메뉴 건너뛰기




Volumn 14, Issue 9, 2013, Pages

Neurexins

Author keywords

[No Author keywords available]

Indexed keywords

NEUREXIN; NEUROLIGIN; CEREBELLIN; ISOPROTEIN; LRRTM1 PROTEIN, HUMAN; MEMBRANE PROTEIN; NERVE CELL ADHESION MOLECULE; NERVE PROTEIN; NEUREXIN IBETA; NEUROLIGIN 1; NRXN1 PROTEIN, HUMAN;

EID: 84884691301     PISSN: 14747596     EISSN: 1474760X     Source Type: Journal    
DOI: 10.1186/gb-2013-14-9-213     Document Type: Article
Times cited : (157)

References (133)
  • 1
    • 0028969264 scopus 로고
    • Cartography of neurexins: more than 1000 isoforms generated by alternative splicing and expressed in distinct subsets of neurons
    • Ullrich B, Ushkaryov YA, Südhof TC: Cartography of neurexins: more than 1000 isoforms generated by alternative splicing and expressed in distinct subsets of neurons. Neuron 1995, 14:497-507.
    • (1995) Neuron , vol.14 , pp. 497-507
    • Ullrich, B.1    Ushkaryov, Y.A.2    Südhof, T.C.3
  • 2
    • 0028241554 scopus 로고
    • Conserved domain structure of beta-neurexins. Unusual cleaved signal sequences in receptor-like neuronal cell-surface proteins
    • Ushkaryov YA, Hata Y, Ichtchenko K, Moomaw C, Afendis S, Slaughter CA, Südhof TC: Conserved domain structure of beta-neurexins. Unusual cleaved signal sequences in receptor-like neuronal cell-surface proteins. J Biol Chem 1994, 269:11987-11992.
    • (1994) J Biol Chem , vol.269 , pp. 11987-11992
    • Ushkaryov, Y.A.1    Hata, Y.2    Ichtchenko, K.3    Moomaw, C.4    Afendis, S.5    Slaughter, C.A.6    Südhof, T.C.7
  • 3
    • 0026769035 scopus 로고
    • Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin
    • Ushkaryov YA, Petrenko AG, Geppert M, Südhof TC: Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin. Science 1992, 257:50-56.
    • (1992) Science , vol.257 , pp. 50-56
    • Ushkaryov, Y.A.1    Petrenko, A.G.2    Geppert, M.3    Südhof, T.C.4
  • 4
    • 70449686185 scopus 로고    scopus 로고
    • Mouse neurexin-1alpha deletion causes correlated electrophysiological and behavioral changes consistent with cognitive impairments
    • Etherton MR, Blaiss CA, Powell CM, Südhof TC: Mouse neurexin-1alpha deletion causes correlated electrophysiological and behavioral changes consistent with cognitive impairments. Proc Natl Acad Sci U S A 2009, 106:17998-18003.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 17998-18003
    • Etherton, M.R.1    Blaiss, C.A.2    Powell, C.M.3    Südhof, T.C.4
  • 9
    • 34250211762 scopus 로고    scopus 로고
    • Activity-dependent validation of excitatory versus inhibitory synapses by neuroligin-1 versus neuroligin-2
    • Chubykin AA, Atasoy D, Etherton MR, Brose N, Kavalali ET, Gibson JR, Südhof TC: Activity-dependent validation of excitatory versus inhibitory synapses by neuroligin-1 versus neuroligin-2. Neuron 2007, 54:919-931.
    • (2007) Neuron , vol.54 , pp. 919-931
    • Chubykin, A.A.1    Atasoy, D.2    Etherton, M.R.3    Brose, N.4    Kavalali, E.T.5    Gibson, J.R.6    Südhof, T.C.7
  • 11
    • 34247116555 scopus 로고    scopus 로고
    • Deletion of alpha-neurexins does not cause a major impairment of axonal pathfinding or synapse formation
    • Dudanova I, Tabuchi K, Rohlmann A, Südhof TC, Missler M: Deletion of alpha-neurexins does not cause a major impairment of axonal pathfinding or synapse formation. J Comp Neurol 2007, 502:261-274.
    • (2007) J Comp Neurol , vol.502 , pp. 261-274
    • Dudanova, I.1    Tabuchi, K.2    Rohlmann, A.3    Südhof, T.C.4    Missler, M.5
  • 12
    • 11144352245 scopus 로고    scopus 로고
    • Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins
    • Graf ER, Zhang X, Jin SX, Linhoff MW, Craig AM: Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins. Cell 2004, 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
  • 13
    • 17844363471 scopus 로고    scopus 로고
    • Postsynaptic assembly induced by neurexin-neuroligin interaction and neurotransmitter
    • Nam CI, Chen L: Postsynaptic assembly induced by neurexin-neuroligin interaction and neurotransmitter. Proc Natl Acad Sci U S A 2005, 102:6137-6142.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6137-6142
    • Nam, C.I.1    Chen, L.2
  • 14
    • 0034625250 scopus 로고    scopus 로고
    • Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons
    • Scheiffele P, Fan J, Choih J, Fetter R, Serafini T: Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons. Cell 2000, 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
  • 15
    • 26944444692 scopus 로고    scopus 로고
    • A splice code for trans-synaptic cell adhesion mediated by binding of neuroligin 1 to alpha-and beta-neurexins
    • Boucard AA, Chubykin AA, Comoletti D, Taylor P, Südhof TC: A splice code for trans-synaptic cell adhesion mediated by binding of neuroligin 1 to alpha-and beta-neurexins. Neuron 2005, 48:229-236.
