메뉴 건너뛰기




Volumn 22, Issue 4, 1999, Pages 809-818

A dynamically regulated 14-3-3, Slob, and Slowpoke potassium channel complex in Drosophila presynaptic nerve terminals

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; MUTANT PROTEIN; POTASSIUM CHANNEL; POTASSIUM ION; PROTEIN 14 3 3; PROTEIN KINASE (CALCIUM,CALMODULIN) II; PROTEIN SLOB; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 0033118606     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80739-4     Document Type: Article
Times cited : (117)

References (78)
  • 3
    • 0030940161 scopus 로고    scopus 로고
    • Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold
    • Apel, E.D., Glass, D.J., Moscoso, L.M., Yancopoulos, G.D., and Sanes, J.R. (1997). Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold. Neuron 18, 623-635.
    • (1997) Neuron , vol.18 , pp. 623-635
    • Apel, E.D.1    Glass, D.J.2    Moscoso, L.M.3    Yancopoulos, G.D.4    Sanes, J.R.5
  • 4
    • 0026413976 scopus 로고
    • A component of calcium-activated potassium channels encoded by the Drosophila slo locus
    • Atkinson, N.S., Robertson, G.A., and Ganetzky, B. (1991). A component of calcium-activated potassium channels encoded by the Drosophila slo locus. Science 253, 551-555.
    • (1991) Science , vol.253 , pp. 551-555
    • Atkinson, N.S.1    Robertson, G.A.2    Ganetzky, B.3
  • 5
    • 0028325752 scopus 로고
    • + channel in rat peptidergic nerve terminals
    • + channel in rat peptidergic nerve terminals. J. Physiol. 475, 241-254.
    • (1994) J. Physiol. , vol.475 , pp. 241-254
    • Bielefeldt, K.1    Jackson, M.B.2
  • 7
    • 0029166558 scopus 로고
    • BCR and RAF form a complex in vivo via 14-3-3 proteins
    • Braselmann, S., and McCormick, F. (1995). BCR and RAF form a complex in vivo via 14-3-3 proteins. EMBO J. 14, 4839-4848.
    • (1995) EMBO J. , vol.14 , pp. 4839-4848
    • Braselmann, S.1    McCormick, F.2
  • 8
    • 0030822692 scopus 로고    scopus 로고
    • Leonardo, a Drosophila 14-3-3 protein involved in learning, regulates presynaptic function
    • Broadie, K., Rushton, E., Skoulakis, E.M.C., and Davis, R.L. (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.C.3    Davis, R.L.4
  • 9
    • 0027508913 scopus 로고
    • Development of the embryonic neuromuscular synapse of Drosophila melanogaster
    • Broadie, K.S., and Bate, M. (1993). Development of the embryonic neuromuscular synapse of Drosophila melanogaster. J. Neurosci. 13, 144-166.
    • (1993) J. Neurosci. , vol.13 , pp. 144-166
    • Broadie, K.S.1    Bate, M.2
  • 10
    • 0029764092 scopus 로고    scopus 로고
    • Transport of CaM kinase along processes elicited by neuronal contact evokes an inhibition of arborization and outgrowth in D. melanogaster cultured neurons
    • Broughton, S.J., Kane, N.S., Yoder, M., Greenspan, R.J., and Robichon, A. (1996). Transport of CaM kinase along processes elicited by neuronal contact evokes an inhibition of arborization and outgrowth in D. melanogaster cultured neurons. J. Cell. Biochem. 62, 484-494.
    • (1996) J. Cell. Biochem. , vol.62 , pp. 484-494
    • Broughton, S.J.1    Kane, N.S.2    Yoder, M.3    Greenspan, R.J.4    Robichon, A.5
  • 11
    • 0029240512 scopus 로고
    • Hot numbers in signal transduction
    • Burbelo, P.D., and Hall, A. (1995). Hot numbers in signal transduction. Curr. Biol. 5, 95-96.
