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Volumn 290, Issue 2, 1997, Pages 349-356

Modeling an extracellular environment for axonal pathfinding and fasciculation in the central nervous system

Author keywords

Brain; Extracellular matrix; Hyaluronan; Proteoglycans; Tenascin

Indexed keywords

PROTEOGLYCAN; SCLEROPROTEIN;

EID: 0030729229     PISSN: 0302766X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004410050940     Document Type: Article
Times cited : (69)

References (98)
  • 1
    • 0028800295 scopus 로고
    • Thrombospondin-4, an extracellular matrix protein expressed in the developing and adult nervous system promotes neurite outgrowth
    • Arber S, Caroni P (1995) Thrombospondin-4, an extracellular matrix protein expressed in the developing and adult nervous system promotes neurite outgrowth. J Cell Biol 131:1083-1094
    • (1995) J Cell Biol , vol.131 , pp. 1083-1094
    • Arber, S.1    Caroni, P.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
    • 0027474006 scopus 로고
    • Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins
    • Aukhil I, Joshi P, Yan Y, Erickson HP (1993) Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins. J Biol Chem 268:2542-2553
    • (1993) J Biol Chem , vol.268 , pp. 2542-2553
    • Aukhil, I.1    Joshi, P.2    Yan, Y.3    Erickson, H.P.4
  • 4
    • 0028235153 scopus 로고
    • Receptor tyrosine phosphatase β is expressed in the form of proteoglycan and binds to the extracellular matrix protein tenascin
    • Barnea G, Grumet M, Milev P, Silvennoinen O, Levy JB, Sap J, Schlessinger J (1994) Receptor tyrosine phosphatase β is expressed in the form of proteoglycan and binds to the extracellular matrix protein tenascin. J Biol Chem 269:14349-14352
    • (1994) J Biol Chem , vol.269 , pp. 14349-14352
    • Barnea, G.1    Grumet, M.2    Milev, P.3    Silvennoinen, O.4    Levy, J.B.5    Sap, J.6    Schlessinger, J.7
  • 6
    • 0023612035 scopus 로고
    • Factors guiding optic fibers in developing Xenopus retina
    • Bork T, Schabtach E, Grant P (1987) Factors guiding optic fibers in developing Xenopus retina. J Comp Neurobiol 264:147-158
    • (1987) J Comp Neurobiol , vol.264 , pp. 147-158
    • Bork, T.1    Schabtach, E.2    Grant, P.3
  • 7
    • 0027509462 scopus 로고
    • Glycosaminoglycans and the regulation of blood coagulation
    • Bourin M-C, Lindahl U (1993) Glycosaminoglycans and the regulation of blood coagulation. Biochem J 289:313-330
    • (1993) Biochem J , vol.289 , pp. 313-330
    • Bourin, M.-C.1    Lindahl, U.2
  • 8
    • 0026252643 scopus 로고
    • Tenascin variants: Differential binding to fibronectin and distinct distribution in cell cultures and tissues
    • Chiquet-Ehrismann R, Matsuoka Y, Hofer U, Spring J, Bernasconi C, Chiquet M (1991) Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues. Cell Regul 2:927-938
    • (1991) Cell Regul , vol.2 , pp. 927-938
    • Chiquet-Ehrismann, R.1    Matsuoka, Y.2    Hofer, U.3    Spring, J.4    Bernasconi, C.5    Chiquet, M.6
  • 9
    • 0030432491 scopus 로고    scopus 로고
    • NCAM is essential for axonal growth and fasciculation in the hippocampus
    • Cremer H, Chazal G, Goridis C, Represa A (1997) NCAM is essential for axonal growth and fasciculation in the hippocampus. Mol Cell Neurosci 8:323-335
    • (1997) Mol Cell Neurosci , vol.8 , pp. 323-335
    • Cremer, H.1    Chazal, G.2    Goridis, C.3    Represa, A.4
  • 10
    • 0028940096 scopus 로고
    • A protein related to extracellular matrix proteins deleted in the mouse mutant reeler
    • D'Arcangelo G, Miao GG, Chen S-C, Soares HD, Morgan JI, Curran T (1995) A protein related to extracellular matrix proteins deleted in the mouse mutant reeler. Nature 374:719-723
    • (1995) Nature , vol.374 , pp. 719-723
    • D'Arcangelo, G.1    Miao, G.G.2    Chen, S.-C.3    Soares, H.D.4    Morgan, J.I.5    Curran, T.6
  • 13
    • 0030582672 scopus 로고    scopus 로고
    • The Drosophila beaten path gene encodes a novel secreted protein that regulates defasciculation at motor axon choice points