    • (2005) Neuron , vol.48 , pp. 229-236
    • Boucard, A.A.1    Chubykin, A.A.2    Comoletti, D.3    Taylor, P.4    Südhof, T.C.5
  • 17
    • 0032567532 scopus 로고    scopus 로고
    • Neurexophilin binding to alphaneurexins. A single LNS domain functions as an independently folding ligand-binding unit
    • Missler M, Hammer RE, Südhof TC: Neurexophilin binding to alphaneurexins. A single LNS domain functions as an independently folding ligand-binding unit. J Biol Chem 1998, 273:34716-34723.
    • (1998) J Biol Chem , vol.273 , pp. 34716-34723
    • Missler, M.1    Hammer, R.E.2    Südhof, T.C.3
  • 18
    • 0344382111 scopus 로고    scopus 로고
    • Neurexophilins form a conserved family of neuropeptide-like glycoproteins
    • Missler M, Südhof TC: Neurexophilins form a conserved family of neuropeptide-like glycoproteins. J Neurosci 1998, 18:3630-3638.
    • (1998) J Neurosci , vol.18 , pp. 3630-3638
    • Missler, M.1    Südhof, T.C.2
  • 22
    • 72149130256 scopus 로고    scopus 로고
    • LRRTM2 functions as a neurexin ligand in promoting excitatory synapse formation
    • Ko J, Fuccillo MV, Malenka RC, Südhof TC: LRRTM2 functions as a neurexin ligand in promoting excitatory synapse formation. Neuron 2009, 64:791-798.
    • (2009) Neuron , vol.64 , pp. 791-798
    • Ko, J.1    Fuccillo, M.V.2    Malenka, R.C.3    Südhof, T.C.4
  • 23
    • 79954486224 scopus 로고    scopus 로고
    • Cbln family proteins promote synapse formation by regulating distinct neurexin signaling pathways in various brain regions
    • Matsuda K, Yuzaki M: Cbln family proteins promote synapse formation by regulating distinct neurexin signaling pathways in various brain regions. Eur J Neurosci 2011, 33:1447-1461.
    • (2011) Eur J Neurosci , vol.33 , pp. 1447-1461
    • Matsuda, K.1    Yuzaki, M.2
  • 24
    • 77953725365 scopus 로고    scopus 로고
    • Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum
    • Uemura T, Lee SJ, Yasumura M, Takeuchi T, Yoshida T, Ra M, Taguchi R, Sakimura K, Mishina M: Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum. Cell 2010, 141:1068-1079.
    • (2010) Cell , vol.141 , pp. 1068-1079
    • Uemura, T.1    Lee, S.J.2    Yasumura, M.3    Takeuchi, T.4    Yoshida, T.5    Ra, M.6    Taguchi, R.7    Sakimura, K.8    Mishina, M.9
  • 25
    • 54049091941 scopus 로고    scopus 로고
    • Neuroligins and neurexins link synaptic function to cognitive disease
    • Südhof TC: Neuroligins and neurexins link synaptic function to cognitive disease. Nature 2008, 455:903-911.
    • (2008) Nature , vol.455 , pp. 903-911
    • Südhof, T.C.1
  • 26
    • 67650750977 scopus 로고    scopus 로고
    • A synaptic trek to autism
    • Bourgeron T: A synaptic trek to autism. Curr Opin Neurobiol 2009, 19:231-234.
    • (2009) Curr Opin Neurobiol , vol.19 , pp. 231-234
    • Bourgeron, T.1
  • 27
    • 84856110031 scopus 로고    scopus 로고
    • The role of neurexins in schizophrenia and autistic spectrum disorder
    • Reichelt AC, Rodgers RJ, Clapcote SJ: The role of neurexins in schizophrenia and autistic spectrum disorder. Neuropharmacology 2012, 62:1519-1526.
    • (2012) Neuropharmacology , vol.62 , pp. 1519-1526
    • Reichelt, A.C.1    Rodgers, R.J.2    Clapcote, S.J.3
  • 28
    • 0027292233 scopus 로고
    • Neurexin III alpha: extensive alternative splicing generates membrane-bound and soluble forms
    • Ushkaryov YA, Südhof TC: Neurexin III alpha: extensive alternative splicing generates membrane-bound and soluble forms. Proc Natl Acad Sci U S A 1993, 90:6410-6414.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 6410-6414
    • Ushkaryov, Y.A.1    Südhof, T.C.2
  • 29
    • 0031983653 scopus 로고    scopus 로고
    • Neurexins: three genes and 1001 products
    • Missler M, Südhof TC: Neurexins: three genes and 1001 products. Trends Genet 1998, 14:20-26.
