메뉴 건너뛰기




Volumn 36, Issue 6, 2013, Pages 363-373

Where no synapses go: Gatekeepers of circuit remodeling and synaptic strength

Author keywords

Dendritic spine; Nogo receptor; Nogo A; Oligodendrocyte myelin glycoprotein (OMgp); Proteoglycan; Synapse stability; Synaptic structure

Indexed keywords

ALPHA AMINO 3 HYDROXY 5 METHYL 4 ISOXAZOLEPROPIONIC ACID; BETA1 INTEGRIN; BRAIN DERIVED NEUROTROPHIC FACTOR; FIBROBLAST GROWTH FACTOR 2; GLUTAMATE DECARBOXYLASE 67; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; MYELIN ASSOCIATED GLYCOPROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 1; OLIGODENDROCYTE MYELIN GLYCOPROTEIN; POSTSYNAPTIC DENSITY PROTEIN 95; PROTEIN NOGO A; PROTEOCHONDROITIN SULFATE; SULFATIDE;

EID: 84878535927     PISSN: 01662236     EISSN: 1878108X     Source Type: Journal    
DOI: 10.1016/j.tins.2013.04.003     Document Type: Review
Times cited : (62)

References (111)
  • 1
    • 69249100460 scopus 로고    scopus 로고
    • Experience-dependent structural synaptic plasticity in the mammalian brain
    • Holtmaat A., Svoboda K. Experience-dependent structural synaptic plasticity in the mammalian brain. Nat. Rev. Neurosci. 2009, 10:647-658.
    • (2009) Nat. Rev. Neurosci. , vol.10 , pp. 647-658
    • Holtmaat, A.1    Svoboda, K.2
  • 2
    • 0032491569 scopus 로고    scopus 로고
    • Large-scale sprouting of cortical connections after peripheral injury in adult macaque monkeys
    • Florence S.L., et al. Large-scale sprouting of cortical connections after peripheral injury in adult macaque monkeys. Science 1998, 282:1117-1121.
    • (1998) Science , vol.282 , pp. 1117-1121
    • Florence, S.L.1
  • 3
    • 1442348904 scopus 로고    scopus 로고
    • The injured spinal cord spontaneously forms a new intraspinal circuit in adult rats
    • Bareyre F.M., et al. The injured spinal cord spontaneously forms a new intraspinal circuit in adult rats. Nat. Neurosci. 2004, 7:269-277.
    • (2004) Nat. Neurosci. , vol.7 , pp. 269-277
    • Bareyre, F.M.1
  • 5
    • 0742288565 scopus 로고    scopus 로고
    • Regeneration beyond the glial scar
    • Silver J., Miller J.H. Regeneration beyond the glial scar. Nat. Rev. Neurosci. 2004, 5:146-156.
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 146-156
    • Silver, J.1    Miller, J.H.2
  • 6
    • 84859920044 scopus 로고    scopus 로고
    • Training and anti-CSPG combination therapy for spinal cord injury
    • Garcia-Alias G., Fawcett J.W. Training and anti-CSPG combination therapy for spinal cord injury. Exp. Neurol. 2012, 235:26-32.
    • (2012) Exp. Neurol. , vol.235 , pp. 26-32
    • Garcia-Alias, G.1    Fawcett, J.W.2
  • 7
    • 81855193754 scopus 로고    scopus 로고
    • Keratan sulfate restricts neural plasticity after spinal cord injury
    • Imagama S., et al. Keratan sulfate restricts neural plasticity after spinal cord injury. J. Neurosci. 2011, 31:17091-17102.
    • (2011) J. Neurosci. , vol.31 , pp. 17091-17102
    • Imagama, S.1
  • 8
    • 79955768330 scopus 로고    scopus 로고
    • The lipid sulfatide is a novel myelin-associated inhibitor of CNS axon outgrowth
    • Winzeler A.M., et al. The lipid sulfatide is a novel myelin-associated inhibitor of CNS axon outgrowth. J. Neurosci. 2011, 31:6481-6492.
    • (2011) J. Neurosci. , vol.31 , pp. 6481-6492
    • Winzeler, A.M.1
  • 9
    • 33746308062 scopus 로고    scopus 로고
    • Glial inhibition of CNS axon regeneration
    • Yiu G., He Z. Glial inhibition of CNS axon regeneration. Nat. Rev. Neurosci. 2006, 7:617-627.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 617-627
    • Yiu, G.1    He, Z.2
  • 10
    • 20844439022 scopus 로고    scopus 로고
    • Blockade of Nogo66, myelin-associated glycoprotein, and oligodendrocyte myelin glycoprotein by soluble Nogo66 receptor promotes axonal sprouting and recovery after spinal injury
    • Li S., et al. Blockade of Nogo66, myelin-associated glycoprotein, and oligodendrocyte myelin glycoprotein by soluble Nogo66 receptor promotes axonal sprouting and recovery after spinal injury. J. Neurosci. 2004, 24:10511-10520.
    • (2004) J. Neurosci. , vol.24 , pp. 10511-10520
    • Li, S.1
  • 11
    • 77954912826 scopus 로고    scopus 로고
    • Anti-Nogo on the go: from animal models to a clinical trial
    • Zorner B., Schwab M.E. Anti-Nogo on the go: from animal models to a clinical trial. Ann. N. Y. Acad. Sci. 2010, 1198(Suppl. 1):E22-E34.
    • (2010) Ann. N. Y. Acad. Sci. , vol.1198 , Issue.SUPPL. 1
    • Zorner, B.1    Schwab, M.E.2
  • 12
    • 77952636619 scopus 로고    scopus 로고
    • MAG and OMgp synergize with Nogo-A to restrict axonal growth and neurological recovery after spinal cord trauma
    • Cafferty W.B., et al. MAG and OMgp synergize with Nogo-A to restrict axonal growth and neurological recovery after spinal cord trauma. J. Neurosci. 2010, 30:6825-6837.
