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Volumn 74, Issue 3, 2003, Pages 417-429

Extracellular Matrix and Matrix Metalloproteinases in Sciatic Nerve

Author keywords

Extracellular matrix; Matrix metalloproteinases; PNS; Sciatic nerve; TIMP

Indexed keywords

GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE; MESSENGER RNA; TISSUE INHIBITOR OF METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 3;

EID: 0242267128     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/jnr.10783     Document Type: Review
Times cited : (60)

References (68)
  • 2
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker AH, Edwards DR, Murphy G. 2002. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J Cell Sci 115:3719-3727.
    • (2002) J Cell Sci , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 5
    • 0031726740 scopus 로고    scopus 로고
    • Schwann cells use a novel collagen-dependent mechanism for fibronectin fibril assembly
    • Chernousov MA, Stahl RC, Carey DJ. 1998. Schwann cells use a novel collagen-dependent mechanism for fibronectin fibril assembly. J Cell Sci 111:2763-2777.
    • (1998) J Cell Sci , vol.111 , pp. 2763-2777
    • Chernousov, M.A.1    Stahl, R.C.2    Carey, D.J.3
  • 6
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: The laminin family of heterotrimers
    • Colognato H, Yurchenco PD. 2000. Form and function: the laminin family of heterotrimers. Dev Dyn 218:213-234.
    • (2000) Dev Dyn , vol.218 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.D.2
  • 8
    • 0034959474 scopus 로고    scopus 로고
    • MMP-related gelatinase activity is strongly induced in scar tissue of injured adult spinal cord and forms pathways for ingrowing neurites
    • Duchossoy Y, Horvat JC, Stettler O. 2001. MMP-related gelatinase activity is strongly induced in scar tissue of injured adult spinal cord and forms pathways for ingrowing neurites. Mol Cell Neurosci 17:945-956.
    • (2001) Mol Cell Neurosci , vol.17 , pp. 945-956
    • Duchossoy, Y.1    Horvat, J.C.2    Stettler, O.3
  • 9
    • 0029996328 scopus 로고    scopus 로고
    • Differential effects of transforming growth factor-beta 1 on the expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in young and old human fibroblasts
    • Edwards DR, Leco KJ, Beaudry PP, Atadja PW, Veillette C, Riabowol KT. 1996. Differential effects of transforming growth factor-beta 1 on the expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in young and old human fibroblasts. Exp Gerontol 31:207-223.
    • (1996) Exp Gerontol , vol.31 , pp. 207-223
    • Edwards, D.R.1    Leco, K.J.2    Beaudry, P.P.3    Atadja, P.W.4    Veillette, C.5    Riabowol, K.T.6
  • 10
    • 0034333458 scopus 로고    scopus 로고
    • Differential spatial distribution and temporal regulation of tissue inhibitor of metalloproteinase mRNA meta expression during rat central nervous system development
    • Fager N, Jaworski DM. 2000. Differential spatial distribution and temporal regulation of tissue inhibitor of metalloproteinase mRNA meta expression during rat central nervous system development. Mech Dev 98:105-109.
    • (2000) Mech Dev , vol.98 , pp. 105-109
    • Fager, N.1    Jaworski, D.M.2
  • 11
    • 0033836577 scopus 로고    scopus 로고
    • MMP-2 and MMP-9 increase the neurite-promoting potential of Schwann cell basal laminae and are upregulated in degenerated nerve
    • Ferguson TA, Muir D. 2000. MMP-2 and MMP-9 increase the neurite-promoting potential of Schwann cell basal laminae and are upregulated in degenerated nerve. Mol Cell Neurosci 16:157-167.
    • (2000) Mol Cell Neurosci , vol.16 , pp. 157-167
    • Ferguson, T.A.1    Muir, D.2
  • 13
    • 0035831302 scopus 로고    scopus 로고
    • Collaboration of fibronectin matrix and neurotrophin in regulating spontaneous transmitter release at developing neuromuscular synapses in Xenopus cell cultures
    • Fu WM, Liou HH, Wang CL. 2001. Collaboration of fibronectin matrix and neurotrophin in regulating spontaneous transmitter release at developing neuromuscular synapses in Xenopus cell cultures. Neurosci Lett 300:115-119.