    • (1998) Trends Genet , vol.14 , pp. 20-26
    • Missler, M.1    Südhof, T.C.2
  • 30
    • 0036270811 scopus 로고    scopus 로고
    • Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing
    • Tabuchi K, Südhof TC: Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing. Genomics 2002, 79:849-859.
    • (2002) Genomics , vol.79 , pp. 849-859
    • Tabuchi, K.1    Südhof, T.C.2
  • 34
    • 33845884040 scopus 로고    scopus 로고
    • Comparative genome analysis of the neurexin gene family in Danio rerio: insights into their functions and evolution
    • Rissone A, Monopoli M, Beltrame M, Bussolino F, Cotelli F, Arese M: Comparative genome analysis of the neurexin gene family in Danio rerio: insights into their functions and evolution. Mol Biol Evol 2007, 24:236-252.
    • (2007) Mol Biol Evol , vol.24 , pp. 236-252
    • Rissone, A.1    Monopoli, M.2    Beltrame, M.3    Bussolino, F.4    Cotelli, F.5    Arese, M.6
  • 35
    • 34249059390 scopus 로고    scopus 로고
    • Neurexin-1 is required for synapse formation and larvae associative learning in Drosophila
    • Zeng X, Sun M, Liu L, Chen F, Wei L, Xie W: Neurexin-1 is required for synapse formation and larvae associative learning in Drosophila. FEBS Lett 2007, 581:2509-2516.
    • (2007) FEBS Lett , vol.581 , pp. 2509-2516
    • Zeng, X.1    Sun, M.2    Liu, L.3    Chen, F.4    Wei, L.5    Xie, W.6
  • 36
    • 77951120000 scopus 로고    scopus 로고
    • Alternative splicing and evolution: diversification, exon definition and function
    • Keren H, Lev-Maor G, Ast G: Alternative splicing and evolution: diversification, exon definition and function. Nat Rev Genet 2010, 11:345-355.
    • (2010) Nat Rev Genet , vol.11 , pp. 345-355
    • Keren, H.1    Lev-Maor, G.2    Ast, G.3
  • 39
  • 41
    • 37849021314 scopus 로고    scopus 로고
    • Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions
    • Chen X, Liu H, Shim AH, Focia PJ, He X: Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions. Nat Struct Mol Biol 2008, 15:50-56.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 50-56
    • Chen, X.1    Liu, H.2    Shim, A.H.3    Focia, P.J.4    He, X.5
  • 42
    • 37049028145 scopus 로고    scopus 로고
    • Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion
    • Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P: Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion. Neuron 2007, 56:979-991.
    • (2007) Neuron , vol.56 , pp. 979-991
    • Fabrichny, I.P.1    Leone, P.2    Sulzenbacher, G.3    Comoletti, D.4    Miller, M.T.5    Taylor, P.6    Bourne, Y.7    Marchot, P.8
  • 43
    • 0033215463 scopus 로고    scopus 로고
    • The structure of the ligand-binding domain of neurexin Ibeta: regulation of LNS domain function by alternative splicing
    • Rudenko G, Nguyen T, Chelliah Y, Südhof TC, Deisenhofer J: The structure of the ligand-binding domain of neurexin Ibeta: regulation of LNS domain function by alternative splicing. Cell 1999, 99:93-101.
    • (1999) Cell , vol.99 , pp. 93-101
    • Rudenko, G.1    Nguyen, T.2    Chelliah, Y.3    Südhof, T.C.4    Deisenhofer, J.5
  • 44
    • 0042736851 scopus 로고    scopus 로고
    • Distinct requirements for heparin and alpha-dystroglycan binding revealed by structure-based mutagenesis of the laminin alpha2 LG4-LG5 domain pair
    • Wizemann H, Garbe JH, Friedrich MV, Timpl R, Sasaki T, Hohenester E: Distinct requirements for heparin and alpha-dystroglycan binding revealed by structure-based mutagenesis of the laminin alpha2 LG4-LG5 domain pair. J Mol Biol 2003, 332:635-642.
    • (2003) J Mol Biol , vol.332 , pp. 635-642
    • Wizemann, H.1    Garbe, J.H.2    Friedrich, M.V.3    Timpl, R.4    Sasaki, T.5    Hohenester, E.6
  • 46
    • 54449086786 scopus 로고    scopus 로고
    • Mutational analysis of the neurexin/neuroligin complex reveals essential and regulatory components
    • Reissner C, Klose M, Fairless R, Missler M: Mutational analysis of the neurexin/neuroligin complex reveals essential and regulatory components. Proc Natl Acad Sci U S A 2008, 105:15124-15129.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15124-15129
    • Reissner, C.1    Klose, M.2    Fairless, R.3    Missler, M.4
  • 47
    • 84863011035 scopus 로고    scopus 로고
    • Calcium binding by synaptotagmin's C2A domain is an essential element of the electrostatic switch that triggers synchronous synaptic transmission
    • Striegel AR, Biela LM, Evans CS, Wang Z, Delehoy JB, Sutton RB, Chapman ER, Reist NE: Calcium binding by synaptotagmin's C2A domain is an essential element of the electrostatic switch that triggers synchronous synaptic transmission. J Neurosci 2012, 32:1253-1260.
