메뉴 건너뛰기




Volumn 32, Issue 7, 2011, Pages 861-872

CaMKII in cerebral ischemia

Author keywords

brain ischemia; CaM kinases; CaMKII; excitotoxicity; glutamate; stroke

Indexed keywords

2 [1 CARBOXY 2 [4 [2 (5 METHYL 2 PHENYL 4 OXAZOLYL)ETHOXY]PHENYL]ETHYLAMINO]BENZOIC ACID METHYL ESTER; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; GLUTAMIC ACID; PROTEIN SERINE THREONINE KINASE INHIBITOR;

EID: 79960039268     PISSN: 16714083     EISSN: 17457254     Source Type: Journal    
DOI: 10.1038/aps.2011.68     Document Type: Review
Times cited : (113)

References (211)
  • 1
    • 77953037882 scopus 로고    scopus 로고
    • Targeting ischemic penumbra: Part i - From pathophysiology to therapeutic strategy
    • Liu S, Levine SR, Winn HR. Targeting ischemic penumbra: part I - from pathophysiology to therapeutic strategy. J Exp Stroke Transl Med 2010; 3: 47-55.
    • (2010) J Exp Stroke Transl Med , vol.3 , pp. 47-55
    • Liu, S.1    Levine, S.R.2    Winn, H.R.3
  • 2
    • 33750515629 scopus 로고    scopus 로고
    • Evolving therapeutic approaches to treating acute ischemic stroke
    • DOI 10.1016/j.jns.2006.06.010, PII S0022510X06002966
    • Weinberger JM. Evolving therapeutic approaches to treating acute ischemic stroke. J Neurol Sci 2006; 249: 101-9. (Pubitemid 44665917)
    • (2006) Journal of the Neurological Sciences , vol.249 , Issue.2 , pp. 101-109
    • Weinberger, J.M.1
  • 4
    • 7644227043 scopus 로고    scopus 로고
    • Mechanisms of hemorrhagic transformation after tissue plasminogen activator reperfusion therapy for ischemic stroke
    • DOI 10.1161/01.STR.0000143219.16695.af
    • Wang X, Tsuji K, Lee SR, Ning M, Furie KL, Buchan AM, et al. Mechanisms of hemorrhagic transformation after tissue plasminogen activator reperfusion therapy for ischemic stroke. Stroke 2004; 35: 2726-30. (Pubitemid 39458380)
    • (2004) Stroke , vol.35 , Issue.11 SUPPL. 1 , pp. 2726-2730
    • Wang, X.1    Tsuji, K.2    Lee, S.-R.3    Ning, M.4    Furie, K.L.5    Buchan, A.M.6    Lo, E.H.7
  • 5
    • 41249090658 scopus 로고    scopus 로고
    • National US estimates of recombinant tissue plasminogen activator use: ICD-9 codes substantially underestimate
    • DOI 10.1161/STROKEAHA.107.490375
    • Kleindorfer D, Lindsell CJ, Brass L, Koroshetz W, Broderick JP. National US estimates of recombinant tissue plasminogen activator use: ICD-9 codes substantially underestimate. Stroke 2008; 39: 924-8. (Pubitemid 351619542)
    • (2008) Stroke , vol.39 , Issue.3 , pp. 924-928
    • Kleindorfer, D.1    Lindsell, C.J.2    Brass, L.3    Koroshetz, W.4    Broderick, J.P.5
  • 6
    • 77954229587 scopus 로고    scopus 로고
    • Effective post- insult neuroprotection by a novel Ca2+/calmodulin- dependent protein kinase II (CaMKII) inhibitor
    • Vest RS, OLeary H, Coultrap SJ, Kindy MS, Bayer KU. Effective post- insult neuroprotection by a novel Ca2+/calmodulin-dependent protein kinase II (CaMKII) inhibitor. J Biol Chem 2010; 285: 20675-82.
    • (2010) J Biol Chem , vol.285 , pp. 20675-82
    • Vest, R.S.1    Oleary, H.2    Coultrap, S.J.3    Kindy, M.S.4    Bayer, K.U.5
  • 7
    • 79953043596 scopus 로고    scopus 로고
    • Excitotoxic neuroprotection and vulnerability with CaMKII inhibition
    • Ashpole NM, Hudmon A. Excitotoxic neuroprotection and vulnerability with CaMKII inhibition. Mol Cell Neurosci 2011; 46: 720-30.
