메뉴 건너뛰기




Volumn 40, Issue 6, 2003, Pages 1185-1197

Regulation of the Ca2+/CaM-responsive pool of CaMKII by scaffold-dependent autophosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

GUANYLATE KINASE; PROTEIN CMG; PROTEIN KINASE (CALCIUM,CALMODULIN) II; UNCLASSIFIED DRUG;

EID: 0347993183     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(03)00786-4     Document Type: Article
Times cited : (94)

References (58)
  • 1
    • 0035859082 scopus 로고    scopus 로고
    • Interaction with the NMDA receptor locks CaMKII in an active conformation
    • Bayer K.U., De Koninck P., Leonard A.S., Hell J.W., Schulman H. Interaction with the NMDA receptor locks CaMKII in an active conformation. Nature. 411:2001;801-805.
    • (2001) Nature , vol.411 , pp. 801-805
    • Bayer, K.U.1    De Koninck, P.2    Leonard, A.S.3    Hell, J.W.4    Schulman, H.5
  • 2
    • 0035930919 scopus 로고    scopus 로고
    • Regulation of signal transduction by protein targeting: The case for CaMKII
    • Bayer K.U., Schulman H. Regulation of signal transduction by protein targeting. the case for CaMKII Biochem. Biophys. Res. Commun. 289:2001;917-923.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 917-923
    • Bayer, K.U.1    Schulman H.f2
  • 4
    • 0035930572 scopus 로고    scopus 로고
    • CASK and protein 4.1 support F-actin nucleation on neurexins
    • Biederer T., Sudhof T.C. CASK and protein 4.1 support F-actin nucleation on neurexins. J. Biol. Chem. 276:2001;47869-47876.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47869-47876
    • Biederer, T.1    Sudhof, T.C.2
  • 5
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand A.H., Perrimon N. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development. 118:1993;401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 7
    • 0030469153 scopus 로고    scopus 로고
    • Synapse maturation and structural plasticity at Drosophila neuromuscular junctions
    • Budnik V. Synapse maturation and structural plasticity at Drosophila neuromuscular junctions. Curr. Opin. Neurobiol. 6:1996;858-867.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 858-867
    • Budnik, V.1
  • 8
    • 0032544613 scopus 로고    scopus 로고
    • A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain
    • Butz S., Okamoto M., Sudhof T.C. A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Cell. 94:1998;773-782.
    • (1998) Cell , vol.94 , pp. 773-782
    • Butz, S.1    Okamoto, M.2    Sudhof, T.C.3
  • 9
    • 0036703649 scopus 로고    scopus 로고
    • Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms
    • Chetkovich D.M., Bunn R.C., Kuo S.H., Kawasaki Y., Kohwi M., Bredt D.S. Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms. J. Neurosci. 22:2002;6415-6425.
    • (2002) J. Neurosci. , vol.22 , pp. 6415-6425
    • Chetkovich, D.M.1    Bunn, R.C.2    Kuo, S.H.3    Kawasaki, Y.4    Kohwi, M.5    Bredt, D.S.6
  • 10
    • 0027340006 scopus 로고
    • 2+/calmodulin-dependent protein kinase II by basal autophosphorylation
    • 2+/calmodulin-dependent protein kinase II by basal autophosphorylation. J. Biol. Chem. 268:1993;7163-7170.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7163-7170
    • Colbran, R.J.1
  • 11
    • 0025301783 scopus 로고
    • Calcium/calmodulin-independent autophosphorylation sites of calcium/calmodulin-dependent protein kinase II
    • Colbran R.J., Soderling T.R. Calcium/calmodulin-independent autophosphorylation sites of calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 265:1990;11213-11219.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11213-11219
    • Colbran, R.J.1    Soderling, T.R.2
  • 12
    • 0024558374 scopus 로고
    • Regulatory domain of calcium/calmodulin-dependent protein kinase II. Mechanism of inhibition and regulation by phosphorylation
    • Colbran R.J., Smith M.K., Schworer C.M., Fong Y.L., Soderling T.R. Regulatory domain of calcium/calmodulin-dependent protein kinase II. Mechanism of inhibition and regulation by phosphorylation. J. Biol. Chem. 264:1989;4800-4804.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4800-4804
    • Colbran, R.J.1    Smith, M.K.2    Schworer, C.M.3    Fong, Y.L.4    Soderling, T.R.5
  • 13
    • 0030910976 scopus 로고    scopus 로고
    • Camguk, Lin-2, and CASK: Novel membrane-associated guanylate kinase homologs that also contain CaM kinase domains
    • Dimitratos S.D., Woods D.F., Bryant P.J. Camguk, Lin-2, and CASK. novel membrane-associated guanylate kinase homologs that also contain CaM kinase domains Mech. Dev. 63:1997;127-130.
