메뉴 건너뛰기




Volumn 89, Issue 5, 2003, Pages 2874-2878

Integrins regulate NMDA receptor-mediated synaptic currents

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINO 7 PHENYLPYRAZOLO[3,4 D]PYRIMIDINE; GLYCYLARGINYLGLYCYLASPARTYLSERYLPROLINE; INTEGRIN; LIGAND; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PEPTIDE; PROTEIN TYROSINE KINASE INHIBITOR; PYRIMIDINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0038216785     PISSN: 00223077     EISSN: None     Source Type: Journal    
DOI: 10.1152/jn.00783.2002     Document Type: Article
Times cited : (87)

References (55)
  • 1
    • 0035369919 scopus 로고    scopus 로고
    • NMDA receptor regulation by Src kinase signalling in excitatory synaptic transmission and plasticity
    • Ali DW and Salter MW. NMDA receptor regulation by Src kinase signalling in excitatory synaptic transmission and plasticity. Curr Opin Neurobiol 11: 336-342. 2001.
    • (2001) Curr Opin Neurobiol , vol.11 , pp. 336-342
    • Ali, D.W.1    Salter, M.W.2
  • 2
    • 0031745571 scopus 로고    scopus 로고
    • Signal transduction and signal modulation by cell adhesion receptors: The role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins
    • Alpin A, Howe A, Alahari S, and Juliano R. Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins. Pharmacol Rev 50: 197-263, 1998.
    • (1998) Pharmacol Rev , vol.50 , pp. 197-263
    • Alpin, A.1    Howe, A.2    Alahari, S.3    Juliano, R.4
  • 3
    • 0031016826 scopus 로고    scopus 로고
    • Arg-Gly-Asp-Ser-Selective adhesion and the stabilization of long-term potentiation: Pharmacological studies and the characterization of a candidate matrix receptor
    • Bahr BA, Staubli U, Xiao P, Chun D, Ji Z-X, Esteban ET, and Lynch G. Arg-Gly-Asp-Ser-Selective adhesion and the stabilization of long-term potentiation: pharmacological studies and the characterization of a candidate matrix receptor. J Neurosci 17: 1320-1329, 1997.
    • (1997) J Neurosci , vol.17 , pp. 1320-1329
    • Bahr, B.A.1    Staubli, U.2    Xiao, P.3    Chun, D.4    Ji, Z.-X.5    Esteban, E.T.6    Lynch, G.7
  • 4
    • 0030271595 scopus 로고    scopus 로고
    • Focalized proteolysis: Spatial and temporal regulation of extracellular matrix degradation at the cell surface
    • Basbaum C and Werb Z. Focalized proteolysis: spatial and temporal regulation of extracellular matrix degradation at the cell surface. Curr Opin Cell Biol 8: 731-738, 1996.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 731-738
    • Basbaum, C.1    Werb, Z.2
  • 5
    • 0037135272 scopus 로고    scopus 로고
    • Uptake and pathogenic effects of amyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists
    • Bi X, Zhou J, Gall CM, and Lynch G. Uptake and pathogenic effects of amyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists. Neuroscience 112: 827-840, 2002.
    • (2002) Neuroscience , vol.112 , pp. 827-840
    • Bi, X.1    Zhou, J.2    Gall, C.M.3    Lynch, G.4
  • 6
    • 0035947801 scopus 로고    scopus 로고
    • Polarized distribution of α5 integrin in the dendrites of hippocampal and cortical neurons
    • Bi X, Zhou J, Lynch G, and Gall CM. Polarized distribution of α5 integrin in the dendrites of hippocampal and cortical neurons. J Comp Neurol 435: 184-193, 2001.
    • (2001) J Comp Neurol , vol.435 , pp. 184-193
    • Bi, X.1    Zhou, J.2    Lynch, G.3    Gall, C.M.4
  • 7
    • 0035144682 scopus 로고    scopus 로고
    • Involvement of the secretory pathway for AMPA receptors in NMDA-induced potentiation in hippocampus
    • Broutman G and Baudry M. Involvement of the secretory pathway for AMPA receptors in NMDA-induced potentiation in hippocampus. J Neurosci 21: 27-34. 2001.
