메뉴 건너뛰기




Volumn 214, Issue , 2014, Pages 101-131

ECM receptors in neuronal structure, synaptic plasticity, and behavior

Author keywords

Cell adhesion receptor; Heparan sulfate proteoglycan; Integrin receptor; L type voltage dependent calcium channel; Lipoprotein receptor; Tetraspanin

Indexed keywords

BETA INTEGRIN; GLUTAMATE RECEPTOR; INTEGRIN; INTEGRIN RECEPTOR; LIPOPROTEIN RECEPTOR; PROTEOHEPARAN SULFATE; SYNDECAN; TETRASPANIN; VERY LOW DENSITY LIPOPROTEIN RECEPTOR; VOLTAGE GATED CALCIUM CHANNEL;

EID: 84922287791     PISSN: 00796123     EISSN: 18757855     Source Type: Book Series    
DOI: 10.1016/B978-0-444-63486-3.00005-0     Document Type: Chapter
Times cited : (71)

References (189)
  • 1
    • 42349095075 scopus 로고    scopus 로고
    • Advances in autism genetics: on the threshold of a new neurobiology
    • Abrahams B.S., Geschwind D.H. Advances in autism genetics: on the threshold of a new neurobiology. Nat. Rev. Genet. 2008, 9:341-355.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 341-355
    • Abrahams, B.S.1    Geschwind, D.H.2
  • 3
    • 0003472502 scopus 로고    scopus 로고
    • American Psychiatric Publishing, Arlington, VA
    • American-Psychiatric-Association Diagnostic and Statistical Manual of Mental Disorders 2013, American Psychiatric Publishing, Arlington, VA. fifth ed.
    • (2013) Diagnostic and Statistical Manual of Mental Disorders
  • 5
    • 0033073443 scopus 로고    scopus 로고
    • Distinct functions of alpha3 and alpha(v) integrin receptors in neuronal migration and laminar organization of the cerebral cortex
    • Anton E.S., Kreidberg J.A., Rakic P. Distinct functions of alpha3 and alpha(v) integrin receptors in neuronal migration and laminar organization of the cerebral cortex. Neuron 1999, 22:277-289.
    • (1999) Neuron , vol.22 , pp. 277-289
    • Anton, E.S.1    Kreidberg, J.A.2    Rakic, P.3
  • 9
    • 84859266427 scopus 로고    scopus 로고
    • Tetraspanins: interactions and interplay with integrins
    • Bassani S., Cingolani L.A. Tetraspanins: interactions and interplay with integrins. Int. J. Biochem. Cell Biol. 2012, 44:703-708.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 703-708
    • Bassani, S.1    Cingolani, L.A.2
  • 10
  • 11
    • 0345894331 scopus 로고    scopus 로고
    • Reelin-mediated signaling locally regulates protein kinase B/Akt and glycogen synthase kinase 3beta
    • Beffert U., Morfini G., Bock H.H., Reyna H., Brady S.T., Herz J. Reelin-mediated signaling locally regulates protein kinase B/Akt and glycogen synthase kinase 3beta. J. Biol. Chem. 2002, 277:49958-49964.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49958-49964
    • Beffert, U.1    Morfini, G.2    Bock, H.H.3    Reyna, H.4    Brady, S.T.5    Herz, J.6
  • 13
    • 0034333146 scopus 로고    scopus 로고
    • Integrins as receptors for laminins
    • Belkin A.M., Stepp M.A. Integrins as receptors for laminins. Microsc. Res. Tech. 2000, 51:280-301.
    • (2000) Microsc. Res. Tech. , vol.51 , pp. 280-301
    • Belkin, A.M.1    Stepp, M.A.2
  • 14
    • 0035798702 scopus 로고    scopus 로고
    • Analysis of the CD151-alpha3beta1 integrin and CD151-tetraspanin interactions by mutagenesis
    • Berditchevski F., Gilbert E., Griffiths M.R., Fitter S., Ashman L., Jenner S.J. Analysis of the CD151-alpha3beta1 integrin and CD151-tetraspanin interactions by mutagenesis. J. Biol. Chem. 2001, 276:41165-41174.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41165-41174
    • Berditchevski, F.1    Gilbert, E.2    Griffiths, M.R.3    Fitter, S.4    Ashman, L.5    Jenner, S.J.6
  • 15
    • 18844391463 scopus 로고    scopus 로고
    • Integrin signaling cascades are operational in adult hippocampal synapses and modulate NMDA receptor physiology
    • Bernard-Trifilo J.A., Kramar E.A., Torp R., Lin C.Y., Pineda E.A., Lynch G., Gall C.M. Integrin signaling cascades are operational in adult hippocampal synapses and modulate NMDA receptor physiology. J. Neurochem. 2005, 93:834-849.
    • (2005) J. Neurochem. , vol.93 , pp. 834-849
    • Bernard-Trifilo, J.A.1    Kramar, E.A.2    Torp, R.3    Lin, C.Y.4    Pineda, E.A.5    Lynch, G.6    Gall, C.M.7
  • 16
    • 67649400549 scopus 로고    scopus 로고
    • The emerging role of synaptic cell-adhesion pathways in the pathogenesis of autism spectrum disorders
    • Betancur C., Sakurai T., Buxbaum J.D. The emerging role of synaptic cell-adhesion pathways in the pathogenesis of autism spectrum disorders. Trends Neurosci. 2009, 32:402-412.
    • (2009) Trends Neurosci. , vol.32 , pp. 402-412
    • Betancur, C.1    Sakurai, T.2    Buxbaum, J.D.3
  • 18
    • 0031772345 scopus 로고    scopus 로고
    • Structural analysis of the sixth immunoglobulin-like domain of mouse neural cell adhesion molecule L1 and its interactions with alpha(v)beta3, alpha(IIb)beta3, and alpha5beta1 integrins
    • Blaess S., Kammerer R.A., Hall H. Structural analysis of the sixth immunoglobulin-like domain of mouse neural cell adhesion molecule L1 and its interactions with alpha(v)beta3, alpha(IIb)beta3, and alpha5beta1 integrins. J. Neurochem. 1998, 71:2615-2625.
    • (1998) J. Neurochem. , vol.71 , pp. 2615-2625
    • Blaess, S.1    Kammerer, R.A.2    Hall, H.3
  • 19
    • 0037425581 scopus 로고    scopus 로고
    • Reelin activates SRC family tyrosine kinases in neurons
    • Bock H.H., Herz J. Reelin activates SRC family tyrosine kinases in neurons. Curr. Biol. 2003, 13:18-26.
    • (2003) Curr. Biol. , vol.13 , pp. 18-26
    • Bock, H.H.1    Herz, J.2
  • 20
    • 0037130587 scopus 로고    scopus 로고
    • Activity-dependent regulation of genes implicated in X-linked non-specific mental retardation
    • Boda B., Mas C., Muller D. Activity-dependent regulation of genes implicated in X-linked non-specific mental retardation. Neuroscience 2002, 114:13-17.
    • (2002) Neuroscience , vol.114 , pp. 13-17
    • Boda, B.1    Mas, C.2    Muller, D.3
  • 21
    • 69949183657 scopus 로고    scopus 로고
    • Brain extracellular matrix in neurodegeneration
    • Bonneh-Barkay D., Wiley C.A. Brain extracellular matrix in neurodegeneration. Brain Pathol. 2009, 19:573-585.
    • (2009) Brain Pathol. , vol.19 , pp. 573-585
    • Bonneh-Barkay, D.1    Wiley, C.A.2
  • 23
    • 34748829242 scopus 로고    scopus 로고
    • The EphA4 receptor regulates dendritic spine remodeling by affecting beta1-integrin signaling pathways
    • Bourgin C., Murai K.K., Richter M., Pasquale E.B. The EphA4 receptor regulates dendritic spine remodeling by affecting beta1-integrin signaling pathways. J. Cell Biol. 2007, 178:1295-1307.
    • (2007) J. Cell Biol. , vol.178 , pp. 1295-1307
    • Bourgin, C.1    Murai, K.K.2    Richter, M.3    Pasquale, E.B.4
  • 24
    • 35348923794 scopus 로고    scopus 로고
    • Use of a chemical genetic technique to identify myosin IIb as a substrate of the Abl-related gene (Arg) tyrosine kinase
    • Boyle S.N., Koleske A.J. Use of a chemical genetic technique to identify myosin IIb as a substrate of the Abl-related gene (Arg) tyrosine kinase. Biochemistry 2007, 46:11614-11620.