    • (2011) Mol Cell Neurosci , vol.46 , pp. 720-30
    • Ashpole, N.M.1    Hudmon, A.2
  • 8
    • 0023137252 scopus 로고
    • Ionic dependence of glutamate neurotoxicity
    • Choi DW. Ionic dependence of glutamate neurotoxicity. J Neurosci 1987; 7: 369-79. (Pubitemid 17017466)
    • (1987) Journal of Neuroscience , vol.7 , Issue.2 , pp. 369-379
    • Choi, D.W.1
  • 9
    • 84948011844 scopus 로고
    • The toxic effect of sodium L-glutamate on the inner layers of the retina
    • Lucas DR, Newhouse JP. The toxic effect of sodium L-glutamate on the inner layers of the retina. AMA Arch Ophthalmol 1957; 58: 193-201.
    • (1957) AMA Arch Ophthalmol , vol.58 , pp. 193-201
    • Lucas, D.R.1    Newhouse, J.P.2
  • 10
    • 0014668762 scopus 로고
    • Brain lesions, obesity, and other disturbances in mice treated with monosodium glutamate
    • Olney JW. Brain lesions, obesity, and other disturbances in mice treated with monosodium glutamate. Science 1969; 164: 719-21.
    • (1969) Science , vol.164 , pp. 719-21
    • Olney, J.W.1
  • 11
    • 0014682523 scopus 로고
    • Brain lesions in an infant rhesus monkey treated with monsodium glutamate
    • Olney JW, Sharpe LG. Brain lesions in an infant rhesus monkey treated with monsodium glutamate. Science 1969; 166: 386-8.
    • (1969) Science , vol.166 , pp. 386-8
    • Olney, J.W.1    Sharpe, L.G.2
  • 12
    • 0018865893 scopus 로고
    • Cortical cellular response in acute subarachnoid hemorrhage
    • Hubschmann OR, Kornhauser D. Cortical cellular response in acute subarachnoid hemorrhage. J Neurosurgery 1980; 52: 456-62. (Pubitemid 10130633)
    • (1980) Journal of Neurosurgery , vol.52 , Issue.4 , pp. 456-462
    • Hubschmann, O.R.1    Kornhauser, D.2
  • 15
    • 1842535186 scopus 로고    scopus 로고
    • Molecular mechanisms underlying specificity of excitotoxic signaling in neurons
    • DOI 10.2174/1566524043479202
    • Aarts MM, Tymianski M. Molecular mechanisms underlying specificity of excitotoxic signaling in neurons. Curr Mol Med 2004; 4: 137-47. (Pubitemid 38425911)
    • (2004) Current Molecular Medicine , vol.4 , Issue.2 , pp. 137-147
    • Aarts, M.M.1    Tymianski, M.2
  • 16
    • 1042301370 scopus 로고    scopus 로고
    • Pathophysiology of cerebral ischemia and brain trauma: Similarities and differences
    • Bramlett HM, Dietrich WD. Pathophysiology of cerebral ischemia and brain trauma: similarities and differences. J Cereb Blood Flow Metab 2004; 24: 133-50. (Pubitemid 38199107)
    • (2004) Journal of Cerebral Blood Flow and Metabolism , vol.24 , Issue.2 , pp. 133-150
    • Bramlett, H.M.1    Dietrich, W.D.2
  • 18
    • 0043180531 scopus 로고    scopus 로고
    • Excitotoxic and excitoprotective mechanisms: Abundant targets for the prevention and treatment of neurodegenerative disorders
    • DOI 10.1385/NMM:3:2:65
    • Mattson MP. Excitotoxic and excitoprotective mechanisms: abundant targets for the prevention and treatment of neurodegenerative disorders. Neuromolecular Med 2003; 3: 65-94. (Pubitemid 37012494)
    • (2003) NeuroMolecular Medicine , vol.3 , Issue.2 , pp. 65-94
    • Mattson, M.P.1
  • 19
    • 0028793257 scopus 로고
    • Glutamate-induced neuronal death: A succession of necrosis or apoptosis depending on mitochondrial function
    • Ankarcrona M, Dypbukt JM, Bonfoco E, Zhivotovsky B, Orrenius S, Lipton SA. Glutamate-induced neuronal death: a succession of necrosis or apoptosis depending on mitochondrial function. Neuron 1995; 15: 961-73.