    • (2010) J. Neurosci. , vol.30 , pp. 6825-6837
    • Cafferty, W.B.1
  • 13
    • 77953653088 scopus 로고    scopus 로고
    • Assessing spinal axon regeneration and sprouting in Nogo-, MAG-, and OMgp-deficient mice
    • Lee J.K., et al. Assessing spinal axon regeneration and sprouting in Nogo-, MAG-, and OMgp-deficient mice. Neuron 2010, 66:663-670.
    • (2010) Neuron , vol.66 , pp. 663-670
    • Lee, J.K.1
  • 14
    • 84859912753 scopus 로고    scopus 로고
    • Role of myelin-associated inhibitors in axonal repair after spinal cord injury
    • Lee J.K., Zheng B. Role of myelin-associated inhibitors in axonal repair after spinal cord injury. Exp. Neurol. 2012, 235:33-42.
    • (2012) Exp. Neurol. , vol.235 , pp. 33-42
    • Lee, J.K.1    Zheng, B.2
  • 15
    • 34447118172 scopus 로고    scopus 로고
    • The Nogo66 receptor NgR1 is required only for the acute growth cone-collapsing but not the chronic growth-inhibitory actions of myelin inhibitors
    • Chivatakarn O., et al. The Nogo66 receptor NgR1 is required only for the acute growth cone-collapsing but not the chronic growth-inhibitory actions of myelin inhibitors. J. Neurosci. 2007, 27:7117-7124.
    • (2007) J. Neurosci. , vol.27 , pp. 7117-7124
    • Chivatakarn, O.1
  • 16
    • 55849086190 scopus 로고    scopus 로고
    • PirB is a functional receptor for myelin inhibitors of axonal regeneration
    • Atwal J.K., et al. PirB is a functional receptor for myelin inhibitors of axonal regeneration. Science 2008, 322:967-970.
    • (2008) Science , vol.322 , pp. 967-970
    • Atwal, J.K.1
  • 17
    • 12844272145 scopus 로고    scopus 로고
    • Genetic deletion of the Nogo receptor does not reduce neurite inhibition in vitro or promote corticospinal tract regeneration in vivo
    • Zheng B., et al. Genetic deletion of the Nogo receptor does not reduce neurite inhibition in vitro or promote corticospinal tract regeneration in vivo. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:1205-1210.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 1205-1210
    • Zheng, B.1
  • 18
    • 7044246002 scopus 로고    scopus 로고
    • Nogo66 receptor prevents raphespinal and rubrospinal axon regeneration and limits functional recovery from spinal cord injury
    • Kim J.E., et al. Nogo66 receptor prevents raphespinal and rubrospinal axon regeneration and limits functional recovery from spinal cord injury. Neuron 2004, 44:439-451.
    • (2004) Neuron , vol.44 , pp. 439-451
    • Kim, J.E.1
  • 19
    • 70350502060 scopus 로고    scopus 로고
    • PTPsigma is a receptor for chondroitin sulfate proteoglycan, an inhibitor of neural regeneration
    • Shen Y., et al. PTPsigma is a receptor for chondroitin sulfate proteoglycan, an inhibitor of neural regeneration. Science 2009, 326:592-596.
    • (2009) Science , vol.326 , pp. 592-596
    • Shen, Y.1
  • 20
    • 80053624921 scopus 로고    scopus 로고
    • Leukocyte common antigen-related phosphatase is a functional receptor for chondroitin sulfate proteoglycan axon growth inhibitors
    • Fisher D., et al. Leukocyte common antigen-related phosphatase is a functional receptor for chondroitin sulfate proteoglycan axon growth inhibitors. J. Neurosci. 2011, 31:14051-14066.
    • (2011) J. Neurosci. , vol.31 , pp. 14051-14066
    • Fisher, D.1
  • 21
    • 84859459689 scopus 로고    scopus 로고
    • A sulfated carbohydrate epitope inhibits axon regeneration after injury
    • Brown J.M., et al. A sulfated carbohydrate epitope inhibits axon regeneration after injury. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:4768-4773.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 4768-4773
    • Brown, J.M.1
  • 22
    • 84860284042 scopus 로고    scopus 로고
    • NgR1 and NgR3 are receptors for chondroitin sulfate proteoglycans
    • Dickendesher T.L., et al. NgR1 and NgR3 are receptors for chondroitin sulfate proteoglycans. Nat. Neurosci. 2012, 15:703-712.
    • (2012) Nat. Neurosci. , vol.15 , pp. 703-712
    • Dickendesher, T.L.1
  • 23
    • 22144460104 scopus 로고    scopus 로고
    • CS-4,6 is differentially upregulated in glial scar and is a potent inhibitor of neurite extension
    • Gilbert R.J., et al. CS-4,6 is differentially upregulated in glial scar and is a potent inhibitor of neurite extension. Mol. Cell. Neurosci. 2005, 29:545-558.
    • (2005) Mol. Cell. Neurosci. , vol.29 , pp. 545-558
    • Gilbert, R.J.1
  • 24
    • 12844262132 scopus 로고    scopus 로고
    • The Nogo66 receptor homolog NgR2 is a sialic acid-dependent receptor selective for myelin-associated glycoprotein
    • Venkatesh K., et al. The Nogo66 receptor homolog NgR2 is a sialic acid-dependent receptor selective for myelin-associated glycoprotein. J. Neurosci. 2005, 25:808-822.
    • (2005) J. Neurosci. , vol.25 , pp. 808-822
    • Venkatesh, K.1
  • 25
    • 84875616437 scopus 로고    scopus 로고
    • LDL receptor-related protein-1 is a sialic acid-independent receptor for myelin-associated glycoprotein (MAG) that functions in neurite outgrowth inhibition by MAG and CNS myelin
    • Stiles T.L., et al. LDL receptor-related protein-1 is a sialic acid-independent receptor for myelin-associated glycoprotein (MAG) that functions in neurite outgrowth inhibition by MAG and CNS myelin. J. Cell Sci. 2013, 126:209-220.