    • (2007) Biochemistry , vol.46 , pp. 11614-11620
    • Boyle, S.N.1    Koleske, A.J.2
  • 25
    • 34447552405 scopus 로고    scopus 로고
    • In vivo roles for matrix metalloproteinase-9 in mature hippocampal synaptic physiology and plasticity
    • Bozdagi O., Nagy V., Kwei K.T., Huntley G.W. In vivo roles for matrix metalloproteinase-9 in mature hippocampal synaptic physiology and plasticity. J. Neurophysiol. 2007, 98:334-344.
    • (2007) J. Neurophysiol. , vol.98 , pp. 334-344
    • Bozdagi, O.1    Nagy, V.2    Kwei, K.T.3    Huntley, G.W.4
  • 26
    • 33750527971 scopus 로고    scopus 로고
    • Integrin signaling through Arg activates p190RhoGAP by promoting its binding to p120RasGAP and recruitment to the membrane
    • Bradley W.D., Hernandez S.E., Settleman J., Koleske A.J. Integrin signaling through Arg activates p190RhoGAP by promoting its binding to p120RasGAP and recruitment to the membrane. Mol. Biol. Cell 2006, 17:4827-4836.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4827-4836
    • Bradley, W.D.1    Hernandez, S.E.2    Settleman, J.3    Koleske, A.J.4
  • 31
    • 78651266928 scopus 로고    scopus 로고
    • Presynaptic calcium channels and alpha3-integrins are complexed with synaptic cleft laminins, cytoskeletal elements and active zone components
    • Carlson S.S., Valdez G., Sanes J.R. Presynaptic calcium channels and alpha3-integrins are complexed with synaptic cleft laminins, cytoskeletal elements and active zone components. J. Neurochem. 2010, 115:654-666.
    • (2010) J. Neurochem. , vol.115 , pp. 654-666
    • Carlson, S.S.1    Valdez, G.2    Sanes, J.R.3
  • 32
    • 79951574616 scopus 로고    scopus 로고
    • Absence of preference for social novelty and increased grooming in integrin beta3 knockout mice: initial studies and future directions
    • Carter M.D., Shah C.R., Muller C.L., Crawley J.N., Carneiro A.M., Veenstra-Vanderweele J. Absence of preference for social novelty and increased grooming in integrin beta3 knockout mice: initial studies and future directions. Autism Res. 2011, 4:57-67.
    • (2011) Autism Res. , vol.4 , pp. 57-67
    • Carter, M.D.1    Shah, C.R.2    Muller, C.L.3    Crawley, J.N.4    Carneiro, A.M.5    Veenstra-Vanderweele, J.6
  • 35
    • 0042125569 scopus 로고    scopus 로고
    • Integrin requirement for hippocampal synaptic plasticity and spatial memory
    • Chan C.S., Weeber E.J., Kurup S., Sweatt J.D., Davis R.L. Integrin requirement for hippocampal synaptic plasticity and spatial memory. J. Neurosci. 2003, 23:7107-7116.
    • (2003) J. Neurosci. , vol.23 , pp. 7107-7116
    • Chan, C.S.1    Weeber, E.J.2    Kurup, S.3    Sweatt, J.D.4    Davis, R.L.5
  • 36
    • 30644461034 scopus 로고    scopus 로고
    • Beta 1-integrins are required for hippocampal AMPA receptor-dependent synaptic transmission, synaptic plasticity, and working memory
    • Chan C.S., Weeber E.J., Zong L., Fuchs E., Sweatt J.D., Davis R.L. Beta 1-integrins are required for hippocampal AMPA receptor-dependent synaptic transmission, synaptic plasticity, and working memory. J. Neurosci. 2006, 26:223-232.
    • (2006) J. Neurosci. , vol.26 , pp. 223-232
    • Chan, C.S.1    Weeber, E.J.2    Zong, L.3    Fuchs, E.4    Sweatt, J.D.5    Davis, R.L.6
  • 38
    • 77952976816 scopus 로고    scopus 로고
    • Alpha8-integrins are required for hippocampal long-term potentiation but not for hippocampal-dependent learning
    • Chan C.S., Chen H., Bradley A., Dragatsis I., Rosenmund C., Davis R.L. alpha8-integrins are required for hippocampal long-term potentiation but not for hippocampal-dependent learning. Genes Brain Behav. 2010, 9:402-410.
    • (2010) Genes Brain Behav. , vol.9 , pp. 402-410
    • Chan, C.S.1    Chen, H.2    Bradley, A.3    Dragatsis, I.4    Rosenmund, C.5    Davis, R.L.6
  • 39
    • 0035902139 scopus 로고    scopus 로고
    • Integrins mediate functional pre- and postsynaptic maturation at a hippocampal synapse
    • Chavis P., Westbrook G. Integrins mediate functional pre- and postsynaptic maturation at a hippocampal synapse. Nature 2001, 411:317-321.
    • (2001) Nature , vol.411 , pp. 317-321
    • Chavis, P.1    Westbrook, G.2
  • 40
    • 84891285054 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of intact human integrin alphaIIbbeta3: new implications for activation-dependent ligand binding
    • Choi W.S., Rice W.J., Stokes D.L., Coller B.S. Three-dimensional reconstruction of intact human integrin alphaIIbbeta3: new implications for activation-dependent ligand binding. Blood 2013, 122:4165-4171.
    • (2013) Blood , vol.122 , pp. 4165-4171
    • Choi, W.S.1    Rice, W.J.2    Stokes, D.L.3    Coller, B.S.4
  • 41
    • 0035934293 scopus 로고    scopus 로고
    • Evidence that integrins contribute to multiple stages in the consolidation of long term potentiation in rat hippocampus
    • Chun D., Gall C.M., Bi X., Lynch G. Evidence that integrins contribute to multiple stages in the consolidation of long term potentiation in rat hippocampus. Neuroscience 2001, 105:815-829.
    • (2001) Neuroscience , vol.105 , pp. 815-829
    • Chun, D.1    Gall, C.M.2    Bi, X.3    Lynch, G.4
  • 42
    • 70449728080 scopus 로고    scopus 로고
    • Differential involvement of beta3 integrin in pre- and postsynaptic forms of adaptation to chronic activity deprivation
    • Cingolani L.A., Goda Y. Differential involvement of beta3 integrin in pre- and postsynaptic forms of adaptation to chronic activity deprivation. Neuron Glia Biol. 2008, 4:179-187.
    • (2008) Neuron Glia Biol. , vol.4 , pp. 179-187
    • Cingolani, L.A.1    Goda, Y.2
  • 43
    • 44649201117 scopus 로고    scopus 로고
    • Activity-dependent regulation of synaptic AMPA receptor composition and abundance by beta3 integrins
    • Cingolani L.A., Thalhammer A., Yu L.M., Catalano M., Ramos T., Colicos M.A., Goda Y. Activity-dependent regulation of synaptic AMPA receptor composition and abundance by beta3 integrins. Neuron 2008, 58:749-762.
    • (2008) Neuron , vol.58 , pp. 749-762
    • Cingolani, L.A.1    Thalhammer, A.2    Yu, L.M.3    Catalano, M.4    Ramos, T.5    Colicos, M.A.6    Goda, Y.7
  • 44
    • 84876668625 scopus 로고    scopus 로고
    • Emerging roles of astrocytes in neural circuit development
    • Clarke L.E., Barres B.A. Emerging roles of astrocytes in neural circuit development. Nat. Rev. Neurosci. 2013, 14:311-321.
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 311-321
    • Clarke, L.E.1    Barres, B.A.2
  • 45
    • 79960559994 scopus 로고    scopus 로고
    • Methamphetamine-associated cleavage of the synaptic adhesion molecule intercellular adhesion molecule-5
    • Conant K., Lonskaya I., Szklarczyk A., Krall C., Steiner J., Maguire-Zeiss K., Lim S.T. Methamphetamine-associated cleavage of the synaptic adhesion molecule intercellular adhesion molecule-5. J. Neurochem. 2011, 118:521-532.
    • (2011) J. Neurochem. , vol.118 , pp. 521-532
    • Conant, K.1    Lonskaya, I.2    Szklarczyk, A.3    Krall, C.4    Steiner, J.5    Maguire-Zeiss, K.6    Lim, S.T.7
  • 47
    • 0035878167 scopus 로고    scopus 로고
    • Glial cell abnormalities in major psychiatric disorders: the evidence and implications
    • Cotter D.R., Pariante C.M., Everall I.P. Glial cell abnormalities in major psychiatric disorders: the evidence and implications. Brain Res. Bull. 2001, 55:585-595.