    • (1995) Neuron , vol.15 , pp. 961-73
    • Ankarcrona, M.1    Dypbukt, J.M.2    Bonfoco, E.3    Zhivotovsky, B.4    Orrenius, S.5    Lipton, S.A.6
  • 20
    • 0030743984 scopus 로고    scopus 로고
    • Susceptibility to apoptosis is enhanced in immature cortical neurons
    • DOI 10.1016/S0006-8993(97)00248-5, PII S0006899397002485
    • McDonald JW, Behrens MI, Chung C, Bhattacharyya T, Choi DW. Susceptibility to apoptosis is enhanced in immature cortical neurons. Brain Res 1997; 759: 228-232. (Pubitemid 27286699)
    • (1997) Brain Research , vol.759 , Issue.2 , pp. 228-232
    • McDonald, J.W.1    Behrens, M.I.2    Chung, C.3    Bhattacharyya, T.4    Choi, D.W.5
  • 21
    • 0141884305 scopus 로고    scopus 로고
    • Diversity in the mechanisms of neuronal cell death
    • DOI 10.1016/S0896-6273(03)00601-9
    • Yuan J, Lipinski M, Degterev A. Diversity in the mechanisms of neuronal cell death. Neuron 2003; 40: 401-13. (Pubitemid 37244104)
    • (2003) Neuron , vol.40 , Issue.2 , pp. 401-413
    • Yuan, J.1    Lipinski, M.2    Degterev, A.3
  • 22
    • 65549098614 scopus 로고    scopus 로고
    • Apoptotic mechanisms after cerebral ischemia
    • Broughton BRS, Reutens DC, Sobey CG. Apoptotic mechanisms after cerebral ischemia. Stroke 2009; 40: e331-9.
    • (2009) Stroke , vol.40
    • Brs, B.1    Reutens, D.C.2    Sobey, C.G.3
  • 23
    • 0023870521 scopus 로고
    • Pharmacology of glutamate neurotoxicity in cortical cell culture: Attenuation by NMDA antagonists
    • Choi DW, Koh JY, Peters S. Pharmacology of glutamate neurotoxicity in cortical cell culture: attenuation by NMDA antagonists. J Neurosci 1988; 8: 185-96. (Pubitemid 18038308)
    • (1988) Journal of Neuroscience , vol.8 , Issue.1 , pp. 185-196
    • Choi, D.W.1    Koh, J.Y.2    Peters, S.3
  • 24
    • 0024344822 scopus 로고
    • Direct evidence that excitotoxicity in cultured neurons is mediated via N-methyl-D-aspartate (NMDA) as well as non-NMDA receptors
    • DOI 10.1111/j.1471-4159.1989.tb07327.x
    • Frandsen A, Drejer J, Schousboe A. Direct evidence that excitotoxicity in cultured neurons is mediated via N-methyl-D-aspartate (NMDA) as well as non-NMDA receptors. J Neurochem 1989; 53: 297-9. (Pubitemid 19158142)
    • (1989) Journal of Neurochemistry , vol.53 , Issue.1 , pp. 297-299
    • Frandsen, A.1    Drejer, J.2    Schousboe, A.3
  • 27
    • 48849089052 scopus 로고    scopus 로고
    • Neuroprotection for ischemic stroke: Past, present and future
    • Ginsberg MD. Neuroprotection for ischemic stroke: past, present and future. Neuropharmacology 2008; 55: 363-89.
    • (2008) Neuropharmacology , vol.55 , pp. 363-89
    • Ginsberg, M.D.1
  • 28
    • 35948947269 scopus 로고    scopus 로고
    • Reviews: On the hypes and falls in neuroprotection: Targeting the NMDA receptor
    • DOI 10.1177/1073858406296259
    • Villmann C, Becker CM. On the hypes and falls in neuroprotection: targeting the NMDA receptor. Neuroscientist 2007; 13: 594-615. (Pubitemid 350077310)
    • (2007) Neuroscientist , vol.13 , Issue.6 , pp. 594-615
    • Villmann, C.1    Becker, C.-M.2
  • 29
    • 0033578855 scopus 로고    scopus 로고
    • Long-term potentiation - A decade of progress?