    • (2013) J. Cell Sci. , vol.126 , pp. 209-220
    • Stiles, T.L.1
  • 26
    • 0037062511 scopus 로고    scopus 로고
    • Gangliosides are functional nerve cell ligands for myelin-associated glycoprotein (MAG), an inhibitor of nerve regeneration
    • Vyas A.A., et al. Gangliosides are functional nerve cell ligands for myelin-associated glycoprotein (MAG), an inhibitor of nerve regeneration. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:8412-8417.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 8412-8417
    • Vyas, A.A.1
  • 27
    • 65949090487 scopus 로고    scopus 로고
    • β1-Integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones
    • Goh E.L., et al. β1-Integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones. Mol. Brain 2008, 1:10.
    • (2008) Mol. Brain , vol.1 , pp. 10
    • Goh, E.L.1
  • 28
    • 46549086820 scopus 로고    scopus 로고
    • Critical period revisited: impact on vision
    • Morishita H., Hensch T.K. Critical period revisited: impact on vision. Curr. Opin. Neurobiol. 2008, 18:101-107.
    • (2008) Curr. Opin. Neurobiol. , vol.18 , pp. 101-107
    • Morishita, H.1    Hensch, T.K.2
  • 29
    • 25844467735 scopus 로고    scopus 로고
    • Experience-driven plasticity of visual cortex limited by myelin and Nogo receptor
    • McGee A.W., et al. Experience-driven plasticity of visual cortex limited by myelin and Nogo receptor. Science 2005, 309:2222-2226.
    • (2005) Science , vol.309 , pp. 2222-2226
    • McGee, A.W.1
  • 30
    • 70449758396 scopus 로고    scopus 로고
    • Classical MHCI molecules regulate retinogeniculate refinement and limit ocular dominance plasticity
    • Datwani A., et al. Classical MHCI molecules regulate retinogeniculate refinement and limit ocular dominance plasticity. Neuron 2009, 64:463-470.
    • (2009) Neuron , vol.64 , pp. 463-470
    • Datwani, A.1
  • 31
    • 33749007674 scopus 로고    scopus 로고
    • PirB restricts ocular-dominance plasticity in visual cortex
    • Syken J., et al. PirB restricts ocular-dominance plasticity in visual cortex. Science 2006, 313:1795-1800.
    • (2006) Science , vol.313 , pp. 1795-1800
    • Syken, J.1
  • 32
    • 0037044829 scopus 로고    scopus 로고
    • Reactivation of ocular dominance plasticity in the adult visual cortex
    • Pizzorusso T., et al. Reactivation of ocular dominance plasticity in the adult visual cortex. Science 2002, 298:1248-1251.
    • (2002) Science , vol.298 , pp. 1248-1251
    • Pizzorusso, T.1
  • 33
    • 33744781051 scopus 로고    scopus 로고
    • Structural and functional recovery from early monocular deprivation in adult rats
    • Pizzorusso T., et al. Structural and functional recovery from early monocular deprivation in adult rats. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:8517-8522.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 8517-8522
    • Pizzorusso, T.1
  • 34
    • 84857641919 scopus 로고    scopus 로고
    • Persistent cortical plasticity by upregulation of chondroitin 6-sulfation
    • Miyata S., et al. Persistent cortical plasticity by upregulation of chondroitin 6-sulfation. Nat. Neurosci. 2012, 15:414-422.
    • (2012) Nat. Neurosci. , vol.15 , pp. 414-422
    • Miyata, S.1
  • 35
    • 77955148070 scopus 로고    scopus 로고
    • Animals lacking link protein have attenuated perineuronal nets and persistent plasticity
    • Carulli D., et al. Animals lacking link protein have attenuated perineuronal nets and persistent plasticity. Brain 2010, 133:2331-2347.
    • (2010) Brain , vol.133 , pp. 2331-2347
    • Carulli, D.1
  • 36
    • 84863492175 scopus 로고    scopus 로고
    • Otx2 binding to perineuronal nets persistently regulates plasticity in the mature visual cortex
    • Beurdeley M., et al. Otx2 binding to perineuronal nets persistently regulates plasticity in the mature visual cortex. J. Neurosci. 2012, 32:9429-9437.
    • (2012) J. Neurosci. , vol.32 , pp. 9429-9437
    • Beurdeley, M.1
  • 37
    • 48449089927 scopus 로고    scopus 로고
    • Experience-dependent transfer of Otx2 homeoprotein into the visual cortex activates postnatal plasticity
    • Sugiyama S., et al. Experience-dependent transfer of Otx2 homeoprotein into the visual cortex activates postnatal plasticity. Cell 2008, 134:508-520.
    • (2008) Cell , vol.134 , pp. 508-520
    • Sugiyama, S.1
  • 38
    • 77956859009 scopus 로고    scopus 로고
    • Oligodendrocyte-myelin glycoprotein and Nogo negatively regulate activity-dependent synaptic plasticity
    • Raiker S.J., et al. Oligodendrocyte-myelin glycoprotein and Nogo negatively regulate activity-dependent synaptic plasticity. J. Neurosci. 2010, 30:12432-12445.
    • (2010) J. Neurosci. , vol.30 , pp. 12432-12445
    • Raiker, S.J.1
  • 39
    • 70449528326 scopus 로고    scopus 로고
    • GPR50 interacts with neuronal NOGO-A and affects neurite outgrowth
    • Grunewald E., et al. GPR50 interacts with neuronal NOGO-A and affects neurite outgrowth. Mol. Cell. Neurosci. 2009, 42:363-371.
    • (2009) Mol. Cell. Neurosci. , vol.42 , pp. 363-371
    • Grunewald, E.1
  • 40
    • 77958492330 scopus 로고    scopus 로고
    • The dual role of the extracellular matrix in synaptic plasticity and homeostasis
    • Dityatev A., et al. 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
  • 41
    • 0036663013 scopus 로고    scopus 로고
    • Localization of Nogo-A and Nogo66 receptor proteins at sites of axon-myelin and synaptic contact
    • Wang X., et al. Localization of Nogo-A and Nogo66 receptor proteins at sites of axon-myelin and synaptic contact. J. Neurosci. 2002, 22:5505-5515.