    • (2001) Neurosci Lett , vol.300 , pp. 115-119
    • Fu, W.M.1    Liou, H.H.2    Wang, C.L.3
  • 14
    • 0030818072 scopus 로고    scopus 로고
    • Fibronectins are essential for heart and blood vessel morphogenesis but are dispensable for initial specification of precursor cells
    • George EL, Baldwin HS, Hynes RO. 1997. Fibronectins are essential for heart and blood vessel morphogenesis but are dispensable for initial specification of precursor cells. Blood 90:3073-3081.
    • (1997) Blood , vol.90 , pp. 3073-3081
    • George, E.L.1    Baldwin, H.S.2    Hynes, R.O.3
  • 15
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • George EL, Georges-Labouesse EN, Patel-King RS, Rayburn H, Hynes RO. 1993. Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development 119:1079-1091.
    • (1993) Development , vol.119 , pp. 1079-1091
    • George, E.L.1    Georges-Labouesse, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 16
    • 0034161684 scopus 로고    scopus 로고
    • T lymphocytes activated by persistent viral infection differentially modify the expression of metalloproteinases and their endogenous inhibitors, TIMPs, in human astrocytes: Relevance to HTLV-I-induced neurological disease
    • Giraudon P, Szymocha R, Buart S, Bernard A, Cartier L, Belin MF, Akaoka H. 2000. T lymphocytes activated by persistent viral infection differentially modify the expression of metalloproteinases and their endogenous inhibitors, TIMPs, in human astrocytes: relevance to HTLV-I-induced neurological disease. J Immunol 164:2718-2727.
    • (2000) J Immunol , vol.164 , pp. 2718-2727
    • Giraudon, P.1    Szymocha, R.2    Buart, S.3    Bernard, A.4    Cartier, L.5    Belin, M.F.6    Akaoka, H.7
  • 17
    • 0034715896 scopus 로고    scopus 로고
    • Insights into extracellular matrix functions from mutant mouse models
    • Gustafsson E, Fassler R. 2000. Insights into extracellular matrix functions from mutant mouse models. Exp Cell Res 261:52-68.
    • (2000) Exp Cell Res , vol.261 , pp. 52-68
    • Gustafsson, E.1    Fassler, R.2
  • 18
    • 0035127422 scopus 로고    scopus 로고
    • Proteoglycans in the nervous system - The quest for functional roles in vivo
    • Hartmann U, Maurer P. 2001. Proteoglycans in the nervous system - the quest for functional roles in vivo. Matrix Biol 20:23-35.
    • (2001) Matrix Biol , vol.20 , pp. 23-35
    • Hartmann, U.1    Maurer, P.2
  • 19
    • 0037067980 scopus 로고    scopus 로고
    • Comparison of matrix metalloproteinase expression during Wallerian degeneration in the central and peripheral nervous systems
    • Hughes PM, Wells GM, Perry VH, Brown MC, Miller KM. 2002. Comparison of matrix metalloproteinase expression during Wallerian degeneration in the central and peripheral nervous systems. Neuroscience 113:273-287.
    • (2002) Neuroscience , vol.113 , pp. 273-287
    • Hughes, P.M.1    Wells, G.M.2    Perry, V.H.3    Brown, M.C.4    Miller, K.M.5
  • 21
    • 0035370582 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitor KB-R7785 attenuates brain damage resulting from permanent focal cerebral ischemia in mice
    • 41-057 44
    • Jiang X, Namura S, Nagata I. 2001. Matrix metalloproteinase inhibitor KB-R7785 attenuates brain damage resulting from permanent focal cerebral ischemia in mice. Neurosci Lett 305:41-057 44.
    • (2001) Neurosci Lett , vol.305
    • Jiang, X.1    Namura, S.2    Nagata, I.3
  • 22
    • 0033546198 scopus 로고    scopus 로고
    • Evidence for combinatorial variability of tenascin-C isoforms and developmental regulation in the mouse central nervous system
    • Joester A, Faissner A. 1999. Evidence for combinatorial variability of tenascin-C isoforms and developmental regulation in the mouse central nervous system. J Biol Chem 274:17144-17151.
