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Volumn 289, Issue 42, 2014, Pages 29350-29364

A combined transgenic proteomic analysis and regulated trafficking of neuroligin-2

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; BRAIN; CELL ADHESION; CELL MEMBRANES; MACHINERY; MAMMALS; MASS SPECTROMETRY; MOLECULAR BIOLOGY; PROTEINS; PURIFICATION;

EID: 84908110073     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.549279     Document Type: Article
Times cited : (35)

References (74)
  • 1
    • 0034721678 scopus 로고    scopus 로고
    • Signal-processing machines at the postsynaptic density
    • Kennedy, M. B. (2000) Signal-processing machines at the postsynaptic density. Science 290, 750-754
    • (2000) Science , vol.290 , pp. 750-754
    • Kennedy, M.B.1
  • 2
    • 34548436564 scopus 로고    scopus 로고
    • Sheng, M., and Hoogenraad, C. C. (2007) The postsynaptic architecture of excitatory synapses: a more quantitative view. Annu. Rev. Biochem. 76, 823-847
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 823-847
    • Sheng, M.1    Hoogenraad, C.C.2
  • 3
    • 0033946468 scopus 로고    scopus 로고
    • Proteomic analysis of NMDA receptor-adhesion protein signaling complexes
    • Husi, H., Ward, M. A., Choudhary, J. S., Blackstock, W. P., and Grant, S. G. (2000) Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat. Neurosci. 3, 661-669
    • (2000) Nat. Neurosci. , vol.3 , pp. 661-669
    • Husi, H.1    Ward, M.A.2    Choudhary, J.S.3    Blackstock, W.P.4    Grant, S.G.5
  • 5
  • 6
    • 69249089272 scopus 로고    scopus 로고
    • Neuroproteomics: Understanding the molecular organization and complexity of the brain
    • Bayés, A., and Grant, S. G. (2009) Neuroproteomics: understanding the molecular organization and complexity of the brain. Nat. Rev. Neurosci. 10, 635-646
    • (2009) Nat. Rev. Neurosci. , vol.10 , pp. 635-646
    • Bayés, A.1    Grant, S.G.2
  • 7
    • 79955652877 scopus 로고    scopus 로고
    • GABAA receptor trafficking- mediated plasticity of inhibitory synapses
    • Luscher, B., Fuchs, T., and Kilpatrick, C. L. (2011) GABAA receptor trafficking- mediated plasticity of inhibitory synapses. Neuron 70, 385-409
    • (2011) Neuron , vol.70 , pp. 385-409
    • Luscher, B.1    Fuchs, T.2    Kilpatrick, C.L.3
  • 8
    • 79960090565 scopus 로고    scopus 로고
    • The dynamic modulation of GABA(A) receptor trafficking and its role in regulating the plasticity of inhibitory synapses
    • Vithlani, M., Terunuma, M., and Moss, S. J. (2011) The dynamic modulation of GABA(A) receptor trafficking and its role in regulating the plasticity of inhibitory synapses. Physiol. Rev. 91, 1009-1022
    • (2011) Physiol. Rev. , vol.91 , pp. 1009-1022
    • Vithlani, M.1    Terunuma, M.2    Moss, S.J.3
  • 9
    • 0042490506 scopus 로고    scopus 로고
    • Colocalization of multiple GABA(A) receptor subtypes with gephyrin at postsynaptic sites
    • Sassoè-Pognetto, M., Panzanelli, P., Sieghart, W., and Fritschy, J. M. (2000) Colocalization of multiple GABA(A) receptor subtypes with gephyrin at postsynaptic sites. J. Comp. Neurol. 420, 481-498
    • (2000) J. Comp. Neurol. , vol.420 , pp. 481-498
    • Sassoè-Pognetto, M.1    Panzanelli, P.2    Sieghart, W.3    Fritschy, J.M.4
  • 10
    • 7244232730 scopus 로고    scopus 로고
    • Neuroligin 2 is exclusively localized to inhibitory synapses
    • Varoqueaux, F., Jamain, S., and Brose, N. (2004) Neuroligin 2 is exclusively localized to inhibitory synapses. Eur. J. Cell Biol. 83, 449-456
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 449-456
    • Varoqueaux, F.1    Jamain, S.2    Brose, N.3
  • 12
    • 11144352245 scopus 로고    scopus 로고
    • Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins
