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Volumn 7, Issue 7, 2012, Pages

14-3-3θ is a binding partner of rat Eag1 Potassium channels

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE; POTASSIUM CHANNEL; POTASSIUM CHANNEL EAG1; PROTEIN 14 3 3; UNCLASSIFIED DRUG;

EID: 84864098814     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0041203     Document Type: Article
Times cited : (14)

References (50)
  • 1
    • 0028292927 scopus 로고
    • A family of potassium channel genes related to eag in Drosophila and mammals
    • Warmke JW, Ganetzky B, (1994) A family of potassium channel genes related to eag in Drosophila and mammals. Proc Natl Acad Sci U S A 91: 3438-3442.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3438-3442
    • Warmke, J.W.1    Ganetzky, B.2
  • 2
    • 0025762715 scopus 로고
    • Determination of the subunit stoichiometry of a voltage-activated potassium channel
    • MacKinnon R, (1991) Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature 350: 232-235.
    • (1991) Nature , vol.350 , pp. 232-235
    • MacKinnon, R.1
  • 3
    • 0033573464 scopus 로고    scopus 로고
    • Cloning of components of a novel subthreshold-activating K(+) channel with a unique pattern of expression in the cerebral cortex
    • Saganich MJ, Vega-Saenz de Miera E, Nadal MS, Baker H, Coetzee WA, et al. (1999) Cloning of components of a novel subthreshold-activating K(+) channel with a unique pattern of expression in the cerebral cortex. J Neurosci 19: 10789-10802.
    • (1999) J Neurosci , vol.19 , pp. 10789-10802
    • Saganich, M.J.1    Vega-Saenz de Miera, E.2    Nadal, M.S.3    Baker, H.4    Coetzee, W.A.5
  • 4
    • 0033865816 scopus 로고    scopus 로고
    • Cloning and functional expression of rat eag2, a new member of the ether-a-go-go family of potassium channels and comparison of its distribution with that of eag1
    • Ludwig J, Weseloh R, Karschin C, Liu Q, Netzer R, et al. (2000) Cloning and functional expression of rat eag2, a new member of the ether-a-go-go family of potassium channels and comparison of its distribution with that of eag1. Mol Cell Neurosci 16: 59-70.
    • (2000) Mol Cell Neurosci , vol.16 , pp. 59-70
    • Ludwig, J.1    Weseloh, R.2    Karschin, C.3    Liu, Q.4    Netzer, R.5
  • 5
    • 0031594634 scopus 로고    scopus 로고
    • Characterization of ether-a-go-go channels present in photoreceptors reveals similarity to IKx, a K+ current in rod inner segments
    • Frings S, Brull N, Dzeja C, Angele A, Hagen V, et al. (1998) Characterization of ether-a-go-go channels present in photoreceptors reveals similarity to IKx, a K+ current in rod inner segments. J Gen Physiol 111: 583-599.
    • (1998) J Gen Physiol , vol.111 , pp. 583-599
    • Frings, S.1    Brull, N.2    Dzeja, C.3    Angele, A.4    Hagen, V.5
  • 6
    • 0035399872 scopus 로고    scopus 로고
    • Differential expression of genes encoding subthreshold-operating voltage-gated K+ channels in brain
    • Saganich MJ, Machado E, Rudy B, (2001) Differential expression of genes encoding subthreshold-operating voltage-gated K+ channels in brain. J Neurosci 21: 4609-4624.
    • (2001) J Neurosci , vol.21 , pp. 4609-4624
    • Saganich, M.J.1    Machado, E.2    Rudy, B.3
  • 7
    • 0033585126 scopus 로고    scopus 로고
    • Purification of an EH domain-binding protein from rat brain that modulates the gating of the rat ether-a-go-go channel
    • Piros ET, Shen L, Huang XY, (1999) Purification of an EH domain-binding protein from rat brain that modulates the gating of the rat ether-a-go-go channel. J Biol Chem 274: 33677-33683.