    • (2012) J Neurosci , vol.32 , pp. 1253-1260
    • Striegel, A.R.1    Biela, L.M.2    Evans, C.S.3    Wang, Z.4    Delehoy, J.B.5    Sutton, R.B.6    Chapman, E.R.7    Reist, N.E.8
  • 48
    • 77953206739 scopus 로고    scopus 로고
    • LRRTMs and neuroligins bind neurexins with a differential code to cooperate in glutamate synapse development
    • Siddiqui TJ, Pancaroglu R, Kang Y, Rooyakkers A, Craig AM: LRRTMs and neuroligins bind neurexins with a differential code to cooperate in glutamate synapse development. J Neurosci 2010, 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
  • 49
    • 0030026657 scopus 로고    scopus 로고
    • Structures, alternative splicing, and neurexin binding of multiple neuroligins
    • Ichtchenko K, Nguyen T, Südhof TC: Structures, alternative splicing, and neurexin binding of multiple neuroligins. J Biol Chem 1996, 271:2676-2682.
    • (1996) J Biol Chem , vol.271 , pp. 2676-2682
    • Ichtchenko, K.1    Nguyen, T.2    Südhof, T.C.3
  • 50
    • 0035367894 scopus 로고    scopus 로고
    • Identification of a novel neuroligin in humans which binds to PSD-95 and has a widespread expression
    • Bolliger MF, Frei K, Winterhalter KH, Gloor SM: Identification of a novel neuroligin in humans which binds to PSD-95 and has a widespread expression. Biochem J 2001, 356:581-588.
    • (2001) Biochem J , vol.356 , pp. 581-588
    • Bolliger, M.F.1    Frei, K.2    Winterhalter, K.H.3    Gloor, S.M.4
  • 52
    • 14544275500 scopus 로고    scopus 로고
    • Neuroscience. Making synapses: a balancing act
    • Hussain NK, Sheng M: Neuroscience. Making synapses: a balancing act. Science 2005, 307:1207-1208.
    • (2005) Science , vol.307 , pp. 1207-1208
    • Hussain, N.K.1    Sheng, M.2
  • 53
    • 33745994650 scopus 로고    scopus 로고
    • Alternative splicing controls selective transsynaptic interactions of the neuroligin-neurexin complex
    • Chih B, Gollan L, Scheiffele P: Alternative splicing controls selective transsynaptic interactions of the neuroligin-neurexin complex. Neuron 2006, 51:171-178.
    • (2006) Neuron , vol.51 , pp. 171-178
    • Chih, B.1    Gollan, L.2    Scheiffele, P.3
  • 55
    • 79958143403 scopus 로고    scopus 로고
    • The crystal structure of the alpha-neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function
    • Miller MT, Mileni M, Comoletti D, Stevens RC, Harel M, Taylor P: The crystal structure of the alpha-neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function. Structure 2011, 19:767-778.
    • (2011) Structure , vol.19 , pp. 767-778
    • Miller, M.T.1    Mileni, M.2    Comoletti, D.3    Stevens, R.C.4    Harel, M.5    Taylor, P.6
  • 57
    • 40049089434 scopus 로고    scopus 로고
    • Regulation of neurexin 1beta tertiary structure and ligand binding through alternative splicing
    • Shen KC, Kuczynska DA, Wu IJ, Murray BH, Sheckler LR, Rudenko G: Regulation of neurexin 1beta tertiary structure and ligand binding through alternative splicing. Structure 2008, 16:422-431.
    • (2008) Structure , vol.16 , pp. 422-431
    • Shen, K.C.1    Kuczynska, D.A.2    Wu, I.J.3    Murray, B.H.4    Sheckler, L.R.5    Rudenko, G.6
  • 59
    • 79955734152 scopus 로고    scopus 로고
    • Structural basis for variantspecific neuroligin-binding by alpha-neurexin
    • Tanaka H, Nogi T, Yasui N, Iwasaki K, Takagi J: Structural basis for variantspecific neuroligin-binding by alpha-neurexin. PLoS ONE 2011, 6:e19411.
    • (2011) PLoS ONE , vol.6
    • Tanaka, H.1    Nogi, T.2    Yasui, N.3    Iwasaki, K.4    Takagi, J.5
  • 60
    • 79958159261 scopus 로고    scopus 로고
    • The structure of neurexin 1alpha reveals features promoting a role as synaptic organizer
    • Chen F, Venugopal V, Murray B, Rudenko G: The structure of neurexin 1alpha reveals features promoting a role as synaptic organizer. Structure 2011, 19:779-789.