    • (2001) J Neurosci , vol.21 , pp. 27-34
    • Broutman, G.1    Baudry, M.2
  • 8
    • 0032538841 scopus 로고    scopus 로고
    • A functional role for specific spliced variants of the alpha 7beta1 integrin in acetylcholine receptor clustering
    • Burkin DJ, Gu M, Hodges BL, Campanelli JT, and Kaufman SJ. A functional role for specific spliced variants of the alpha7beta1 integrin in acetylcholine receptor clustering. J Cell Biol 143: 1067-1075, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 1067-1075
    • Burkin, D.J.1    Gu, M.2    Hodges, B.L.3    Campanelli, J.T.4    Kaufman, S.J.5
  • 9
    • 0029890005 scopus 로고    scopus 로고
    • Protein tyrosine kinase-mediated potentiation of currents from cloned NMDA receptors
    • Chen SJ and Leonard JP. Protein tyrosine kinase-mediated potentiation of currents from cloned NMDA receptors. J Neurochem 67: 194-200, 1996.
    • (1996) J Neurochem , vol.67 , pp. 194-200
    • Chen, S.J.1    Leonard, J.P.2
  • 10
    • 0035934293 scopus 로고    scopus 로고
    • Evidence that integrins contribute to multiple stages in the consolidation of long term potentiation
    • Chun D, Gall CM, Bi X, and Lynch G. Evidence that integrins contribute to multiple stages in the consolidation of long term potentiation. Neuroscience 105: 815-829, 2001.
    • (2001) Neuroscience , vol.105 , pp. 815-829
    • Chun, D.1    Gall, C.M.2    Bi, X.3    Lynch, G.4
  • 11
    • 0033847622 scopus 로고    scopus 로고
    • Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules
    • Davis GE, Bayless KJ, Davis MJ, and Meininger GA. Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules. Am J Pathol 156: 1489-1498, 2000.
    • (2000) Am J Pathol , vol.156 , pp. 1489-1498
    • Davis, G.E.1    Bayless, K.J.2    Davis, M.J.3    Meininger, G.A.4
  • 13
    • 0034683575 scopus 로고    scopus 로고
    • 2+-dependent modulation of surface expression of brain-derived neurotrophic factor receptors in hippocampal neurons
    • 2+-dependent modulation of surface expression of brain-derived neurotrophic factor receptors in hippocampal neurons. J Cell Biol 150: 1423-1433, 2000.
    • (2000) J Cell Biol , vol.150 , pp. 1423-1433
    • Du, J.1    Feng, L.2    Yang, F.3    Lu, B.4
  • 14
    • 0029984047 scopus 로고    scopus 로고
    • The regional and ultrastructural distribution of the α8 integrin subunit in the developing and adult rat brain suggests a role in synaptic plasticity
    • Einheber S, Schnapp L, Salzer J, Cappiello Z, and Milner TA. The regional and ultrastructural distribution of the α8 integrin subunit in the developing and adult rat brain suggests a role in synaptic plasticity. J Comp Neurol 370: 105-134, 1996.
    • (1996) J Comp Neurol , vol.370 , pp. 105-134
    • Einheber, S.1    Schnapp, L.2    Salzer, J.3    Cappiello, Z.4    Milner, T.A.5
  • 15
    • 0033053365 scopus 로고    scopus 로고
    • Proteolysis of neuronal cell adhesion molecule by the tissue plasminogen activator-plasmin system after kainate injection in the mouse hippocampus
    • Endo A, Nagai N, Urano T, Takada Y, Hashimoto K, and Takada A. Proteolysis of neuronal cell adhesion molecule by the tissue plasminogen activator-plasmin system after kainate injection in the mouse hippocampus. Neurosci Res 33: 1-8, 1999.