    • (2001) Brain Res. Bull. , vol.55 , pp. 585-595
    • Cotter, D.R.1    Pariante, C.M.2    Everall, I.P.3
  • 48
    • 0035369112 scopus 로고    scopus 로고
    • NMDA receptor subunits: diversity, development and disease
    • Cullcandy S., Brickley S., Farrant M. NMDA receptor subunits: diversity, development and disease. Curr. Opin. Neurobiol. 2001, 11:327-335.
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 327-335
    • Cullcandy, S.1    Brickley, S.2    Farrant, M.3
  • 49
    • 80053927770 scopus 로고    scopus 로고
    • Casting a net on dendritic spines: the extracellular matrix and its receptors
    • Dansie L.E., Ethell I.M. Casting a net on dendritic spines: the extracellular matrix and its receptors. Dev. Neurobiol. 2011, 71:956-981.
    • (2011) Dev. Neurobiol. , vol.71 , pp. 956-981
    • Dansie, L.E.1    Ethell, I.M.2
  • 50
    • 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., Fawcett J.W. Composition of perineuronal net extracellular matrix in rat brain: a different disaccharide composition for the net-associated proteoglycans. J. Biol. Chem. 2006, 281:17789-17800.
    • (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
  • 51
    • 72949119124 scopus 로고    scopus 로고
    • Integrins in cancer: biological implications and therapeutic opportunities
    • Desgrosellier J.S., Cheresh D.A. Integrins in cancer: biological implications and therapeutic opportunities. Nat. Rev. Cancer 2010, 10:9-22.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 9-22
    • Desgrosellier, J.S.1    Cheresh, D.A.2
  • 52
    • 0028972484 scopus 로고
    • The alpha-dystroglycan-beta-dystroglycan complex. Membrane organization and relationship to an agrin receptor
    • Deyst K.A., Bowe M.A., Leszyk J.D., Fallon J.R. The alpha-dystroglycan-beta-dystroglycan complex. Membrane organization and relationship to an agrin receptor. J. Biol. Chem. 1995, 270:25956-25959.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25956-25959
    • Deyst, K.A.1    Bowe, M.A.2    Leszyk, J.D.3    Fallon, J.R.4
  • 53
    • 0037704306 scopus 로고    scopus 로고
    • Extracellular matrix molecules and synaptic plasticity
    • Dityatev A., Schachner M. Extracellular matrix molecules and synaptic plasticity. Nat. Rev. Neurosci. 2003, 4:456-468.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 456-468
    • Dityatev, A.1    Schachner, M.2
  • 54
    • 70449704590 scopus 로고    scopus 로고
    • Modulation of synaptic transmission and plasticity by cell adhesion and repulsion molecules
    • Dityatev A., Bukalo O., Schachner M. Modulation of synaptic transmission and plasticity by cell adhesion and repulsion molecules. Neuron Glia Biol. 2008, 4:197-209.
    • (2008) Neuron Glia Biol. , vol.4 , pp. 197-209
    • Dityatev, A.1    Bukalo, O.2    Schachner, M.3
  • 55
    • 77958492330 scopus 로고    scopus 로고
    • The dual role of the extracellular matrix in synaptic plasticity and homeostasis
    • Dityatev A., Schachner M., Sonderegger P. The dual role of the extracellular matrix in synaptic plasticity and homeostasis. Nat. Rev. Neurosci. 2010, 11:735-746.
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 735-746
    • Dityatev, A.1    Schachner, M.2    Sonderegger, P.3
  • 57
    • 84867227874 scopus 로고    scopus 로고
    • Synaptic dysfunction in depression: potential therapeutic targets
    • Duman R.S., Aghajanian G.K. Synaptic dysfunction in depression: potential therapeutic targets. Science 2012, 338:68-72.
    • (2012) Science , vol.338 , pp. 68-72
    • Duman, R.S.1    Aghajanian, G.K.2
  • 60
    • 34547957954 scopus 로고    scopus 로고
    • Matrix metalloproteinases in brain development and remodeling: synaptic functions and targets
    • Ethell I.M., Ethell D.W. Matrix metalloproteinases in brain development and remodeling: synaptic functions and targets. J. Neurosci. Res. 2007, 85:2813-2823.
    • (2007) J. Neurosci. Res. , vol.85 , pp. 2813-2823
    • Ethell, I.M.1    Ethell, D.W.2
  • 61
    • 0033535040 scopus 로고    scopus 로고
    • Cell surface heparan sulfate proteoglycan syndecan-2 induces the maturation of dendritic spines in rat hippocampal neurons
    • Ethell I.M., Yamaguchi Y. Cell surface heparan sulfate proteoglycan syndecan-2 induces the maturation of dendritic spines in rat hippocampal neurons. J. Cell Biol. 1999, 144:575-586.
    • (1999) J. Cell Biol. , vol.144 , pp. 575-586
    • Ethell, I.M.1    Yamaguchi, Y.2
  • 63
    • 0037104764 scopus 로고    scopus 로고
    • Impairment of L-type Ca2+ channel-dependent forms of hippocampal synaptic plasticity in mice deficient in the extracellular matrix glycoprotein tenascin-C
    • Evers M.R., Salmen B., Bukalo O., Rollenhagen A., Bosl M.R., Morellini F., Bartsch U., Dityatev A., Schachner M. Impairment of L-type Ca2+ channel-dependent forms of hippocampal synaptic plasticity in mice deficient in the extracellular matrix glycoprotein tenascin-C. J. Neurosci. 2002, 22:7177-7194.
    • (2002) J. Neurosci. , vol.22 , pp. 7177-7194
    • Evers, M.R.1    Salmen, B.2    Bukalo, O.3    Rollenhagen, A.4    Bosl, M.R.5    Morellini, F.6    Bartsch, U.7    Dityatev, A.8    Schachner, M.9
  • 64
    • 0030823158 scopus 로고    scopus 로고
    • Effects of age, sex, and ethnicity on the association between apolipoprotein E genotype and Alzheimer disease. A meta-analysis. APOE and Alzheimer Disease Meta-Analysis Consortium
    • Farrer L.A., Cupples L.A., Haines J.L., Hyman B., Kukull W.A., Mayeux R., Myers R.H., Pericak-Vance M.A., Risch N., Van Duijn C.M. Effects of age, sex, and ethnicity on the association between apolipoprotein E genotype and Alzheimer disease. A meta-analysis. APOE and Alzheimer Disease Meta-Analysis Consortium. JAMA 1997, 278:1349-1356.
    • (1997) JAMA , vol.278 , pp. 1349-1356
    • Farrer, L.A.1    Cupples, L.A.2    Haines, J.L.3    Hyman, B.4    Kukull, W.A.5    Mayeux, R.6    Myers, R.H.7    Pericak-Vance, M.A.8    Risch, N.9    Van Duijn, C.M.10
  • 65
    • 79551670394 scopus 로고    scopus 로고
    • Reelin regulates cadherin function via Dab1/Rap1 to control neuronal migration and lamination in the neocortex
    • Franco S.J., Martinez-Garay I., Gil-Sanz C., Harkins-Perry S.R., Muller U. Reelin regulates cadherin function via Dab1/Rap1 to control neuronal migration and lamination in the neocortex. Neuron 2011, 69:482-497.
    • (2011) Neuron , vol.69 , pp. 482-497
    • Franco, S.J.1    Martinez-Garay, I.2    Gil-Sanz, C.3    Harkins-Perry, S.R.4    Muller, U.5
  • 66
    • 39549119763 scopus 로고    scopus 로고
    • Activity-induced synaptic capture and exocytosis of the neuronal serine protease neurotrypsin
    • Frischknecht R., Fejtova A., Viesti M., Stephan A., Sonderegger P. Activity-induced synaptic capture and exocytosis of the neuronal serine protease neurotrypsin. J. Neurosci. 2008, 28:1568-1579.
    • (2008) J. Neurosci. , vol.28 , pp. 1568-1579
    • Frischknecht, R.1    Fejtova, A.2    Viesti, M.3    Stephan, A.4    Sonderegger, P.5
  • 67
    • 0033869852 scopus 로고    scopus 로고
    • Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration
    • Gao Y., Li M., Chen W., Simons M. Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration. J. Cell. Physiol. 2000, 184:373-379.
    • (2000) J. Cell. Physiol. , vol.184 , pp. 373-379
    • Gao, Y.1    Li, M.2    Chen, W.3    Simons, M.4
  • 68
    • 0033985644 scopus 로고    scopus 로고
    • Decreased dendritic spine density on prefrontal cortical pyramidal neurons in schizophrenia
    • Glantz L.A., Lewis D.A. Decreased dendritic spine density on prefrontal cortical pyramidal neurons in schizophrenia. Arch. Gen. Psychiatry 2000, 57:65-73.