    • Fambrough D, Goodman CS (1996) The Drosophila beaten path gene encodes a novel secreted protein that regulates defasciculation at motor axon choice points. Cell 87:1049-1058
    • (1996) Cell , vol.87 , pp. 1049-1058
    • Fambrough, D.1    Goodman, C.S.2
  • 14
    • 0028813381 scopus 로고
    • A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C
    • Fischer D, Chiquet-Ehrismann R, Bernasconi C, Chiquet M (1995) A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C. J Biol Chem 270:3378-3384
    • (1995) J Biol Chem , vol.270 , pp. 3378-3384
    • Fischer, D.1    Chiquet-Ehrismann, R.2    Bernasconi, C.3    Chiquet, M.4
  • 15
    • 0022653933 scopus 로고
    • Neurite outgrowth patterns in cerebellar microexplant cultures are affected by antibodies to the cell surface glycoprotein L1
    • Fischer G, Künemund V, Schachner M (1986) Neurite outgrowth patterns in cerebellar microexplant cultures are affected by antibodies to the cell surface glycoprotein L1. J Neurosci 6:605-612
    • (1986) J Neurosci , vol.6 , pp. 605-612
    • Fischer, G.1    Künemund, V.2    Schachner, M.3
  • 18
    • 0028227022 scopus 로고
    • The neuronal chondroitin sulfate proteoglycan neurocan binds to the neural cell adhesion molecules Ng-CAM/L1/NILE and N-CAM and inhibits neuronal adhesion and neurite outgrowth
    • Friedlander DR, Milev P, Karthikeyan L, Margolis RK, Margolis RU, Grumet M (1994) The neuronal chondroitin sulfate proteoglycan neurocan binds to the neural cell adhesion molecules Ng-CAM/L1/NILE and N-CAM and inhibits neuronal adhesion and neurite outgrowth. J Cell Biol 125:669-680
    • (1994) J Cell Biol , vol.125 , pp. 669-680
    • Friedlander, D.R.1    Milev, P.2    Karthikeyan, L.3    Margolis, R.K.4    Margolis, R.U.5    Grumet, M.6
  • 19
    • 0026646196 scopus 로고
    • The high molecular weight cat-301 chondroitin sulfate proteoglycan from brain is related to the large aggregating proteoglycan from cartilage, aggrecan
    • Fryer HJL, Kelly GM, Molinaro L, Hockfield S (1992) The high molecular weight cat-301 chondroitin sulfate proteoglycan from brain is related to the large aggregating proteoglycan from cartilage, aggrecan. J Biol Chem 267:9874-9883
    • (1992) J Biol Chem , vol.267 , pp. 9874-9883
    • Fryer, H.J.L.1    Kelly, G.M.2    Molinaro, L.3    Hockfield, S.4
  • 20
    • 0027397492 scopus 로고
    • Molecular characterization and in situ mRNA localization of the neural recognition molecule JI-160/180: A modular structure similar to tenascin
    • Fuss B, Wintergerst E-S, Bartsch U, Schachner M (1993) Molecular characterization and in situ mRNA localization of the neural recognition molecule JI-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
  • 22
    • 0029958839 scopus 로고    scopus 로고
    • Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor
    • Gesemann M, Cavalli V, Denzer AJ, Brancaccio A, Schumacher B, Ruegg MA (1996) Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor. Neuron 16:755-767
    • (1996) Neuron , vol.16 , pp. 755-767
    • Gesemann, M.1    Cavalli, V.2    Denzer, A.J.3    Brancaccio, A.4    Schumacher, B.5    Ruegg, M.A.6
  • 23
    • 0030948030 scopus 로고    scopus 로고
    • Tenascin-C synthesis and influence on axonal growth during rat cortical development
    • Götz M, Bolz J, Jöster A, Faissner A (1997) Tenascin-C synthesis and influence on axonal growth during rat cortical development. Eur J Neurosci 9:496-506
    • (1997) Eur J Neurosci , vol.9 , pp. 496-506
    • Götz, M.1    Bolz, J.2    Jöster, A.3    Faissner, A.4
  • 24
    • 0027492207 scopus 로고
    • Functional characterization of chondroitin sulfate proteoglycans of brain: Interaction with neurons and neural cell adhesion molecules
    • Grumet M, Flaccus A, Margolis RU (1993) Functional characterization of chondroitin sulfate proteoglycans of brain: interaction with neurons and neural cell adhesion molecules. J Cell Biol 120:815-824
    • (1993) J Cell Biol , vol.120 , pp. 815-824
    • Grumet, M.1    Flaccus, A.2    Margolis, R.U.3
  • 25
    • 0028360757 scopus 로고
    • Interactions with tenascin and differential effects on cell adhesion of neurocan and phosphacan, two major chondroitin sulfate proteoglycans of nervous tissue