    • (1997) Mech. Dev. , vol.63 , pp. 127-130
    • Dimitratos, S.D.1    Woods, D.F.2    Bryant, P.J.3
  • 15
    • 0037088921 scopus 로고    scopus 로고
    • Rapid synaptic remodeling by protein kinase C: Reciprocal translocation of NMDA receptors and calcium/calmodulin-dependent kinase II
    • Fong D.K., Rao A., Crump F.T., Craig A.M. Rapid synaptic remodeling by protein kinase C. reciprocal translocation of NMDA receptors and calcium/calmodulin-dependent kinase II J. Neurosci. 22:2002;2153-2164.
    • (2002) J. Neurosci. , vol.22 , pp. 2153-2164
    • Fong, D.K.1    Rao, A.2    Crump, F.T.3    Craig, A.M.4
  • 16
    • 0020406591 scopus 로고
    • Male courtship in Drosophila: The conditioned response to immature males and its genetic control
    • Gailey D.A., Jackson F.R., Siegel R.W. Male courtship in Drosophila: The conditioned response to immature males and its genetic control. Genetics. 102:1982;771-782.
    • (1982) Genetics , vol.102 , pp. 771-782
    • Gailey, D.A.1    Jackson, F.R.2    Siegel, R.W.3
  • 17
    • 0035282948 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II and postsynaptic density 95 for binding to the NR2A subunit of the NMDA receptor
    • 2+/calmodulin-dependent protein kinase II and postsynaptic density 95 for binding to the NR2A subunit of the NMDA receptor. J. Neurosci. 21:2001;1501-1509.
    • (2001) J. Neurosci. , vol.21 , pp. 1501-1509
    • Gardoni, F.1    Schrama, L.H.2    Kamal, A.3    Gispen, W.H.4    Cattabeni, F.5    Di Luca, M.6
  • 18
    • 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., Greenspan R.J. Inhibition of calcium/calmodulin-dependent protein kinase in Drosophila disrupts behavioral plasticity. Neuron. 10:1993;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    Greenspan, R.J.5
  • 19
    • 0026806967 scopus 로고
    • 2+/ calmodulin-dependent protein kinase analyzed by site-directed mutagenesis
    • 2+/calmodulin-dependent protein kinase analyzed by site-directed mutagenesis. J. Biol. Chem. 267:1992;17216-17224.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17216-17224
    • Hanson, P.I.1    Schulman, H.2
  • 20
    • 0028306195 scopus 로고
    • Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals
    • Hanson P.I., Meyer T., Stryer L., Schulman H. Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals. Neuron. 12:1994;943-956.
    • (1994) Neuron , vol.12 , pp. 943-956
    • Hanson, P.I.1    Meyer, T.2    Stryer, L.3    Schulman, H.4
  • 21
    • 0029914941 scopus 로고    scopus 로고
    • Cask: A novel dlg/PSD95 homolog with an n-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins
    • Hata Y., Butz S., Sudhof T.C. Cask. a novel dlg/PSD95 homolog with an n-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins J. Neurosci. 16:1996;2488-2494.
    • (1996) J. Neurosci. , vol.16 , pp. 2488-2494
    • Hata, Y.1    Butz, S.2    Sudhof, T.C.3
  • 22
    • 0030067804 scopus 로고    scopus 로고
    • The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins
    • Hoskins R., Hajnal A.F., Harp S.A., Kim S.K. The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins. Development. 122:1996;97-111.