    • (1995) Curr. Biol. , vol.5 , pp. 95-96
    • Burbelo, P.D.1    Hall, A.2
  • 13
    • 0025912627 scopus 로고
    • Protein kinase activity closely associated with a reconstituted calcium-activated potassium channel
    • Chung, S.K., Reinhart, P.H., Martin, B.L., Brautigan, D., and Levitan, I.B. (1991). Protein kinase activity closely associated with a reconstituted calcium-activated potassium channel. Science 253, 560-562.
    • (1991) Science , vol.253 , pp. 560-562
    • Chung, S.K.1    Reinhart, P.H.2    Martin, B.L.3    Brautigan, D.4    Levitan, I.B.5
  • 14
    • 0030965089 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of nicotinic acetylcholine receptor mediates Grb2 binding
    • Colledge, M., and Froehner, S.C. (1997). Tyrosine phosphorylation of nicotinic acetylcholine receptor mediates Grb2 binding. J. Neurosci. 17, 5038-5045.
    • (1997) J. Neurosci. , vol.17 , pp. 5038-5045
    • Colledge, M.1    Froehner, S.C.2
  • 18
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong, H., O'Brien, R.J., Fung, E.T., Lanahan, A.A., Worley, P.F., and Huganir, R.L. (1997). GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature 386, 279-284.
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H.1    O'Brien, R.J.2    Fung, E.T.3    Lanahan, A.A.4    Worley, P.F.5    Huganir, R.L.6
  • 19
    • 0029991047 scopus 로고    scopus 로고
    • Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit
    • Ehlers, M.D., Zhang, S., Bernhardt, J.P., and Huganir, R.L. (1996). Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell 84, 745-755.
    • (1996) Cell , vol.84 , pp. 745-755
    • Ehlers, M.D.1    Zhang, S.2    Bernhardt, J.P.3    Huganir, R.L.4
  • 20
    • 0031972719 scopus 로고    scopus 로고
    • Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments
    • Ehlers, M.D., Fung, E.T., O'Brien, R.J., and Huganir, R.L. (1998). Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments. J. Neurosci. 18, 720-730.
    • (1998) J. Neurosci. , vol.18 , pp. 720-730
    • Ehlers, M.D.1    Fung, E.T.2    O'Brien, R.J.3    Huganir, R.L.4
  • 21
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S., and Song, O. (1989). A novel genetic system to detect protein-protein interactions. Nature 340, 245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 23
    • 0029773535 scopus 로고    scopus 로고
    • Functional interaction of Src family kinases with the acetylcholine receptor in C2 myotubes
    • Fuhrer, C., and Hall, Z.W. (1996). Functional interaction of Src family kinases with the acetylcholine receptor in C2 myotubes. J. Biol. Chem. 271, 32474-32481.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32474-32481
    • Fuhrer, C.1    Hall, Z.W.2
  • 24
    • 0026914806 scopus 로고
    • Analysis of repolarization of presynaptic motor terminals in Drosophila larvae using potassium channel-blocking drugs and mutations
    • Gho, M., and Ganetzky, B. (1992). Analysis of repolarization of presynaptic motor terminals in Drosophila larvae using potassium channel-blocking drugs and mutations. J. Exp. Biol. 170, 93-111.
    • (1992) J. Exp. Biol. , vol.170 , pp. 93-111
    • Gho, M.1    Ganetzky, B.2
  • 25
    • 0027538509 scopus 로고
    • Inhibition of calcium/calmodulin-dependent protein kinase in Drosophila disrupts behavioral plasticity
    • Griffith, L.C., Verselis, L.M., Aitken, K.M., Kyriacou, C.P., Danho, W., and Greenspan, R.J. (1993). Inhibition of calcium/calmodulin-dependent protein kinase in Drosophila disrupts behavioral plasticity. Neuron 10, 501-509.
    • (1993) Neuron , vol.10 , pp. 501-509
    • Griffith, L.C.1    Verselis, L.M.2    Aitken, K.M.3    Kyriacou, C.P.4    Danho, W.5    Greenspan, R.J.6
  • 26
    • 0029832189 scopus 로고    scopus 로고
    • Functional diversity in alternatively spliced isoforms of Drosophila calcium/calmodulin-dependent protein kinase II
    • Guptaroy, B., Beckingham, K., and Griffith, L.C. (1996). Functional diversity in alternatively spliced isoforms of Drosophila calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 271, 19846-19851.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19846-19851
    • Guptaroy, B.1    Beckingham, K.2    Griffith, L.C.3
  • 27
    • 0027354449 scopus 로고
    • Synaptic structure and development: The neuromuscular junction
    • Hall, Z.W., and Sanes, J.R. (1993). Synaptic structure and development: The neuromuscular junction. Cell 72, 99-121.