    • (1999) Neurosci Res , vol.33 , pp. 1-8
    • Endo, A.1    Nagai, N.2    Urano, T.3    Takada, Y.4    Hashimoto, K.5    Takada, A.6
  • 17
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti FG and Ruoslahti E. Integrin signaling. Science 285: 1028-1032, 1999.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 18
    • 0036139881 scopus 로고    scopus 로고
    • LTP leads to rapid surface expression of NMDA but not AMPA receptors in adult rat CA1
    • Grosshans DR, Clayton DA, Coultrap SJ, and Browning MD. LTP leads to rapid surface expression of NMDA but not AMPA receptors in adult rat CA1. Nat Neurosci 5: 27-33, 2001.
    • (2001) Nat Neurosci , vol.5 , pp. 27-33
    • Grosshans, D.R.1    Clayton, D.A.2    Coultrap, S.J.3    Browning, M.D.4
  • 19
    • 0000009441 scopus 로고    scopus 로고
    • Integrin-mediated short-term memory in Drosophila
    • Grotewiel MS, Beck CD, Wu CF, and Greenspan RJ. Integrin-mediated short-term memory in Drosophila. Nature 18: 7847-7855, 1998.
    • (1998) Nature , vol.18 , pp. 7847-7855
    • Grotewiel, M.S.1    Beck, C.D.2    Wu, C.F.3    Greenspan, R.J.4
  • 20
    • 0029886174 scopus 로고    scopus 로고
    • Membrane depolarization induces calcuim-dependent secretion of tissue plasminogen activator
    • Gualandris A, Jones TE, Strickland S, and Tsirka SE. Membrane depolarization induces calcuim-dependent secretion of tissue plasminogen activator. J Neurosci 16: 2220-2225, 1996.
    • (1996) J Neurosci , vol.16 , pp. 2220-2225
    • Gualandris, A.1    Jones, T.E.2    Strickland, S.3    Tsirka, S.E.4
  • 21
    • 0033382249 scopus 로고    scopus 로고
    • Phosphorylation dependent interaction of the N-methyl-D-aspartate receptor epsilon 2 subunit with phosphatidylinositol 3-kinase
    • Hisatsune C, Umemori H, Mishina M, and Yamamoto T. Phosphorylation dependent interaction of the N-methyl-D-aspartate receptor epsilon 2 subunit with phosphatidylinositol 3-kinase. Genes Cells 4: 657-666, 1999.
    • (1999) Genes Cells , vol.4 , pp. 657-666
    • Hisatsune, C.1    Umemori, H.2    Mishina, M.3    Yamamoto, T.4
  • 22
    • 0032539049 scopus 로고    scopus 로고
    • Proteolysis of cell adhesion molecules by serine proteases: A role in long term potentiation?
    • Hoffman KB, Martinez J, and Lynch G. Proteolysis of cell adhesion molecules by serine proteases: a role in long term potentiation? Brain Res 811: 29-33, 1998.
    • (1998) Brain Res , vol.811 , pp. 29-33
    • Hoffman, K.B.1    Martinez, J.2    Lynch, G.3
  • 23
    • 0026770377 scopus 로고
    • Integrins, versatility, modulation, and signaling in cell adhesion
    • Hynes R. Integrins, versatility, modulation, and signaling in cell adhesion. Cell 69: 11-25, 1992.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.1
  • 24
    • 0029887725 scopus 로고    scopus 로고
    • Subtype-specific regulation of recombinant NMDA receptor-channels by protein tyrosine kinases of the src family
    • Kohr G and Seeburg PH. Subtype-specific regulation of recombinant NMDA receptor-channels by protein tyrosine kinases of the src family. J Physiol 492: 445-452, 1996.
    • (1996) J Physiol , vol.492 , pp. 445-452
    • Kohr, G.1    Seeburg, P.H.2
  • 25
    • 0036499748 scopus 로고    scopus 로고
    • Alpha3 integrin receptors contribute to the consolidation of long term potentiation
    • Kramár EA, Bernard JA, Gall CM, and Lynch G. Alpha3 integrin receptors contribute to the consolidation of long term potentiation. Neuroscience 110: 29-39, 2002.
