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Volumn 105, Issue 31, 2008, Pages 10768-10773

An allosteric model of calmodulin explains differential activation of PP2B and CaMKII (Proceedings of the National Academy of Sciences of the United States of America (2008) 105, 31, (10768-10773) DOI: 10.1073/pnas.0804672105);An allosteric model of calmodulin explains differential activation of PP2B and CaMKII

Author keywords

Allostery; Calcium binding; Conformational transition; Cooperativity; Synaptic plasticity

Indexed keywords

CALCINEURIN; CALCIUM; CALMODULIN; PROTEIN KINASE (CALCIUM,CALMODULIN) II;

EID: 49449096617     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0810309105     Document Type: Erratum
Times cited : (70)

References (64)
  • 1
    • 0015799240 scopus 로고
    • Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path
    • Bliss TV, Lomo T (1973) Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path. J Physiol 232:331-356.
    • (1973) J Physiol , vol.232 , pp. 331-356
    • Bliss, T.V.1    Lomo, T.2
  • 2
    • 0034042406 scopus 로고    scopus 로고
    • Synaptic plasticity and memory: An evaluation of the hypothesis
    • Martin SJ, Grimwood PD, Morris RG (2000) Synaptic plasticity and memory: An evaluation of the hypothesis. Annu Rev Neurosci 23:649-711.
    • (2000) Annu Rev Neurosci , vol.23 , pp. 649-711
    • Martin, S.J.1    Grimwood, P.D.2    Morris, R.G.3
  • 3
    • 0024341227 scopus 로고
    • A mechanism for the Hebb and the anti-Hebb processes underlying learning and memory
    • Lisman J (1989) A mechanism for the Hebb and the anti-Hebb processes underlying learning and memory. Proc Natl Acad Sci USA 86:9574-9578.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9574-9578
    • Lisman, J.1
  • 4
    • 0017854367 scopus 로고
    • Stimulation of brain membrane protein phosphorylation by calcium and an endogenous heat-stable protein
    • Schulman H, Greengard P (1978) Stimulation of brain membrane protein phosphorylation by calcium and an endogenous heat-stable protein. Nature 271:478-479.
    • (1978) Nature , vol.271 , pp. 478-479
    • Schulman, H.1    Greengard, P.2
  • 5
    • 0018040458 scopus 로고    scopus 로고
    • Schulman H, Greengard P (1978) Ca2+-dependent protein phosphorylation system in membranes from various tissues, and its activation by calcium-dependent regulator. Proc Natl Acad Sci USA 75:5432-5436.
    • Schulman H, Greengard P (1978) Ca2+-dependent protein phosphorylation system in membranes from various tissues, and its activation by "calcium-dependent regulator." Proc Natl Acad Sci USA 75:5432-5436.
  • 6
    • 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
  • 7
    • 0034702259 scopus 로고    scopus 로고
    • Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity
    • Lee HK, Barbarosie M, Kameyama K, Bear MF, Huganir RL (2000) Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity. Nature 405:955-959.
    • (2000) Nature , vol.405 , pp. 955-959
    • Lee, H.K.1    Barbarosie, M.2    Kameyama, K.3    Bear, M.F.4    Huganir, R.L.5
  • 8
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction
    • Hayashi Y, et al. (2000) Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction. Science 287:2262-2267.
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1
  • 9
    • 0026742451 scopus 로고
    • Impaired spatial learning in alpha-calcium-calmodulin kinase II mutant mice
    • Silva AJ, Paylor R, Wehner JM, Tonegawa S (1992) Impaired spatial learning in alpha-calcium-calmodulin kinase II mutant mice. Science 257:206-211.
    • (1992) Science , vol.257 , pp. 206-211
    • Silva, A.J.1    Paylor, R.2    Wehner, J.M.3    Tonegawa, S.4
  • 11
    • 0016156102 scopus 로고
    • Cyclic 3:5-nucleotide phosphodiesterase. Purification, characterization, and active form of the protein activator from bovine brain
    • Lin YM, Liu YP, Cheung WY (1974) Cyclic 3:5-nucleotide phosphodiesterase. Purification, characterization, and active form of the protein activator from bovine brain. J Biol Chem 249:4943-4954.