    • Grumet M, Milev P, Sakurai T, Karthikeyan L, Bourdon M, Margolis RK, Margolis RU (1994) Interactions with tenascin and differential effects on cell adhesion of neurocan and phosphacan, two major chondroitin sulfate proteoglycans of nervous tissue. J Biol Chem 269:12142-12146
    • (1994) J Biol Chem , vol.269 , pp. 12142-12146
    • Grumet, M.1    Milev, P.2    Sakurai, T.3    Karthikeyan, L.4    Bourdon, M.5    Margolis, R.K.6    Margolis, R.U.7
  • 26
    • 0023192060 scopus 로고
    • Visualisation of neural cell adhesion molecule by electron microscopy
    • Hall AK, Rutishauser U (1987) Visualisation of neural cell adhesion molecule by electron microscopy. J Cell Biol 104:1579-1586
    • (1987) J Cell Biol , vol.104 , pp. 1579-1586
    • Hall, A.K.1    Rutishauser, U.2
  • 28
    • 0030272647 scopus 로고    scopus 로고
    • Dystroglycan: An extracellular matrix receptor linked to the cytoskeleton
    • Henry MD, Campbell KP (1996) Dystroglycan: an extracellular matrix receptor linked to the cytoskeleton. Curr Opin Cell Biol 8:625-631
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 625-631
    • Henry, M.D.1    Campbell, K.P.2
  • 29
    • 0026788499 scopus 로고
    • Expression of S-laminin and laminin in the developing rat central nervous system
    • Hunter DD, Llinas R, Ard M, Merlie JP, Sanes JR (1992) Expression of S-laminin and laminin in the developing rat central nervous system. J Comp Neurobiol 323:238-251
    • (1992) J Comp Neurobiol , vol.323 , pp. 238-251
    • Hunter, D.D.1    Llinas, R.2    Ard, M.3    Merlie, J.P.4    Sanes, J.R.5
  • 30
    • 0028609835 scopus 로고
    • The human laminin β2 chain (S-laminin): Structure, expression in fetal tissues and chromosomal assignment of the LAMB2 gene
    • Iivanainen A, Vuolteenaho R, Sainio K, Eddy R, Shows TB, Sariola H, Tryggvason K (1994) The human laminin β2 chain (S-laminin): structure, expression in fetal tissues and chromosomal assignment of the LAMB2 gene. Matrix Biol 14:489-197
    • (1994) Matrix Biol , vol.14 , pp. 489-1197
    • Iivanainen, A.1    Vuolteenaho, R.2    Sainio, K.3    Eddy, R.4    Shows, T.B.5    Sariola, H.6    Tryggvason, K.7
  • 31
    • 0030010512 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo RV, Murdoch AD (1996) Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J 10:598-614
    • (1996) FASEB J , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 32
    • 0029905441 scopus 로고    scopus 로고
    • Gene therapy by skeletal muscle expression of decorin prevents fibrotic disease in rat kidney
    • Isaka Y, Brees DK, Ikegaya K, Kaneda Y, Imai E, Noble NA, Border WA (1996) Gene therapy by skeletal muscle expression of decorin prevents fibrotic disease in rat kidney. Nat Med 2:418-423
    • (1996) Nat Med , vol.2 , pp. 418-423
    • Isaka, Y.1    Brees, D.K.2    Ikegaya, K.3    Kaneda, Y.4    Imai, E.5    Noble, N.A.6    Border, W.A.7
  • 33
    • 0027534369 scopus 로고
    • A large chondroitin sulfate proteoglycan has the characteristics of a general extracellular matrix component of adult brain
    • Iwata M, Carlson SS (1993) A large chondroitin sulfate proteoglycan has the characteristics of a general extracellular matrix component of adult brain. J Neurosci 13:195-207
    • (1993) J Neurosci , vol.13 , pp. 195-207
    • Iwata, M.1    Carlson, S.S.2
  • 34
    • 0027321176 scopus 로고
    • A brain extracellular matrix proteoglycan forms aggregates with hyaluronan
    • Iwata M, Wight TN, Carlson SS (1993) A brain extracellular matrix proteoglycan forms aggregates with hyaluronan. J Biol Chem 168:15061-15069
    • (1993) J Biol Chem , vol.168 , pp. 15061-15069
    • Iwata, M.1    Wight, T.N.2    Carlson, S.S.3
  • 35
    • 0024535988 scopus 로고
    • A detailed model of cytotactin: Protein homologies, alternative RNA splicing, and binding regions
    • Jones FS, Hoffman S, Cunningham BA, Edelman G (1989) A detailed model of cytotactin: protein homologies, alternative RNA splicing, and binding regions. Proc Natl Acad Sci USA 86:1905-1909
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1905-1909