    • (2011) Structure , vol.19 , pp. 779-789
    • Chen, F.1    Venugopal, V.2    Murray, B.3    Rudenko, G.4
  • 62
    • 77955504111 scopus 로고    scopus 로고
    • The macromolecular architecture of extracellular domain of alphaNRXN1: domain organization, flexibility, and insights into transsynaptic disposition
    • Comoletti D, Miller MT, Jeffries CM, Wilson J, Demeler B, Taylor P, Trewhella J, Nakagawa T: The macromolecular architecture of extracellular domain of alphaNRXN1: domain organization, flexibility, and insights into transsynaptic disposition. Structure 2010, 18:1044-1053.
    • (2010) Structure , vol.18 , pp. 1044-1053
    • Comoletti, D.1    Miller, M.T.2    Jeffries, C.M.3    Wilson, J.4    Demeler, B.5    Taylor, P.6    Trewhella, J.7    Nakagawa, T.8
  • 63
    • 79958170313 scopus 로고    scopus 로고
    • Unveiled alpha-neurexins take center stage
    • Reissner C, Missler M: Unveiled alpha-neurexins take center stage. Structure 2011, 19:749-750.
    • (2011) Structure , vol.19 , pp. 749-750
    • Reissner, C.1    Missler, M.2
  • 64
    • 84864301573 scopus 로고    scopus 로고
    • Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin
    • Tanaka H, Miyazaki N, Matoba K, Nogi T, Iwasaki K, Takagi J: Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin. Cell Rep 2012, 2:101-110.
    • (2012) Cell Rep , vol.2 , pp. 101-110
    • Tanaka, H.1    Miyazaki, N.2    Matoba, K.3    Nogi, T.4    Iwasaki, K.5    Takagi, J.6
  • 67
    • 0028958250 scopus 로고
    • Neurexins are differentially expressed in the embryonic nervous system of mice
    • Püschel AW, Betz H: Neurexins are differentially expressed in the embryonic nervous system of mice. J Neurosci 1995, 15:2849-2856.
    • (1995) J Neurosci , vol.15 , pp. 2849-2856
    • Püschel, A.W.1    Betz, H.2
  • 68
    • 0033623808 scopus 로고    scopus 로고
    • Expression of neurexin Ialpha splice variants in sympathetic neurons: selective changes during differentiation and in response to neurotrophins
    • Patzke H, Ernsberger U: Expression of neurexin Ialpha splice variants in sympathetic neurons: selective changes during differentiation and in response to neurotrophins. Mol Cell Neurosci 2000, 15:561-572.
    • (2000) Mol Cell Neurosci , vol.15 , pp. 561-572
    • Patzke, H.1    Ernsberger, U.2
  • 70
    • 84862776679 scopus 로고    scopus 로고
    • Glutamate receptor delta1 induces preferentially inhibitory presynaptic differentiation of cortical neurons by interacting with neurexins through cerebellin precursor protein subtypes
    • Yasumura M, Yoshida T, Lee SJ, Uemura T, Joo JY, Mishina M: Glutamate receptor delta1 induces preferentially inhibitory presynaptic differentiation of cortical neurons by interacting with neurexins through cerebellin precursor protein subtypes. J Neurochem 2012, 121:705-716.
    • (2012) J Neurochem , vol.121 , pp. 705-716
    • Yasumura, M.1    Yoshida, T.2    Lee, S.J.3    Uemura, T.4    Joo, J.Y.5    Mishina, M.6
  • 71
    • 84861462554 scopus 로고    scopus 로고
    • Diurnal rhythms in neurexins transcripts and inhibitory/excitatory synapse scaffold proteins in the biological clock
    • Shapiro-Reznik M, Jilg A, Lerner H, Earnest DJ, Zisapel N: Diurnal rhythms in neurexins transcripts and inhibitory/excitatory synapse scaffold proteins in the biological clock. PLoS One 2012, 7:e37894.
    • (2012) PLoS One , vol.7
    • Shapiro-Reznik, M.1    Jilg, A.2    Lerner, H.3    Earnest, D.J.4    Zisapel, N.5
  • 74
    • 79954529302 scopus 로고    scopus 로고
    • Dynamic changes in neurexins' alternative splicing: role of Rho-associated protein kinases and relevance to memory formation
    • Rozic G, Lupowitz Z, Piontkewitz Y, Zisapel N: Dynamic changes in neurexins' alternative splicing: role of Rho-associated protein kinases and relevance to memory formation. PLoS One 2011, 6:e18579.
    • (2011) PLoS One , vol.6
    • Rozic, G.1    Lupowitz, Z.2    Piontkewitz, Y.3    Zisapel, N.4
  • 75
    • 38349098974 scopus 로고    scopus 로고
    • Induction of GABAergic postsynaptic differentiation by alpha-neurexins
    • Kang Y, Zhang X, Dobie F, Wu H, Craig AM: Induction of GABAergic postsynaptic differentiation by alpha-neurexins. J Biol Chem 2008, 283:2323-2334.
    • (2008) J Biol Chem , vol.283 , pp. 2323-2334
    • Kang, Y.1    Zhang, X.2    Dobie, F.3    Wu, H.4    Craig, A.M.5
  • 77
    • 0029914941 scopus 로고    scopus 로고
    • CASK: a novel dlg/PSD95 homolog with an Nterminal calmodulin-dependent protein kinase domain identified by interaction with neurexins
    • Hata Y, Butz S, Südhof TC: CASK: a novel dlg/PSD95 homolog with an Nterminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J Neurosci 1996, 16:2488-2494.