    • (1999) J Biol Chem , vol.274 , pp. 17144-17151
    • Joester, A.1    Faissner, A.2
  • 23
    • 0035113059 scopus 로고    scopus 로고
    • The structure and function of tenascins in the nervous system
    • Joester A, Faissner A. 2001. The structure and function of tenascins in the nervous system. Matrix Biol 20:13-22.
    • (2001) Matrix Biol , vol.20 , pp. 13-22
    • Joester, A.1    Faissner, A.2
  • 24
    • 0031948880 scopus 로고    scopus 로고
    • Adhesion molecules and inherited diseases of the human nervous system
    • Kamiguchi H, Hlavin ML, Yamasaki M, Lemmon V. 1998. Adhesion molecules and inherited diseases of the human nervous system. Annu Rev Neurosci 21:97-125.
    • (1998) Annu Rev Neurosci , vol.21 , pp. 97-125
    • Kamiguchi, H.1    Hlavin, M.L.2    Yamasaki, M.3    Lemmon, V.4
  • 27
    • 0030898796 scopus 로고    scopus 로고
    • The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction
    • Knauper V, Cowell S, Smith B, Lopez-Otin C, O'Shea M, Morris H, Zardi L, Murphy G. 1997. The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction. J Biol Chem 272:7608-7616.
    • (1997) J Biol Chem , vol.272 , pp. 7608-7616
    • Knauper, V.1    Cowell, S.2    Smith, B.3    Lopez-Otin, C.4    O'Shea, M.5    Morris, H.6    Zardi, L.7    Murphy, G.8
  • 28
    • 0036222734 scopus 로고    scopus 로고
    • The modulation of matrix metalloproteinase and ADAM gene expression in human chondrocytes by interleukin-1 and oncostatin M: A time-course study using real-time quantitative reverse transcription-polymerase chain reaction
    • Koshy PJ, Lundy CJ, Rowan AD, Porter S, Edwards DR, Hogan A, Clark IM, Cawston TE. 2002. The modulation of matrix metalloproteinase and ADAM gene expression in human chondrocytes by interleukin-1 and oncostatin M: a time-course study using real-time quantitative reverse transcription-polymerase chain reaction. Arthritis Rheum 46:961-967.
    • (2002) Arthritis Rheum , vol.46 , pp. 961-967
    • Koshy, P.J.1    Lundy, C.J.2    Rowan, A.D.3    Porter, S.4    Edwards, D.R.5    Hogan, A.6    Clark, I.M.7    Cawston, T.E.8
  • 29
    • 0034668731 scopus 로고    scopus 로고
    • Motor axon pathfinding in the peripheral nervous system
    • Krull CE, Koblar SA. 2000. Motor axon pathfinding in the peripheral nervous system. Brain Res Bull 53:479-487.
    • (2000) Brain Res Bull , vol.53 , pp. 479-487
    • Krull, C.E.1    Koblar, S.A.2
  • 30
    • 0032798871 scopus 로고    scopus 로고
    • Complete exon-intron organization and chromosomal location of the gene for mouse type XIII collagen (col13a1) and comparison with its human homologue
    • Kvist AP, Latvanlehto A, Sund M, Horelli-Kuitunen N, Rehn M, Palotie A, Beier D, Pihlajaniemi T. 1999. Complete exon-intron organization and chromosomal location of the gene for mouse type XIII collagen (col13a1) and comparison with its human homologue. Matrix Biol 18:261-274.
    • (1999) Matrix Biol , vol.18 , pp. 261-274
    • Kvist, A.P.1    Latvanlehto, A.2    Sund, M.3    Horelli-Kuitunen, N.4    Rehn, M.5    Palotie, A.6    Beier, D.7    Pihlajaniemi, T.8
  • 32
    • 0030442578 scopus 로고    scopus 로고
    • Basement membrane and repair of injury to peripheral nerve: Defining a potential role for macrophages, matrix metalloproteinases, and tissue inhibitor of metalloproteinases-1
    • La Fleur M, Underwood JL, Rappolee DA, Werb Z. 1996. Basement membrane and repair of injury to peripheral nerve: defining a potential role for macrophages, matrix metalloproteinases, and tissue inhibitor of metalloproteinases-1. J Exp Med 184:2311-2326.