    • Jones, F.S.1    Hoffman, S.2    Cunningham, B.A.3    Edelman, G.4
  • 36
    • 0028867444 scopus 로고
    • Purification of a meningeal cell-derived chondroitin sulfate proteoglycan with neurotrophic activity for brain neurons and its identification as biglycan
    • Junghans U, Koops A, Westmeyer A, Kappler J, Meyer HE, Müller HW (1995) Purification of a meningeal cell-derived chondroitin sulfate proteoglycan with neurotrophic activity for brain neurons and its identification as biglycan. Eur J Neurosci 7:2341-2350
    • (1995) Eur J Neurosci , vol.7 , pp. 2341-2350
    • Junghans, U.1    Koops, A.2    Westmeyer, A.3    Kappler, J.4    Meyer, H.E.5    Müller, H.W.6
  • 39
    • 0028080261 scopus 로고
    • The leucine rich repeat: A versatile binding motif
    • Kobe B, Deisenhofer J (1994) The leucine rich repeat: a versatile binding motif. Trends Biochem Sci 19:415-421
    • (1994) Trends Biochem Sci , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 40
    • 0030066356 scopus 로고    scopus 로고
    • Semaphorins: Mediators of repulsive growth cone guidance
    • Kolodkin AL (1996) Semaphorins: mediators of repulsive growth cone guidance. Trends Cell Biol 6:15-22
    • (1996) Trends Cell Biol , vol.6 , pp. 15-22
    • Kolodkin, A.L.1
  • 41
    • 0030032097 scopus 로고    scopus 로고
    • The developing avian retina expresses agrin isoforms during synaptogenesis
    • Kröger S, Horton SE, Honig LS (1996) The developing avian retina expresses agrin isoforms during synaptogenesis. J Neurobiol 29:165-182
    • (1996) J Neurobiol , vol.29 , pp. 165-182
    • Kröger, S.1    Horton, S.E.2    Honig, L.S.3
  • 42
    • 0022461523 scopus 로고
    • Cell recognition by neuronal growth cones in a simple vertebrate embryo
    • Kuwada JY (1986) Cell recognition by neuronal growth cones in a simple vertebrate embryo. Science 233:740-746
    • (1986) Science , vol.233 , pp. 740-746
    • Kuwada, J.Y.1
  • 44
    • 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, Hockfield S (1997) A family of activity-dependent neuronal cell-surface chondroitin sulfate proteoglycans in cat visual cortex. J Neurosci 17:1928-1939
    • (1997) J Neurosci , vol.17 , pp. 1928-1939
    • Lander, C.1    Kind, P.2    Maleski, M.3    Hockfield, S.4
  • 45
    • 0029915873 scopus 로고    scopus 로고
    • S103L reactive chondroitin sulfate proteoglycan (aggrecan) mRNA expressed in developing chick brain and cartilage is encoded by a single gene
    • Li H, Domowicz M, Hennig A, Schwartz NB (1996) S103L reactive chondroitin sulfate proteoglycan (aggrecan) mRNA expressed in developing chick brain and cartilage is encoded by a single gene. Mol Brain Res 36:309-321
    • (1996) Mol Brain Res , vol.36 , pp. 309-321
    • Li, H.1    Domowicz, M.2    Hennig, A.3    Schwartz, N.B.4
  • 46
    • 0027959402 scopus 로고
    • Genetic analysis of fasciclin II in Drosophila: Defasciculation, refasciculation and altered fasciculation
    • Lin DM, Fetter RD, Kopczynski C, Grenningloh G, Goodman CS (1994) Genetic analysis of fasciclin II in Drosophila: defasciculation, refasciculation and altered fasciculation. Neuron 13:1055-1069
    • (1994) Neuron , vol.13 , pp. 1055-1069
    • Lin, D.M.1    Fetter, R.D.2    Kopczynski, C.3    Grenningloh, G.4    Goodman, C.S.5
  • 47
    • 0025836594 scopus 로고
    • JI/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth
    • Lochter A, Vaughan L, Kaplony A, Prochiantz A, Schachner M, Faissner A (1991) JI/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth. J Cell Biol 113:1159-1171
    • (1991) J Cell Biol , vol.113 , pp. 1159-1171
    • Lochter, A.1    Vaughan, L.2    Kaplony, A.3    Prochiantz, A.4    Schachner, M.5    Faissner, A.6
  • 48
    • 0031053932 scopus 로고    scopus 로고
    • Laminin and mechanism of neuronal outgrowth
    • Luckenbill-Edds L (1997) Laminin and mechanism of neuronal outgrowth. Brain Res Rev 23:1-27
    • (1997) Brain Res Rev , vol.23 , pp. 1-27
    • Luckenbill-Edds, L.1
  • 49
    • 0027373701 scopus 로고
    • Collapsin: A protein in brain that induces the collapse and paralysis of neuronal growth cones