    • (1996) J Neurosci , vol.16 , pp. 2488-2494
    • Hata, Y.1    Butz, S.2    Südhof, T.C.3
  • 78
    • 0034704089 scopus 로고    scopus 로고
    • Mints as adaptors. Direct binding to neurexins and recruitment of munc18
    • Biederer T, Südhof TC: Mints as adaptors. Direct binding to neurexins and recruitment of munc18. J Biol Chem 2000, 275:39803-39806.
    • (2000) J Biol Chem , vol.275 , pp. 39803-39806
    • Biederer, T.1    Südhof, T.C.2
  • 79
    • 0040962408 scopus 로고    scopus 로고
    • Association of neuronal calcium channels with modular adaptor proteins
    • Maximov A, Südhof TC, Bezprozvanny I: Association of neuronal calcium channels with modular adaptor proteins. J Biol Chem 1999, 274:24453-24456.
    • (1999) J Biol Chem , vol.274 , pp. 24453-24456
    • Maximov, A.1    Südhof, T.C.2    Bezprozvanny, I.3
  • 82
    • 58149400148 scopus 로고    scopus 로고
    • Deletion of Mint proteins decreases amyloid production in transgenic mouse models of Alzheimer's disease
    • Ho A, Liu X, Südhof TC: Deletion of Mint proteins decreases amyloid production in transgenic mouse models of Alzheimer's disease. J Neurosci 2008, 28:14392-14400.
    • (2008) J Neurosci , vol.28 , pp. 14392-14400
    • Ho, A.1    Liu, X.2    Südhof, T.C.3
  • 84
    • 84861947988 scopus 로고    scopus 로고
    • alpha2delta expression sets presynaptic calcium channel abundance and release probability
    • Hoppa MB, Lana B, Margas W, Dolphin AC, Ryan TA: alpha2delta expression sets presynaptic calcium channel abundance and release probability. Nature 2012, 486:122-125.
    • (2012) Nature , vol.486 , pp. 122-125
    • Hoppa, M.B.1    Lana, B.2    Margas, W.3    Dolphin, A.C.4    Ryan, T.A.5
  • 86
    • 13544269142 scopus 로고    scopus 로고
    • Control of excitatory and inhibitory synapse formation by neuroligins
    • Chih B, Engelman H, Scheiffele P: Control of excitatory and inhibitory synapse formation by neuroligins. Science 2005, 307:1324-1328.
    • (2005) Science , vol.307 , pp. 1324-1328
    • Chih, B.1    Engelman, H.2    Scheiffele, P.3
  • 89
    • 77956095784 scopus 로고    scopus 로고
    • Alternative splicing of neuroligin regulates the rate of presynaptic differentiation
    • Lee H, Dean C, Isacoff E: Alternative splicing of neuroligin regulates the rate of presynaptic differentiation. J Neurosci 2010, 30:11435-11446.
    • (2010) J Neurosci , vol.30 , pp. 11435-11446
    • Lee, H.1    Dean, C.2    Isacoff, E.3
  • 90
    • 33846564563 scopus 로고    scopus 로고
    • Retrograde modulation of presynaptic release probability through signaling mediated by PSD-95-neuroligin
    • Futai K, Kim MJ, Hashikawa T, Scheiffele P, Sheng M, Hayashi Y: Retrograde modulation of presynaptic release probability through signaling mediated by PSD-95-neuroligin. Nat Neurosci 2007, 10:186-195.
    • (2007) Nat Neurosci , vol.10 , pp. 186-195
    • Futai, K.1    Kim, M.J.2    Hashikawa, T.3    Scheiffele, P.4    Sheng, M.5    Hayashi, Y.6
  • 91
    • 7244232730 scopus 로고    scopus 로고
    • Neuroligin 2 is exclusively localized to inhibitory synapses
    • Varoqueaux F, Jamain S, Brose N: Neuroligin 2 is exclusively localized to inhibitory synapses. Eur J Cell Biol 2004, 83:449-456.
    • (2004) Eur J Cell Biol , vol.83 , pp. 449-456
    • Varoqueaux, F.1    Jamain, S.2    Brose, N.3
  • 92
    • 78651107671 scopus 로고    scopus 로고
    • Differential dynamics and activity-dependent regulation of alpha-and beta-neurexins at developing GABAergic synapses
    • Fu Y, Huang ZJ: Differential dynamics and activity-dependent regulation of alpha-and beta-neurexins at developing GABAergic synapses. Proc Natl Acad Sci U S A 2010, 107:22699-22704.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 22699-22704
    • Fu, Y.1    Huang, Z.J.2
  • 102
    • 79951562124 scopus 로고    scopus 로고
    • Behavioral profiles of mouse models for autism spectrum disorders
    • Ey E, Leblond CS, Bourgeron T: Behavioral profiles of mouse models for autism spectrum disorders. Autism Res 2011, 4:5-16.