    • Graf, E. R., Zhang, X., Jin, S. X., Linhoff, M. W., and Craig, A. M. (2004) Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins. Cell 119, 1013-1026
    • (2004) Cell , vol.119 , pp. 1013-1026
    • Graf, E.R.1    Zhang, X.2    Jin, S.X.3    Linhoff, M.W.4    Craig, A.M.5
  • 14
    • 65549084943 scopus 로고    scopus 로고
    • Inhibitory postsynaptic membrane specializations are formed in gephyrin-deficient mice
    • O'Sullivan, G. A., Hofer, W., and Betz, H. (2009) Inhibitory postsynaptic membrane specializations are formed in gephyrin-deficient mice. Neurosci. Lett. 458, 106-110
    • (2009) Neurosci. Lett. , vol.458 , pp. 106-110
    • O'sullivan, G.A.1    Hofer, W.2    Betz, H.3
  • 17
    • 84880329347 scopus 로고    scopus 로고
    • Developmental delays and reduced pup ultrasonic vocalizations but normal sociability in mice lacking the postsynaptic cell adhesion protein neuroligin2
    • Wöhr, M., Silverman, J. L., Scattoni, M. L., Turner, S. M., Harris, M. J., Saxena, R., and Crawley, J. N. (2013) Developmental delays and reduced pup ultrasonic vocalizations but normal sociability in mice lacking the postsynaptic cell adhesion protein neuroligin2. Behav. Brain Res. 251, 50-64
    • (2013) Behav. Brain Res. , vol.251 , pp. 50-64
    • Wöhr, M.1    Silverman, J.L.2    Scattoni, M.L.3    Turner, S.M.4    Harris, M.J.5    Saxena, R.6    Crawley, J.N.7
  • 19
    • 84874387968 scopus 로고    scopus 로고
    • Interaction between autism-linked MDGAs and neuroligins suppresses inhibitory synapse development
    • Pettem, K. L., Yokomaku, D., Takahashi, H., Ge, Y., and Craig, A. M. (2013) Interaction between autism-linked MDGAs and neuroligins suppresses inhibitory synapse development. J. Cell Biol. 200, 321-336
    • (2013) J. Cell Biol. , vol.200 , pp. 321-336
    • Pettem, K.L.1    Yokomaku, D.2    Takahashi, H.3    Ge, Y.4    Craig, A.M.5
  • 20
    • 77955930508 scopus 로고    scopus 로고
    • Interaction proteomics: Characterization of protein complexes using tandem affinity purificationmass spectrometry
    • Völkel, P., Le Faou, P., and Angrand, P. O. (2010) Interaction proteomics: characterization of protein complexes using tandem affinity purificationmass spectrometry. Biochem. Soc. Trans. 38, 883-887
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 883-887
    • Völkel, P.1    Le Faou, P.2    Angrand, P.O.3
  • 21
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., and Séraphin, B. (1999) A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030-1032
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Séraphin, B.6
  • 24
    • 80052027753 scopus 로고    scopus 로고
    • Coordinated increase in inhibitory and excitatory synapses onto retinal ganglion cells during development
    • Soto, F., Bleckert, A., Lewis, R., Kang, Y., Kerschensteiner, D., Craig, A. M., and Wong, R. O. (2011) Coordinated increase in inhibitory and excitatory synapses onto retinal ganglion cells during development. Neural. Dev. 6, 31
    • (2011) Neural. Dev. , vol.6 , pp. 31
    • Soto, F.1    Bleckert, A.2    Lewis, R.3    Kang, Y.4    Kerschensteiner, D.5    Craig, A.M.6    Wong, R.O.7
  • 25
    • 34548864370 scopus 로고    scopus 로고
    • Culturing hippocampal neurons
    • Kaech, S., and Banker, G. (2006) Culturing hippocampal neurons. Nat. Protoc. 1, 2406-2415
    • (2006) Nat. Protoc. , vol.1 , pp. 2406-2415
    • Kaech, S.1    Banker, G.2
  • 26
    • 0034625250 scopus 로고    scopus 로고
    • Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons
    • Scheiffele, P., Fan, J., Choih, J., Fetter, R., and Serafini, T. (2000) Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons. Cell 101, 657-669
    • (2000) Cell , vol.101 , pp. 657-669
    • Scheiffele, P.1    Fan, J.2    Choih, J.3    Fetter, R.4    Serafini, T.5