    • (1996) J Exp Med , vol.184 , pp. 2311-2326
    • La Fleur, M.1    Underwood, J.L.2    Rappolee, D.A.3    Werb, Z.4
  • 33
    • 0034842248 scopus 로고    scopus 로고
    • The expression profile of matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) in lesions and normal appearing white matter of multiple sclerosis
    • Lindberg RL, De Groot CJ, Montagne L, Freitag P, van der Valk P, Kappos L, Leppert D. 2001. The expression profile of matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) in lesions and normal appearing white matter of multiple sclerosis. Brain 124:1743-1753.
    • (2001) Brain , vol.124 , pp. 1743-1753
    • Lindberg, R.L.1    De Groot, C.J.2    Montagne, L.3    Freitag, P.4    Van der Valk, P.5    Kappos, L.6    Leppert, D.7
  • 34
    • 0031053932 scopus 로고    scopus 로고
    • Laminin and the mechanism of neuronal out-growth
    • Luckenbill-Edds L. 1997. Laminin and the mechanism of neuronal out-growth. Brain Res Brain Res Rev 23:1-27.
    • (1997) Brain Res Brain Res Rev , vol.23 , pp. 1-27
    • Luckenbill-Edds, L.1
  • 35
    • 0033491886 scopus 로고    scopus 로고
    • The tenascin-C knockout revisited
    • Mackie EJ, Tucker RP. 1999. The tenascin-C knockout revisited. J Cell Sci 112:3847-3853.
    • (1999) J Cell Sci , vol.112 , pp. 3847-3853
    • Mackie, E.J.1    Tucker, R.P.2
  • 37
    • 0030115294 scopus 로고    scopus 로고
    • Role of laminin and integrin interactions in growth cone guidance
    • McKerracher L, Chamoux M, Arregui CO. 1996. Role of laminin and integrin interactions in growth cone guidance. Mol Neurobiol 12:95-116.
    • (1996) Mol Neurobiol , vol.12 , pp. 95-116
    • McKerracher, L.1    Chamoux, M.2    Arregui, C.O.3
  • 38
    • 0031971199 scopus 로고    scopus 로고
    • Effects of collagenase-cleavage of type I collagen on alpha2beta1 integrin-mediated cell adhesion
    • Messent AJ, Tuckwell DS, Knauper V, Humphries MJ, Murphy G, Gavrilovic J. 1998. Effects of collagenase-cleavage of type I collagen on alpha2beta1 integrin-mediated cell adhesion. J Cell Sci 111:1127-1135.
    • (1998) J Cell Sci , vol.111 , pp. 1127-1135
    • Messent, A.J.1    Tuckwell, D.S.2    Knauper, V.3    Humphries, M.J.4    Murphy, G.5    Gavrilovic, J.6
  • 40
    • 0026601095 scopus 로고
    • Stromelysin generates a fibronectin fragment that inhibits Schwann cell proliferation
    • Muir D, Manthorpe M. 1992. Stromelysin generates a fibronectin fragment that inhibits Schwann cell proliferation. J Cell Biol 116:177-185.
    • (1992) J Cell Biol , vol.116 , pp. 177-185
    • Muir, D.1    Manthorpe, M.2
  • 41
    • 0032820711 scopus 로고    scopus 로고
    • Proteolysis and cell migration: Creating a path?
    • Murphy G, Gavrilovic J. 1999. Proteolysis and cell migration: creating a path? Curr Opin Cell Biol 11:614-621.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 614-621
    • Murphy, G.1    Gavrilovic, J.2
  • 43
    • 0036758650 scopus 로고    scopus 로고
    • Matrix metalloproteinases limit functional recovery after spinal cord injury by modulation of early vascular events
    • Noble LJ, Donovan F, Igarashi T, Goussev S, Werb Z. 2002. Matrix metalloproteinases limit functional recovery after spinal cord injury by modulation of early vascular events. J Neurosci 22:7526-7535.