    • (1974) J Biol Chem , vol.249 , pp. 4943-4954
    • Lin, Y.M.1    Liu, Y.P.2    Cheung, W.Y.3
  • 12
    • 16344391174 scopus 로고    scopus 로고
    • The role of calmodulin as a signal integrator for synaptic plasticity
    • Xia Z, Storm DR (2005) The role of calmodulin as a signal integrator for synaptic plasticity. Nat Rev Neurosci 6:267-276.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 267-276
    • Xia, Z.1    Storm, D.R.2
  • 13
    • 0019320688 scopus 로고
    • The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain
    • Watterson DM, Sharief F, Vanaman TC (1980) The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain. J Biol Chem 255:962-975.
    • (1980) J Biol Chem , vol.255 , pp. 962-975
    • Watterson, D.M.1    Sharief, F.2    Vanaman, T.C.3
  • 14
    • 0029159794 scopus 로고
    • Solution structure of calcium-free calmodulin
    • Kuboniwa H, et al. (1995) Solution structure of calcium-free calmodulin. Nat Struct Biol 2:768-776.
    • (1995) Nat Struct Biol , vol.2 , pp. 768-776
    • Kuboniwa, H.1
  • 15
    • 0021881565 scopus 로고
    • Three-dimensional structure of calmodulin
    • Babu YS, et al. (1985) Three-dimensional structure of calmodulin. Nature 315:37-40.
    • (1985) Nature , vol.315 , pp. 37-40
    • Babu, Y.S.1
  • 16
    • 0018967724 scopus 로고
    • Positive cooperative binding of calcium to bovine brain calmodulin
    • Crouch TH, Klee CB (1980) Positive cooperative binding of calcium to bovine brain calmodulin. Biochemistry 19:3692-3698.
    • (1980) Biochemistry , vol.19 , pp. 3692-3698
    • Crouch, T.H.1    Klee, C.B.2
  • 17
    • 0022500180 scopus 로고
    • Direct comparison of Ca2+ requirements for calmodulin interaction with and activation of protein phosphatase
    • Kincaid RL, Vaughan M (1986) Direct comparison of Ca2+ requirements for calmodulin interaction with and activation of protein phosphatase. Proc Natl Acad Sci USA 83:1193-1197.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 1193-1197
    • Kincaid, R.L.1    Vaughan, M.2
  • 18
    • 33749343007 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase II (CaMKII) is activated by calmodulin with two bound calciums
    • Shifman JM, Choi MH, Mihalas S, Mayo SL, Kennedy MB (2006) Ca2+/calmodulin-dependent protein kinase II (CaMKII) is activated by calmodulin with two bound calciums. Proc Natl Acad Sci USA 103:13968-13973.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13968-13973
    • Shifman, J.M.1    Choi, M.H.2    Mihalas, S.3    Mayo, S.L.4    Kennedy, M.B.5
  • 19
    • 0021100478 scopus 로고
    • Free energy coupling in the interactions between Ca2+, calmodulin, and phosphorylase kinase
    • Burger D, Stein EA, Cox JA (1983) Free energy coupling in the interactions between Ca2+, calmodulin, and phosphorylase kinase. J Biol Chem 258:14733-14739.
    • (1983) J Biol Chem , vol.258 , pp. 14733-14739
    • Burger, D.1    Stein, E.A.2    Cox, J.A.3
  • 20
    • 0021129756 scopus 로고
    • Quantitation of energy coupling between Ca2+, calmodulin, skeletal muscle myosin light chain kinase, and kinase substrates
    • Olwin BB, Edelman AM, Krebs EG, Storm DR (1984) Quantitation of energy coupling between Ca2+, calmodulin, skeletal muscle myosin light chain kinase, and kinase substrates. J Biol Chem 259:10949-10955.
    • (1984) J Biol Chem , vol.259 , pp. 10949-10955
    • Olwin, B.B.1    Edelman, A.M.2    Krebs, E.G.3    Storm, D.R.4
  • 21
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux JP (1965) On the nature of allosteric transitions: A plausible model. J Mol Biol 12:88-118.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 22
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex
    • Meador WE, Means AR, Quiocho FA (1992) Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Science 257:1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 23
    • 31044452100 scopus 로고    scopus 로고
    • Structure of calmodulin bound to a calcineurin peptide: A new way of making an old binding mode
    • Ye Q, Li X, Wong A, Wei Q, Jia Z (2006) Structure of calmodulin bound to a calcineurin peptide: A new way of making an old binding mode. Biochemistry 45:738-745.