    • Malenka RC, Nicoll RA. Long-term potentiation - a decade of progress? Science 1999; 285: 1870-4.
    • (1999) Science , vol.285 , pp. 1870-4
    • Malenka, R.C.1    Nicoll, R.A.2
  • 30
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioural memory
    • DOI 10.1038/nrn753
    • Lisman J, Schulman H, Cline H. The molecular basis of CaMKII function in synaptic and behavioural memory. Nat Rev Neurosci 2002; 3: 175-90. (Pubitemid 135706588)
    • (2002) Nature Reviews Neuroscience , vol.3 , Issue.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 31
    • 0035997377 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II: The role of structure and autoregulation in cellular function
    • DOI 10.1146/annurev.biochem.71.110601.135410
    • Hudmon A, Schulman H. Neuronal Ca2+/calmodulin-dependent protein kinase II: the role of structure and autoregulation in cellular function. Annu Rev Biochem 2002; 71: 473-510. (Pubitemid 34800228)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 473-510
    • Hudmon, A.1    Schulman, H.2
  • 33
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S. The protein kinase complement of the human genome. Science 2002; 298: 1912-34. (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 34
    • 0029125761 scopus 로고
    • Human calcium-calmodulin dependent protein kinase I: CDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase i kinase
    • Haribabu B, Hook SS, Selbert MA, Goldstein EG, Tomhave ED , Edelman AM, et al. Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase. EMBO J 1995; 14: 3679-86.
    • (1995) EMBO J , vol.14 , pp. 3679-86
    • Haribabu, B.1    Hook, S.S.2    Ma, S.3    Goldstein, E.G.4    Tomhave, E.D.5    Edelman, A.M.6
  • 35
    • 0022519298 scopus 로고
    • 2+-triggered molecular switch
    • Miller SG, Kennedy MB. Regulation of brain type II Ca2+/ calmodulindependent protein kinase by autophosphorylation: a Ca2+-triggered molecular switch. Cell 1986; 44: 861-70. (Pubitemid 16045332)
    • (1986) Cell , vol.44 , Issue.6 , pp. 861-870
    • Miller, S.G.1    Kennedy, M.B.2
  • 37
    • 0022929859 scopus 로고
    • 2+(calmodulin)-dependent protein kinase II by an autophosphorylation mechanism
    • Schworer CM, Colbran RJ, Soderling TR. Reversible generation of a Ca2+-independent form of Ca2+(calmodulin)-dependent protein kinase II by an autophosphorylation mechanism. J Biol Chem 1986; 261: 8581-4. (Pubitemid 17205046)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.19 , pp. 8581-8584
    • Schworer, C.M.1    Colbran, R.J.2    Soderling, T.R.3
  • 38
    • 0034640259 scopus 로고    scopus 로고
    • Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIα, and truncated CaM kinase IIα reveal a unique organization for its structural core and functional domains
    • DOI 10.1074/jbc.275.19.14354
    • Kolodziej SJ, Hudmon A, Waxham MN, Stoops JK. Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase II and truncated CaM kinase II reveal a unique organization for its structural core and functional domains. J Biol Chem 2000; 275: 14354-9. (Pubitemid 30339718)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.19 , pp. 14354-14359
    • Kolodziej, S.J.1    Hudmon, A.2    Waxham, M.N.3    Stoops, J.K.4
  • 39
    • 13444311622 scopus 로고    scopus 로고
    • Bidirectional signals transduced by DAPK-ER K interaction promote the apoptotic effect of DAPK
    • Chen CH, Wang WJ, Kuo JC, Tsai HC, Lin JR, Chang ZF. Bidirectional signals transduced by DAPK-ER K interaction promote the apoptotic effect of DAPK. EMBO J 2005; 24: 294-304.
    • (2005) EMBO J , vol.24 , pp. 294-304
    • Chen, C.H.1    Wang, W.J.2    Kuo, J.C.3    Tsai, H.C.4    Lin, J.R.5    Chang, Z.F.6
  • 40
    • 33746359639 scopus 로고    scopus 로고
    • The death-associated protein kinases: Structure, function, and beyond
    • DOI 10.1146/annurev.biochem.75.103004.142615
    • Bialik S, Kimchi A. The death-associated protein kinases: structure, function, and beyond. Annu Rev Biochem 2006; 75: 189-210. (Pubitemid 44118031)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 189-210
    • Bialik, S.1    Kimchi, A.2
  • 42
    • 63849261100 scopus 로고    scopus 로고
    • Structure and function of AMPactivated protein kinase
    • Oakhill JS, Scott JW, Kemp BE. Structure and function of AMPactivated protein kinase. Acta Physiol 2009; 196: 3-14.