  • 27
    • 77953206739 scopus 로고    scopus 로고
    • LRRTMs and neuroligins bind neurexins with a differential code to cooperate in glutamate synapse development
    • Siddiqui, T. J., Pancaroglu, R., Kang, Y., Rooyakkers, A., and Craig, A. M. (2010) LRRTMs and neuroligins bind neurexins with a differential code to cooperate in glutamate synapse development. J. Neurosci. 30, 7495-7506
    • (2010) J. Neurosci. , vol.30 , pp. 7495-7506
    • Siddiqui, T.J.1    Pancaroglu, R.2    Kang, Y.3    Rooyakkers, A.4    Craig, A.M.5
  • 28
    • 33646464124 scopus 로고    scopus 로고
    • Structure function and splice site analysis of the synaptogenic activity of the neurexin- 1 beta LNS domain
    • Graf, E. R., Kang, Y., Hauner, A. M., and Craig, A. M. (2006) Structure function and splice site analysis of the synaptogenic activity of the neurexin- 1 beta LNS domain. J. Neurosci. 26, 4256-4265
    • (2006) J. Neurosci. , vol.26 , pp. 4256-4265
    • Graf, E.R.1    Kang, Y.2    Hauner, A.M.3    Craig, A.M.4
  • 30
    • 33845973020 scopus 로고    scopus 로고
    • Quantitative comparison of caste differences in honeybee hemolymph
    • Chan, Q. W., Howes, C. G., and Foster, L. J. (2006) Quantitative comparison of caste differences in honeybee hemolymph. Mol. Cell Proteomics 5, 2252-2262
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 2252-2262
    • Chan, Q.W.1    Howes, C.G.2    Foster, L.J.3
  • 31
    • 0037032628 scopus 로고    scopus 로고
    • Microcolumns with self-assembled particle frits for proteomics
    • Ishihama, Y., Rappsilber, J., Andersen, J. S., and Mann, M. (2002) Microcolumns with self-assembled particle frits for proteomics. J. Chromatogr. A 979, 233-239
    • (2002) J. Chromatogr. A , vol.979 , pp. 233-239
    • Ishihama, Y.1    Rappsilber, J.2    Andersen, J.S.3    Mann, M.4
  • 32
    • 27944474776 scopus 로고    scopus 로고
    • ErmineJ: Tool for functional analysis of gene expression data sets
    • Lee, H. K., Braynen, W., Keshav, K., and Pavlidis, P. (2005) ErmineJ: tool for functional analysis of gene expression data sets.BMCBioinformatics 6, 269
    • (2005) BMCBioinformatics , vol.6 , pp. 269
    • Lee, H.K.1    Braynen, W.2    Keshav, K.3    Pavlidis, P.4
  • 33
    • 84863445395 scopus 로고    scopus 로고
    • The role of neurexins and neuroligins in the formation, maturation, and function of vertebrate synapses
    • Krueger, D. D., Tuffy, L. P., Papadopoulos, T., and Brose, N. (2012) The role of neurexins and neuroligins in the formation, maturation, and function of vertebrate synapses. Curr. Opin. Neurobiol. 22, 412-422
    • (2012) Curr. Opin. Neurobiol. , vol.22 , pp. 412-422
    • Krueger, D.D.1    Tuffy, L.P.2    Papadopoulos, T.3    Brose, N.4
  • 35
    • 33846867244 scopus 로고    scopus 로고
    • Neurexin-neuroligin signaling in synapse development
    • Craig, A. M., and Kang, Y. (2007) Neurexin-neuroligin signaling in synapse development. Curr. Opin. Neurobiol. 17, 43-52
    • (2007) Curr. Opin. Neurobiol. , vol.17 , pp. 43-52
    • Craig, A.M.1    Kang, Y.2
  • 37
    • 33244459814 scopus 로고    scopus 로고
    • Dynamic remodeling of dendritic arbors in GABAergic interneurons of adult visual cortex
    • Lee, W. C., Huang, H., Feng, G., Sanes, J. R., Brown, E. N., So, P. T., and Nedivi, E. (2006) Dynamic remodeling of dendritic arbors in GABAergic interneurons of adult visual cortex. PLoS Biol. 4, e29
    • (2006) PLoS Biol. , vol.4 , pp. e29
    • Lee, W.C.1    Huang, H.2    Feng, G.3    Sanes, J.R.4    Brown, E.N.5    So, P.T.6    Nedivi, E.7
  • 38
    • 46849083268 scopus 로고    scopus 로고
    • Neuronal diversity and temporal dynamics: The unity of hippocampal circuit operations
    • Klausberger, T., and Somogyi, P. (2008) Neuronal diversity and temporal dynamics: the unity of hippocampal circuit operations. Science 321, 53-57