    • (2002) J. Neurosci. , vol.22 , pp. 5505-5515
    • Wang, X.1
  • 42
    • 40849102868 scopus 로고    scopus 로고
    • Synaptic function for the Nogo66 receptor NgR1: regulation of dendritic spine morphology and activity-dependent synaptic strength
    • Lee H., et al. Synaptic function for the Nogo66 receptor NgR1: regulation of dendritic spine morphology and activity-dependent synaptic strength. J. Neurosci. 2008, 28:2753-2765.
    • (2008) J. Neurosci. , vol.28 , pp. 2753-2765
    • Lee, H.1
  • 43
    • 20044383455 scopus 로고    scopus 로고
    • LAR receptor protein tyrosine phosphatases in the development and maintenance of excitatory synapses
    • Dunah A.W., et al. LAR receptor protein tyrosine phosphatases in the development and maintenance of excitatory synapses. Nat. Neurosci. 2005, 8:458-467.
    • (2005) Nat. Neurosci. , vol.8 , pp. 458-467
    • Dunah, A.W.1
  • 44
    • 32344447373 scopus 로고    scopus 로고
    • The HSPGs syndecan and dallylike bind the receptor phosphatase LAR and exert distinct effects on synaptic development
    • Johnson K.G., et al. The HSPGs syndecan and dallylike bind the receptor phosphatase LAR and exert distinct effects on synaptic development. Neuron 2006, 49:517-531.
    • (2006) Neuron , vol.49 , pp. 517-531
    • Johnson, K.G.1
  • 45
    • 78751694593 scopus 로고    scopus 로고
    • Postsynaptic TrkC and presynaptic PTPσ function as a bidirectional excitatory synaptic organizing complex
    • Takahashi H., et al. Postsynaptic TrkC and presynaptic PTPσ function as a bidirectional excitatory synaptic organizing complex. Neuron 2011, 69:287-303.
    • (2011) Neuron , vol.69 , pp. 287-303
    • Takahashi, H.1
  • 46
    • 80053025841 scopus 로고    scopus 로고
    • IL-1 receptor accessory protein-like 1 associated with mental retardation and autism mediates synapse formation by trans-synaptic interaction with protein tyrosine phosphatase delta
    • Yoshida T., et al. IL-1 receptor accessory protein-like 1 associated with mental retardation and autism mediates synapse formation by trans-synaptic interaction with protein tyrosine phosphatase delta. J. Neurosci. 2011, 31:13485-13499.
    • (2011) J. Neurosci. , vol.31 , pp. 13485-13499
    • Yoshida, T.1
  • 47
    • 4744352010 scopus 로고    scopus 로고
    • Neuronal LRP1 functionally associates with postsynaptic proteins and is required for normal motor function in mice
    • May P., et al. Neuronal LRP1 functionally associates with postsynaptic proteins and is required for normal motor function in mice. Mol. Cell. Biol. 2004, 24:8872-8883.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8872-8883
    • May, P.1
  • 48
    • 79955480084 scopus 로고    scopus 로고
    • Stabilising influence: integrins in regulation of synaptic plasticity
    • McGeachie A.B., et al. 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
  • 49
    • 77957728129 scopus 로고    scopus 로고
    • Nogo-A stabilizes the architecture of hippocampal neurons
    • Zagrebelsky M., et al. Nogo-A stabilizes the architecture of hippocampal neurons. J. Neurosci. 2010, 30:13220-13234.
    • (2010) J. Neurosci. , vol.30 , pp. 13220-13234
    • Zagrebelsky, M.1
  • 50
    • 78650513680 scopus 로고    scopus 로고
    • Dendritic spine alterations in neocortical pyramidal neurons following postnatal neuronal Nogo-A knockdown
    • Pradhan A.D., et al. Dendritic spine alterations in neocortical pyramidal neurons following postnatal neuronal Nogo-A knockdown. Dev. Neurosci. 2010, 32:313-320.
    • (2010) Dev. Neurosci. , vol.32 , pp. 313-320
    • Pradhan, A.D.1
  • 51
    • 84856711993 scopus 로고    scopus 로고
    • The Nogo receptor family restricts synapse number in the developing hippocampus
    • Wills Z.P., et al. The Nogo receptor family restricts synapse number in the developing hippocampus. Neuron 2012, 73:466-481.
    • (2012) Neuron , vol.73 , pp. 466-481
    • Wills, Z.P.1
  • 52
    • 84870989006 scopus 로고    scopus 로고
    • Perisynaptic chondroitin sulfate proteoglycans restrict structural plasticity in an integrin-dependent manner
    • Orlando C., et al. Perisynaptic chondroitin sulfate proteoglycans restrict structural plasticity in an integrin-dependent manner. J. Neurosci. 2012, 32:18009-18017.
    • (2012) J. Neurosci. , vol.32 , pp. 18009-18017
    • Orlando, C.1
  • 53
    • 32544455943 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II-mediated actin reorganization
    • 2+/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
  • 54
    • 38749109233 scopus 로고    scopus 로고
    • The N-terminal domain of Nogo-A inhibits cell adhesion and axonal outgrowth by an integrin-specific mechanism
    • Hu F., Strittmatter S.M. The N-terminal domain of Nogo-A inhibits cell adhesion and axonal outgrowth by an integrin-specific mechanism. J. Neurosci. 2008, 28:1262-1269.
    • (2008) J. Neurosci. , vol.28 , pp. 1262-1269
    • Hu, F.1    Strittmatter, S.M.2
  • 55
    • 79955766629 scopus 로고    scopus 로고
    • Integrin activation promotes axon growth on inhibitory chondroitin sulfate proteoglycans by enhancing integrin signaling
    • Tan C.L., et al. Integrin activation promotes axon growth on inhibitory chondroitin sulfate proteoglycans by enhancing integrin signaling. J. Neurosci. 2011, 31:6289-6295.