    • (2009) Acta Physiol , vol.196 , pp. 3-14
    • Oakhill, J.S.1    Scott, J.W.2    Kemp, B.E.3
  • 43
    • 52049121528 scopus 로고    scopus 로고
    • Calmodulinkinases: Modulators of neuronal development and plasticity
    • Wayman GA, Lee YS, Tokumitsu H, Silva A, Soderling TR. Calmodulinkinases: modulators of neuronal development and plasticity. Neuron 2008; 59: 914-31.
    • (2008) Neuron , vol.59 , pp. 914-31
    • Wayman, G.A.1    Lee, Y.S.2    Tokumitsu, H.3    Silva, A.4    Soderling, T.R.5
  • 44
    • 0024455621 scopus 로고
    • Tissue-specific expression of four types of rat calmodulin-dependent protein kinase II mRNAs
    • Tobimatsu T, Fujisawa H. Tissue-specific expression of four types of rat calmodulin-dependent protein kinase II mRNAs. J Biol Chem 1989; 264: 17907-12. (Pubitemid 19279256)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.30 , pp. 17907-17912
    • Tobimatsu, T.1    Fujisawa, H.2
  • 45
    • 0345465661 scopus 로고    scopus 로고
    • Developmental expression of the CaM kinase II isoforms: Ubiquitous γ- and δ-CaM kinase II are the early isoforms and most abundant in the developing nervous system
    • DOI 10.1016/S0169-328X(99)00131-X, PII S0169328X9900131X
    • Bayer KU, Lohler J, Schulman H, Harbers K. Developmental expression of the CaM kinase II isoforms: ubiquitous gamma- and delta- CaM kinase II are the early isoforms and most abundant in the developing nervous system. Brain Res Mol Brain Res 1999; 70: 147-54. (Pubitemid 29278617)
    • (1999) Molecular Brain Research , vol.70 , Issue.1 , pp. 147-154
    • Bayer, K.-U.1    Lohler, J.2    Schulman, H.3    Harbers, K.4
  • 46
    • 0022375477 scopus 로고
    • 2+/calmodulin-dependent protein kinase in rat brain
    • Erondu NE, Kennedy MB. Regional distribution of type II Ca2+/ calmodulin-dependent protein kinase in rat brain. J Neurosci 1985; 5: 3270-7. (Pubitemid 16182607)
    • (1985) Journal of Neuroscience , vol.5 , Issue.12 , pp. 3270-3277
    • Erondu, N.E.1    Kennedy, M.B.2
  • 47
    • 0024263288 scopus 로고
    • Immunohistochemical investigation of ischemic and postischemic damage after bilateral carotid occlusion in gerbils
    • Hatakeyama T, Matsumoto M, Brengman J, Yanagihara T. Immunohistochemical investigation of ischemic and postischemic damage after bilateral carotid occlusion in gerbils. Stroke 1988; 19: 1526-34. (Pubitemid 19005809)
    • (1988) Stroke , vol.19 , Issue.12 , pp. 1526-1534
    • Hatakeyama, T.1    Matsumoto, M.2    Brengman, J.M.3    Yanagihara, T.4
  • 48
    • 0026637195 scopus 로고
    • Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice
    • Silva AJ, Stevens CF, Tonegawa S, Wang Y. Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice. Science 1992; 257: 201-6.
    • (1992) Science , vol.257 , pp. 201-6
    • Silva, A.J.1    Stevens, C.F.2    Tonegawa, S.3    Wang, Y.4
  • 49
    • 0026742451 scopus 로고
    • Impaired spatial learning in alpha-calcium-calmodulin kinase II mutant mice
    • Silva AJ, Paylor R, Wehner JM, Tonegawa S. Impaired spatial learning in alpha-calcium-calmodulin kinase II mutant mice. Science 1992; 257: 206-11.