    • Luo Y, Raible D, Raper JA (1993) Collapsin: a protein in brain that induces the collapse and paralysis of neuronal growth cones. Cell 75:217-227
    • (1993) Cell , vol.75 , pp. 217-227
    • Luo, Y.1    Raible, D.2    Raper, J.A.3
  • 51
    • 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 RK, Margolis RU (1994) 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 USA 91:2512-2516
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2512-2516
    • Maurel, P.1    Rauch, U.2    Flad, M.3    Margolis, R.K.4    Margolis, R.U.5
  • 52
    • 0024358887 scopus 로고
    • Subplate neurons pioneer the first axon pathway from the cerebral cortex
    • McConnell SK, Ghosh A, Shatz CJ (1989) Subplate neurons pioneer the first axon pathway from the cerebral cortex. Science 245:978-982
    • (1989) Science , vol.245 , pp. 978-982
    • McConnell, S.K.1    Ghosh, A.2    Shatz, C.J.3
  • 53
    • 0028123375 scopus 로고
    • Developmental expression in the rat cerebellum of SC1, a putative brain extracellular matrix glycoprotein related to SPARK
    • Mendis DB, Shahin S, Gurd JW, Brown IR (1994) Developmental expression in the rat cerebellum of SC1, a putative brain extracellular matrix glycoprotein related to SPARK. Brain Res 633:197-205
    • (1994) Brain Res , vol.633 , pp. 197-205
    • Mendis, D.B.1    Shahin, S.2    Gurd, J.W.3    Brown, I.R.4
  • 54
    • 0028865943 scopus 로고
    • Chondroitin sulfate and chondroitin/keratan sulfate proteoglycans of nervous tissue: Developmental changes of neurocan and phosphacan
    • Meyer-Puttlitz B, Milev P, Junker E, Zimmer I, Margolis RU, Margolis RK (1995) Chondroitin sulfate and chondroitin/keratan sulfate proteoglycans of nervous tissue: developmental changes of neurocan and phosphacan. J Neurochem 65:2327-2337
    • (1995) J Neurochem , vol.65 , pp. 2327-2337
    • Meyer-Puttlitz, B.1    Milev, P.2    Junker, E.3    Zimmer, I.4    Margolis, R.U.5    Margolis, R.K.6
  • 55
    • 0030043021 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycans in the developing central nervous system. II. Immunocytochemical localization of neurocan and phosphacan
    • Meyer-Puttlitz B, Junker E, Margolis RU, Margolis RK (1996) Chondroitin sulfate proteoglycans in the developing central nervous system. II. Immunocytochemical localization of neurocan and phosphacan. J Comp Neurol 366:44-54
    • (1996) J Comp Neurol , vol.366 , pp. 44-54
    • Meyer-Puttlitz, B.1    Junker, E.2    Margolis, R.U.3    Margolis, R.K.4
  • 56
    • 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
  • 57
    • 0028879844 scopus 로고
    • Complex-type asparagine-linked oligosaccharides on phosphacan and protein-tyrosine phosphatase-β mediate their binding to neural cell adhesion molecules and tenascin
    • Milev P, Meyer-Puttlitz B, Margolis RK, Margolis RU (1995) Complex-type asparagine-linked oligosaccharides on phosphacan and protein-tyrosine phosphatase-β mediate their binding to neural cell adhesion molecules and tenascin. J Biol Chem 270:24650-24653
    • (1995) J Biol Chem , vol.270 , pp. 24650-24653
    • Milev, P.1    Meyer-Puttlitz, B.2    Margolis, R.K.3    Margolis, R.U.4
  • 58
    • 0023924614 scopus 로고
    • Thrombospondin is present in articular cartilage and is synthezised by articular chondrocytes
    • Miller RR, McDevitt CA (1988) Thrombospondin is present in articular cartilage and is synthezised by articular chondrocytes. Biochem Biophys Res Commun 153:708-714
    • (1988) Biochem Biophys Res Commun , vol.153 , pp. 708-714
    • Miller, R.R.1    McDevitt, C.A.2
  • 59
    • 0029026390 scopus 로고
    • Chondroitin sulfate protoglycans in the developing cerebral cortex: The distribution of neurocan distinguishes forming afferent and efferent axonal pathways
    • Miller B, Sheppard AM, Bicknese AR, Pearlman AL (1995) Chondroitin sulfate protoglycans in the developing cerebral cortex: the distribution of neurocan distinguishes forming afferent and efferent axonal pathways. J Comp Neurol 355:615-628
    • (1995) J Comp Neurol , vol.355 , pp. 615-628
    • Miller, B.1    Sheppard, A.M.2    Bicknese, A.R.3    Pearlman, A.L.4
  • 60
    • 0028314130 scopus 로고