    • (2011) J. Neurosci. , vol.31 , pp. 6289-6295
    • Tan, C.L.1
  • 56
    • 33746895084 scopus 로고    scopus 로고
    • Neurotrophins support regenerative axon assembly over CSPGs by an ECM-integrin-independent mechanism
    • Zhou F.Q., et al. Neurotrophins support regenerative axon assembly over CSPGs by an ECM-integrin-independent mechanism. J. Cell Sci. 2006, 119:2787-2796.
    • (2006) J. Cell Sci. , vol.119 , pp. 2787-2796
    • Zhou, F.Q.1
  • 57
    • 84862576493 scopus 로고    scopus 로고
    • Astrocyte glypicans 4 and 6 promote formation of excitatory synapses via GluA1 AMPA receptors
    • Allen N.J., et al. Astrocyte glypicans 4 and 6 promote formation of excitatory synapses via GluA1 AMPA receptors. Nature 2012, 486:410-414.
    • (2012) Nature , vol.486 , pp. 410-414
    • Allen, N.J.1
  • 59
    • 33846071446 scopus 로고    scopus 로고
    • An RNAi-based approach identifies molecules required for glutamatergic and GABAergic synapse development
    • Paradis S., et al. An RNAi-based approach identifies molecules required for glutamatergic and GABAergic synapse development. Neuron 2007, 53:217-232.
    • (2007) Neuron , vol.53 , pp. 217-232
    • Paradis, S.1
  • 60
    • 72949100509 scopus 로고    scopus 로고
    • Secreted semaphorins control spine distribution and morphogenesis in the postnatal CNS
    • Tran T.S., et al. Secreted semaphorins control spine distribution and morphogenesis in the postnatal CNS. Nature 2009, 462:1065-1069.
    • (2009) Nature , vol.462 , pp. 1065-1069
    • Tran, T.S.1
  • 61
    • 17044413281 scopus 로고    scopus 로고
    • Secreted semaphorins modulate synaptic transmission in the adult hippocampus
    • Sahay A., et al. Secreted semaphorins modulate synaptic transmission in the adult hippocampus. J. Neurosci. 2005, 25:3613-3620.
    • (2005) J. Neurosci. , vol.25 , pp. 3613-3620
    • Sahay, A.1
  • 62
    • 67651156246 scopus 로고    scopus 로고
    • Semaphorin 5B mediates synapse elimination in hippocampal neurons
    • O'Connor T.P., et al. Semaphorin 5B mediates synapse elimination in hippocampal neurons. Neural Dev. 2009, 4:18.
    • (2009) Neural Dev. , vol.4 , pp. 18
    • O'Connor, T.P.1
  • 63
    • 80054023203 scopus 로고    scopus 로고
    • Role of leucine-rich repeat proteins in the development and function of neural circuits
    • De Wit J., et al. Role of leucine-rich repeat proteins in the development and function of neural circuits. Annu. Rev. Cell Dev. Biol. 2011, 27:697-729.
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 697-729
    • De Wit, J.1
  • 64
    • 12344250057 scopus 로고    scopus 로고
    • Transient and persistent dendritic spines in the neocortex in vivo
    • Holtmaat A.J., et al. Transient and persistent dendritic spines in the neocortex in vivo. Neuron 2005, 45:279-291.
    • (2005) Neuron , vol.45 , pp. 279-291
    • Holtmaat, A.J.1
  • 65
    • 84876450980 scopus 로고    scopus 로고
    • Anatomical plasticity of adult brain is titrated by Nogo receptor 1
    • Akbik F.V., et al. Anatomical plasticity of adult brain is titrated by Nogo receptor 1. Neuron 2013, 77:859-866.
    • (2013) Neuron , vol.77 , pp. 859-866
    • Akbik, F.V.1
  • 66
    • 0035959932 scopus 로고    scopus 로고
    • EphB/syndecan-2 signaling in dendritic spine morphogenesis
    • Ethell I.M., et al. EphB/syndecan-2 signaling in dendritic spine morphogenesis. Neuron 2001, 31:1001-1013.
    • (2001) Neuron , vol.31 , pp. 1001-1013
    • Ethell, I.M.1
  • 67
    • 0037187643 scopus 로고    scopus 로고
    • Drosophila liprin-alpha and the receptor phosphatase Dlar control synapse morphogenesis
    • Kaufmann N., et al. Drosophila liprin-alpha and the receptor phosphatase Dlar control synapse morphogenesis. Neuron 2002, 34:27-38.
    • (2002) Neuron , vol.34 , pp. 27-38
    • Kaufmann, N.1
  • 68
    • 0036396896 scopus 로고    scopus 로고
    • Syndecan-3-deficient mice exhibit enhanced LTP and impaired hippocampus-dependent memory
    • Kaksonen M., et al. Syndecan-3-deficient mice exhibit enhanced LTP and impaired hippocampus-dependent memory. Mol. Cell. Neurosci. 2002, 21:158-172.
    • (2002) Mol. Cell. Neurosci. , vol.21 , pp. 158-172
    • Kaksonen, M.1
  • 69
    • 0036838079 scopus 로고    scopus 로고
    • Brevican-deficient mice display impaired hippocampal CA1 long-term potentiation but show no obvious deficits in learning and memory
    • Brakebusch C., et al. Brevican-deficient mice display impaired hippocampal CA1 long-term potentiation but show no obvious deficits in learning and memory. Mol. Cell. Biol. 2002, 22:7417-7427.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7417-7427
    • Brakebusch, C.1
  • 70
    • 10444257969 scopus 로고    scopus 로고
    • Semaphorin 5A is a bifunctional axon guidance cue regulated by heparan and chondroitin sulfate proteoglycans
    • Kantor D.B., et al. Semaphorin 5A is a bifunctional axon guidance cue regulated by heparan and chondroitin sulfate proteoglycans. Neuron 2004, 44:961-975.
    • (2004) Neuron , vol.44 , pp. 961-975
    • Kantor, D.B.1
  • 71
    • 79955470793 scopus 로고    scopus 로고
    • Proteoglycan-specific molecular switch for RPTPsigma clustering and neuronal extension
    • Coles C.H., et al. Proteoglycan-specific molecular switch for RPTPsigma clustering and neuronal extension. Science 2011, 332:484-488.