    • (2002) Neuroscience , vol.110 , pp. 29-39
    • Kramár, E.A.1    Bernard, J.A.2    Gall, C.M.3    Lynch, G.4
  • 27
    • 0029093990 scopus 로고
    • Differential tyrosine phosphorylation of N-methyl-D-aspartate receptor subunits
    • Lau LF and Huganir RL. Differential tyrosine phosphorylation of N-methyl-D-aspartate receptor subunits. J Biol Chem 270: 20036-20041, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 20036-20041
    • Lau, L.F.1    Huganir, R.L.2
  • 28
    • 0036083122 scopus 로고    scopus 로고
    • Long-term potentiation alters the modulator pharmacology of AMPA-type glutamate receptors
    • Lin B, Brucher FA, Colgin LL, and Lynch G. Long-term potentiation alters the modulator pharmacology of AMPA-type glutamate receptors. J Neurophysiol 87: 2790-2800, 2002.
    • (2002) J Neurophysiol , vol.87 , pp. 2790-2800
    • Lin, B.1    Brucher, F.A.2    Colgin, L.L.3    Lynch, G.4
  • 29
    • 0038577646 scopus 로고    scopus 로고
    • Integrin surface expression is increased by AMPA-class glutamate receptor activation: Evidence from GluR1-transfected Cos7 cells
    • Lin C and Gall C. Integrin surface expression is increased by AMPA-class glutamate receptor activation: evidence from GluR1-transfected Cos7 cells. Am Soc Cell Biol Abstr, 2737: 2002.
    • (2002) Am Soc Cell Biol Abstr , vol.2737
    • Lin, C.1    Gall, C.2
  • 30
    • 0001048711 scopus 로고    scopus 로고
    • Src activation in the induction of long-term potentiation in CA1 hippocampal neurons
    • Lu YM, Roder JC, Davidow J, and Salter MW. Src activation in the induction of long-term potentiation in CA1 hippocampal neurons. Science 279: 1363-1367, 1998.
    • (1998) Science , vol.279 , pp. 1363-1367
    • Lu, Y.M.1    Roder, J.C.2    Davidow, J.3    Salter, M.W.4
  • 31
    • 0032410716 scopus 로고    scopus 로고
    • Time-dependent reversal of dentate LTP by 5 Hz stimulation
    • Martin SJ. Time-dependent reversal of dentate LTP by 5 Hz stimulation. Neuroreport 9: 3775-3781, 1998.
    • (1998) Neuroreport , vol.9 , pp. 3775-3781
    • Martin, S.J.1
  • 32
    • 0036222549 scopus 로고    scopus 로고
    • Sensing the environment: A historical perspective on integrin signal transduction
    • Miranti CK and Brugge JS. Sensing the environment: a historical perspective on integrin signal transduction. Nat Cell Biol 4: 83-90, 2002.
    • (2002) Nat Cell Biol , vol.4 , pp. 83-90
    • Miranti, C.K.1    Brugge, J.S.2
  • 33
    • 0030808413 scopus 로고    scopus 로고
    • RGDN peptide interactions with endothelial a5β1 integrin causes sustained endothelin-dependent vasoconstriction of rat skeletal muscle arterioles
    • Mogford JE, Davis GE, and Meininger GA. RGDN peptide interactions with endothelial a5β1 integrin causes sustained endothelin-dependent vasoconstriction of rat skeletal muscle arterioles. J Clin Invest 100: 1647-1653, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 1647-1653
    • Mogford, J.E.1    Davis, G.E.2    Meininger, G.A.3
  • 37
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher M and Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 304: 30-33, 1984.
    • (1984) Nature , vol.304 , pp. 30-33
    • Pierschbacher, M.1    Ruoslahti, E.2
  • 38
    • 0033103707 scopus 로고    scopus 로고
    • Integrin subunit gene expression is regionally differentiated in adult brain
    • Pinkstaff JK, Detterich J, Lynch G, and Gall C. Integrin subunit gene expression is regionally differentiated in adult brain, J Neurosci 19: 1541-1556, 1999.
    • (1999) J Neurosci , vol.19 , pp. 1541-1556
    • Pinkstaff, J.K.1    Detterich, J.2    Lynch, G.3    Gall, C.4
  • 39
    • 0038577673 scopus 로고    scopus 로고
    • Integrin receptors regulate BDNF and trk gene expression in hippocampal neurons
    • Pinkstaff JK, Yong AP, Lynch G, and Gall CM. Integrin receptors regulate BDNF and trk gene expression in hippocampal neurons. Soc Neurosci Abstr 24: 2015, 1998.