    • (2011) Autism Res , vol.4 , pp. 5-16
    • Ey, E.1    Leblond, C.S.2    Bourgeron, T.3
  • 103
  • 108
    • 79960627779 scopus 로고    scopus 로고
    • An autism-associated point mutation in the neuroligin cytoplasmic tail selectively impairs AMPA receptor-mediated synaptic transmission in hippocampus
    • Etherton MR, Tabuchi K, Sharma M, Ko J, Südhof TC: An autism-associated point mutation in the neuroligin cytoplasmic tail selectively impairs AMPA receptor-mediated synaptic transmission in hippocampus. EMBO J 2011, 30:2908-2919.
    • (2011) EMBO J , vol.30 , pp. 2908-2919
    • Etherton, M.R.1    Tabuchi, K.2    Sharma, M.3    Ko, J.4    Südhof, T.C.5
  • 110
    • 3543136466 scopus 로고    scopus 로고
    • Disorder-associated mutations lead to functional inactivation of neuroligins
    • Chih B, Afridi SK, Clark L, Scheiffele P: Disorder-associated mutations lead to functional inactivation of neuroligins. Hum Mol Genet 2004, 13:1471-1477.
    • (2004) Hum Mol Genet , vol.13 , pp. 1471-1477
    • Chih, B.1    Afridi, S.K.2    Clark, L.3    Scheiffele, P.4
  • 113
    • 38749109672 scopus 로고    scopus 로고
    • GFP Reconstitution Across Synaptic Partners (GRASP) defines cell contacts and synapses in living nervous systems
    • Feinberg EH, Vanhoven MK, Bendesky A, Wang G, Fetter RD, Shen K, Bargmann CI: GFP Reconstitution Across Synaptic Partners (GRASP) defines cell contacts and synapses in living nervous systems. Neuron 2008, 57:353-363.
    • (2008) Neuron , vol.57 , pp. 353-363
    • Feinberg, E.H.1    Vanhoven, M.K.2    Bendesky, A.3    Wang, G.4    Fetter, R.D.5    Shen, K.6    Bargmann, C.I.7
  • 114
    • 33646464124 scopus 로고    scopus 로고
    • Structure function and splice site analysis of the synaptogenic activity of the neurexin-1 beta LNS domain
    • Graf ER, Kang Y, Hauner AM, Craig AM: Structure function and splice site analysis of the synaptogenic activity of the neurexin-1 beta LNS domain. J Neurosci 2006, 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
  • 117
    • 34848910696 scopus 로고    scopus 로고
    • Preconditioning ischemia attenuates increased neurexin-neuroligin1-PSD-95 interaction after transient cerebral ischemia in rat hippocampus
    • Li C, Han D, Zhang F, Zhou C, Yu HM, Zhang GY: Preconditioning ischemia attenuates increased neurexin-neuroligin1-PSD-95 interaction after transient cerebral ischemia in rat hippocampus. Neurosci Lett 2007, 426:192-197.
    • (2007) Neurosci Lett , vol.426 , pp. 192-197
    • Li, C.1    Han, D.2    Zhang, F.3    Zhou, C.4    Yu, H.M.5    Zhang, G.Y.6
  • 118
    • 85027934678 scopus 로고    scopus 로고
    • Neurexins and neuroligins: recent insights from invertebrates
    • Knight D, Xie W, Boulianne GL: Neurexins and neuroligins: recent insights from invertebrates. Mol Neurobiol 2011, 44:426-440.
    • (2011) Mol Neurobiol , vol.44 , pp. 426-440
    • Knight, D.1    Xie, W.2    Boulianne, G.L.3
  • 120
    • 79960931882 scopus 로고    scopus 로고
    • Neurexins and neuroligins: synapses look out of the nervous system
    • Bottos A, Rissone A, Bussolino F, Arese M: Neurexins and neuroligins: synapses look out of the nervous system. Cell Mol Life Sci 2011, 68:2655-2666.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 2655-2666
    • Bottos, A.1    Rissone, A.2    Bussolino, F.3    Arese, M.4
  • 121
    • 0036402241 scopus 로고    scopus 로고
    • Identification and characterization of heart-specific splicing of human neurexin 3 mRNA (NRXN3)
    • Occhi G, Rampazzo A, Beffagna G, Antonio Danieli G: Identification and characterization of heart-specific splicing of human neurexin 3 mRNA (NRXN3). Biochem Biophys Res Commun 2002, 298:151-155.
    • (2002) Biochem Biophys Res Commun , vol.298 , pp. 151-155
    • Occhi, G.1    Rampazzo, A.2    Beffagna, G.3    Antonio Danieli, G.4
  • 122
    • 84857463269 scopus 로고    scopus 로고
    • Neurexin-1alpha contributes to insulin-containing secretory granule docking
    • Mosedale M, Egodage S, Calma RC, Chi NW, Chessler SD: Neurexin-1alpha contributes to insulin-containing secretory granule docking. J Biol Chem 2012, 287:6350-6361.