    • (1996) Development , vol.122 , pp. 97-111
    • Hoskins, R.1    Hajnal, A.F.2    Harp, S.A.3    Kim, S.K.4
  • 23
    • 0034673760 scopus 로고    scopus 로고
    • Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
    • Hsueh Y.P., Wang T.F., Yang F.C., Sheng M. Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2. Nature. 404:2000;298-302.
    • (2000) Nature , vol.404 , pp. 298-302
    • Hsueh, Y.P.1    Wang, T.F.2    Yang, F.C.3    Sheng, M.4
  • 24
    • 0032514263 scopus 로고    scopus 로고
    • Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    • Hsueh Y.P., Yang F.C., Kharazia V., Naisbitt S., Cohen A.R., Weinberg R.J., Sheng M. Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses. J. Cell Biol. 142:1998;139-151.
    • (1998) J. Cell Biol. , vol.142 , pp. 139-151
    • Hsueh, Y.P.1    Yang, F.C.2    Kharazia, V.3    Naisbitt, S.4    Cohen, A.R.5    Weinberg, R.J.6    Sheng, M.7
  • 25
    • 0032920596 scopus 로고    scopus 로고
    • Mapping of the anatomical circuit of CaM kinase-dependent courtship conditioning in Drosophila
    • Joiner M.A., Griffith L.C. Mapping of the anatomical circuit of CaM kinase-dependent courtship conditioning in Drosophila. Learn. Mem. 6:1999;177-192.
    • (1999) Learn. Mem. , vol.6 , pp. 177-192
    • Joiner, M.A.1    Griffith, L.C.2
  • 26
    • 0033529567 scopus 로고    scopus 로고
    • Regulation of DLG localization at synapses by CaMKII-dependent phosphorylation
    • Koh Y.H., Popova E., Thomas U., Griffith L.C., Budnik V. Regulation of DLG localization at synapses by CaMKII-dependent phosphorylation. Cell. 98:1999;353-363.
    • (1999) Cell , vol.98 , pp. 353-363
    • Koh, Y.H.1    Popova, E.2    Thomas, U.3    Griffith, L.C.4    Budnik, V.5
  • 27
    • 0027959402 scopus 로고
    • Genetic analysis of Fasciclin II in Drosophila: Defasciculation, refasciculation, and altered fasciculation
    • Lin D.M., Fetter R.D., Kopczynski C., Grenningloh G., Goodman C.S. Genetic analysis of Fasciclin II in Drosophila. defasciculation, refasciculation, and altered fasciculation Neuron. 13:1994;1055-1069.
    • (1994) Neuron , vol.13 , pp. 1055-1069
    • Lin, D.M.1    Fetter, R.D.2    Kopczynski, C.3    Grenningloh, G.4    Goodman, C.S.5
  • 28
    • 0034731301 scopus 로고    scopus 로고
    • Identification and characterization of a SUMO-1 conjugation system that modifies neuronal calcium/calmodulin-dependent protein kinase II in Drosophila melanogaster
    • Long X., Griffith L.C. Identification and characterization of a SUMO-1 conjugation system that modifies neuronal calcium/calmodulin-dependent protein kinase II in Drosophila melanogaster. J. Biol. Chem. 275:2000;40765-40776.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40765-40776
    • Long, X.1    Griffith, L.C.2
  • 29
    • 0024348039 scopus 로고
    • 2+/calmodulin-dependent protein kinase
    • 2+/ calmodulin-dependent protein kinase. J. Neurosci. 9:1989;2020-2032.
    • (1989) J. Neurosci. , vol.9 , pp. 2020-2032
    • Lou, L.L.1    Schulman, H.2
  • 30
    • 0024461379 scopus 로고
    • Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP
    • Malinow R., Schulman H., Tsien R.W. Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP. Science. 245:1989;862-866.
    • (1989) Science , vol.245 , pp. 862-866
    • Malinow, R.1    Schulman, H.2    Tsien, R.W.3
  • 31
    • 0029922260 scopus 로고    scopus 로고
    • A new Drosophila Ca2+/calmodulin-dependent protein kinase (Caki) is localized in the central nervous system and implicated in walking speed
    • Martin J.-R., Ollo R. A new Drosophila Ca2+/calmodulin-dependent protein kinase (Caki) is localized in the central nervous system and implicated in walking speed. EMBO J. 15:1996;1865-1876.