    • (2008) Science , vol.321 , pp. 53-57
    • Klausberger, T.1    Somogyi, P.2
  • 39
    • 84864353034 scopus 로고    scopus 로고
    • Molecular and functional heterogeneity of GABAergic synapses
    • Fritschy, J. M., Panzanelli, P., and Tyagarajan, S. K. (2012) Molecular and functional heterogeneity of GABAergic synapses. Cell Mol. Life Sci. 69, 2485-2499
    • (2012) Cell Mol. Life Sci. , vol.69 , pp. 2485-2499
    • Fritschy, J.M.1    Panzanelli, P.2    Tyagarajan, S.K.3
  • 40
    • 0022595736 scopus 로고
    • Alkyl glycoside detergents: Synthesis and applications to the study of membrane proteins
    • VanAken, T., Foxall-VanAken, S., Castleman, S., and Ferguson-Miller, S. (1986) Alkyl glycoside detergents: synthesis and applications to the study of membrane proteins. Methods Enzymol. 125, 27-35
    • (1986) Methods Enzymol. , vol.125 , pp. 27-35
    • Vanaken, T.1    Foxall-Vanaken, S.2    Castleman, S.3    Ferguson-Miller, S.4
  • 42
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • McMahon, H. T., and Boucrot, E. (2011) Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 12, 517-533
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 517-533
    • McMahon, H.T.1    Boucrot, E.2
  • 44
    • 0041327729 scopus 로고    scopus 로고
    • Myosin VI: Two distinct roles in endocytosis
    • Hasson, T. (2003) Myosin VI: two distinct roles in endocytosis. J. Cell Sci. 116, 3453-3461
    • (2003) J. Cell Sci. , vol.116 , pp. 3453-3461
    • Hasson, T.1
  • 45
    • 84872183810 scopus 로고    scopus 로고
    • The retromer complex: Endosomal protein recycling and beyond
    • Seaman, M. N. (2012) The retromer complex: endosomal protein recycling and beyond. J. Cell Sci. 125, 4693-4702
    • (2012) J. Cell Sci. , vol.125 , pp. 4693-4702
    • Seaman, M.N.1
  • 46
    • 84880078204 scopus 로고    scopus 로고
    • In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10 (zDHHC1/3/11)- mediated neurochondrin palmitoylation in its targeting to Rab5-positive endosomes
    • Oku, S., Takahashi, N., Fukata, Y., and Fukata, M. (2013) In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10 (zDHHC1/3/11)- mediated neurochondrin palmitoylation in its targeting to Rab5-positive endosomes. J. Biol. Chem. 288, 19816-19829
    • (2013) J. Biol. Chem. , vol.288 , pp. 19816-19829
    • Oku, S.1    Takahashi, N.2    Fukata, Y.3    Fukata, M.4
  • 48
    • 84901988137 scopus 로고    scopus 로고
    • Membrane-associated cargo recycling by tubule-based endosomal sorting
    • van Weering, J. R., and Cullen, P. J. (2014) Membrane-associated cargo recycling by tubule-based endosomal sorting. Semin. Cell Dev. Biol. 31, 40-47
    • (2014) Semin. Cell Dev. Biol. , vol.31 , pp. 40-47
    • Van Weering, J.R.1    Cullen, P.J.2
  • 50
    • 34848892693 scopus 로고    scopus 로고
    • Neuroligin-3 is a neuronal adhesion protein at GABAergic and glutamatergic synapses
    • Budreck, E. C., and Scheiffele, P. (2007) Neuroligin-3 is a neuronal adhesion protein at GABAergic and glutamatergic synapses. Eur. J. Neurosci. 26, 1738-1748
    • (2007) Eur. J. Neurosci. , vol.26 , pp. 1738-1748
    • Budreck, E.C.1    Scheiffele, P.2
  • 53
    • 0033514448 scopus 로고    scopus 로고
    • Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses
    • Song, J. Y., Ichtchenko, K., Südhof, T. C., and Brose, N. (1999) Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses. Proc. Natl. Acad. Sci. U.S.A. 96, 1100-1105
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1100-1105
    • Song, J.Y.1    Ichtchenko, K.2    Südhof, T.C.3    Brose, N.4
  • 55
    • 0038178996 scopus 로고    scopus 로고
    • GABA-A receptor subtypes in the brain: A paradigm for CNS drug discovery?