    • (1993) Cell , vol.72 , pp. 99-121
    • Hall, Z.W.1    Sanes, J.R.2
  • 28
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988). Antibodies: A Laboratory Manual (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press).
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 29
    • 0031972834 scopus 로고    scopus 로고
    • Growth factor receptor tyrosine kinases acutely regulate neuronal sodium channels through the Src signaling pathway
    • Hilborn, M.D., Vaillancourt, R.R., and Rane, S.G. (1998). Growth factor receptor tyrosine kinases acutely regulate neuronal sodium channels through the Src signaling pathway. J. Neurosci. 18, 590-600.
    • (1998) J. Neurosci. , vol.18 , pp. 590-600
    • Hilborn, M.D.1    Vaillancourt, R.R.2    Rane, S.G.3
  • 30
    • 0030473947 scopus 로고    scopus 로고
    • Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain
    • Holmes, T.C., Fadool, D.A., Ren, R., and Levitan, I.B. (1996). Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain. Science 274, 2089-2091.
    • (1996) Science , vol.274 , pp. 2089-2091
    • Holmes, T.C.1    Fadool, D.A.2    Ren, R.3    Levitan, I.B.4
  • 31
    • 0030695214 scopus 로고    scopus 로고
    • Expression of voltage-gated potassium channels decreases cellular protein tyrosine phosphorylation
    • Holmes, T.C., Berman, K., Swartz, J.E., Dagan, D., and Levitan, I.B. (1997). Expression of voltage-gated potassium channels decreases cellular protein tyrosine phosphorylation. J. Neurosci. 17, 8964-8974.
    • (1997) J. Neurosci. , vol.17 , pp. 8964-8974
    • Holmes, T.C.1    Berman, K.2    Swartz, J.E.3    Dagan, D.4    Levitan, I.B.5
  • 32
    • 0028053408 scopus 로고
    • Potassium channel induction by the Ras/Raf signal transduction cascade
    • Huang, Y., and Rane, S.G. (1994). Potassium channel induction by the Ras/Raf signal transduction cascade. J. Biol. Chem. 269, 31183-31189.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31183-31189
    • Huang, Y.1    Rane, S.G.2
  • 34
    • 0032055396 scopus 로고    scopus 로고
    • SynGAP: A synaptic RasGAP that associates with the PSD-95/SAP90 protein family
    • Kim, J.H., Liao, D., Lau, L.-F., and Huganir, R.L. (1998). SynGAP: A synaptic RasGAP that associates with the PSD-95/SAP90 protein family. Neuron 20, 683-691.
    • (1998) Neuron , vol.20 , pp. 683-691
    • Kim, J.H.1    Liao, D.2    Lau, L.-F.3    Huganir, R.L.4
  • 36
    • 0030953744 scopus 로고    scopus 로고
    • Requirement for Drosophila 14-3-3zeta in Raf-dependent photoreceptor development
    • Kockel, L., Vorbrüggen, G., Jäckle, H., Mlodzik, M., and Bohmann, D. (1997). Requirement for Drosophila 14-3-3zeta in Raf-dependent photoreceptor development. Genes Dev. 11, 1140-1147.
    • (1997) Genes Dev. , vol.11 , pp. 1140-1147
    • Kockel, L.1    Vorbrüggen, G.2    Jäckle, H.3    Mlodzik, M.4    Bohmann, D.5
  • 37
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H.-C., Schenker, LT., Kennedy, M.B., and Seeburg, P.H. (1995). Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269, 1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.-C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 39
    • 0028324395 scopus 로고
    • Modulation of ion channels by protein phosphorylation and dephosphorylation
    • Levitan, I.B. (1994). Modulation of ion channels by protein phosphorylation and dephosphorylation. Annu. Rev. Physiol. 56, 193-212.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 193-212
    • Levitan, I.B.1
  • 41
    • 0032520827 scopus 로고    scopus 로고
    • Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1
    • Lin, J.W., Wyszynski, M., Madvavan, R., Sealock, R., Kim, J.U., and Sheng, M. (1998). Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1. J. Neurosci. 18, 2017-2027.