    • (2006) Biochemistry , vol.45 , pp. 738-745
    • Ye, Q.1    Li, X.2    Wong, A.3    Wei, Q.4    Jia, Z.5
  • 24
    • 0014014862 scopus 로고
    • On the nature of allosteric transitions: Implications of non-exclusive ligand binding
    • Rubin MM, Changeux JP (1966) On the nature of allosteric transitions: Implications of non-exclusive ligand binding. J Mol Biol 21:265-274.
    • (1966) J Mol Biol , vol.21 , pp. 265-274
    • Rubin, M.M.1    Changeux, J.P.2
  • 25
    • 0030987202 scopus 로고    scopus 로고
    • Intermolecular tuning of calmodulin by target peptides and proteins: Differential effects on Ca2+ binding and implications for kinase activation
    • Peersen OB, Madsen TS, Falke JJ (1997) Intermolecular tuning of calmodulin by target peptides and proteins: Differential effects on Ca2+ binding and implications for kinase activation. Protein Sci 6:794-807.
    • (1997) Protein Sci , vol.6 , pp. 794-807
    • Peersen, O.B.1    Madsen, T.S.2    Falke, J.J.3
  • 26
    • 0030008340 scopus 로고    scopus 로고
    • Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences
    • Bayley PM, Findlay WA, Martin SR (1996) Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences. Protein Sci 5:1215-1228.
    • (1996) Protein Sci , vol.5 , pp. 1215-1228
    • Bayley, P.M.1    Findlay, W.A.2    Martin, S.R.3
  • 27
    • 33845368513 scopus 로고    scopus 로고
    • COPASI - a COmplex PAthway SImulator
    • Hoops S, et al. (2006) COPASI - a COmplex PAthway SImulator. Bioinformatics 22:3067-3074.
    • (2006) Bioinformatics , vol.22 , pp. 3067-3074
    • Hoops, S.1
  • 28
    • 0021337336 scopus 로고
    • Sequential (1984) Conformational changes in calmodulin upon binding of calcium
    • Burger D, Cox JA, Comte M, Stein EA Sequential (1984) Conformational changes in calmodulin upon binding of calcium. Biochemistry 23:1966-1971.
    • (1966) Biochemistry , vol.23
    • Burger, D.1    Cox, J.A.2    Comte, M.3    Stein, E.A.4
  • 29
    • 0019406008 scopus 로고
    • Effects of cations on affinity of calmodulin for calcium: Ordered binding of calcium ions allows the specific activation of calmodulin-stimulated enzymes
    • Haiech J, Klee CB, Demaille JG (1981) Effects of cations on affinity of calmodulin for calcium: Ordered binding of calcium ions allows the specific activation of calmodulin-stimulated enzymes. Biochemistry 20:3890-3897.
    • (1981) Biochemistry , vol.20 , pp. 3890-3897
    • Haiech, J.1    Klee, C.B.2    Demaille, J.G.3
  • 30
    • 0028037632 scopus 로고
    • Determination of calcium-binding constants by flow dialysis
    • Porumb T (1994) Determination of calcium-binding constants by flow dialysis. Anal Biochem 220:227-237.
    • (1994) Anal Biochem , vol.220 , pp. 227-237
    • Porumb, T.1
  • 32
    • 2542600181 scopus 로고    scopus 로고
    • Mechanism of the T286A-mutant alphaCaMKII interactions with Ca2+/calmodulin and ATP
    • Tzortzopoulos A, Török K (2004) Mechanism of the T286A-mutant alphaCaMKII interactions with Ca2+/calmodulin and ATP. Biochemistry 43:6404-6414.
    • (2004) Biochemistry , vol.43 , pp. 6404-6414
    • Tzortzopoulos, A.1    Török, K.2
  • 33
    • 33646823604 scopus 로고    scopus 로고
    • Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome
    • Collins MO, et al. (2006) Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome. J Neurochem 97:16-23.