    • The cartilage proteoglycan aggregate: Assembly through combined protein-carbohydrate and protein-protein interactions
    • Mörgelin M, Heinegard D, Engel J, Paulson M (1994) The cartilage proteoglycan aggregate: assembly through combined protein-carbohydrate and protein-protein interactions. Biophys Chem 50:113-128
    • (1994) Biophys Chem , vol.50 , pp. 113-128
    • Mörgelin, M.1    Heinegard, D.2    Engel, J.3    Paulson, M.4
  • 61
    • 0028908326 scopus 로고
    • Abberant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin β2
    • Noakes PG, Gautam M, Mudd J, Sanes JR, Merlie JP (1995) Abberant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin β2. Nature 374:258-262
    • (1995) Nature , vol.374 , pp. 258-262
    • Noakes, P.G.1    Gautam, M.2    Mudd, J.3    Sanes, J.R.4    Merlie, J.P.5
  • 62
    • 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
  • 63
    • 0029088317 scopus 로고
    • New insights into the function of collagens from genetic analysis
    • Olsen BR (1995) New insights into the function of collagens from genetic analysis. Curr Opin Cell Biol 7:720-727
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 720-727
    • Olsen, B.R.1
  • 64
    • 0028350412 scopus 로고
    • Developmentally regulated expression of a brain specific species of chondroitin sulfate proteoglycan, neurocan, identified with a monoclonal antibody 1G2 in rat cerebrum
    • Oohira A, Matsui F, Watanabe E, Kushima Y, Maeda N (1994) Developmentally regulated expression of a brain specific species of chondroitin sulfate proteoglycan, neurocan, identified with a monoclonal antibody 1G2 in rat cerebrum. Neuroscience 60:145-157
    • (1994) Neuroscience , vol.60 , pp. 145-157
    • Oohira, A.1    Matsui, F.2    Watanabe, E.3    Kushima, Y.4    Maeda, N.5
  • 65
    • 0029616028 scopus 로고
    • Tenascin-C and the development of articular cartilage
    • Pacifici M (1995) Tenascin-C and the development of articular cartilage. Matrix Biol 14:689-698
    • (1995) Matrix Biol , vol.14 , pp. 689-698
    • Pacifici, M.1
  • 66
    • 0030026572 scopus 로고    scopus 로고
    • Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins
    • Pall EA, Bolton KM, Ervasti (1996) Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins. J Biol Chem 271:3817-3821
    • (1996) J Biol Chem , vol.271 , pp. 3817-3821
    • Pall, E.A.1    Bolton, K.M.2    Ervasti3
  • 67
    • 0024590223 scopus 로고
    • Isolation and partial characterization of a glial hyaluronate-binding protein
    • Perides G, Lane WS, Andrews D, Dahl D, Bignami A (1989) Isolation and partial characterization of a glial hyaluronate-binding protein. J Biol Chem 264:5981-5987
    • (1989) J Biol Chem , vol.264 , pp. 5981-5987
    • Perides, G.1    Lane, W.S.2    Andrews, D.3    Dahl, D.4    Bignami, A.5
  • 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
    • 0000588602 scopus 로고    scopus 로고
    • Articular cartilage
    • Comper WD (ed) Harwood, Amsterdam
    • Ratcliffe A, Mow VC (1996) Articular cartilage. In: Comper WD (ed) Extracellular matrix vol 1. Harwood, Amsterdam, pp 234-302
    • (1996) Extracellular Matrix , vol.1 , pp. 234-302
    • Ratcliffe, A.1    Mow, V.C.2
  • 70
    • 0026320302 scopus 로고
    • Isolation and characterisation of developmentally regulated chondroitin sulfate and chondroitin/keratan sulfate proteoglycans of brain identified with monoclonal antibodies
    • Rauch U, Gao P, Janetzko A, Flaccus A, Hilgenberg L, Tekotte H, Margolis RK, Margolis RU (1991) Isolation and characterisation of developmentally regulated chondroitin sulfate and chondroitin/keratan sulfate proteoglycans of brain identified with monoclonal antibodies. J Biol Chem 266:14785-14801
    • (1991) J Biol Chem , vol.266 , pp. 14785-14801
    • Rauch, U.1    Gao, P.2    Janetzko, A.3    Flaccus, A.4    Hilgenberg, L.5    Tekotte, H.6    Margolis, R.K.7    Margolis, R.U.8
  • 71
    • 0026758360 scopus 로고
    • Cloning and primary structure of neurocan, a developmentally regulated, aggregating chondroitin sulfate proteoglycan of brain