    • Whiting, P. J. (2003) GABA-A receptor subtypes in the brain: a paradigm for CNS drug discovery? Drug Discov. Today 8, 445-450
    • (2003) Drug Discov. Today , vol.8 , pp. 445-450
    • Whiting, P.J.1
  • 57
    • 79959916248 scopus 로고    scopus 로고
    • The cell adhesion molecule neurofascin stabilizes axoaxonic GABAergic terminals at the axon initial segment
    • Kriebel, M., Metzger, J., Trinks, S., Chugh, D., Harvey, R. J., Harvey, K., and Volkmer, H. (2011) The cell adhesion molecule neurofascin stabilizes axoaxonic GABAergic terminals at the axon initial segment. J. Biol. Chem. 286, 24385-24393
    • (2011) J. Biol. Chem. , vol.286 , pp. 24385-24393
    • Kriebel, M.1    Metzger, J.2    Trinks, S.3    Chugh, D.4    Harvey, R.J.5    Harvey, K.6    Volkmer, H.7
  • 58
    • 84861534003 scopus 로고    scopus 로고
    • Adistal axonal cytoskeleton forms an intra-axonal boundary that controls axon initial segment assembly
    • Galiano, M. R., Jha, S., Ho, T. S., Zhang, C., Ogawa, Y., Chang, K. J., Stankewich, M. C., Mohler, P. J., and Rasband, M. N. (2012)Adistal axonal cytoskeleton forms an intra-axonal boundary that controls axon initial segment assembly. Cell 149, 1125-1139
    • (2012) Cell , vol.149 , pp. 1125-1139
    • Galiano, M.R.1    Jha, S.2    Ho, T.S.3    Zhang, C.4    Ogawa, Y.5    Chang, K.J.6    Stankewich, M.C.7    Mohler, P.J.8    Rasband, M.N.9
  • 59
    • 84870062364 scopus 로고    scopus 로고
    • The perineuronal net component of the extracellular matrix in plasticity and epilepsy
    • McRae, P. A., and Porter, B. E. (2012) The perineuronal net component of the extracellular matrix in plasticity and epilepsy. Neurochem. Int. 61, 963-972
    • (2012) Neurochem. Int. , vol.61 , pp. 963-972
    • McRae, P.A.1    Porter, B.E.2
  • 60
    • 0035155083 scopus 로고    scopus 로고
    • Reduced perisomatic inhibition, increased excitatory transmission, and impaired long-term potentiation in mice deficient for the extracellular matrix glycoprotein tenascin-R
    • Saghatelyan, A. K., Dityatev, A., Schmidt, S., Schuster, T., Bartsch, U., and Schachner, M. (2001) Reduced perisomatic inhibition, increased excitatory transmission, and impaired long-term potentiation in mice deficient for the extracellular matrix glycoprotein tenascin-R. Mol. Cell Neurosci. 17, 226-240
    • (2001) Mol. Cell Neurosci. , vol.17 , pp. 226-240
    • Saghatelyan, A.K.1    Dityatev, A.2    Schmidt, S.3    Schuster, T.4    Bartsch, U.5    Schachner, M.6
  • 61
    • 0037450354 scopus 로고    scopus 로고
    • Tenascin-R-deficient mice show structural alterations of symmetric perisomatic synapses in the CA1 region of the hippocampus
    • Nikonenko, A., Schmidt, S., Skibo, G., Brückner, G., and Schachner, M. (2003) Tenascin-R-deficient mice show structural alterations of symmetric perisomatic synapses in the CA1 region of the hippocampus. J. Comp. Neurol. 456, 338-349
    • (2003) J. Comp. Neurol. , vol.456 , pp. 338-349
    • Nikonenko, A.1    Schmidt, S.2    Skibo, G.3    Brückner, G.4    Schachner, M.5
  • 62
    • 0027292233 scopus 로고
    • Neurexin III α: Extensive alternative splicing generates membrane-bound and soluble forms