    • (2000) Arch. Gen. Psychiatry , vol.57 , pp. 65-73
    • Glantz, L.A.1    Lewis, D.A.2
  • 69
    • 0034682827 scopus 로고    scopus 로고
    • Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction
    • Gotthardt M., Trommsdorff M., Nevitt M.F., Shelton J., Richardson J.A., Stockinger W., Nimpf J., Herz J. Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. J. Biol. Chem. 2000, 275:25616-25624.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25616-25624
    • Gotthardt, M.1    Trommsdorff, M.2    Nevitt, M.F.3    Shelton, J.4    Richardson, J.A.5    Stockinger, W.6    Nimpf, J.7    Herz, J.8
  • 70
    • 70349756958 scopus 로고    scopus 로고
    • Loss of dendrite stabilization by the Abl-related gene (Arg) kinase regulates behavioral flexibility and sensitivity to cocaine
    • Gourley S.L., Koleske A.J., Taylor J.R. Loss of dendrite stabilization by the Abl-related gene (Arg) kinase regulates behavioral flexibility and sensitivity to cocaine. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:16859-16864.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16859-16864
    • Gourley, S.L.1    Koleske, A.J.2    Taylor, J.R.3
  • 71
    • 84857084499 scopus 로고    scopus 로고
    • Arg kinase regulates prefrontal dendritic spine refinement and cocaine-induced plasticity
    • Gourley S.L., Olevska A., Warren M.S., Taylor J.R., Koleske A.J. Arg kinase regulates prefrontal dendritic spine refinement and cocaine-induced plasticity. J. Neurosci. 2012, 32:2314-2323.
    • (2012) J. Neurosci. , vol.32 , pp. 2314-2323
    • Gourley, S.L.1    Olevska, A.2    Warren, M.S.3    Taylor, J.R.4    Koleske, A.J.5
  • 72
    • 0034733733 scopus 로고    scopus 로고
    • Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin
    • Grootjans J.J., Reekmans G., Ceulemans H., David G. Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin. J. Biol. Chem. 2000, 275:19933-19941.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19933-19941
    • Grootjans, J.J.1    Reekmans, G.2    Ceulemans, H.3    David, G.4
  • 73
    • 77952928699 scopus 로고    scopus 로고
    • Integrin signaling switches the cytoskeletal and exocytic machinery that drives neuritogenesis
    • Gupton S.L., Gertler F.B. Integrin signaling switches the cytoskeletal and exocytic machinery that drives neuritogenesis. Dev. Cell 2010, 18:725-736.
    • (2010) Dev. Cell , vol.18 , pp. 725-736
    • Gupton, S.L.1    Gertler, F.B.2
  • 75
    • 26844507074 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related proteins (LRPs), Alzheimer's and cognition
    • Harris-White M.E., Frautschy S.A. Low density lipoprotein receptor-related proteins (LRPs), Alzheimer's and cognition. Curr. Drug Targets CNS Neurol. Disord. 2005, 4:469-480.
    • (2005) Curr. Drug Targets CNS Neurol. Disord. , vol.4 , pp. 469-480
    • Harris-White, M.E.1    Frautschy, S.A.2
  • 76
    • 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., 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. 1999, 842:15-29.
    • (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
  • 78
    • 51049122842 scopus 로고    scopus 로고
    • Targeting of tetraspanin proteins-potential benefits and strategies
    • Hemler M.E. Targeting of tetraspanin proteins-potential benefits and strategies. Nat. Rev. Drug Discov. 2008, 7:747-758.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 747-758
    • Hemler, M.E.1
  • 79
    • 0346433978 scopus 로고    scopus 로고
    • Activity-dependent redistribution and essential role of cortactin in dendritic spine morphogenesis
    • Hering H., Sheng M. Activity-dependent redistribution and essential role of cortactin in dendritic spine morphogenesis. J. Neurosci. 2003, 23:11759-11769.
    • (2003) J. Neurosci. , vol.23 , pp. 11759-11769
    • Hering, H.1    Sheng, M.2
  • 80
    • 33750333569 scopus 로고    scopus 로고
    • Reelin, lipoprotein receptors and synaptic plasticity
    • Herz J., Chen Y. Reelin, lipoprotein receptors and synaptic plasticity. Nat. Rev. Neurosci. 2006, 7:850-859.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 850-859
    • Herz, J.1    Chen, Y.2
  • 81
    • 0032514263 scopus 로고    scopus 로고
    • Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    • Hsueh Y.P., Yang F.C., Kharazia V., Naisbitt S., Cohen A.R., Weinberg R.J., Sheng M. Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses. J. Cell Biol. 1998, 142:139-151.
    • (1998) J. Cell Biol. , vol.142 , pp. 139-151
    • Hsueh, Y.P.1    Yang, F.C.2    Kharazia, V.3    Naisbitt, S.4    Cohen, A.R.5    Weinberg, R.J.6    Sheng, M.7
  • 82
    • 33751082371 scopus 로고    scopus 로고
    • Distinct roles of the beta 1-class integrins at the developing and the mature hippocampal excitatory synapse
    • Huang Z., Shimazu K., Woo N.H., Zang K., Muller U., Lu B., Reichardt L.F. Distinct roles of the beta 1-class integrins at the developing and the mature hippocampal excitatory synapse. J. Neurosci. 2006, 26:11208-11219.
    • (2006) J. Neurosci. , vol.26 , pp. 11208-11219
    • Huang, Z.1    Shimazu, K.2    Woo, N.H.3    Zang, K.4    Muller, U.5    Lu, B.6    Reichardt, L.F.7
  • 83
    • 0028801525 scopus 로고
    • Distinct LTP induction mechanisms: contribution of NMDA receptors and voltage-dependent calcium channels
    • Huber K.M., Mauk M.D., Kelly P.T. Distinct LTP induction mechanisms: contribution of NMDA receptors and voltage-dependent calcium channels. J. Neurophysiol. 1995, 73:270-279.
    • (1995) J. Neurophysiol. , vol.73 , pp. 270-279
    • Huber, K.M.1    Mauk, M.D.2    Kelly, P.T.3
  • 85
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 86
    • 79952754299 scopus 로고    scopus 로고
    • Astrocytes control glutamate receptor levels at developing synapses through SPARC-beta-integrin interactions
    • Jones E.V., Bernardinelli Y., Tse Y.C., Chierzi S., Wong T.P., Murai K.K. Astrocytes control glutamate receptor levels at developing synapses through SPARC-beta-integrin interactions. J. Neurosci. 2011, 31:4154-4165.
    • (2011) J. Neurosci. , vol.31 , pp. 4154-4165
    • Jones, E.V.1    Bernardinelli, Y.2    Tse, Y.C.3    Chierzi, S.4    Wong, T.P.5    Murai, K.K.6
  • 88
    • 0034626870 scopus 로고    scopus 로고
    • The dendritic architecture of prefrontal pyramidal neurons in schizophrenic patients
    • Kalus P., Muller T.J., Zuschratter W., Senitz D. The dendritic architecture of prefrontal pyramidal neurons in schizophrenic patients. Neuroreport 2000, 11:3621-3625.
    • (2000) Neuroreport , vol.11 , pp. 3621-3625
    • Kalus, P.1    Muller, T.J.2    Zuschratter, W.3    Senitz, D.4
  • 89
    • 0033797735 scopus 로고    scopus 로고
    • Dendritic anomalies in disorders associated with mental retardation
    • Kaufmann W.E., Moser H.W. Dendritic anomalies in disorders associated with mental retardation. Cereb. Cortex 2000, 10:981-991.
    • (2000) Cereb. Cortex , vol.10 , pp. 981-991
    • Kaufmann, W.E.1    Moser, H.W.2
  • 90
    • 0033807656 scopus 로고    scopus 로고
    • Dendritic cytoskeletal protein expression in mental retardation: an immunohistochemical study of the neocortex in Rett syndrome
    • Kaufmann W.E., MacDonald S.M., Altamura C.R. Dendritic cytoskeletal protein expression in mental retardation: an immunohistochemical study of the neocortex in Rett syndrome. Cereb. Cortex 2000, 10:992-1004.
    • (2000) Cereb. Cortex , vol.10 , pp. 992-1004
    • Kaufmann, W.E.1    MacDonald, S.M.2    Altamura, C.R.3
  • 91
    • 84883511018 scopus 로고    scopus 로고
    • Arg kinase signaling in dendrite and synapse stabilization pathways: memory, cocaine sensitivity, and stress
    • Kerrisk M.E., Koleske A.J. Arg kinase signaling in dendrite and synapse stabilization pathways: memory, cocaine sensitivity, and stress. Int. J. Biochem. Cell Biol. 2013, 45:2496-2500.