    • (1999) J Biol Chem , vol.274 , pp. 33677-33683
    • Piros, E.T.1    Shen, L.2    Huang, X.Y.3
  • 8
    • 0342646981 scopus 로고    scopus 로고
    • Inhibition of human ether a go-go potassium channels by Ca(2+)/calmodulin
    • Schonherr R, Lober K, Heinemann SH, (2000) Inhibition of human ether a go-go potassium channels by Ca(2+)/calmodulin. Embo J 19: 3263-3271.
    • (2000) Embo J , vol.19 , pp. 3263-3271
    • Schonherr, R.1    Lober, K.2    Heinemann, S.H.3
  • 9
    • 33644961982 scopus 로고    scopus 로고
    • Inhibition of human ether a go-go potassium channels by Ca2+/calmodulin binding to the cytosolic N- and C-termini
    • Ziechner U, Schonherr R, Born AK, Gavrilova-Ruch O, Glaser RW, et al. (2006) Inhibition of human ether a go-go potassium channels by Ca2+/calmodulin binding to the cytosolic N- and C-termini. FEBS J 273: 1074-1086.
    • (2006) FEBS J , vol.273 , pp. 1074-1086
    • Ziechner, U.1    Schonherr, R.2    Born, A.K.3    Gavrilova-Ruch, O.4    Glaser, R.W.5
  • 10
    • 1642404319 scopus 로고    scopus 로고
    • The eag potassium channel binds and locally activates calcium/calmodulin-dependent protein kinase II
    • Sun XX, Hodge JJ, Zhou Y, Nguyen M, Griffith LC, (2004) The eag potassium channel binds and locally activates calcium/calmodulin-dependent protein kinase II. J Biol Chem 279: 10206-10214.
    • (2004) J Biol Chem , vol.279 , pp. 10206-10214
    • Sun, X.X.1    Hodge, J.J.2    Zhou, Y.3    Nguyen, M.4    Griffith, L.C.5
  • 11
    • 0037025337 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II phosphorylates and regulates the Drosophila eag potassium channel
    • Wang Z, Wilson GF, Griffith LC, (2002) Calcium/calmodulin-dependent protein kinase II phosphorylates and regulates the Drosophila eag potassium channel. J Biol Chem 277: 24022-24029.
    • (2002) J Biol Chem , vol.277 , pp. 24022-24029
    • Wang, Z.1    Wilson, G.F.2    Griffith, L.C.3
  • 12
    • 0036606735 scopus 로고    scopus 로고
    • Molecular mechanisms of CaMKII activation in neuronal plasticity
    • Fink CC, Meyer T, (2002) Molecular mechanisms of CaMKII activation in neuronal plasticity. Curr Opin Neurobiol 12: 293-299.
    • (2002) Curr Opin Neurobiol , vol.12 , pp. 293-299
    • Fink, C.C.1    Meyer, T.2
  • 13
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioural memory
    • Lisman J, Schulman H, Cline H, (2002) The molecular basis of CaMKII function in synaptic and behavioural memory. Nat Rev Neurosci 3: 175-190.
    • (2002) Nat Rev Neurosci , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 14
    • 0347993183 scopus 로고    scopus 로고
    • Regulation of the Ca2+/CaM-responsive pool of CaMKII by scaffold-dependent autophosphorylation
    • Lu CS, Hodge JJ, Mehren J, Sun XX, Griffith LC, (2003) Regulation of the Ca2+/CaM-responsive pool of CaMKII by scaffold-dependent autophosphorylation. Neuron 40: 1185-1197.
    • (2003) Neuron , vol.40 , pp. 1185-1197
    • Lu, C.S.1    Hodge, J.J.2    Mehren, J.3    Sun, X.X.4    Griffith, L.C.5
  • 15
    • 19044368337 scopus 로고    scopus 로고
    • Camguk/CASK enhances Ether-a-go-go potassium current by a phosphorylation-dependent mechanism
    • Marble DD, Hegle AP, Snyder ED, 2nd, Dimitratos S, Bryant PJ, et al (2005) Camguk/CASK enhances Ether-a-go-go potassium current by a phosphorylation-dependent mechanism. J Neurosci 25: 4898-4907.