    • (1998) Soc Neurosci Abstr , vol.24 , pp. 2015
    • Pinkstaff, J.K.1    Yong, A.P.2    Lynch, G.3    Gall, C.M.4
  • 40
    • 0024320887 scopus 로고
    • Degradation of extracellular matrix by neuronal proteases
    • Pittman RN and Buettner HM. Degradation of extracellular matrix by neuronal proteases. Dev Neurosci 11: 361-375, 1989.
    • (1989) Dev Neurosci , vol.11 , pp. 361-375
    • Pittman, R.N.1    Buettner, H.M.2
  • 41
    • 0034724337 scopus 로고    scopus 로고
    • Colocalization of integrin receptors and reelin in dendritic spine postsynaptic densities of adult nonhuman primate cortex
    • Rodriguez MA, Pesold C, Liu WS, Kriho V, Guidotti A, Pappas GD, and Costa E. Colocalization of integrin receptors and reelin in dendritic spine postsynaptic densities of adult nonhuman primate cortex. Proc Natl Acad Sci USA 97: 3550-3555, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3550-3555
    • Rodriguez, M.A.1    Pesold, C.2    Liu, W.S.3    Kriho, V.4    Guidotti, A.5    Pappas, G.D.6    Costa, E.7
  • 42
    • 0029775681 scopus 로고    scopus 로고
    • RGD other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol 12: 697-715, 1996.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 43
    • 0031915021 scopus 로고    scopus 로고
    • Integrin signalling and tyrosine phosphorylation: Just the FAKs?
    • Schlaepfer D and Hunter T. Integrin signalling and tyrosine phosphorylation: just the FAKs? Trends Cell Biol 8: 151-157, 1998.
    • (1998) Trends Cell Biol , vol.8 , pp. 151-157
    • Schlaepfer, D.1    Hunter, T.2
  • 44
    • 0035813328 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the neural recognition molecules L1, NCAM, and its isoform NCAM180, the NCAM-associated polysialic acid, beta1 integrin and the extracellular matrix molecule tenascin-R in synapses of the adult rat hippocampus
    • Schuster T, Krug M, Stalder M, Hackel N, Gerardy-Schahn R, and Schachner M. Immunoelectron microscopic localization of the neural recognition molecules L1, NCAM, and its isoform NCAM180, the NCAM-associated polysialic acid, beta1 integrin and the extracellular matrix molecule tenascin-R in synapses of the adult rat hippocampus. J Neurobiol 49: 142-158, 2001.
    • (2001) J Neurobiol , vol.49 , pp. 142-158
    • Schuster, T.1    Krug, M.2    Stalder, M.3    Hackel, N.4    Gerardy-Schahn, R.5    Schachner, M.6
  • 46
    • 0242487406 scopus 로고    scopus 로고
    • Time-dependent reversal of long-term potentiation by an integrin antagonist
    • Staubli U, Chun D, and Lynch G. Time-dependent reversal of long-term potentiation by an integrin antagonist. J Neurosci 18: 3460-3469, 1998.
    • (1998) J Neurosci , vol.18 , pp. 3460-3469
    • Staubli, U.1    Chun, D.2    Lynch, G.3
  • 47
    • 0025263801 scopus 로고
    • Stable depression of potentiated synaptic responses in the hippocampus with 1-5 Hz stimulation
    • Staubli U and Lynch G. Stable depression of potentiated synaptic responses in the hippocampus with 1-5 Hz stimulation. Brain Res 513: 113-118, 1990.