    • (1998) J. Neurosci. , vol.18 , pp. 2017-2027
    • Lin, J.W.1    Wyszynski, M.2    Madvavan, R.3    Sealock, R.4    Kim, J.U.5    Sheng, M.6
  • 42
    • 0027360771 scopus 로고
    • Panning transfected cells for electrophysiological studies
    • Margolskee, R.F., McHendry-Rinde, B., and Horn, R. (1993). Panning transfected cells for electrophysiological studies. Biotechniques 15, 906-911.
    • (1993) Biotechniques , vol.15 , pp. 906-911
    • Margolskee, R.F.1    McHendry-Rinde, B.2    Horn, R.3
  • 43
    • 0028926916 scopus 로고
    • Functional role of the β subunit of high conductance calcium-activated potassium channels
    • McManus, O.B., Helms, L.M.H., Pallanck, L., Ganetzky, B., Swanson, R., and Leonard, R.J. (1995). Functional role of the β subunit of high conductance calcium-activated potassium channels. Neuron 14, 645-650.
    • (1995) Neuron , vol.14 , pp. 645-650
    • McManus, O.B.1    Helms, L.M.H.2    Pallanck, L.3    Ganetzky, B.4    Swanson, R.5    Leonard, R.J.6
  • 44
    • 0028032296 scopus 로고
    • 14-3-3: Modulators of signaling proteins?
    • Morrison, D. (1994). 14-3-3: Modulators of signaling proteins? SciEnce 266, 56-57.
    • (1994) Science , vol.266 , pp. 56-57
    • Morrison, D.1
  • 46
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A.J., Tanner, J.W., Allen, P.M., and Shaw, A.S. (1996). Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84, 889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 47
    • 0032510974 scopus 로고    scopus 로고
    • Reconstitution of β-adrenergic modulation of large conductance, calcium-activated potassium (Maxi-K) channels in Xenopus oocytes
    • Nara, M., Dhulipala, P.D.K., Wang, Y.-X., and Kotlikoff, M.I. (1998). Reconstitution of β-adrenergic modulation of large conductance, calcium-activated potassium (Maxi-K) channels in Xenopus oocytes. J. Biol. Chem. 273, 14920-14924.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14920-14924
    • Nara, M.1    Dhulipala, P.D.K.2    Wang, Y.-X.3    Kotlikoff, M.I.4
  • 49
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T., and Scott, J.D. (1997). Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 50
    • 0029042633 scopus 로고
    • Kinase and phosphatase activities intimately associated with a reconstituted calcium-dependent potassium channel
    • Reinhart, P.H., and Levitan, I.B. (1995). Kinase and phosphatase activities intimately associated with a reconstituted calcium-dependent potassium channel. J. Neurosci. 15, 4572-4579.
    • (1995) J. Neurosci. , vol.15 , pp. 4572-4579
    • Reinhart, P.H.1    Levitan, I.B.2
  • 51
    • 0025955210 scopus 로고
    • Modulation of calcium-activated potassium channels from rat brain by protein kinase A and phosphatase 2A
    • Reinhart, P.H., Chung, S.K., Martin, B.L., Brautigan, D.L., and LeviTan, I.B. (1991). Modulation of calcium-activated potassium channels from rat brain by protein kinase A and phosphatase 2A. J. Neurosci. 11, 1627-1635.
    • (1991) J. Neurosci. , vol.11 , pp. 1627-1635
    • Reinhart, P.H.1    Chung, S.K.2    Martin, B.L.3    Brautigan, D.L.4    Levitan, I.B.5
  • 53
    • 0026596694 scopus 로고
    • Presynaptic calcium signals and transmitter release are modulated by calcium-activated potassium channels
    • Robitaille, R., and Charlton, M.P. (1992). Presynaptic calcium signals and transmitter release are modulated by calcium-activated potassium channels. J. Neurosci. 12, 297-305.