    • (2005) J Neurosci , vol.25 , pp. 4898-4907
    • Marble, D.D.1    Hegle, A.P.2    Snyder 2nd, E.D.3    Dimitratos, S.4    Bryant, P.J.5
  • 16
    • 14944375001 scopus 로고    scopus 로고
    • Differential localization of rat Eag1 and Eag2 K+ channels in hippocampal neurons
    • Jeng CJ, Chang CC, Tang CY, (2005) Differential localization of rat Eag1 and Eag2 K+ channels in hippocampal neurons. Neuroreport 16: 229-233.
    • (2005) Neuroreport , vol.16 , pp. 229-233
    • Jeng, C.J.1    Chang, C.C.2    Tang, C.Y.3
  • 17
    • 79960990417 scopus 로고    scopus 로고
    • Distal end of carboxyl terminus is not essential for the assembly of rat Eag1 potassium channels
    • Chen IH, Hu JH, Jow GM, Chuang CC, Lee TT, et al. (2011) Distal end of carboxyl terminus is not essential for the assembly of rat Eag1 potassium channels. J Biol Chem 286: 27183-27196.
    • (2011) J Biol Chem , vol.286 , pp. 27183-27196
    • Chen, I.H.1    Hu, J.H.2    Jow, G.M.3    Chuang, C.C.4    Lee, T.T.5
  • 18
    • 0036903892 scopus 로고    scopus 로고
    • Counting channels: a tutorial guide on ion channel fluctuation analysis
    • Alvarez O, Gonzalez C, Latorre R, (2002) Counting channels: a tutorial guide on ion channel fluctuation analysis. Adv Physiol Educ 26: 327-341.
    • (2002) Adv Physiol Educ , vol.26 , pp. 327-341
    • Alvarez, O.1    Gonzalez, C.2    Latorre, R.3
  • 19
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: a historic overview
    • Aitken A, (2006) 14-3-3 proteins: a historic overview. Semin Cancer Biol 16: 162-172.
    • (2006) Semin Cancer Biol , vol.16 , pp. 162-172
    • Aitken, A.1
  • 20
    • 33644877400 scopus 로고    scopus 로고
    • 14-3-3 proteins: a number of functions for a numbered protein
    • Bridges D, Moorhead GB, (2005) 14-3-3 proteins: a number of functions for a numbered protein. Sci STKE 2005: re10.
    • (2005) Sci STKE , vol.2005
    • Bridges, D.1    Moorhead, G.B.2
  • 21
    • 0030822692 scopus 로고    scopus 로고
    • Leonardo, a Drosophila 14-3-3 protein involved in learning, regulates presynaptic function
    • Broadie K, Rushton E, Skoulakis EM, Davis RL, (1997) Leonardo, a Drosophila 14-3-3 protein involved in learning, regulates presynaptic function. Neuron 19: 391-402.
    • (1997) Neuron , vol.19 , pp. 391-402
    • Broadie, K.1    Rushton, E.2    Skoulakis, E.M.3    Davis, R.L.4
  • 22
    • 33748686429 scopus 로고    scopus 로고
    • Modulation of inactivation properties of CaV2.2 channels by 14-3-3 proteins
    • Li Y, Wu Y, Zhou Y, (2006) Modulation of inactivation properties of CaV2.2 channels by 14-3-3 proteins. Neuron 51: 755-771.
    • (2006) Neuron , vol.51 , pp. 755-771
    • Li, Y.1    Wu, Y.2    Zhou, Y.3
  • 23
    • 0035503073 scopus 로고    scopus 로고
    • Conditional rescue of olfactory learning and memory defects in mutants of the 14-3-3zeta gene leonardo
    • Philip N, Acevedo SF, Skoulakis EM, (2001) Conditional rescue of olfactory learning and memory defects in mutants of the 14-3-3zeta gene leonardo. J Neurosci 21: 8417-8425.