    • (2006) J Neurochem , vol.97 , pp. 16-23
    • Collins, M.O.1
  • 34
    • 23844516687 scopus 로고    scopus 로고
    • Mass of the postsynaptic density and enumeration of three key molecules
    • Chen X, et al. (2005) Mass of the postsynaptic density and enumeration of three key molecules. Proc Natl Acad Sci USA 102:11551-11556.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11551-11556
    • Chen, X.1
  • 35
    • 33745617102 scopus 로고    scopus 로고
    • Relative and absolute quantification of postsynaptic density proteome isolated from rat forebrain and cerebellum
    • Cheng D, et al. (2006) Relative and absolute quantification of postsynaptic density proteome isolated from rat forebrain and cerebellum. Mol Cell Proteomics 5:1158-1170.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1158-1170
    • Cheng, D.1
  • 36
    • 0020307706 scopus 로고
    • Quantitative determinations of calmodulin in the supernatant and particulate fractions of mammalian tissues
    • Kakiuchi S, et al. (1982) Quantitative determinations of calmodulin in the supernatant and particulate fractions of mammalian tissues. J Biochem 92:1041-1048.
    • (1982) J Biochem , vol.92 , pp. 1041-1048
    • Kakiuchi, S.1
  • 37
    • 0021771759 scopus 로고
    • Calmodulin X (Ca2+)4 is the active calmodulin-calcium species activating the calcium-, calmodulin-dependent protein kinase of cardiac sarcoplasmic reticulum in the regulation of the calcium pump
    • Pifl C, et al. (1984) Calmodulin X (Ca2+)4 is the active calmodulin-calcium species activating the calcium-, calmodulin-dependent protein kinase of cardiac sarcoplasmic reticulum in the regulation of the calcium pump. Biochim Biophys Acta 773:197-206.
    • (1984) Biochim Biophys Acta , vol.773 , pp. 197-206
    • Pifl, C.1
  • 38
    • 0037670369 scopus 로고    scopus 로고
    • Bidirectional synaptic plasticity as a consequence of interdependent Ca2+-controlled phosphorylation and dephosphorylation pathways
    • d'Alcantara P, Schiffmann S, Swillens S (2003) Bidirectional synaptic plasticity as a consequence of interdependent Ca2+-controlled phosphorylation and dephosphorylation pathways. Eur J Neurosci 17:2521-2528.
    • (2003) Eur J Neurosci , vol.17 , pp. 2521-2528
    • d'Alcantara, P.1    Schiffmann, S.2    Swillens, S.3
  • 39
    • 0001145764 scopus 로고
    • The combinations of haemoglobin with oxygen and with carbon monoxide
    • Hill AV (1913) The combinations of haemoglobin with oxygen and with carbon monoxide. Biochem J 5:471-480.
    • (1913) Biochem J , vol.5 , pp. 471-480
    • Hill, A.V.1
  • 40
    • 0348010289 scopus 로고    scopus 로고
    • Distribution of postsynaptic density (PSD)-95 and Ca2+/calmodulin-dependent protein kinase II at the PSD
    • Petersen JD, et al. (2003) Distribution of postsynaptic density (PSD)-95 and Ca2+/calmodulin-dependent protein kinase II at the PSD. J Neurosci 23:11270-11278.
    • (2003) J Neurosci , vol.23 , pp. 11270-11278
    • Petersen, J.D.1
  • 41
    • 0023032057 scopus 로고
    • The distribution of calcineurin in rat brain by light and electron microscopic immunohistochemistry and enzyme-immunoassay
    • Goto S, Matsukado Y, Mihara Y, Inoue N, Miyamoto E (1986) The distribution of calcineurin in rat brain by light and electron microscopic immunohistochemistry and enzyme-immunoassay. Brain Res 397:161-172.
    • (1986) Brain Res , vol.397 , pp. 161-172
    • Goto, S.1    Matsukado, Y.2    Mihara, Y.3    Inoue, N.4    Miyamoto, E.5
  • 42
    • 0033616783 scopus 로고    scopus 로고
    • Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties
    • Mirzoeva S, et al. (1999) Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties. Biochemistry 38:3936-3947.
    • (1999) Biochemistry , vol.38 , pp. 3936-3947
    • Mirzoeva, S.1
  • 43
    • 0001314221 scopus 로고
    • The hemoglobin system
    • Adair GS (1925) The hemoglobin system. J Biol Chem 63:529-545.