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 2496-2500
    • Kerrisk, M.E.1    Koleske, A.J.2
  • 92
    • 84876213804 scopus 로고    scopus 로고
    • Integrin alpha3 is required for late postnatal stability of dendrite arbors, dendritic spines and synapses, and mouse behavior
    • Kerrisk M.E., Greer C.A., Koleske A.J. Integrin alpha3 is required for late postnatal stability of dendrite arbors, dendritic spines and synapses, and mouse behavior. J. Neurosci. 2013, 33:6742-6752.
    • (2013) J. Neurosci. , vol.33 , pp. 6742-6752
    • Kerrisk, M.E.1    Greer, C.A.2    Koleske, A.J.3
  • 94
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M., Carman C.V., Springer T.A. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 2003, 301:1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 95
    • 71449125786 scopus 로고    scopus 로고
    • Overexpression of low-density lipoprotein receptor in the brain markedly inhibits amyloid deposition and increases extracellular a beta clearance
    • Kim J., Castellano J.M., Jiang H., Basak J.M., Parsadanian M., Pham V., Mason S.M., Paul S.M., Holtzman D.M. Overexpression of low-density lipoprotein receptor in the brain markedly inhibits amyloid deposition and increases extracellular a beta clearance. Neuron 2009, 64:632-644.
    • (2009) Neuron , vol.64 , pp. 632-644
    • Kim, J.1    Castellano, J.M.2    Jiang, H.3    Basak, J.M.4    Parsadanian, M.5    Pham, V.6    Mason, S.M.7    Paul, S.M.8    Holtzman, D.M.9
  • 96
    • 0031866384 scopus 로고    scopus 로고
    • N-syndecan and HB-GAM (heparin-binding growth-associated molecule) associate with early axonal tracts in the rat brain
    • Kinnunen A., Kinnunen T., Kaksonen M., Nolo R., Panula P., Rauvala H. N-syndecan and HB-GAM (heparin-binding growth-associated molecule) associate with early axonal tracts in the rat brain. Eur. J. Neurosci. 1998, 10:635-648.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 635-648
    • Kinnunen, A.1    Kinnunen, T.2    Kaksonen, M.3    Nolo, R.4    Panula, P.5    Rauvala, H.6
  • 97
    • 0032562591 scopus 로고    scopus 로고
    • Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth
    • Kinnunen T., Kaksonen M., Saarinen J., Kalkkinen N., Peng H.B., Rauvala H. Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth. J. Biol. Chem. 1998, 273:10702-10708.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10702-10708
    • Kinnunen, T.1    Kaksonen, M.2    Saarinen, J.3    Kalkkinen, N.4    Peng, H.B.5    Rauvala, H.6
  • 100
    • 0036499748 scopus 로고    scopus 로고
    • Alpha3 integrin receptors contribute to the consolidation of long-term potentiation
    • Kramar E.A., Bernard J.A., Gall C.M., Lynch G. Alpha3 integrin receptors contribute to the consolidation of long-term potentiation. Neuroscience 2002, 110:29-39.
    • (2002) Neuroscience , vol.110 , pp. 29-39
    • Kramar, E.A.1    Bernard, J.A.2    Gall, C.M.3    Lynch, G.4
  • 103
    • 65649119024 scopus 로고    scopus 로고
    • Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion
    • Lapetina S., Mader C.C., Machida K., Mayer B.J., Koleske A.J. Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion. J. Cell Biol. 2009, 185:503-519.
    • (2009) J. Cell Biol. , vol.185 , pp. 503-519
    • Lapetina, S.1    Mader, C.C.2    Machida, K.3    Mayer, B.J.4    Koleske, A.J.5
  • 104
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • Lau T.L., Kim C., Ginsberg M.H., Ulmer T.S. The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling. EMBO J. 2009, 28:1351-1361.
    • (2009) EMBO J. , vol.28 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 105
    • 0033556704 scopus 로고    scopus 로고
    • Reg1ulatory role and molecular interactions of a cell-surface heparan sulfate proteoglycan (N-syndecan) in hippocampal long-term potentiation
    • Lauri S.E., Kaukinen S., Kinnunen T., Ylinen A., Imai S., Kaila K., Taira T., Rauvala H. Reg1ulatory role and molecular interactions of a cell-surface heparan sulfate proteoglycan (N-syndecan) in hippocampal long-term potentiation. J. Neurosci. 1999, 19:1226-1235.
    • (1999) J. Neurosci. , vol.19 , pp. 1226-1235
    • Lauri, S.E.1    Kaukinen, S.2    Kinnunen, T.3    Ylinen, A.4    Imai, S.5    Kaila, K.6    Taira, T.7    Rauvala, H.8
  • 106
    • 2342508828 scopus 로고    scopus 로고
    • Reduced spinophilin but not microtubule-associated protein 2 expression in the hippocampal formation in schizophrenia and mood disorders: molecular evidence for a pathology of dendritic spines
    • Law A.J., Weickert C.S., Hyde T.M., Kleinman J.E., Harrison P.J. Reduced spinophilin but not microtubule-associated protein 2 expression in the hippocampal formation in schizophrenia and mood disorders: molecular evidence for a pathology of dendritic spines. Am. J. Psychiatry 2004, 161:1848-1855.
    • (2004) Am. J. Psychiatry , vol.161 , pp. 1848-1855
    • Law, A.J.1    Weickert, C.S.2    Hyde, T.M.3    Kleinman, J.E.4    Harrison, P.J.5
  • 107
    • 0038216785 scopus 로고    scopus 로고
    • Integrins regulate NMDA receptor-mediated synaptic currents
    • Lin B., Arai A.C., Lynch G., Gall C.M. Integrins regulate NMDA receptor-mediated synaptic currents. J. Neurophysiol. 2003, 89:2874-2878.
    • (2003) J. Neurophysiol. , vol.89 , pp. 2874-2878
    • Lin, B.1    Arai, A.C.2    Lynch, G.3    Gall, C.M.4
  • 108
    • 22244458242 scopus 로고    scopus 로고
    • AMPA receptor stimulation increases alpha5beta1 integrin surface expression, adhesive function and signaling
    • Lin C.Y., Lynch G., Gall C.M. AMPA receptor stimulation increases alpha5beta1 integrin surface expression, adhesive function and signaling. J. Neurochem. 2005, 94:531-546.
    • (2005) J. Neurochem. , vol.94 , pp. 531-546
    • Lin, C.Y.1    Lynch, G.2    Gall, C.M.3
  • 109
    • 34249867935 scopus 로고    scopus 로고
    • Syndecan-2 induces filopodia and dendritic spine formation via the neurofibromin-PKA-Ena/VASP pathway
    • Lin Y.L., Lei Y.T., Hong C.J., Hsueh Y.P. Syndecan-2 induces filopodia and dendritic spine formation via the neurofibromin-PKA-Ena/VASP pathway. J. Cell Biol. 2007, 177:829-841.
    • (2007) J. Cell Biol. , vol.177 , pp. 829-841
    • Lin, Y.L.1    Lei, Y.T.2    Hong, C.J.3    Hsueh, Y.P.4
  • 110
    • 77954385137 scopus 로고    scopus 로고
    • Induction of filopodia-like protrusions by transmembrane agrin: role of agrin glycosaminoglycan chains and Rho-family GTPases
    • Lin L., Mccroskery S., Ross J.M., Chak Y., Neuhuber B., Daniels M.P. Induction of filopodia-like protrusions by transmembrane agrin: role of agrin glycosaminoglycan chains and Rho-family GTPases. Exp. Cell Res. 2010, 316:2260-2277.
    • (2010) Exp. Cell Res. , vol.316 , pp. 2260-2277
    • Lin, L.1    Mccroskery, S.2    Ross, J.M.3    Chak, Y.4    Neuhuber, B.5    Daniels, M.P.6
  • 111
    • 84873045444 scopus 로고    scopus 로고
    • Abl2/Arg controls dendritic spine and dendrite arbor stability via distinct cytoskeletal control pathways
    • Lin Y.C., Yeckel M.F., Koleske A.J. Abl2/Arg controls dendritic spine and dendrite arbor stability via distinct cytoskeletal control pathways. J. Neurosci. 2013, 33:1846-1857.
    • (2013) J. Neurosci. , vol.33 , pp. 1846-1857
    • Lin, Y.C.1    Yeckel, M.F.2    Koleske, A.J.3
  • 112
    • 84865425266 scopus 로고    scopus 로고
    • Arg/Abl2 modulates the affinity and stoichiometry of binding of cortactin to F-actin
    • Macgrath S.M., Koleske A.J. Arg/Abl2 modulates the affinity and stoichiometry of binding of cortactin to F-actin. Biochemistry 2012, 51:6644-6653.