    • (2011) Science , vol.332 , pp. 484-488
    • Coles, C.H.1
  • 72
    • 0242494082 scopus 로고    scopus 로고
    • Mammalian brain morphogenesis and midline axon guidance require heparan sulfate
    • Inatani M., et al. Mammalian brain morphogenesis and midline axon guidance require heparan sulfate. Science 2003, 302:1044-1046.
    • (2003) Science , vol.302 , pp. 1044-1046
    • Inatani, M.1
  • 73
    • 84867148827 scopus 로고    scopus 로고
    • The extracellular matrix proteoglycan perlecan facilitates transmembrane semaphorin-mediated repulsive guidance
    • Cho J.Y., et al. The extracellular matrix proteoglycan perlecan facilitates transmembrane semaphorin-mediated repulsive guidance. Genes Dev. 2012, 26:2222-2235.
    • (2012) Genes Dev. , vol.26 , pp. 2222-2235
    • Cho, J.Y.1
  • 74
    • 80053920712 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycans regulate astrocyte-dependent synaptogenesis and modulate synaptic activity in primary embryonic hippocampal neurons
    • Pyka M., et al. Chondroitin sulfate proteoglycans regulate astrocyte-dependent synaptogenesis and modulate synaptic activity in primary embryonic hippocampal neurons. Eur. J. Neurosci. 2011, 33:2187-2202.
    • (2011) Eur. J. Neurosci. , vol.33 , pp. 2187-2202
    • Pyka, M.1
  • 75
    • 0036430039 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 increases functional excitatory synapses on hippocampal neurons
    • Li A.J., et al. Fibroblast growth factor-2 increases functional excitatory synapses on hippocampal neurons. Eur. J. Neurosci. 2002, 16:1313-1324.
    • (2002) Eur. J. Neurosci. , vol.16 , pp. 1313-1324
    • Li, A.J.1
  • 76
    • 79952295895 scopus 로고    scopus 로고
    • NogoA restricts synaptic plasticity in the adult hippocampus on a fast time scale
    • Delekate A., et al. NogoA restricts synaptic plasticity in the adult hippocampus on a fast time scale. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:2569-2574.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2569-2574
    • Delekate, A.1
  • 77
    • 76149126141 scopus 로고    scopus 로고
    • Pincher-generated Nogo-A endosomes mediate growth cone collapse and retrograde signaling
    • Joset A., et al. Pincher-generated Nogo-A endosomes mediate growth cone collapse and retrograde signaling. J. Cell Biol. 2010, 188:271-285.
    • (2010) J. Cell Biol. , vol.188 , pp. 271-285
    • Joset, A.1
  • 78
    • 82955187501 scopus 로고    scopus 로고
    • Neuronal Nogo-A regulates glutamate receptor subunit expression in hippocampal neurons
    • Peng X., et al. Neuronal Nogo-A regulates glutamate receptor subunit expression in hippocampal neurons. J. Neurochem. 2011, 119:1183-1193.
    • (2011) J. Neurochem. , vol.119 , pp. 1183-1193
    • Peng, X.1
  • 79
    • 84862195665 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase sigma regulates synapse structure, function and plasticity
    • Horn K.E., et al. Receptor protein tyrosine phosphatase sigma regulates synapse structure, function and plasticity. J. Neurochem. 2012, 122:147-161.
    • (2012) J. Neurochem. , vol.122 , pp. 147-161
    • Horn, K.E.1
  • 80
    • 1542291070 scopus 로고    scopus 로고
    • Mice deficient for the extracellular matrix glycoprotein tenascin-r show physiological and structural hallmarks of increased hippocampal excitability, but no increased susceptibility to seizures in the pilocarpine model of epilepsy
    • Brenneke F., et al. Mice deficient for the extracellular matrix glycoprotein tenascin-r show physiological and structural hallmarks of increased hippocampal excitability, but no increased susceptibility to seizures in the pilocarpine model of epilepsy. Neuroscience 2004, 124:841-855.
    • (2004) Neuroscience , vol.124 , pp. 841-855
    • Brenneke, F.1
  • 81
    • 67649766804 scopus 로고    scopus 로고
    • Brain extracellular matrix affects AMPA receptor lateral mobility and short-term synaptic plasticity
    • Frischknecht R., et al. Brain extracellular matrix affects AMPA receptor lateral mobility and short-term synaptic plasticity. Nat. Neurosci. 2009, 12:897-904.
    • (2009) Nat. Neurosci. , vol.12 , pp. 897-904
    • Frischknecht, R.1
  • 82
    • 8844263909 scopus 로고    scopus 로고
    • Activated CREB is sufficient to overcome inhibitors in myelin and promote spinal axon regeneration in vivo
    • Gao Y., et al. Activated CREB is sufficient to overcome inhibitors in myelin and promote spinal axon regeneration in vivo. Neuron 2004, 44:609-621.
    • (2004) Neuron , vol.44 , pp. 609-621
    • Gao, Y.1
  • 83
    • 0347694856 scopus 로고    scopus 로고
    • Neurotrophins elevate cAMP to reach a threshold required to overcome inhibition by MAG through extracellular signal-regulated kinase-dependent inhibition of phosphodiesterase
    • Gao Y., et al. Neurotrophins elevate cAMP to reach a threshold required to overcome inhibition by MAG through extracellular signal-regulated kinase-dependent inhibition of phosphodiesterase. J. Neurosci. 2003, 23:11770-11777.