    • Rauch U, Karthikeyan L, Maurel P, Margolis RU, Margolis RK (1992) Cloning and primary structure of neurocan, a developmentally regulated, aggregating chondroitin sulfate proteoglycan of brain. J Biol Chem 267:19536-19547
    • (1992) J Biol Chem , vol.267 , pp. 19536-19547
    • Rauch, U.1    Karthikeyan, L.2    Maurel, P.3    Margolis, R.U.4    Margolis, R.K.5
  • 72
    • 0030054721 scopus 로고    scopus 로고
    • Structural and electron microscopic analysis of neurocan and recombinant neurocan fragments
    • Retzler C, Wiedemann H, Kulbe G, Rauch U (1996) Structural and electron microscopic analysis of neurocan and recombinant neurocan fragments. J Biol Chem 271:17107-17113
    • (1996) J Biol Chem , vol.271 , pp. 17107-17113
    • Retzler, C.1    Wiedemann, H.2    Kulbe, G.3    Rauch, U.4
  • 73
    • 0029670544 scopus 로고    scopus 로고
    • Agrin, laminin β2 (s-laminin) and ARIA: Their role in neuromuscular development
    • Ruegg MA (1996) Agrin, laminin β2 (s-laminin) and ARIA: their role in neuromuscular development. Curr Opin Neurobiol 6:97-103
    • (1996) Curr Opin Neurobiol , vol.6 , pp. 97-103
    • Ruegg, M.A.1
  • 74
    • 0029823181 scopus 로고    scopus 로고
    • Brain extracellular matrix
    • Ruoslahti E (1996) Brain extracellular matrix. Glycobiology 6:489-492
    • (1996) Glycobiology , vol.6 , pp. 489-492
    • Ruoslahti, E.1
  • 75
    • 0026080765 scopus 로고
    • Proteoglycans as modulators of growth factor activities
    • Ruoslahti E, Yamaguchi Y (1991) Proteoglycans as modulators of growth factor activities. Cell 64:867-869
    • (1991) Cell , vol.64 , pp. 867-869
    • Ruoslahti, E.1    Yamaguchi, Y.2
  • 77
    • 0028138219 scopus 로고
    • The netrins define a family of axon outgrowth-promoting proteins homologous to C. elegans UNC-6
    • Scrafini T, Kennedy TE, Galko MJ, Mirzayan C, Jessel TM, Tessier-Lavigne M (1994) The netrins define a family of axon outgrowth-promoting proteins homologous to C. elegans UNC-6 Cell 78:409-424
    • (1994) Cell , vol.78 , pp. 409-424
    • Scrafini, T.1    Kennedy, T.E.2    Galko, M.J.3    Mirzayan, C.4    Jessel, T.M.5    Tessier-Lavigne, M.6
  • 79
    • 0026348710 scopus 로고
    • Changes in the distribution of extracellular matrix components accompany early morphogenetic events of mammalian cortical development
    • Sheppard AM, Hamilton SK, Pearlman AL (1991) Changes in the distribution of extracellular matrix components accompany early morphogenetic events of mammalian cortical development. J Neurosci 11:3928-3942
    • (1991) J Neurosci , vol.11 , pp. 3928-3942
    • Sheppard, A.M.1    Hamilton, S.K.2    Pearlman, A.L.3
  • 81
    • 0020450136 scopus 로고
    • Afferent and efferent connections of the striate and extrastriate visual cortex of the normal and reeler mouse
    • Simmons PA, Lemmon V, Pearlman AL (1982) Afferent and efferent connections of the striate and extrastriate visual cortex of the normal and reeler mouse. J Comp Neurol 211:295-308
    • (1982) J Comp Neurol , vol.211 , pp. 295-308
    • Simmons, P.A.1    Lemmon, V.2    Pearlman, A.L.3
  • 82
    • 0026548436 scopus 로고
    • Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease
    • Snow AD, Mar H, Nochlin D, Kresse H, Wight TN (1992) Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease. J Histochem Cytochem 40:105-113
    • (1992) J Histochem Cytochem , vol.40 , pp. 105-113
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kresse, H.4    Wight, T.N.5
  • 84
    • 0029583304 scopus 로고
    • Differential expression of the small chondroitin/dermatan sulfate proteoglycans decorin and biglycan after injury of the adult rat brain
    • Stichel CC, Kappler J, Junghans U, Koops A, Kresse H, Müller HW (1995) Differential expression of the small chondroitin/dermatan sulfate proteoglycans decorin and biglycan after injury of the adult rat brain. Brain Res 704:263-274
    • (1995) Brain Res , vol.704 , pp. 263-274
    • Stichel, C.C.1    Kappler, J.2    Junghans, U.3    Koops, A.4    Kresse, H.5    Müller, H.W.6
  • 85
    • 0028823323 scopus 로고
    • Tissue- and age-specific expression patterns of alternatively spliced agrin mRNA transcripts in embryonic rat suggest novel developmental role