    • (2012) Biochemistry , vol.51 , pp. 6644-6653
    • Macgrath, S.M.1    Koleske, A.J.2
  • 118
    • 13444249941 scopus 로고    scopus 로고
    • Selective ablation of alphav integrins in the central nervous system leads to cerebral hemorrhage, seizures, axonal degeneration and premature death
    • McCarty J.H., Lacy-Hulbert A., Charest A., Bronson R.T., Crowley D., Housman D., Savill J., Roes J., Hynes R.O. Selective ablation of alphav integrins in the central nervous system leads to cerebral hemorrhage, seizures, axonal degeneration and premature death. Development 2005, 132:165-176.
    • (2005) Development , vol.132 , pp. 165-176
    • McCarty, J.H.1    Lacy-Hulbert, A.2    Charest, A.3    Bronson, R.T.4    Crowley, D.5    Housman, D.6    Savill, J.7    Roes, J.8    Hynes, R.O.9
  • 119
    • 68349146507 scopus 로고    scopus 로고
    • Transmembrane agrin regulates dendritic filopodia and synapse formation in mature hippocampal neuron cultures
    • Mccroskery S., Bailey A., Lin L., Daniels M.P. Transmembrane agrin regulates dendritic filopodia and synapse formation in mature hippocampal neuron cultures. Neuroscience 2009, 163:168-179.
    • (2009) Neuroscience , vol.163 , pp. 168-179
    • Mccroskery, S.1    Bailey, A.2    Lin, L.3    Daniels, M.P.4
  • 120
    • 79955480084 scopus 로고    scopus 로고
    • A stabilising influence: integrins in regulation of synaptic plasticity
    • Mcgeachie A.B., Cingolani L.A., Goda Y. A stabilising influence: integrins in regulation of synaptic plasticity. Neurosci. Res. 2011, 70:24-29.
    • (2011) Neurosci. Res. , vol.70 , pp. 24-29
    • Mcgeachie, A.B.1    Cingolani, L.A.2    Goda, Y.3
  • 121
    • 84865328557 scopus 로고    scopus 로고
    • Beta3 integrin is dispensable for conditioned fear and hebbian forms of plasticity in the hippocampus
    • Mcgeachie A.B., Skrzypiec A.E., Cingolani L.A., Letellier M., Pawlak R., Goda Y. beta3 integrin is dispensable for conditioned fear and hebbian forms of plasticity in the hippocampus. Eur. J. Neurosci. 2012, 36:2461-2469.
    • (2012) Eur. J. Neurosci. , vol.36 , pp. 2461-2469
    • Mcgeachie, A.B.1    Skrzypiec, A.E.2    Cingolani, L.A.3    Letellier, M.4    Pawlak, R.5    Goda, Y.6
  • 124
    • 0141891986 scopus 로고    scopus 로고
    • Regulation of neuronal morphogenesis and synaptic function by Abl family kinases
    • Moresco E.M., Koleske A.J. Regulation of neuronal morphogenesis and synaptic function by Abl family kinases. Curr. Opin. Neurobiol. 2003, 13:535-544.
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 535-544
    • Moresco, E.M.1    Koleske, A.J.2
  • 125
    • 21544462279 scopus 로고    scopus 로고
    • Integrin-mediated dendrite branch maintenance requires Abelson (Abl) family kinases
    • Moresco E.M., Donaldson S., Williamson A., Koleske A.J. Integrin-mediated dendrite branch maintenance requires Abelson (Abl) family kinases. J. Neurosci. 2005, 25:6105-6118.
    • (2005) J. Neurosci. , vol.25 , pp. 6105-6118
    • Moresco, E.M.1    Donaldson, S.2    Williamson, A.3    Koleske, A.J.4
  • 127
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • Moser M., Nieswandt B., Ussar S., Pozgajova M., Fassler R. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat. Med. 2008, 14:325-330.
    • (2008) Nat. Med. , vol.14 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fassler, R.5
  • 129
    • 80053896208 scopus 로고    scopus 로고
    • Regulation of axonal outgrowth and pathfinding by integrin-ECM interactions
    • Myers J.P., Santiago-Medina M., Gomez T.M. Regulation of axonal outgrowth and pathfinding by integrin-ECM interactions. Dev. Neurobiol. 2011, 71:901-923.
    • (2011) Dev. Neurobiol. , vol.71 , pp. 901-923
    • Myers, J.P.1    Santiago-Medina, M.2    Gomez, T.M.3
  • 132
    • 33645380797 scopus 로고    scopus 로고
    • Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant alpha3beta1, alpha6beta1, alpha7beta1 and alpha6beta4 integrins
    • Nishiuchi R., Takagi J., Hayashi M., Ido H., Yagi Y., Sanzen N., Tsuji T., Yamada M., Sekiguchi K. Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant alpha3beta1, alpha6beta1, alpha7beta1 and alpha6beta4 integrins. Matrix Biol. 2006, 25:189-197.
    • (2006) Matrix Biol. , vol.25 , pp. 189-197
    • Nishiuchi, R.1    Takagi, J.2    Hayashi, M.3    Ido, H.4    Yagi, Y.5    Sanzen, N.6    Tsuji, T.7    Yamada, M.8    Sekiguchi, K.9
  • 133
    • 0347318070 scopus 로고    scopus 로고
    • Reelin promotes hippocampal dendrite development through the VLDLR/ApoER2-Dab1 pathway
    • Niu S., Renfro A., Quattrocchi C.C., Sheldon M., D'Arcangelo G. Reelin promotes hippocampal dendrite development through the VLDLR/ApoER2-Dab1 pathway. Neuron 2004, 41:71-84.
    • (2004) Neuron , vol.41 , pp. 71-84
    • Niu, S.1    Renfro, A.2    Quattrocchi, C.C.3    Sheldon, M.4    D'Arcangelo, G.5
  • 134
    • 84870989006 scopus 로고    scopus 로고
    • Perisynaptic chondroitin sulfate proteoglycans restrict structural plasticity in an integrin-dependent manner
    • 18017a
    • Orlando C., Ster J., Gerber U., Fawcett J.W., Raineteau O. Perisynaptic chondroitin sulfate proteoglycans restrict structural plasticity in an integrin-dependent manner. J. Neurosci. 2012, 32:18009-18017. 18017a.
    • (2012) J. Neurosci. , vol.32 , pp. 18009-18017
    • Orlando, C.1    Ster, J.2    Gerber, U.3    Fawcett, J.W.4    Raineteau, O.5
  • 136
    • 0043033220 scopus 로고    scopus 로고
    • Semaphorin 7A promotes axon outgrowth through integrins and MAPKs
    • Pasterkamp R.J., Peschon J.J., Spriggs M.K., Kolodkin A.L. Semaphorin 7A promotes axon outgrowth through integrins and MAPKs. Nature 2003, 424:398-405.
    • (2003) Nature , vol.424 , pp. 398-405
    • Pasterkamp, R.J.1    Peschon, J.J.2    Spriggs, M.K.3    Kolodkin, A.L.4
  • 137
    • 1842422617 scopus 로고    scopus 로고
    • The role of ECM molecules in activity-dependent synaptic development and plasticity
    • Pavlov I., Lauri S., Taira T., Rauvala H. The role of ECM molecules in activity-dependent synaptic development and plasticity. Birth Defects Res. C Embryo Today 2004, 72:12-24.
    • (2004) Birth Defects Res. C Embryo Today , vol.72 , pp. 12-24
    • Pavlov, I.1    Lauri, S.2    Taira, T.3    Rauvala, H.4
  • 138
    • 0025781539 scopus 로고
    • Evidence that matrix recognition contributes to stabilization but not induction of Ltp
    • Peng X., Bahr B.A., Staubli U., Vanderklish P.W., Lynch G. Evidence that matrix recognition contributes to stabilization but not induction of Ltp. Neuroreport 1991, 2:461-464.
    • (1991) Neuroreport , vol.2 , pp. 461-464
    • Peng, X.1    Bahr, B.A.2    Staubli, U.3    Vanderklish, P.W.4    Lynch, G.5
  • 139
    • 0033103707 scopus 로고    scopus 로고
    • Integrin subunit gene expression is regionally differentiated in adult brain
    • Pinkstaff J.K., Detterich J., Lynch G., Gall C. Integrin subunit gene expression is regionally differentiated in adult brain. J. Neurosci. 1999, 19:1541-1556.