    • (1990) Brain Res , vol.513 , pp. 113-118
    • Staubli, U.1    Lynch, G.2
  • 48
    • 0028786699 scopus 로고
    • Thrombospondin mediates calcium mobilization in fibroblasts via its Arg-Gly-Asp and carboxyl-terminal domains
    • Tsao PW and Mousa SA. Thrombospondin mediates calcium mobilization in fibroblasts via its Arg-Gly-Asp and carboxyl-terminal domains. J Biol Chem 270: 23747-23753, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 23747-23753
    • Tsao, P.W.1    Mousa, S.A.2
  • 49
    • 0031021357 scopus 로고    scopus 로고
    • An extracellular proteolytic cascade promotes neuronal degeneration in the mouse hippocampus
    • Tsirka S, Bugge T, Degen JL, and Strickland S. An extracellular proteolytic cascade promotes neuronal degeneration in the mouse hippocampus. J Neurosci 17: 543-552, 1997.
    • (1997) J Neurosci , vol.17 , pp. 543-552
    • Tsirka, S.1    Bugge, T.2    Degen, J.L.3    Strickland, S.4
  • 50
    • 0031694935 scopus 로고    scopus 로고
    • Integrin signaling: Tyrosine phosphorylation events in focal adhesions
    • Vuori K. Integrin signaling: tyrosine phosphorylation events in focal adhesions. J Membr Biol 165: 191-199, 1998.
    • (1998) J Membr Biol , vol.165 , pp. 191-199
    • Vuori, K.1
  • 51
    • 0028360327 scopus 로고
    • Regulation of NMDA receptors by tyrosine kinases and phosphatases
    • Wang YT and Salter MW. Regulation of NMDA receptors by tyrosine kinases and phosphatases. Nature 369: 233-235, 1994.
    • (1994) Nature , vol.369 , pp. 233-235
    • Wang, Y.T.1    Salter, M.W.2
  • 52
    • 0036551388 scopus 로고    scopus 로고
    • Rapid neuromodulatory actions of integrin ligands
    • Wildering WC, Herman PM, and Bulloch AGM. Rapid neuromodulatory actions of integrin ligands. J Neurosci 22: 2419-2426, 2002.
    • (2002) J Neurosci , vol.22 , pp. 2419-2426
    • Wildering, W.C.1    Herman, P.M.2    Bulloch, A.G.M.3
  • 53
    • 0035839636 scopus 로고    scopus 로고
    • Regulation of the L-type calcium channel by α5β1 integrin requires signaling between focal adhesion proteins
    • Wu X, Davis GE, Meininger GA, Wilson E, and Davis MJ. Regulation of the L-type calcium channel by α5β1 integrin requires signaling between focal adhesion proteins. J Biol Chem 276: 30285-30292, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 30285-30292
    • Wu, X.1    Davis, G.E.2    Meininger, G.A.3    Wilson, E.4    Davis, M.J.5
  • 54
    • 0032487441 scopus 로고    scopus 로고
    • Modulation of calcium current in arteriolar smooth muscle by alphav beta3 and alpha5 beta1 integrin ligands
    • Wu X, Mogford JE, Platts SH, Davis GE, Meininger GA, and Davis MJ. Modulation of calcium current in arteriolar smooth muscle by alphav beta3 and alpha5 beta1 integrin ligands. J Cell Biol 143: 241-252, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 241-252
    • Wu, X.1    Mogford, J.E.2    Platts, S.H.3    Davis, G.E.4    Meininger, G.A.5    Davis, M.J.6
  • 55
    • 0034689030 scopus 로고    scopus 로고
    • The tissue plasminogen activator (tPA)/plasmin extracellular proteolytic system regulates seizure-induced hippocampal mossy fiber outgrowth through a proteoglycan substrate
    • Wu YP, Siao CJ, Lu W, Sung TC, Frohman MA, Milev P, Bugge TH, Degen JL, Levine JM, Margolis RU, and Tsirka SE. The tissue plasminogen activator (tPA)/plasmin extracellular proteolytic system regulates seizure-induced hippocampal mossy fiber outgrowth through a proteoglycan substrate. J Cell Biol 148: 1295-1304, 2000.
    • (2000) J Cell Biol , vol.148 , pp. 1295-1304
    • Wu, Y.P.1    Siao, C.J.2    Lu, W.3    Sung, T.C.4    Frohman, M.A.5    Milev, P.6    Bugge, T.H.7    Degen, J.L.8    Levine, J.M.9    Margolis, R.U.10    Tsirka, S.E.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.