    • (2002) J Neurosci , vol.22 , pp. 7526-7535
    • Noble, L.J.1    Donovan, F.2    Igarashi, T.3    Goussev, S.4    Werb, Z.5
  • 44
    • 0037359601 scopus 로고    scopus 로고
    • Elevated membrane-type matrix metalloproteinases in gliomas revealed by profiling proteases and inhibitors in human cancer cells
    • Nuttall RK, Pennington CJ, Taplin J, Wheal A, Yong VW, Forsyth PA, Edwards DR. 2003. Elevated membrane-type matrix metalloproteinases in gliomas revealed by profiling proteases and inhibitors in human cancer cells. Mol Cancer Res 1:333-345.
    • (2003) Mol Cancer Res , vol.1 , pp. 333-345
    • Nuttall, R.K.1    Pennington, C.J.2    Taplin, J.3    Wheal, A.4    Yong, V.W.5    Forsyth, P.A.6    Edwards, D.R.7
  • 45
  • 46
    • 0022587125 scopus 로고
    • Changes in thickness of collagen fibrils in the
    • Osawa T, Ide C. 1986. Changes in thickness of collagen fibrils in the. Acta Anat (Basel) 125:245-251.
    • (1986) Acta Anat (Basel) , vol.125 , pp. 245-251
    • Osawa, T.1    Ide, C.2
  • 48
    • 0031059914 scopus 로고    scopus 로고
    • The extracellular matrix in neural crest-cell migration
    • Perris R. 1997. The extracellular matrix in neural crest-cell migration. Trends Neurosci 20:23-31.
    • (1997) Trends Neurosci , vol.20 , pp. 23-31
    • Perris, R.1
  • 49
    • 0030957735 scopus 로고    scopus 로고
    • Neuronal laminins and their cellular receptors
    • Powell SK, Kleinman HK. 1997. Neuronal laminins and their cellular receptors. Int J Biochem Cell Biol 29:401-414.
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 401-414
    • Powell, S.K.1    Kleinman, H.K.2
  • 51
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • Primakoff P, Myles DG. 2000. The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet 16:83-87.
    • (2000) Trends Genet , vol.16 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 52
    • 0025010542 scopus 로고
    • Molecular heterogeneity of basal laminae: Isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere
    • Sanes JR, Engvall E, Butkowski R, Hunter DD. 1990. Molecular heterogeneity of basal laminae: isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere. J Cell Biol 111:1685-1699.
    • (1990) J Cell Biol , vol.111 , pp. 1685-1699
    • Sanes, J.R.1    Engvall, E.2    Butkowski, R.3    Hunter, D.D.4
  • 53
    • 0033621668 scopus 로고    scopus 로고
    • Upregulation and interaction of TNFalpha and gelatinases A and B in painful peripheral nerve injury
    • Shubayev VI, Myers RR. 2000. Upregulation and interaction of TNFalpha and gelatinases A and B in painful peripheral nerve injury. Brain Res 855:83-89.
    • (2000) Brain Res , vol.855 , pp. 83-89
    • Shubayev, V.I.1    Myers, R.R.2
  • 54
    • 0036006118 scopus 로고    scopus 로고
    • Endoneurial remodeling by TNFalph- and TNFalpha-releasing proteases. A spatial and temporal co-localization study in painful neuropathy
    • Shubayev VI, Myers RR. 2002. Endoneurial remodeling by TNFalph- and TNFalpha-releasing proteases. A spatial and temporal co-localization study in painful neuropathy. J Peripheral Nerv Syst 7:28-36.
    • (2002) J Peripheral Nerv Syst , vol.7 , pp. 28-36
    • Shubayev, V.I.1    Myers, R.R.2
  • 55
    • 0035140103 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression and inhibition after sciatic nerve axotomy
    • Siebert H, Dippel N, Mader M, Weber F, Bruck W. 2001. Matrix metalloproteinase expression and inhibition after sciatic nerve axotomy. J Neuropathol Exp Neurol 60:85-93.
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 85-93
    • Siebert, H.1    Dippel, N.2    Mader, M.3    Weber, F.4    Bruck, W.5
  • 56
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht MD, Werb Z. 2001. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 17:463-516.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 57
    • 0342803709 scopus 로고    scopus 로고
    • Collagen degradation and platelet-derived growth factor stimulate the migration of vascular smooth muscle cells
    • Stringa E, Knauper V, Murphy G, Gavrilovic J. 2000. Collagen degradation and platelet-derived growth factor stimulate the migration of vascular smooth muscle cells. J Cell Sci 113:2055-2064.