    • (1992) J. Neurosci. , vol.12 , pp. 297-305
    • Robitaille, R.1    Charlton, M.P.2
  • 54
    • 0027365126 scopus 로고
    • Functional colocalization of calcium and calcium-gated potassium channels in control of transmitter release
    • Robitaille, R., Garcia, M.L., Kaczorowski, G.J., and Charlton, M.P. (1993). Functional colocalization of calcium and calcium-gated potassium channels in control of transmitter release. Neuron 11, 645-655.
    • (1993) Neuron , vol.11 , pp. 645-655
    • Robitaille, R.1    Garcia, M.L.2    Kaczorowski, G.J.3    Charlton, M.P.4
  • 57
    • 0030852701 scopus 로고    scopus 로고
    • A novel calcium-sensing domain in the BK channel
    • Schreiber, M., and Salkoff, L. (1997). A novel calcium-sensing domain in the BK channel. Biophys. J. 73, 1355-1363.
    • (1997) Biophys. J. , vol.73 , pp. 1355-1363
    • Schreiber, M.1    Salkoff, L.2
  • 58
    • 0030035145 scopus 로고    scopus 로고
    • Activation of protein kinase C inhibits calcium-activated potassium channels in rat pituitary tumour cells
    • Shipston, M.J., and Armstrong, D.L. (1996). Activation of protein kinase C inhibits calcium-activated potassium channels in rat pituitary tumour cells. J. Physiol. 493, 665-672.
    • (1996) J. Physiol. , vol.493 , pp. 665-672
    • Shipston, M.J.1    Armstrong, D.L.2
  • 59
    • 0030294611 scopus 로고    scopus 로고
    • Olfactory learning deficits in mutants for leonardo, a Drosophila gene encoding a 14-3-3 protein
    • Skoulakis, E.M.C., and Davis, R.L. (1996). Olfactory learning deficits in mutants for leonardo, a Drosophila gene encoding a 14-3-3 protein. Neuron 17, 931-944.
    • (1996) Neuron , vol.17 , pp. 931-944
    • Skoulakis, E.M.C.1    Davis, R.L.2
  • 60
    • 0001868286 scopus 로고
    • P element-mediated transformation
    • D.B. Roberts, ed. (Oxford: IRL Press)
    • Spradling, A.C. (1986). P element-mediated transformation. In Drosophila: A Practical Approach, D.B. Roberts, ed. (Oxford: IRL Press), pp. 175-197.
    • (1986) Drosophila: A Practical Approach , pp. 175-197
    • Spradling, A.C.1
  • 61
    • 0026529594 scopus 로고
    • Characterization of a Drosophila melanogaster gene similar to the mammalian genes encoding the tyrosine/tryptophan hydroxylase activator and protein kinase C inhibitor proteins
    • Swanson, K.D., and Ganguly, R. (1992). Characterization of a Drosophila melanogaster gene similar to the mammalian genes encoding the tyrosine/tryptophan hydroxylase activator and protein kinase C inhibitor proteins. Gene 113, 183-190.
    • (1992) Gene , vol.113 , pp. 183-190
    • Swanson, K.D.1    Ganguly, R.2
  • 62
    • 0028090250 scopus 로고
    • Binding of the nicotinic acetylcholine receptor to SH2 domains of Fyn and Fyk protein tyrosine kinases
    • Swope, S.L., and Huganir, R.L. (1994). Binding of the nicotinic acetylcholine receptor to SH2 domains of Fyn and Fyk protein tyrosine kinases. J. Biol. Chem. 269, 29817-29824.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29817-29824
    • Swope, S.L.1    Huganir, R.L.2
  • 63
    • 0026693501 scopus 로고
    • Phosphorylation of ligand-gated ion channels: A possible mode of synaptic plasticity
    • Swope, S.L., Moss, S.J., Blackstone, C.D., and Huganir, R.L. (1992). Phosphorylation of ligand-gated ion channels: A possible mode of synaptic plasticity. FASEB J. 6, 2514-2523.