    • (2001) J Neurosci , vol.21 , pp. 8417-8425
    • Philip, N.1    Acevedo, S.F.2    Skoulakis, E.M.3
  • 24
    • 47749117157 scopus 로고    scopus 로고
    • The functional interaction of 14-3-3 proteins with the ERK1/2 scaffold KSR1 occurs in an isoform-specific manner
    • Jagemann LR, Perez-Rivas LG, Ruiz EJ, Ranea JA, Sanchez-Jimenez F, et al. (2008) The functional interaction of 14-3-3 proteins with the ERK1/2 scaffold KSR1 occurs in an isoform-specific manner. J Biol Chem 283: 17450-17462.
    • (2008) J Biol Chem , vol.283 , pp. 17450-17462
    • Jagemann, L.R.1    Perez-Rivas, L.G.2    Ruiz, E.J.3    Ranea, J.A.4    Sanchez-Jimenez, F.5
  • 25
    • 77951921902 scopus 로고    scopus 로고
    • Mammalian Per-Arnt-Sim proteins in environmental adaptation
    • McIntosh BE, Hogenesch JB, Bradfield CA, (2010) Mammalian Per-Arnt-Sim proteins in environmental adaptation. Annu Rev Physiol 72: 625-645.
    • (2010) Annu Rev Physiol , vol.72 , pp. 625-645
    • McIntosh, B.E.1    Hogenesch, J.B.2    Bradfield, C.A.3
  • 26
    • 84856234056 scopus 로고    scopus 로고
    • Structure of the carboxy-terminal region of a KCNH channel
    • Brelidze TI, Carlson AE, Sankaran B, Zagotta WN, (2012) Structure of the carboxy-terminal region of a KCNH channel. Nature 481: 530-533.
    • (2012) Nature , vol.481 , pp. 530-533
    • Brelidze, T.I.1    Carlson, A.E.2    Sankaran, B.3    Zagotta, W.N.4
  • 28
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion G, Avruch J, (2002) 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J Biol Chem 277: 3061-3064.
    • (2002) J Biol Chem , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 29
    • 0037112395 scopus 로고    scopus 로고
    • Interaction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3
    • Rajan S, Preisig-Muller R, Wischmeyer E, Nehring R, Hanley PJ, et al. (2002) Interaction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3. J Physiol 545: 13-26.
    • (2002) J Physiol , vol.545 , pp. 13-26
    • Rajan, S.1    Preisig-Muller, R.2    Wischmeyer, E.3    Nehring, R.4    Hanley, P.J.5
  • 30
    • 0142211242 scopus 로고    scopus 로고
    • The binding site for regulatory 14-3-3 protein in plant plasma membrane H+-ATPase: involvement of a region promoting phosphorylation-independent interaction in addition to the phosphorylation-dependent C-terminal end
    • Fuglsang AT, Borch J, Bych K, Jahn TP, Roepstorff P, et al. (2003) The binding site for regulatory 14-3-3 protein in plant plasma membrane H+-ATPase: involvement of a region promoting phosphorylation-independent interaction in addition to the phosphorylation-dependent C-terminal end. J Biol Chem 278: 42266-42272.
    • (2003) J Biol Chem , vol.278 , pp. 42266-42272
    • Fuglsang, A.T.1    Borch, J.2    Bych, K.3    Jahn, T.P.4    Roepstorff, P.5
  • 31
    • 33846999287 scopus 로고    scopus 로고
    • Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis
    • Ottmann C, Yasmin L, Weyand M, Veesenmeyer JL, Diaz MH, et al. (2007) Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Embo J 26: 902-913.
    • (2007) Embo J , vol.26 , pp. 902-913
    • Ottmann, C.1    Yasmin, L.2    Weyand, M.3    Veesenmeyer, J.L.4    Diaz, M.H.5
  • 32
    • 0035977072 scopus 로고    scopus 로고
    • 14-3-3 proteins mediate an essential anti-apoptotic signal
    • Masters SC, Fu H, (2001) 14-3-3 proteins mediate an essential anti-apoptotic signal. J Biol Chem 276: 45193-45200.