    • (1925) J Biol Chem , vol.63 , pp. 529-545
    • Adair, G.S.1
  • 44
    • 0035383944 scopus 로고    scopus 로고
    • An M cell model of calcium dynamics and frequency-dependence of calmodulin activation in dendritic spines
    • Franks KM, Bartol TM, Sejnowski TJ (2001) An M cell model of calcium dynamics and frequency-dependence of calmodulin activation in dendritic spines. Neurocomputing 38-40:9-16.
    • (2001) Neurocomputing , vol.38-40 , pp. 9-16
    • Franks, K.M.1    Bartol, T.M.2    Sejnowski, T.J.3
  • 45
    • 33746913130 scopus 로고    scopus 로고
    • Naoki H, Sakamira Y, Ishii S (2005) Local signaling with molecular diffusion as a decoder of Ca2+ signals in synaptic plasticity. Mol Syst Biol 1:2005.0027.
    • Naoki H, Sakamira Y, Ishii S (2005) Local signaling with molecular diffusion as a decoder of Ca2+ signals in synaptic plasticity. Mol Syst Biol 1:2005.0027.
  • 46
    • 0029005929 scopus 로고
    • Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements
    • Tjandra N, Kuboniwa H, Ren H, Bax A (1995) Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements. Eur J Biochem 230:1014-1024.
    • (1995) Eur J Biochem , vol.230 , pp. 1014-1024
    • Tjandra, N.1    Kuboniwa, H.2    Ren, H.3    Bax, A.4
  • 47
    • 0033527588 scopus 로고    scopus 로고
    • Structural dynamics in the C-terminal domain of calmodulin at low calcium levels
    • Malmendal A, Evenäs J, Forsén S, Akke M (1999) Structural dynamics in the C-terminal domain of calmodulin at low calcium levels. J Mol Biol 293:883-899.
    • (1999) J Mol Biol , vol.293 , pp. 883-899
    • Malmendal, A.1    Evenäs, J.2    Forsén, S.3    Akke, M.4
  • 48
    • 0035953757 scopus 로고    scopus 로고
    • Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin
    • Schumacher MA, Rivard AF, Bächinger HP, Adelman JP (2001) Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin. Nature 410:1120-1124.
    • (2001) Nature , vol.410 , pp. 1120-1124
    • Schumacher, M.A.1    Rivard, A.F.2    Bächinger, H.P.3    Adelman, J.P.4
  • 49
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • Bhalla US, Iyengar R (1999) Emergent properties of networks of biological signaling pathways. Science 283:381-387.
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Iyengar, R.2
  • 50
    • 49449115320 scopus 로고
    • Allosteric competition in calmodulin
    • Czerlinski GH (1984) Allosteric competition in calmodulin. Physiol Chem Phys Med NMR 16:437-447.
    • (1984) Physiol Chem Phys Med NMR , vol.16 , pp. 437-447
    • Czerlinski, G.H.1
  • 51
    • 35548964668 scopus 로고    scopus 로고
    • A 1.3-A structure of zinc-bound N-terminal domain of calmodulin elucidates potential early ion-binding step
    • Warren JT, Guo Q, Tang W-J (2007) A 1.3-A structure of zinc-bound N-terminal domain of calmodulin elucidates potential early ion-binding step. J Mol Biol 374:517-527.
    • (2007) J Mol Biol , vol.374 , pp. 517-527
    • Warren, J.T.1    Guo, Q.2    Tang, W.-J.3
  • 52
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 A resolution
    • Babu YS, Bugg CE, Cook WJ (1988) Structure of calmodulin refined at 2.2 A resolution. J Mol Biol 204:191-204.
    • (1988) J Mol Biol , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 53
    • 0141594755 scopus 로고    scopus 로고
    • A closed compact structure of native Ca(2+)-calmodulin
    • Fallon JL, Quiocho FA (2003) A closed compact structure of native Ca(2+)-calmodulin. Structure 11:1303-1307.
    • (2003) Structure , vol.11 , pp. 1303-1307
    • Fallon, J.L.1    Quiocho, F.A.2
  • 54
    • 0037165139 scopus 로고    scopus 로고
    • Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
    • Drum CL, et al. (2002) Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415:396-402.