    • (1999) J. Neurosci. , vol.19 , pp. 1541-1556
    • Pinkstaff, J.K.1    Detterich, J.2    Lynch, G.3    Gall, C.4
  • 140
    • 84856397822 scopus 로고    scopus 로고
    • Beta3 integrin interacts directly with GluA2 AMPA receptor subunit and regulates AMPA receptor expression in hippocampal neurons
    • Pozo K., Cingolani L.A., Bassani S., Laurent F., Passafaro M., Goda Y. beta3 integrin interacts directly with GluA2 AMPA receptor subunit and regulates AMPA receptor expression in hippocampal neurons. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:1323-1328.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 1323-1328
    • Pozo, K.1    Cingolani, L.A.2    Bassani, S.3    Laurent, F.4    Passafaro, M.5    Goda, Y.6
  • 142
    • 33845606845 scopus 로고    scopus 로고
    • Differential reelin-induced enhancement of NMDA and AMPA receptor activity in the adult hippocampus
    • Qiu S., Zhao L.F., Korwek K.M., Weeber E.J. Differential reelin-induced enhancement of NMDA and AMPA receptor activity in the adult hippocampus. J. Neurosci. 2006, 26:12943-12955.
    • (2006) J. Neurosci. , vol.26 , pp. 12943-12955
    • Qiu, S.1    Zhao, L.F.2    Korwek, K.M.3    Weeber, E.J.4
  • 143
    • 0034706389 scopus 로고    scopus 로고
    • Rho proteins and the cellular mechanisms of mental retardation
    • Ramakers G.J. Rho proteins and the cellular mechanisms of mental retardation. Am. J. Med. Genet. 2000, 94:367-371.
    • (2000) Am. J. Med. Genet. , vol.94 , pp. 367-371
    • Ramakers, G.J.1
  • 144
    • 54049106103 scopus 로고    scopus 로고
    • Failure of neuronal homeostasis results in common neuropsychiatric phenotypes
    • Ramocki M.B., Zoghbi H.Y. Failure of neuronal homeostasis results in common neuropsychiatric phenotypes. Nature 2008, 455:912-918.
    • (2008) Nature , vol.455 , pp. 912-918
    • Ramocki, M.B.1    Zoghbi, H.Y.2
  • 145
    • 33644961448 scopus 로고    scopus 로고
    • Extracellular matrix molecules and synaptic plasticity: immunomapping of intracellular and secreted Reelin in the adult rat brain
    • Ramos-Moreno T., Galazo M.J., Porrero C., Martinez-Cerdeno V., Clasca F. Extracellular matrix molecules and synaptic plasticity: immunomapping of intracellular and secreted Reelin in the adult rat brain. Eur. J. Neurosci. 2006, 23:401-422.
    • (2006) Eur. J. Neurosci. , vol.23 , pp. 401-422
    • Ramos-Moreno, T.1    Galazo, M.J.2    Porrero, C.3    Martinez-Cerdeno, V.4    Clasca, F.5
  • 146
    • 0028216755 scopus 로고
    • Isolation of a neuronal cell surface receptor of heparin binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3)
    • Raulo E., Chernousov M.A., Carey D.J., Nolo R., Rauvala H. Isolation of a neuronal cell surface receptor of heparin binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3). J. Biol. Chem. 1994, 269:12999-13004.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12999-13004
    • Raulo, E.1    Chernousov, M.A.2    Carey, D.J.3    Nolo, R.4    Rauvala, H.5
  • 147
    • 0027374047 scopus 로고
    • Apolipoprotein E in sporadic Alzheimer's disease: allelic variation and receptor interactions
    • Rebeck G.W., Reiter J.S., Strickland D.K., Hyman B.T. Apolipoprotein E in sporadic Alzheimer's disease: allelic variation and receptor interactions. Neuron 1993, 11:575-580.
    • (1993) Neuron , vol.11 , pp. 575-580
    • Rebeck, G.W.1    Reiter, J.S.2    Strickland, D.K.3    Hyman, B.T.4
  • 150
    • 70449723320 scopus 로고    scopus 로고
    • Reelin and apoE actions on signal transduction, synaptic function and memory formation
    • Rogers J.T., Weeber E.J. Reelin and apoE actions on signal transduction, synaptic function and memory formation. Neuron Glia Biol. 2008, 4:259-270.
    • (2008) Neuron Glia Biol. , vol.4 , pp. 259-270
    • Rogers, J.T.1    Weeber, E.J.2
  • 153
    • 79955467998 scopus 로고    scopus 로고
    • Ephrin Bs are essential components of the Reelin pathway to regulate neuronal migration
    • Senturk A., Pfennig S., Weiss A., Burk K., Acker-Palmer A. Ephrin Bs are essential components of the Reelin pathway to regulate neuronal migration. Nature 2011, 472:356-360.
    • (2011) Nature , vol.472 , pp. 356-360
    • Senturk, A.1    Pfennig, S.2    Weiss, A.3    Burk, K.4    Acker-Palmer, A.5
  • 156
    • 32544455943 scopus 로고    scopus 로고
    • Integrins control dendritic spine plasticity in hippocampal neurons through NMDA receptor and Ca2+/calmodulin-dependent protein kinase II-mediated actin reorganization
    • Shi Y., Ethell I.M. Integrins control dendritic spine plasticity in hippocampal neurons through NMDA receptor and Ca2+/calmodulin-dependent protein kinase II-mediated actin reorganization. J. Neurosci. 2006, 26:1813-1822.
    • (2006) J. Neurosci. , vol.26 , pp. 1813-1822
    • Shi, Y.1    Ethell, I.M.2
  • 157
    • 80053912306 scopus 로고    scopus 로고
    • Role of extracellular matrix proteins and their receptors in the development of the vertebrate neuromuscular junction
    • Singhal N., Martin P.T. Role of extracellular matrix proteins and their receptors in the development of the vertebrate neuromuscular junction. Dev. Neurobiol. 2011, 71:982-1005.
    • (2011) Dev. Neurobiol. , vol.71 , pp. 982-1005
    • Singhal, N.1    Martin, P.T.2
  • 158
    • 0025318477 scopus 로고
    • An inhibitor of integrin receptors blocks long-term potentiation
    • Staubli U., Vanderklish P., Lynch G. An inhibitor of integrin receptors blocks long-term potentiation. Behav. Neural Biol. 1990, 53:1-5.
    • (1990) Behav. Neural Biol. , vol.53 , pp. 1-5
    • Staubli, U.1    Vanderklish, P.2    Lynch, G.3
  • 159
    • 0036397986 scopus 로고    scopus 로고
    • Fibronectin domains of extracellular matrix molecule tenascin-C modulate hippocampal learning and synaptic plasticity
    • Strekalova T., Sun M., Sibbe M., Evers M., Dityatev A., Gass P., Schachner M. Fibronectin domains of extracellular matrix molecule tenascin-C modulate hippocampal learning and synaptic plasticity. Mol. Cell. Neurosci. 2002, 21:173-187.
    • (2002) Mol. Cell. Neurosci. , vol.21 , pp. 173-187
    • Strekalova, T.1    Sun, M.2    Sibbe, M.3    Evers, M.4    Dityatev, A.5    Gass, P.6    Schachner, M.7
  • 160
    • 0036470147 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 undergoes expression and activation during dendritic remodeling in adult hippocampus
    • Szklarczyk A., Lapinska J., Rylski M., McKay R.D., Kaczmarek L. Matrix metalloproteinase-9 undergoes expression and activation during dendritic remodeling in adult hippocampus. J. Neurosci. 2002, 22:920-930.
    • (2002) J. Neurosci. , vol.22 , pp. 920-930
    • Szklarczyk, A.1    Lapinska, J.2    Rylski, M.3    McKay, R.D.4    Kaczmarek, L.5
  • 161
    • 0031056896 scopus 로고    scopus 로고
    • Interstitial deletion of chromosome 1q [del(1)(q24q25.3)] identified by fluorescence in situ hybridization and gene dosage analysis of apolipoprotein a-II, coagulation factor V, and antithrombin III
    • Takano T., Yamanouchi Y., Mori Y., Kudo S., Nakayama T., Sugiura M., Hashira S., Abe T. Interstitial deletion of chromosome 1q [del(1)(q24q25.3)] identified by fluorescence in situ hybridization and gene dosage analysis of apolipoprotein a-II, coagulation factor V, and antithrombin III. Am. J. Med. Genet. 1997, 68:207-210.
    • (1997) Am. J. Med. Genet. , vol.68 , pp. 207-210
    • Takano, T.1    Yamanouchi, Y.2    Mori, Y.3    Kudo, S.4    Nakayama, T.5    Sugiura, M.6    Hashira, S.7    Abe, T.8
  • 163
    • 84894057272 scopus 로고    scopus 로고
    • Cell adhesion and homeostatic synaptic plasticity
    • Thalhammer A., Cingolani L.A. Cell adhesion and homeostatic synaptic plasticity. Neuropharmacology 2014, 78:23-30.