    • (2001) J Biol Chem , vol.276 , pp. 45193-45200
    • Masters, S.C.1    Fu, H.2
  • 33
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty MK, Morrison DK, (2004) Unlocking the code of 14-3-3. J Cell Sci 117: 1875-1884.
    • (2004) J Cell Sci , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 34
    • 27444433260 scopus 로고    scopus 로고
    • 14-3-3 proteins: regulators of numerous eukaryotic proteins
    • van Heusden GP, (2005) 14-3-3 proteins: regulators of numerous eukaryotic proteins. IUBMB Life 57: 623-629.
    • (2005) IUBMB Life , vol.57 , pp. 623-629
    • van Heusden, G.P.1
  • 35
    • 0037090803 scopus 로고    scopus 로고
    • 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity
    • Kagan A, Melman YF, Krumerman A, McDonald TV, (2002) 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity. Embo J 21: 1889-1898.
    • (2002) Embo J , vol.21 , pp. 1889-1898
    • Kagan, A.1    Melman, Y.F.2    Krumerman, A.3    McDonald, T.V.4
  • 36
    • 20144386846 scopus 로고    scopus 로고
    • 14-3-3 proteins modulate the expression of epithelial Na+ channels by phosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase
    • Ichimura T, Yamamura H, Sasamoto K, Tominaga Y, Taoka M, et al. (2005) 14-3-3 proteins modulate the expression of epithelial Na+ channels by phosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase. J Biol Chem 280: 13187-13194.
    • (2005) J Biol Chem , vol.280 , pp. 13187-13194
    • Ichimura, T.1    Yamamura, H.2    Sasamoto, K.3    Tominaga, Y.4    Taoka, M.5
  • 37
    • 77951220423 scopus 로고    scopus 로고
    • Coactivator recruitment: a new role for PAS domains in transcriptional regulation by the bHLH-PAS family
    • Partch CL, Gardner KH, (2010) Coactivator recruitment: a new role for PAS domains in transcriptional regulation by the bHLH-PAS family. J Cell Physiol 223: 553-557.
    • (2010) J Cell Physiol , vol.223 , pp. 553-557
    • Partch, C.L.1    Gardner, K.H.2
  • 38
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: internal sensors of oxygen, redox potential, and light
    • Taylor BL, Zhulin IB, (1999) PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol Mol Biol Rev 63: 479-506.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 39
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • Zagotta WN, Olivier NB, Black KD, Young EC, Olson R, et al. (2003) Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature 425: 200-205.
    • (2003) Nature , vol.425 , pp. 200-205
    • Zagotta, W.N.1    Olivier, N.B.2    Black, K.D.3    Young, E.C.4    Olson, R.5
  • 40
    • 70350514521 scopus 로고    scopus 로고
    • Absence of direct cyclic nucleotide modulation of mEAG1 and hERG1 channels revealed with fluorescence and electrophysiological methods
    • Brelidze TI, Carlson AE, Zagotta WN, (2009) Absence of direct cyclic nucleotide modulation of mEAG1 and hERG1 channels revealed with fluorescence and electrophysiological methods. J Biol Chem 284: 27989-27997.
    • (2009) J Biol Chem , vol.284 , pp. 27989-27997
    • Brelidze, T.I.1    Carlson, A.E.2    Zagotta, W.N.3
  • 41
    • 62949118937 scopus 로고    scopus 로고
    • Roles of surface residues of intracellular domains of heag potassium channels
    • Stevens L, Ju M, Wray D, (2009) Roles of surface residues of intracellular domains of heag potassium channels. European Biophysics Journal 38: 523-532.
    • (2009) European Biophysics Journal , vol.38 , pp. 523-532
    • Stevens, L.1    Ju, M.2    Wray, D.3
  • 42
    • 33751176024 scopus 로고    scopus 로고
    • Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels
    • Heusser K, Yuan H, Neagoe I, Tarasov AI, Ashcroft FM, et al. (2006) Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels. J Cell Sci 119: 4353-4363.