    • Stone DM, Nikolics K (1995) Tissue- and age-specific expression patterns of alternatively spliced agrin mRNA transcripts in embryonic rat suggest novel developmental role. J Neurosci 15:6767-6778
    • (1995) J Neurosci , vol.15 , pp. 6767-6778
    • Stone, D.M.1    Nikolics, K.2
  • 87
    • 0028084897 scopus 로고
    • Disaccharide composition of heparan sulfates: Brain, nervous tissue storage organelles, kidney, and lung
    • Tekotte H, Engel M, Margolis RU, Margolis RK (1994) Disaccharide composition of heparan sulfates: brain, nervous tissue storage organelles, kidney, and lung. J Neurochem 62:1126-1130
    • (1994) J Neurochem , vol.62 , pp. 1126-1130
    • Tekotte, H.1    Engel, M.2    Margolis, R.U.3    Margolis, R.K.4
  • 88
    • 0029959555 scopus 로고    scopus 로고
    • The molecular biology of axon guidance
    • Tessier-Lavigne M, Goodman CS (1996) The molecular biology of axon guidance. Science 274:1123-1133
    • (1996) Science , vol.274 , pp. 1123-1133
    • Tessier-Lavigne, M.1    Goodman, C.S.2
  • 89
    • 0030462678 scopus 로고    scopus 로고
    • Dystroglycan in the cerebellum is a laminin alpha 2-chain binding protein at the glial-vascular interface and is expressed in Purkinje cells
    • Tian M, Jacobson C, Gee SH, Campbell KP, Carbonetto S, Jucker M (1996) Dystroglycan in the cerebellum is a laminin alpha 2-chain binding protein at the glial-vascular interface and is expressed in Purkinje cells. Eur J Neurosci 8:2739-2747
    • (1996) Eur J Neurosci , vol.8 , pp. 2739-2747
    • Tian, M.1    Jacobson, C.2    Gee, S.H.3    Campbell, K.P.4    Carbonetto, S.5    Jucker, M.6
  • 90
    • 0030271572 scopus 로고    scopus 로고
    • Macromolecular organization of basement membranes
    • Timpl R (1996) Macromolecular organization of basement membranes. Curr Opin Cell Biol 8:618-624
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 618-624
    • Timpl, R.1
  • 92
    • 0030575182 scopus 로고    scopus 로고
    • Binding of contactin/F11 to the fibronectin type III domains 5 and 6 of tenascin is inhibited by heparin
    • Weber P, Ferber P, Fischer R, Winterhalter KH, Vaughan L (1996) Binding of contactin/F11 to the fibronectin type III domains 5 and 6 of tenascin is inhibited by heparin. FEBS Lett 389:304-308
    • (1996) FEBS Lett , vol.389 , pp. 304-308
    • Weber, P.1    Ferber, P.2    Fischer, R.3    Winterhalter, K.H.4    Vaughan, L.5
  • 93
    • 0025965905 scopus 로고
    • Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis
    • Weller A, Beck S, Ekblom P (1991) Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis. J Cell Biol 112:355-362
    • (1991) J Cell Biol , vol.112 , pp. 355-362
    • Weller, A.1    Beck, S.2    Ekblom, P.3
  • 95
    • 0028233391 scopus 로고
    • Molecular cloning of brevican, a novel brain proteoglycan of the aggrecan/versican family
    • Yamada H, Watanabe K, Shimonaka M, Yamaguchi Y (1994) Molecular cloning of brevican, a novel brain proteoglycan of the aggrecan/versican family. J Biol Chem 269:10119-10126
    • (1994) J Biol Chem , vol.269 , pp. 10119-10126
    • Yamada, H.1    Watanabe, K.2    Shimonaka, M.3    Yamaguchi, Y.4
  • 96
    • 0029796370 scopus 로고    scopus 로고
    • Differential effects of the integrins α9β1, αvβ3, and αvβ6 on cell proliferative responses to tenascin. Roles of the β subunit extracellular and cytoplasmic domains
    • Yokosaki Y, Monis H, Chen J, Sheppard D (1996) Differential effects of the integrins α9β1, αvβ3, and αvβ6 on cell proliferative responses to tenascin. Roles of the β subunit extracellular and cytoplasmic domains. J Biol Chem 271:24144-24150
    • (1996) J Biol Chem , vol.271 , pp. 24144-24150
    • Yokosaki, Y.1    Monis, H.2    Chen, J.3    Sheppard, D.4
  • 97
    • 0024397823 scopus 로고
    • Multiple domains of the large fibroblast proteoglycan, versican
    • Zimmermann DR, Ruoslahti F (1989) Multiple domains of the large fibroblast proteoglycan, versican. EMBO J 8:2975-2981
    • (1989) EMBO J , vol.8 , pp. 2975-2981
    • Zimmermann, D.R.1    Ruoslahti, F.2


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