    • (2003) J. Neurosci. , vol.23 , pp. 11770-11777
    • Gao, Y.1
  • 84
    • 77949897122 scopus 로고    scopus 로고
    • Overcoming amino-Nogo-induced inhibition of cell spreading and neurite outgrowth by 12-O-tetradecanoylphorbol-13-acetate-type tumor promoters
    • Deng K., et al. Overcoming amino-Nogo-induced inhibition of cell spreading and neurite outgrowth by 12-O-tetradecanoylphorbol-13-acetate-type tumor promoters. J. Biol. Chem. 2010, 285:6425-6433.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6425-6433
    • Deng, K.1
  • 85
    • 84859949701 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycans down-regulate spine formation in cortical neurons by targeting tropomyosin-related kinase B (TrkB) protein
    • Kurihara D., Yamashita T. Chondroitin sulfate proteoglycans down-regulate spine formation in cortical neurons by targeting tropomyosin-related kinase B (TrkB) protein. J. Biol. Chem. 2012, 287:13822-13828.
    • (2012) J. Biol. Chem. , vol.287 , pp. 13822-13828
    • Kurihara, D.1    Yamashita, T.2
  • 86
    • 5344244073 scopus 로고    scopus 로고
    • Translational regulatory mechanisms in persistent forms of synaptic plasticity
    • Kelleher R.J., et al. Translational regulatory mechanisms in persistent forms of synaptic plasticity. Neuron 2004, 44:59-73.
    • (2004) Neuron , vol.44 , pp. 59-73
    • Kelleher, R.J.1
  • 87
    • 84862266808 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor activation of CaM-kinase kinase via transient receptor potential canonical channels induces the translation and synaptic incorporation of GluA1-containing calcium-permeable AMPA receptors
    • Fortin D.A., et al. Brain-derived neurotrophic factor activation of CaM-kinase kinase via transient receptor potential canonical channels induces the translation and synaptic incorporation of GluA1-containing calcium-permeable AMPA receptors. J. Neurosci. 2012, 32:8127-8137.
    • (2012) J. Neurosci. , vol.32 , pp. 8127-8137
    • Fortin, D.A.1
  • 88
    • 33749038646 scopus 로고    scopus 로고
    • Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission
    • Fukata Y., et al. Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission. Science 2006, 313:1792-1795.
    • (2006) Science , vol.313 , pp. 1792-1795
    • Fukata, Y.1
  • 89
    • 77952475331 scopus 로고    scopus 로고
    • LGI1 is a Nogo receptor 1 ligand that antagonizes myelin-based growth inhibition
    • Thomas R., et al. LGI1 is a Nogo receptor 1 ligand that antagonizes myelin-based growth inhibition. J. Neurosci. 2010, 30:6607-6612.
    • (2010) J. Neurosci. , vol.30 , pp. 6607-6612
    • Thomas, R.1
  • 90
    • 5644289669 scopus 로고    scopus 로고
    • Zinc metalloproteinase-mediated cleavage of the human Nogo66 receptor
    • Walmsley A.R., et al. Zinc metalloproteinase-mediated cleavage of the human Nogo66 receptor. J. Cell Sci. 2004, 117:4591-4602.
    • (2004) J. Cell Sci. , vol.117 , pp. 4591-4602
    • Walmsley, A.R.1
  • 91
    • 80052400914 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinase-3 regulates neuronal responsiveness to myelin through Nogo66 receptor 1 cleavage
    • Ferraro G.B., et al. Membrane-type matrix metalloproteinase-3 regulates neuronal responsiveness to myelin through Nogo66 receptor 1 cleavage. J. Biol. Chem. 2011, 286:31418-31424.
    • (2011) J. Biol. Chem. , vol.286 , pp. 31418-31424
    • Ferraro, G.B.1
  • 92
    • 0037361917 scopus 로고    scopus 로고
    • Activity-induced and developmental downregulation of the Nogo receptor
    • Josephson A., et al. Activity-induced and developmental downregulation of the Nogo receptor. Cell Tissue Res. 2003, 311:333-342.
    • (2003) Cell Tissue Res. , vol.311 , pp. 333-342
    • Josephson, A.1
  • 93
    • 37749015642 scopus 로고    scopus 로고
    • Exercise normalizes levels of MAG and Nogo-A growth inhibitors after brain trauma
    • Chytrova G., et al. Exercise normalizes levels of MAG and Nogo-A growth inhibitors after brain trauma. Eur. J. Neurosci. 2008, 27:1-11.
    • (2008) Eur. J. Neurosci. , vol.27 , pp. 1-11
    • Chytrova, G.1
  • 94
    • 69049114964 scopus 로고    scopus 로고
    • Exercise-induced improvement in cognitive performance after traumatic brain injury in rats is dependent on BDNF activation
    • Griesbach G.S., et al. Exercise-induced improvement in cognitive performance after traumatic brain injury in rats is dependent on BDNF activation. Brain Res. 2009, 1288:105-115.
    • (2009) Brain Res. , vol.1288 , pp. 105-115
    • Griesbach, G.S.1
  • 95
    • 0343329765 scopus 로고    scopus 로고
    • Physical exercise induces FGF-2 and its mRNA in the hippocampus
    • Gomez-Pinilla F., et al. Physical exercise induces FGF-2 and its mRNA in the hippocampus. Brain Res. 1997, 764:1-8.
    • (1997) Brain Res. , vol.764 , pp. 1-8
    • Gomez-Pinilla, F.1
  • 96
    • 69449093524 scopus 로고    scopus 로고
    • Chondroitinase ABC treatment opens a window of opportunity for task-specific rehabilitation
    • Garcia-Alias G., et al. Chondroitinase ABC treatment opens a window of opportunity for task-specific rehabilitation. Nat. Neurosci. 2009, 12:1145-1151.
    • (2009) Nat. Neurosci. , vol.12 , pp. 1145-1151
    • Garcia-Alias, G.1
  • 97
    • 84856525430 scopus 로고    scopus 로고
    • NOGO66 receptor deficient mice show slow acquisition of spatial memory task performance
    • Van Gaalen M.M., et al. NOGO66 receptor deficient mice show slow acquisition of spatial memory task performance. Neurosci. Lett. 2012, 510:58-61.