    • (2006) J Cell Sci , vol.119 , pp. 4353-4363
    • Heusser, K.1    Yuan, H.2    Neagoe, I.3    Tarasov, A.I.4    Ashcroft, F.M.5
  • 43
    • 33745825514 scopus 로고    scopus 로고
    • Inhibitory interaction of the plasma membrane Na+/Ca2+ exchangers with the 14-3-3 proteins
    • Pulina MV, Rizzuto R, Brini M, Carafoli E, (2006) Inhibitory interaction of the plasma membrane Na+/Ca2+ exchangers with the 14-3-3 proteins. J Biol Chem 281: 19645-19654.
    • (2006) J Biol Chem , vol.281 , pp. 19645-19654
    • Pulina, M.V.1    Rizzuto, R.2    Brini, M.3    Carafoli, E.4
  • 44
    • 0029046812 scopus 로고
    • Crystal structure of the zeta isoform of the 14-3-3 protein
    • Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, et al. (1995) Crystal structure of the zeta isoform of the 14-3-3 protein. Nature 376: 191-194.
    • (1995) Nature , vol.376 , pp. 191-194
    • Liu, D.1    Bienkowska, J.2    Petosa, C.3    Collier, R.J.4    Fu, H.5
  • 45
    • 0028979375 scopus 로고
    • Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways
    • Xiao B, Smerdon SJ, Jones DH, Dodson GG, Soneji Y, et al. (1995) Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature 376: 188-191.
    • (1995) Nature , vol.376 , pp. 188-191
    • Xiao, B.1    Smerdon, S.J.2    Jones, D.H.3    Dodson, G.G.4    Soneji, Y.5
  • 46
    • 38049079819 scopus 로고    scopus 로고
    • Differential localization of rat Eag1 and Eag2 potassium channels in the retina
    • Jow GM, Jeng CJ, (2008) Differential localization of rat Eag1 and Eag2 potassium channels in the retina. Neurosci Lett 431: 12-16.
    • (2008) Neurosci Lett , vol.431 , pp. 12-16
    • Jow, G.M.1    Jeng, C.J.2
  • 47
    • 33845989449 scopus 로고    scopus 로고
    • Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling
    • Angrand PO, Segura I, Volkel P, Ghidelli S, Terry R, et al. (2006) Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling. Mol Cell Proteomics 5: 2211-2227.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2211-2227
    • Angrand, P.O.1    Segura, I.2    Volkel, P.3    Ghidelli, S.4    Terry, R.5
  • 48
    • 0033165926 scopus 로고    scopus 로고
    • Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin
    • Naisbitt S, Kim E, Tu JC, Xiao B, Sala C, et al. (1999) Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin. Neuron 23: 569-582.
    • (1999) Neuron , vol.23 , pp. 569-582
    • Naisbitt, S.1    Kim, E.2    Tu, J.C.3    Xiao, B.4    Sala, C.5
  • 49
    • 0033166537 scopus 로고    scopus 로고
    • Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins
    • Tu JC, Xiao B, Naisbitt S, Yuan JP, Petralia RS, et al. (1999) Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins. Neuron 23: 583-592.
    • (1999) Neuron , vol.23 , pp. 583-592
    • Tu, J.C.1    Xiao, B.2    Naisbitt, S.3    Yuan, J.P.4    Petralia, R.S.5
  • 50
    • 67149141899 scopus 로고    scopus 로고
    • Targeted tandem affinity purification of PSD-95 recovers core postsynaptic complexes and schizophrenia susceptibility proteins
    • Fernandez E, Collins MO, Uren RT, Kopanitsa MV, Komiyama NH, et al. (2009) Targeted tandem affinity purification of PSD-95 recovers core postsynaptic complexes and schizophrenia susceptibility proteins. Mol Syst Biol 5: 269.
    • (2009) Mol Syst Biol , vol.5 , pp. 269
    • Fernandez, E.1    Collins, M.O.2    Uren, R.T.3    Kopanitsa, M.V.4    Komiyama, N.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.