    • (2014) Neuropharmacology , vol.78 , pp. 23-30
    • Thalhammer, A.1    Cingolani, L.A.2
  • 164
    • 84858225391 scopus 로고    scopus 로고
    • 2012 Alzheimer's disease facts and figures
    • Thies W., Bleiler L. 2012 Alzheimer's disease facts and figures. Alzheimers Dement. 2012, 8:131-168.
    • (2012) Alzheimers Dement. , vol.8 , pp. 131-168
    • Thies, W.1    Bleiler, L.2
  • 165
    • 0030982564 scopus 로고    scopus 로고
    • Regulation of dendritic growth and remodeling by Rho, Rac, and Cdc42
    • Threadgill R., Bobb K., Ghosh A. Regulation of dendritic growth and remodeling by Rho, Rac, and Cdc42. Neuron 1997, 19:625-634.
    • (1997) Neuron , vol.19 , pp. 625-634
    • Threadgill, R.1    Bobb, K.2    Ghosh, A.3
  • 169
    • 0036343699 scopus 로고    scopus 로고
    • Neuronal changes in normal human aging and Alzheimer's disease
    • Uylings H.B., De Brabander J.M. Neuronal changes in normal human aging and Alzheimer's disease. Brain Cogn. 2002, 49:268-276.
    • (2002) Brain Cogn. , vol.49 , pp. 268-276
    • Uylings, H.B.1    De Brabander, J.M.2
  • 170
    • 58049191338 scopus 로고    scopus 로고
    • Extracellular proteolysis by matrix metalloproteinase-9 drives dendritic spine enlargement and long-term potentiation coordinately
    • Wang X.B., Bozdagi O., Nikitczuk J.S., Zhai Z.W., Zhou Q., Huntley G.W. Extracellular proteolysis by matrix metalloproteinase-9 drives dendritic spine enlargement and long-term potentiation coordinately. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:19520-19525.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 19520-19525
    • Wang, X.B.1    Bozdagi, O.2    Nikitczuk, J.S.3    Zhai, Z.W.4    Zhou, Q.5    Huntley, G.W.6
  • 173
    • 34147119506 scopus 로고    scopus 로고
    • Alpha5 integrin signaling regulates the formation of spines and synapses in hippocampal neurons
    • Webb D.J., Zhang H., Majumdar D., Horwitz A.F. alpha5 integrin signaling regulates the formation of spines and synapses in hippocampal neurons. J. Biol. Chem. 2007, 282:6929-6935.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6929-6935
    • Webb, D.J.1    Zhang, H.2    Majumdar, D.3    Horwitz, A.F.4
  • 176
    • 58149472662 scopus 로고    scopus 로고
    • Integrin expression is altered after acute and chronic cocaine
    • Wiggins A.T., Pacchioni A.M., Kalivas P.W. Integrin expression is altered after acute and chronic cocaine. Neurosci. Lett. 2009, 450:321-323.
    • (2009) Neurosci. Lett. , vol.450 , pp. 321-323
    • Wiggins, A.T.1    Pacchioni, A.M.2    Kalivas, P.W.3
  • 178
    • 0041529510 scopus 로고    scopus 로고
    • Agrin is a chimeric proteoglycan with the attachment sites for heparan sulfate/chondroitin sulfate located in two multiple serine-glycine clusters
    • Winzen U., Cole G.J., Halfter W. Agrin is a chimeric proteoglycan with the attachment sites for heparan sulfate/chondroitin sulfate located in two multiple serine-glycine clusters. J. Biol. Chem. 2003, 278:30106-30114.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30106-30114
    • Winzen, U.1    Cole, G.J.2    Halfter, W.3
  • 179
    • 84880642453 scopus 로고    scopus 로고
    • Autism spectrum disorder causes, mechanisms, and treatments: focus on neuronal synapses
    • Won H., Mah W., Kim E. Autism spectrum disorder causes, mechanisms, and treatments: focus on neuronal synapses. Front. Mol. Neurosci. 2013, 6:19.
    • (2013) Front. Mol. Neurosci. , vol.6 , pp. 19
    • Won, H.1    Mah, W.2    Kim, E.3
  • 180
    • 0035479818 scopus 로고    scopus 로고
    • Syndecan-4 and focal adhesion function
    • Woods A., Couchman J.R. Syndecan-4 and focal adhesion function. Curr. Opin. Cell Biol. 2001, 13:578-583.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 578-583
    • Woods, A.1    Couchman, J.R.2
  • 181
    • 84862777657 scopus 로고    scopus 로고
    • Integrins as receptor targets for neurological disorders
    • Wu X., Reddy D.S. Integrins as receptor targets for neurological disorders. Pharmacol. Ther. 2012, 134:68-81.
    • (2012) Pharmacol. Ther. , vol.134 , pp. 68-81
    • Wu, X.1    Reddy, D.S.2
  • 183
    • 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. 2000, 57:276-289.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 276-289
    • Yamaguchi, Y.1
  • 184
    • 80054720546 scopus 로고    scopus 로고
    • Laminin-beta1 impairs spatial learning through inhibition of ERK/MAPK and SGK1 signaling
    • Yang Y.C., Ma Y.L., Liu W.T., Lee E.H. Laminin-beta1 impairs spatial learning through inhibition of ERK/MAPK and SGK1 signaling. Neuropsychopharmacology 2011, 36:2571-2586.
    • (2011) Neuropsychopharmacology , vol.36 , pp. 2571-2586
    • Yang, Y.C.1    Ma, Y.L.2    Liu, W.T.3    Lee, E.H.4
  • 185
    • 0034331438 scopus 로고    scopus 로고
    • Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphoinositide 4-kinase
    • Yauch R.L., Hemler M.E. Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphoinositide 4-kinase. Biochem. J. 2000, 351(Pt 3):629-637.
    • (2000) Biochem. J. , vol.351 , pp. 629-637
    • Yauch, R.L.1    Hemler, M.E.2
  • 186
    • 0034737471 scopus 로고    scopus 로고
    • Direct extracellular contact between integrin alpha(3)beta(1) and TM4SF protein CD151
    • Yauch R.L., Kazarov A.R., Desai B., Lee R.T., Hemler M.E. Direct extracellular contact between integrin alpha(3)beta(1) and TM4SF protein CD151. J. Biol. Chem. 2000, 275:9230-9238.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9230-9238
    • Yauch, R.L.1    Kazarov, A.R.2    Desai, B.3    Lee, R.T.4    Hemler, M.E.5
  • 187
    • 0031882047 scopus 로고    scopus 로고
    • The Arg-Gly-Asp motif in the cell adhesion molecule L1 promotes neurite outgrowth via interaction with the alphavbeta3 integrin
    • Yip P.M., Zhao X., Montgomery A.M., Siu C.H. The Arg-Gly-Asp motif in the cell adhesion molecule L1 promotes neurite outgrowth via interaction with the alphavbeta3 integrin. Mol. Biol. Cell 1998, 9:277-290.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 277-290
    • Yip, P.M.1    Zhao, X.2    Montgomery, A.M.3    Siu, C.H.4
  • 188
    • 66349118008 scopus 로고    scopus 로고
    • A novel de novo 1.1Mb duplication of 17q21.33 associated with cognitive impairment and other anomalies
    • Zahir F.R., Langlois S., Gall K., Eydoux P., Marra M.A., Friedman J.M. A novel de novo 1.1Mb duplication of 17q21.33 associated with cognitive impairment and other anomalies. Am. J. Med. Genet. A 2009, 149A:1257-1262.
    • (2009) Am. J. Med. Genet. A , vol.149 A , pp. 1257-1262
    • Zahir, F.R.1    Langlois, S.2    Gall, K.3    Eydoux, P.4    Marra, M.A.5    Friedman, J.M.6
  • 189
    • 0034651082 scopus 로고    scopus 로고
    • Role of tissue plasminogen activator receptor LRP in hippocampal long-term potentiation
    • Zhuo M., Holtzman D.M., Li Y., Osaka H., Demaro J., Jacquin M., Bu G. Role of tissue plasminogen activator receptor LRP in hippocampal long-term potentiation. J. Neurosci. 2000, 20:542-549.
    • (2000) J. Neurosci. , vol.20 , pp. 542-549
    • Zhuo, M.1    Holtzman, D.M.2    Li, Y.3    Osaka, H.4    Demaro, J.5    Jacquin, M.6    Bu, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.