    • (2012) Neurosci. Lett. , vol.510 , pp. 58-61
    • Van Gaalen, M.M.1
  • 98
    • 73949151869 scopus 로고    scopus 로고
    • Nogo receptor 1 regulates formation of lasting memories
    • Karlen A., et al. Nogo receptor 1 regulates formation of lasting memories. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:20476-20481.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20476-20481
    • Karlen, A.1
  • 99
    • 69949184925 scopus 로고    scopus 로고
    • Perineuronal nets protect fear memories from erasure
    • Gogolla N., et al. Perineuronal nets protect fear memories from erasure. Science 2009, 325:1258-1261.
    • (2009) Science , vol.325 , pp. 1258-1261
    • Gogolla, N.1
  • 100
    • 58149376506 scopus 로고    scopus 로고
    • Genetic variants of Nogo66 receptor with possible association to schizophrenia block myelin inhibition of axon growth
    • Budel S., et al. Genetic variants of Nogo66 receptor with possible association to schizophrenia block myelin inhibition of axon growth. J. Neurosci. 2008, 28:13161-13172.
    • (2008) J. Neurosci. , vol.28 , pp. 13161-13172
    • Budel, S.1
  • 101
    • 84876333883 scopus 로고    scopus 로고
    • Nogo and Nogo receptor: relevance to schizophrenia?
    • Willi R., Schwab M.E. Nogo and Nogo receptor: relevance to schizophrenia?. Neurobiol. Dis. 2013, 10.1016/j.nbd.2013.01.011.
    • (2013) Neurobiol. Dis.
    • Willi, R.1    Schwab, M.E.2
  • 102
    • 55049092546 scopus 로고    scopus 로고
    • Chondroitin-4-sulfation negatively regulates axonal guidance and growth
    • Wang H., et al. Chondroitin-4-sulfation negatively regulates axonal guidance and growth. J. Cell Sci. 2008, 121:3083-3091.
    • (2008) J. Cell Sci. , vol.121 , pp. 3083-3091
    • Wang, H.1
  • 103
    • 84861416926 scopus 로고    scopus 로고
    • Mouse development is not obviously affected by the absence of dermatan sulfate epimerase 2 in spite of a modified brain dermatan sulfate composition
    • Bartolini B., et al. Mouse development is not obviously affected by the absence of dermatan sulfate epimerase 2 in spite of a modified brain dermatan sulfate composition. Glycobiology 2012, 22:1007-1016.
    • (2012) Glycobiology , vol.22 , pp. 1007-1016
    • Bartolini, B.1
  • 104
    • 84874704840 scopus 로고    scopus 로고
    • Roles of chondroitin sulfate and dermatan sulfate in the formation of a lesion scar and axonal regeneration after traumatic injury of the mouse brain
    • Li H.P., et al. Roles of chondroitin sulfate and dermatan sulfate in the formation of a lesion scar and axonal regeneration after traumatic injury of the mouse brain. J. Neurotrauma 2013, 30:413-425.
    • (2013) J. Neurotrauma , vol.30 , pp. 413-425
    • Li, H.P.1
  • 105
    • 47749132343 scopus 로고    scopus 로고
    • Ganglioside inhibition of neurite outgrowth requires Nogo receptor function: identification of interaction sites and development of novel antagonists
    • Williams G., et al. Ganglioside inhibition of neurite outgrowth requires Nogo receptor function: identification of interaction sites and development of novel antagonists. J. Biol. Chem. 2008, 283:16641-16652.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16641-16652
    • Williams, G.1
  • 106
    • 32544432829 scopus 로고    scopus 로고
    • Alzheimer precursor protein interaction with the Nogo66 receptor reduces amyloid-beta plaque deposition
    • Park J.H., et al. Alzheimer precursor protein interaction with the Nogo66 receptor reduces amyloid-beta plaque deposition. J. Neurosci. 2006, 26:1386-1395.
    • (2006) J. Neurosci. , vol.26 , pp. 1386-1395
    • Park, J.H.1
  • 107
    • 66049091564 scopus 로고    scopus 로고
    • Identification of BLyS (B lymphocyte stimulator), a non-myelin-associated protein, as a functional ligand for Nogo66 receptor
    • Zhang L., et al. Identification of BLyS (B lymphocyte stimulator), a non-myelin-associated protein, as a functional ligand for Nogo66 receptor. J. Neurosci. 2009, 29:6348-6352.
    • (2009) J. Neurosci. , vol.29 , pp. 6348-6352
    • Zhang, L.1
  • 108
    • 79961234695 scopus 로고    scopus 로고
    • Cartilage acidic protein-1B (LOTUS), an endogenous Nogo receptor antagonist for axon tract formation
    • Sato Y., et al. Cartilage acidic protein-1B (LOTUS), an endogenous Nogo receptor antagonist for axon tract formation. Science 2011, 333:769-773.
    • (2011) Science , vol.333 , pp. 769-773
    • Sato, Y.1
  • 109
    • 84868256872 scopus 로고    scopus 로고
    • Olfactomedin 1 interacts with the Nogo A receptor complex to regulate axon growth
    • Nakaya N., et al. Olfactomedin 1 interacts with the Nogo A receptor complex to regulate axon growth. J. Biol. Chem. 2012, 287:37171-37184.
    • (2012) J. Biol. Chem. , vol.287 , pp. 37171-37184
    • Nakaya, N.1
  • 110
    • 80052678347 scopus 로고    scopus 로고
    • Interaction between amyloid precursor protein and Nogo receptors regulates amyloid deposition
    • Zhou X., et al. Interaction between amyloid precursor protein and Nogo receptors regulates amyloid deposition. FASEB J. 2011, 25:3146-3156.
    • (2011) FASEB J. , vol.25 , pp. 3146-3156
    • Zhou, X.1
  • 111
    • 84876231872 scopus 로고    scopus 로고
    • Synthetic microRNA-mediated downregulation of Nogo-A in transgenic rats reveals its role as regulator of synaptic plasticity and cognitive function
    • Tews B., et al. Synthetic microRNA-mediated downregulation of Nogo-A in transgenic rats reveals its role as regulator of synaptic plasticity and cognitive function. Proc Natl Acad Sci U S A 2013, 110:6583-6588.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 6583-6588
    • Tews, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.