    • Ushkaryov, Y. A., and Südhof, T. C. (1993) Neurexin III α: extensive alternative splicing generates membrane-bound and soluble forms. Proc. Natl. Acad. Sci. U.S.A. 90, 6410-6414
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6410-6414
    • Ushkaryov, Y.A.1    Südhof, T.C.2
  • 63
    • 78951488794 scopus 로고    scopus 로고
    • Processing of the synaptic cell adhesion molecule neurexin-3β by Alzheimer disease α- And γ-secretases
    • Bot, N., Schweizer, C., Ben Halima, S., and Fraering, P. C. (2011) Processing of the synaptic cell adhesion molecule neurexin-3β by Alzheimer disease α- and γ-secretases. J. Biol. Chem. 286, 2762-2773
    • (2011) J. Biol. Chem. , vol.286 , pp. 2762-2773
    • Bot, N.1    Schweizer, C.2    Ben Halima, S.3    Fraering, P.C.4
  • 64
    • 79955761820 scopus 로고    scopus 로고
    • Presenilin/ γ- Secretase regulates neurexin processing at synapses
    • Saura, C. A., Servián-Morilla, E., and Scholl, F. G. (2011) Presenilin/ γ- secretase regulates neurexin processing at synapses. PLoS One 6, e19430
    • (2011) PLoS One , vol.6 , pp. e19430
    • Saura, C.A.1    Servián-Morilla, E.2    Scholl, F.G.3
  • 69
    • 0033258164 scopus 로고    scopus 로고
    • Short communication: Altered synaptic clustering of GABAA receptors in mice lacking dystrophin (mdx mice)
    • Knuesel, I., Mastrocola, M., Zuellig, R. A., Bornhauser, B., Schaub, M. C., and Fritschy, J. M. (1999) Short communication: altered synaptic clustering of GABAA receptors in mice lacking dystrophin (mdx mice). Eur. J. Neurosci. 11, 4457-4462
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 4457-4462
    • Knuesel, I.1    Mastrocola, M.2    Zuellig, R.A.3    Bornhauser, B.4    Schaub, M.C.5    Fritschy, J.M.6
  • 72
    • 84860274120 scopus 로고    scopus 로고
    • Clustered dynamics of inhibitory synapses and dendritic spines in the adult neocortex
    • Chen, J. L., Villa, K. L., Cha, J. W., So, P. T., Kubota, Y., and Nedivi, E. (2012) Clustered dynamics of inhibitory synapses and dendritic spines in the adult neocortex. Neuron 74, 361-373
    • (2012) Neuron , vol.74 , pp. 361-373
    • Chen, J.L.1    Villa, K.L.2    Cha, J.W.3    So, P.T.4    Kubota, Y.5    Nedivi, E.6
  • 73
    • 84888863551 scopus 로고    scopus 로고
    • Light microscopy mapping of connections in the intact brain
    • Kim, S. Y., Chung, K., and Deisseroth, K. (2013) Light microscopy mapping of connections in the intact brain. Trends Cogn. Sci. 17, 596-599
    • (2013) Trends Cogn. Sci. , vol.17 , pp. 596-599
    • Kim, S.Y.1    Chung, K.2    Deisseroth, K.3
  • 74
    • 78751694593 scopus 로고    scopus 로고
    • Postsynaptic TrkC and presynaptic PTPsigma function as a bidirectional excitatory synaptic organizing complex
    • Takahashi, H., Arstikaitis, P., Prasad, T., Bartlett, T. E., Wang, Y. T., Murphy, T. H., and Craig, A. M. (2011) Postsynaptic TrkC and presynaptic PTPsigma function as a bidirectional excitatory synaptic organizing complex. Neuron 69, 287-303
    • (2011) Neuron , vol.69 , pp. 287-303
    • Takahashi, H.1    Arstikaitis, P.2    Prasad, T.3    Bartlett, T.E.4    Wang, Y.T.5    Murphy, T.H.6    Craig, A.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.