    • (1996) EMBO J. , vol.15 , pp. 1865-1876
    • Martin, J.-R.1    Ollo, R.2
  • 32
    • 0040962408 scopus 로고    scopus 로고
    • Association of neuronal calcium channels with modular adaptor proteins
    • Maximov A., Sudhof T.C., Bezprozvanny I. Association of neuronal calcium channels with modular adaptor proteins. J. Biol. Chem. 274:1999;24453-24456.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24453-24456
    • Maximov, A.1    Sudhof, T.C.2    Bezprozvanny, I.3
  • 33
    • 0029066116 scopus 로고
    • CaMKII regulates the frequency-response function of hippocampal synapses for the production of both LTD and LTP
    • Mayford M., Wang J., Kandel E.R., O'Dell T.J. CaMKII regulates the frequency-response function of hippocampal synapses for the production of both LTD and LTP. Cell. 81:1995;891-904.
    • (1995) Cell , vol.81 , pp. 891-904
    • Mayford, M.1    Wang, J.2    Kandel, E.R.3    O'dell, T.J.4
  • 34
    • 0026718175 scopus 로고
    • Calmodulin trapping by calcium-calmodulin-dependent protein kinase
    • Meyer T., Hanson P.I., Stryer L., Schulman H. Calmodulin trapping by calcium-calmodulin-dependent protein kinase. Science. 256:1992;1199-1202.
    • (1992) Science , vol.256 , pp. 1199-1202
    • Meyer, T.1    Hanson, P.I.2    Stryer, L.3    Schulman, H.4
  • 35
    • 0037123779 scopus 로고    scopus 로고
    • Electrical silencing of Drosophila pacemaker neurons stops the free-running circadian clock
    • Nitabach M.N., Blau J., Holmes T.C. Electrical silencing of Drosophila pacemaker neurons stops the free-running circadian clock. Cell. 109:2002;485-495.
    • (2002) Cell , vol.109 , pp. 485-495
    • Nitabach, M.N.1    Blau, J.2    Holmes, T.C.3
  • 36
    • 0036848075 scopus 로고    scopus 로고
    • The Drosophila Wnt, wingless, provides an essential signal for pre- and postsynaptic differentiation
    • Packard M., Koo E.S., Gorczyca M., Sharpe J., Cumberledge S., Budnik V. The Drosophila Wnt, wingless, provides an essential signal for pre- and postsynaptic differentiation. Cell. 111:2002;319-330.
    • (2002) Cell , vol.111 , pp. 319-330
    • Packard, M.1    Koo, E.S.2    Gorczyca, M.3    Sharpe, J.4    Cumberledge, S.5    Budnik, V.6
  • 37
    • 0036087316 scopus 로고    scopus 로고
    • Regulation of neuronal excitability in Drosophila by constitutively active CaMKII
    • Park D., Coleman M.J., Hodge J.J.L., Budnik V., Griffith L.C. Regulation of neuronal excitability in Drosophila by constitutively active CaMKII. J. Neurobiol. 52:2002;24-42.
    • (2002) J. Neurobiol. , vol.52 , pp. 24-42
    • Park, D.1    Coleman, M.J.2    Hodge, J.J.L.3    Budnik, V.4    Griffith, L.C.5
  • 38
    • 0025294106 scopus 로고
    • 2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain
    • 2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain. J. Biol. Chem. 265:1990;11204-11212.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11204-11212
    • Patton, B.L.1    Miller, S.G.2    Kennedy, M.B.3
  • 39
    • 0000639902 scopus 로고
    • Identification of functionally significant phosphorylation sites on neuronal proteins and preparation of antibodies that recognize them
    • Patton B.L., Miller S.G., Kennedy M.B. Identification of functionally significant phosphorylation sites on neuronal proteins and preparation of antibodies that recognize them. Methods Neurosci. 6:1991;158-176.