    • (2000) J Cell Sci , vol.113 , pp. 2055-2064
    • Stringa, E.1    Knauper, V.2    Murphy, G.3    Gavrilovic, J.4
  • 59
    • 0033791419 scopus 로고    scopus 로고
    • Influence of laminin-2 on Schwann cell-axon interactions
    • Uziyel Y, Hall S, Cohen J. 2000. Influence of laminin-2 on Schwann cell-axon interactions. Glia 32:109-121.
    • (2000) Glia , vol.32 , pp. 109-121
    • Uziyel, Y.1    Hall, S.2    Cohen, J.3
  • 60
    • 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 MF, Thomasset N. 1999. Spatiotemporal expression patterns of metalloproteinases and their inhibitors in the postnatal developing rat cerebellum. J Neurosci 19:4994-5004.
    • (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
  • 61
    • 0037081132 scopus 로고    scopus 로고
    • Quantitative reverse transcription-polymerase chain reaction (RT-PCR): A comparison of primer-dropping, competitive, and real-time RT-PCRS
    • Wall SJ, Edwards DR. 2002. Quantitative reverse transcription-polymerase chain reaction (RT-PCR): a comparison of primer-dropping, competitive, and real-time RT-PCRS. Anal Biochem 300:269-273.
    • (2002) Anal Biochem , vol.300 , pp. 269-273
    • Wall, S.J.1    Edwards, D.R.2
  • 62
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: Regulating cellular ecology
    • Werb Z. 1997. ECM and cell surface proteolysis: regulating cellular ecology. Cell 91:439-442.
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 63
    • 0034046570 scopus 로고    scopus 로고
    • Relationship between fascicle size and perineurial collagen IV content in diabetic and control human peripheral nerve
    • Williams PE, Lowry A, Hill R, Masson E. 2000. Relationship between fascicle size and perineurial collagen IV content in diabetic and control human peripheral nerve. Histopathology 36:551-555.
    • (2000) Histopathology , vol.36 , pp. 551-555
    • Williams, P.E.1    Lowry, A.2    Hill, R.3    Masson, E.4
  • 65
    • 0031449805 scopus 로고    scopus 로고
    • Isolation of a tenascin-R binding protein from mouse brain membranes. A phosphacan-related chondroitin sulfate proteoglycan
    • 32092-2057 32101
    • Xiao ZC, Bartsch U, Margolis RK, Rougon G, Montag D, Schachner M. 1997. Isolation of a tenascin-R binding protein from mouse brain membranes. A phosphacan-related chondroitin sulfate proteoglycan. J Biol Chem 272:32092-2057 32101.
    • (1997) J Biol Chem , vol.272
    • Xiao, Z.C.1    Bartsch, U.2    Margolis, R.K.3    Rougon, G.4    Montag, D.5    Schachner, M.6
  • 66
    • 0035405886 scopus 로고    scopus 로고
    • Metalloproteinases in biology and pathology of the nervous system
    • Yong VW, Power C, Forsyth P, Edwards DR. 2001. Metalloproteinases in biology and pathology of the nervous system. Nat Rev Neurosci 2:502-511.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 502-511
    • Yong, V.W.1    Power, C.2    Forsyth, P.3    Edwards, D.R.4
  • 67
  • 68
    • 0032527889 scopus 로고    scopus 로고
    • Neuronal matrix metalloproteinase-2 degrades and inactivates a neurite-inhibiting chondroitin sulfate proteoglycan
    • Zuo J, Ferguson TA, Hernandez YJ, Stetler-Stevenson WG, Muir D. 1998. Neuronal matrix metalloproteinase-2 degrades and inactivates a neurite-inhibiting chondroitin sulfate proteoglycan. J Neurosci 18:5203-5211.
    • (1998) J Neurosci , vol.18 , pp. 5203-5211
    • Zuo, J.1    Ferguson, T.A.2    Hernandez, Y.J.3    Stetler-Stevenson, W.G.4    Muir, D.5


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