    • (1992) FASEB J. , vol.6 , pp. 2514-2523
    • Swope, S.L.1    Moss, S.J.2    Blackstone, C.D.3    Huganir, R.L.4
  • 65
    • 0032577674 scopus 로고    scopus 로고
    • Glucocorticoid regulation of calcium-activated potassium channels mediated by serine/threonine protein phosphatase
    • Tian, L., Knaus, H.-G., and Shipston, M.J. (1998). Glucocorticoid regulation of calcium-activated potassium channels mediated by serine/threonine protein phosphatase. J. Biol. Chem. 273, 13531-13536.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13531-13536
    • Tian, L.1    Knaus, H.-G.2    Shipston, M.J.3
  • 67
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • Tzivion, G., Luo, Z., and Avruch, J. (1998). A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity. Nature 394, 88-92.
    • (1998) Nature , vol.394 , pp. 88-92
    • Tzivion, G.1    Luo, Z.2    Avruch, J.3
  • 69
    • 0028956758 scopus 로고
    • Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase
    • Wallace, B.C. (1995). Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase. J. Cell Biol. 128, 1121-1129.
    • (1995) J. Cell Biol. , vol.128 , pp. 1121-1129
    • Wallace, B.C.1
  • 70
    • 0028578762 scopus 로고
    • Concomitant alterations of physiological and developmental plasticity at CaM kinase II-inhibited synapses in Drosophila
    • Wang, J., Renger, J., Griffith, L.C., Greenspan, R.J., and Wu, C.-F. (1994). Concomitant alterations of physiological and developmental plasticity at CaM kinase II-inhibited synapses in Drosophila. Neuron 13, 1373-1384.
    • (1994) Neuron , vol.13 , pp. 1373-1384
    • Wang, J.1    Renger, J.2    Griffith, L.C.3    Greenspan, R.J.4    Wu, C.-F.5
  • 73
    • 0027531062 scopus 로고
    • Potassium channel stimulation by natriuretic peptides through cGMP-dependent dephosphorylation
    • White, R.E., Lee, A.B., Shcherbatko, A.D., Lincoln, T.M., Schonbrunn, A., and Armstrong, D.L. (1993). Potassium channel stimulation by natriuretic peptides through cGMP-dependent dephosphorylation. Nature 361, 263-266.
    • (1993) Nature , vol.361 , pp. 263-266
    • White, R.E.1    Lee, A.B.2    Shcherbatko, A.D.3    Lincoln, T.M.4    Schonbrunn, A.5    Armstrong, D.L.6
  • 75
    • 0032053989 scopus 로고    scopus 로고
    • dSlo interacting protein 1, a novel protein that interacts with large-conductance calcium-activated potassium channels
    • Xia, X.-M., Hirschberg, B., Smolik, S., Forte, M., and Adelman, J.P. (1998b). dSlo interacting protein 1, a novel protein that interacts with large-conductance calcium-activated potassium channels. J. Neurosci. 18, 2360-2369.
    • (1998) J. Neurosci. , vol.18 , pp. 2360-2369
    • Xia, X.-M.1    Hirschberg, B.2    Smolik, S.3    Forte, M.4    Adelman, J.P.5
  • 76
    • 18544393408 scopus 로고    scopus 로고
    • Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins
    • Xiao, B., Tu, J.C., Petralia, R.S., Yuan, J.P., Doan, A., Breder, C.D., Ruggiero, A., Lanahan, A.A., Wenthold, R.J., and Worley, P.F. (1998). Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins. Neuron 21, 707-716.
    • (1998) Neuron , vol.21 , pp. 707-716
    • Xiao, B.1    Tu, J.C.2    Petralia, R.S.3    Yuan, J.P.4    Doan, A.5    Breder, C.D.6    Ruggiero, A.7    Lanahan, A.A.8    Wenthold, R.J.9    Worley, P.F.10
  • 78
    • 0031053363 scopus 로고    scopus 로고
    • NMDA channel regulation by channel-associated protein tyrosine kinase Src
    • Yu, X.-M., Askalan, R., Keil, G.J., and Salter, M.W. (1997). NMDA channel regulation by channel-associated protein tyrosine kinase Src. Science 275, 674-678.
    • (1997) Science , vol.275 , pp. 674-678
    • Yu, X.-M.1    Askalan, R.2    Keil, G.J.3    Salter, M.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.