    • (1991) Methods Neurosci. , vol.6 , pp. 158-176
    • Patton, B.L.1    Miller, S.G.2    Kennedy, M.B.3
  • 40
    • 0023932685 scopus 로고
    • Calcium/calmodulin-dependent protein kinase II. Characterization of distinct calmodulin binding and inhibitory domains
    • Payne M.E., Fong Y.L., Ono T., Colbran R.J., Kemp B.E., Soderling T.R., Means A.R. Calcium/calmodulin-dependent protein kinase II. Characterization of distinct calmodulin binding and inhibitory domains. J. Biol. Chem. 263:1988;7190-7195.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7190-7195
    • Payne, M.E.1    Fong, Y.L.2    Ono, T.3    Colbran, R.J.4    Kemp, B.E.5    Soderling, T.R.6    Means, A.R.7
  • 41
    • 0042848901 scopus 로고    scopus 로고
    • Activity-dependent remodeling of presynaptic inputs by postsynaptic expression of activated CaMKII
    • Pratt K.G., Watt A.J., Griffith L.C., Nelson S.B., Turrigiano G.G. Activity-dependent remodeling of presynaptic inputs by postsynaptic expression of activated CaMKII. Neuron. 39:2003;269-281.
    • (2003) Neuron , vol.39 , pp. 269-281
    • Pratt, K.G.1    Watt, A.J.2    Griffith, L.C.3    Nelson, S.B.4    Turrigiano, G.G.5
  • 43
    • 0033515884 scopus 로고    scopus 로고
    • Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation
    • Shen K., Meyer T. Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation. Science. 284:1999;162-166.
    • (1999) Science , vol.284 , pp. 162-166
    • Shen, K.1    Meyer, T.2
  • 44
    • 0032148396 scopus 로고    scopus 로고
    • CaMKIIβ functions as an F-actin targeting module that localizes CaMKIIα/β heterooligomers to dendritic spines
    • Shen K., Teruel M.N., Subramanian K., Meyer T. CaMKIIβ functions as an F-actin targeting module that localizes CaMKIIα/β heterooligomers to dendritic spines. Neuron. 21:1998;593-606.
    • (1998) Neuron , vol.21 , pp. 593-606
    • Shen, K.1    Teruel, M.N.2    Subramanian, K.3    Meyer, T.4
  • 45
    • 0018413205 scopus 로고
    • Conditioned responses in courtship behavior of normal and mutant Drosophila
    • Siegel R.W., Hall J.C. Conditioned responses in courtship behavior of normal and mutant Drosophila. Proc. Natl. Acad. Sci. USA. 76:1979;565-578.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 565-578
    • Siegel, R.W.1    Hall, J.C.2
  • 46
    • 0026526799 scopus 로고
    • Functional determinants in the autoinhibitory domain of calcium/calmodulin-dependent protein kinase II
    • Smith M.K., Colbran R.J., Brickey D.A., Soderling T.R. Functional determinants in the autoinhibitory domain of calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 267:1992;1761-1768.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1761-1768
    • Smith, M.K.1    Colbran, R.J.2    Brickey, D.A.3    Soderling, T.R.4
  • 47
    • 0030446290 scopus 로고    scopus 로고
    • Deficiency of protein phosphatase 2A uncouples the nuclear and centrosome cycles and prevents attachment of microtubules to the kinetochore in Drosophila microtubule star (mts) embryos
    • Snaith H.A., Armstrong C.G., Guo Y., Kaiser K., Cohen P.T. Deficiency of protein phosphatase 2A uncouples the nuclear and centrosome cycles and prevents attachment of microtubules to the kinetochore in Drosophila microtubule star (mts) embryos. J. Cell Sci. 109:1996;3001-3012.
    • (1996) J. Cell Sci. , vol.109 , pp. 3001-3012
    • Snaith, H.A.1    Armstrong, C.G.2    Guo, Y.3    Kaiser, K.4    Cohen, P.T.5
  • 48
    • 0028486257 scopus 로고
    • The role of calcium-calmodulin kinase II in three forms of synaptic plasticity
    • Stevens C.F., Tonegawa S., Wang Y. The role of calcium-calmodulin kinase II in three forms of synaptic plasticity. Curr. Biol. 4:1994;687-693.