    • (2002) Nature , vol.415 , pp. 396-402
    • Drum, C.L.1
  • 55
    • 0023190718 scopus 로고
    • The dynamics of free calcium in dendritic spines in response to repetitive synaptic input
    • Gamble E, Koch C (1987) The dynamics of free calcium in dendritic spines in response to repetitive synaptic input. Science 236:1311-1315.
    • (1987) Science , vol.236 , pp. 1311-1315
    • Gamble, E.1    Koch, C.2
  • 56
    • 0036655823 scopus 로고    scopus 로고
    • Biochemical signaling networks decode temporal patterns of synaptic input
    • Bhalla US (2002) Biochemical signaling networks decode temporal patterns of synaptic input. J Comput Neurosci 13:49-62.
    • (2002) J Comput Neurosci , vol.13 , pp. 49-62
    • Bhalla, U.S.1
  • 57
    • 0030058273 scopus 로고    scopus 로고
    • Amechanism for synaptic frequency detection through autophosphorylation of CaM kinase II
    • Dosemeci A, Albers RW (1996) Amechanism for synaptic frequency detection through autophosphorylation of CaM kinase II. Biophys J 70:2493-2501.
    • (1996) Biophys J , vol.70 , pp. 2493-2501
    • Dosemeci, A.1    Albers, R.W.2
  • 58
    • 0032498172 scopus 로고    scopus 로고
    • Sensitivity of CaM kinase II to the frequency of Ca2+ oscillations
    • De Koninck P, Schulman H (1998) Sensitivity of CaM kinase II to the frequency of Ca2+ oscillations. Science 279:227-230.
    • (1998) Science , vol.279 , pp. 227-230
    • De Koninck, P.1    Schulman, H.2
  • 59
    • 0344739838 scopus 로고    scopus 로고
    • Sensitivity of CaM kinase II to the frequency of Ca2+ oscillations: A simple model
    • Dupont G, Houart G, De Koninck P (2003) Sensitivity of CaM kinase II to the frequency of Ca2+ oscillations: A simple model. Cell Calcium 34:485-497.
    • (2003) Cell Calcium , vol.34 , pp. 485-497
    • Dupont, G.1    Houart, G.2    De Koninck, P.3
  • 60
    • 4744362769 scopus 로고    scopus 로고
    • Protein phosphatases and calcium/calmodulin-dependent protein kinase II-dependent synaptic plasticity
    • Colbran RJ (2004) Protein phosphatases and calcium/calmodulin-dependent protein kinase II-dependent synaptic plasticity. J Neurosci 24:8404-8409.
    • (2004) J Neurosci , vol.24 , pp. 8404-8409
    • Colbran, R.J.1
  • 61
    • 32544447355 scopus 로고    scopus 로고
    • Transition from reversible to persistent binding of CaMKII to postsynaptic sites and NR2B
    • Bayer KU, et al. (2006) Transition from reversible to persistent binding of CaMKII to postsynaptic sites and NR2B. J Neurosci 26:1164-1174.
    • (2006) J Neurosci , vol.26 , pp. 1164-1174
    • Bayer, K.U.1
  • 62
    • 0030281174 scopus 로고    scopus 로고
    • A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions
    • Edelstein SJ, Schaad O, Henry E, Bertrand D, Changeux JP (1996) A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions. Biol Cybernet 75:361-379.
    • (1996) Biol Cybernet , vol.75 , pp. 361-379
    • Edelstein, S.J.1    Schaad, O.2    Henry, E.3    Bertrand, D.4    Changeux, J.P.5
  • 63
    • 0020057121 scopus 로고
    • Determination of the free-energy coupling for binding of calcium ions and troponin I to calmodulin
    • Keller CH, Olwin BB, LaPorte DC, Storm DR (1982) Determination of the free-energy coupling for binding of calcium ions and troponin I to calmodulin. Biochemistry 21:156-162.
    • (1982) Biochemistry , vol.21 , pp. 156-162
    • Keller, C.H.1    Olwin, B.B.2    LaPorte, D.C.3    Storm, D.R.4
  • 64
    • 42949129270 scopus 로고    scopus 로고
    • Acoupled equilibrium shift mechanism in calmodulin-mediated signal transduction
    • Gsponer J, et al. (2008)Acoupled equilibrium shift mechanism in calmodulin-mediated signal transduction. Structure (London) 16:736-746.
    • (2008) Structure (London) , vol.16 , pp. 736-746
    • Gsponer, J.1


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