    Hockfield, S.4


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