    • (1994) Curr. Biol. , vol.4 , pp. 687-693
    • Stevens, C.F.1    Tonegawa, S.2    Wang, Y.3
  • 49
    • 0032516819 scopus 로고    scopus 로고
    • Autophosphorylation-dependent targeting of calcium/calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl-D-aspartate receptor
    • Strack S., Colbran R.J. Autophosphorylation-dependent targeting of calcium/calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl-D-aspartate receptor. J. Biol. Chem. 273:1998;20689-20692.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20689-20692
    • Strack, S.1    Colbran, R.J.2
  • 50
    • 0030946102 scopus 로고    scopus 로고
    • Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density
    • Strack S., Choi S., Lovinger D.M., Colbran R.J. Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density. J. Biol. Chem. 272:1997;13467-13470.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13467-13470
    • Strack, S.1    Choi, S.2    Lovinger, D.M.3    Colbran, R.J.4
  • 51
    • 0034682735 scopus 로고    scopus 로고
    • Association of calcium/calmodulin-dependent kinase II with developmentally regulated splice variants of the postsynaptic density protein densin-180
    • Strack S., Robison A.J., Bass M.A., Colbran R.J. Association of calcium/calmodulin-dependent kinase II with developmentally regulated splice variants of the postsynaptic density protein densin-180. J. Biol. Chem. 275:2000;25061-25064.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25061-25064
    • Strack, S.1    Robison, A.J.2    Bass, M.A.3    Colbran, R.J.4
  • 52
    • 0020852539 scopus 로고
    • Conditioned courtship in Drosophila and its mediation by association of chemical cues
    • Tompkins L., Siegel R.W., Gailey D.A., Hall J.C. Conditioned courtship in Drosophila and its mediation by association of chemical cues. Behav. Genet. 13:1983;565-578.
    • (1983) Behav. Genet. , vol.13 , pp. 565-578
    • Tompkins, L.1    Siegel, R.W.2    Gailey, D.A.3    Hall, J.C.4
  • 53
    • 0035863159 scopus 로고    scopus 로고
    • Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin
    • Walikonis R.S., Oguni A., Khorosheva E.M., Jeng C.J., Asuncion F.J., Kennedy M.B. Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin. J. Neurosci. 21:2001;423-433.
    • (2001) J. Neurosci. , vol.21 , pp. 423-433
    • Walikonis, R.S.1    Oguni, A.2    Khorosheva, E.M.3    Jeng, C.J.4    Asuncion, F.J.5    Kennedy, M.B.6
  • 54
    • 0031595594 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II by autophosphorylation analyzed by site-directed mutagenesis
    • 2+/calmodulin-dependent protein kinase II by autophosphorylation analyzed by site-directed mutagenesis. J. Neurochem. 71:1998;378-387.
    • (1998) J. Neurochem. , vol.71 , pp. 378-387
    • Wang, Z.1    Palmer, G.2    Griffith, L.C.3
  • 55
    • 0032498213 scopus 로고    scopus 로고
    • Stabilization of dendritic arbor structure in vivo by CaMKII
    • Wu G.Y., Cline H.T. Stabilization of dendritic arbor structure in vivo by CaMKII. Science. 279:1998;222-226.
    • (1998) Science , vol.279 , pp. 222-226
    • Wu, G.Y.1    Cline, H.T.2
  • 56
    • 0020623145 scopus 로고
    • Potassium currents in Drosophila: Different components affected by mutations of two genes
    • Wu C.F., Ganetzky B., Haugland F.N., Liu A.X. Potassium currents in Drosophila: different components affected by mutations of two genes. Science. 220:1983;1076-1078.
    • (1983) Science , vol.220 , pp. 1076-1078
    • Wu, C.F.1    Ganetzky, B.2    Haugland, F.N.3    Liu, A.X.4
  • 57
    • 0033543561 scopus 로고    scopus 로고
    • Structural examination of autoregulation of multifunctional calcium/calmodulin-dependent protein kinase II
    • Yang E., Schulman H. Structural examination of autoregulation of multifunctional calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 274:1999;26199-26208.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26199-26208
    • Yang, E.1    Schulman, H.2
  • 58
    • 0018692044 scopus 로고
    • Learning as a process of selection and amplification
    • Young J.Z. Learning as a process of selection and amplification. J. R. Soc. Med. 72:1979;801-814.
    • (1979) J. R. Soc. Med. , vol.72 , pp. 801-814
    • Young, J.Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.