    • (2012) J Biol Chem , vol.287 , pp. 6350-6361
    • Mosedale, M.1    Egodage, S.2    Calma, R.C.3    Chi, N.W.4    Chessler, S.D.5
  • 123
    • 57349156187 scopus 로고    scopus 로고
    • Expression of neurexin, neuroligin, and their cytoplasmic binding partners in the pancreatic beta-cells and the involvement of neuroligin in insulin secretion
    • Suckow AT, Comoletti D, Waldrop MA, Mosedale M, Egodage S, Taylor P, Chessler SD: Expression of neurexin, neuroligin, and their cytoplasmic binding partners in the pancreatic beta-cells and the involvement of neuroligin in insulin secretion. Endocrinology 2008, 149:6006-6017.
    • (2008) Endocrinology , vol.149 , pp. 6006-6017
    • Suckow, A.T.1    Comoletti, D.2    Waldrop, M.A.3    Mosedale, M.4    Egodage, S.5    Taylor, P.6    Chessler, S.D.7
  • 124
    • 84862005664 scopus 로고    scopus 로고
    • Transcellular neuroligin-2 interactions enhance insulin secretion and are integral to pancreatic beta cell function
    • Suckow AT, Zhang C, Egodage S, Comoletti D, Taylor P, Miller MT, Sweet IR, Chessler SD: Transcellular neuroligin-2 interactions enhance insulin secretion and are integral to pancreatic beta cell function. J Biol Chem 2012, 287:19816-19826.
    • (2012) J Biol Chem , vol.287 , pp. 19816-19826
    • Suckow, A.T.1    Zhang, C.2    Egodage, S.3    Comoletti, D.4    Taylor, P.5    Miller, M.T.6    Sweet, I.R.7    Chessler, S.D.8
  • 126
    • 84879970825 scopus 로고    scopus 로고
    • Presynaptic neurexin-3 alternative splicing trans-synaptically controls postsynaptic AMPA receptor trafficking
    • Aoto J, Martinelli DC, Malenka RC, Tabuchi K, Südhof TC: Presynaptic neurexin-3 alternative splicing trans-synaptically controls postsynaptic AMPA receptor trafficking. Cell 2013, 154:75-88.
    • (2013) Cell , vol.154 , pp. 75-88
    • Aoto, J.1    Martinelli, D.C.2    Malenka, R.C.3    Tabuchi, K.4    Südhof, T.C.5
  • 127
    • 84868156898 scopus 로고    scopus 로고
    • Neuroligin-1 induces neurite outgrowth through interaction with neurexin-1beta and activation of fibroblast growth factor receptor-1
    • Gjorlund MD, Nielsen J, Pankratova S, Li S, Korshunova I, Bock E, Berezin V: Neuroligin-1 induces neurite outgrowth through interaction with neurexin-1beta and activation of fibroblast growth factor receptor-1. FASEB J 2012, 26:4174-4186.
    • (2012) FASEB J , vol.26 , pp. 4174-4186
    • Gjorlund, M.D.1    Nielsen, J.2    Pankratova, S.3    Li, S.4    Korshunova, I.5    Bock, E.6    Berezin, V.7
  • 128
    • 23344441592 scopus 로고    scopus 로고
    • Neurexophilin 3 is highly localized in cortical and cerebellar regions and is functionally important for sensorimotor gating and motor coordination
    • Beglopoulos V, Montag-Sallaz M, Rohlmann A, Piechotta K, Ahmad M, Montag D, Missler M: Neurexophilin 3 is highly localized in cortical and cerebellar regions and is functionally important for sensorimotor gating and motor coordination. Mol Cell Biol 2005, 25:7278-7288.
    • (2005) Mol Cell Biol , vol.25 , pp. 7278-7288
    • Beglopoulos, V.1    Montag-Sallaz, M.2    Rohlmann, A.3    Piechotta, K.4    Ahmad, M.5    Montag, D.6    Missler, M.7
  • 130
    • 17144377429 scopus 로고    scopus 로고
    • Solution structure of AF-6 PDZ domain and its interaction with the C-terminal peptides from Neurexin and Bcr
    • Zhou H, Xu Y, Yang Y, Huang A, Wu J, Shi Y: Solution structure of AF-6 PDZ domain and its interaction with the C-terminal peptides from Neurexin and Bcr. J Biol Chem 2005, 280:13841-13847.
    • (2005) J Biol Chem , vol.280 , pp. 13841-13847
    • Zhou, H.1    Xu, Y.2    Yang, Y.3    Huang, A.4    Wu, J.5    Shi, Y.6
  • 131
    • 0036368445 scopus 로고    scopus 로고
    • Expression of neurexin ligands, the neuroligins and the neurexophilins, in the developing and adult rodent olfactory bulb
    • Clarris HJ, McKeown S, Key B: Expression of neurexin ligands, the neuroligins and the neurexophilins, in the developing and adult rodent olfactory bulb. Int J Dev Biol 2002, 46:649-652.
    • (2002) Int J Dev Biol , vol.46 , pp. 649-652
    • Clarris, H.J.1    McKeown, S.2    Key, B.3
  • 133
    • 84969318061 scopus 로고    scopus 로고
    • GenBank. [http://ncbi.nlm.nih.gov/genbank/].


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.