    • (1992) Science , vol.257 , pp. 206-11
    • Silva, A.J.1    Paylor, R.2    Wehner, J.M.3    Tonegawa, S.4
  • 50
    • 0038392870 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent kinase II
    • DOI 10.1016/S1097-2765(03)00171-0
    • Hoelz A, Nairn AC, Kuriyan J. Crystal structure of a tetradecameric assembly of the association domain of Ca2+/calmodulin-dependent kinase II. Mol Cell 2003; 11: 1241-51. (Pubitemid 36645143)
    • (2003) Molecular Cell , vol.11 , Issue.5 , pp. 1241-1251
    • Hoelz, A.1    Nairn, A.C.2    Kuriyan, J.3
  • 51
    • 28344445756 scopus 로고    scopus 로고
    • Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme
    • DOI 10.1016/j.cell.2005.10.029, PII S0092867405011736
    • Rosenberg OS, Deindl S, Sung RJ, Nairn AC, Kuriyan J. Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme. Cell 2005; 123: 849-60. (Pubitemid 41721031)
    • (2005) Cell , vol.123 , Issue.5 , pp. 849-860
    • Rosenberg, O.S.1    Deindl, S.2    Sung, R.-J.3    Nairn, A.C.4    Kuriyan, J.5
  • 52
    • 33644936426 scopus 로고    scopus 로고
    • Oligomerization states of the association domain and the holoenyzme of Ca/CaM kinase II
    • Rosenberg OS, Deindl S, Comolli LR , Hoelz A, Downing KH, Nairn AC, et al. Oligomerization states of the association domain and the holoenyzme of Ca/CaM kinase II. FEBS J 2006; 273: 682-94.
    • (2006) FEBS J , vol.273 , pp. 682-94
    • Rosenberg, O.S.1    Deindl, S.2    Comolli, L.R.3    Hoelz, A.4    Downing, K.H.5    Nairn, A.C.6
  • 53
    • 77955039883 scopus 로고    scopus 로고
    • Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation
    • Rellos P, Pike AC, Niesen FH, Salah E, Lee WH, von Delft F, et al. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS Biol 2010; 8: e1000426.
    • (2010) PLoS Biol , vol.8
    • Rellos, P.1    Pike, A.C.2    Niesen, F.H.3    Salah, E.4    Lee, W.H.5    Von Delft, F.6
  • 54
    • 0032185669 scopus 로고    scopus 로고
    • αKAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle
    • DOI 10.1093/emboj/17.19.5598
    • Bayer KU, Harbers K, Schulman H. alphaKAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle. EMBO J 1998; 17: 5598-605. (Pubitemid 28445971)
    • (1998) EMBO Journal , vol.17 , Issue.19 , pp. 5598-5605
    • Bayer, K.-U.1    Harbers, K.2    Schulman, H.3
  • 55
    • 0017854367 scopus 로고
    • Stimulation of brain membrane protein phosphorylation by calcium and an endogenous heat-stable protein
    • Schulman H, Greengard P. Stimulation of brain membrane protein phosphorylation by calcium and an endogenous heat-stable protein. Nature 1978; 271: 478-9. (Pubitemid 8257927)
    • (1978) Nature , vol.271 , Issue.5644 , pp. 478-479
    • Schulman, H.1    Greengard, P.2
  • 56
    • 0021032297 scopus 로고
    • Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain
    • Bennett MK, Erondu NE, Kennedy MB. Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain. J Biol Chem 1983; 258: 12735-44. (Pubitemid 14231188)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.20 , pp. 12735-12744
    • Bennett, M.K.1    Erondu, N.E.2    Kennedy, M.B.3
  • 57
    • 0024789308 scopus 로고
    • Expression and characterization of calmodulin-dependent protein kinase II from cloned cDNAs in Chinese hamster ovary cells
    • Yamauchi T, Ohsako S, Deguchi T. Expression and characterization of calmodulin-dependent protein kinase II from cloned cDNAs in Chinese hamster ovary cells. J Biol Chem 1989; 264: 19108-16. (Pubitemid 19285818)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.32 , pp. 19108-19116
    • Yamauchi, T.1    Ohsako, S.2    Deguchi, T.3
  • 58
    • 0032553432 scopus 로고    scopus 로고
    • Identification of domains essential for the assembly of calcium/calmodulin-dependent protein kinase II holoenzymes
    • DOI 10.1074/jbc.273.47.31555
    • Kolb SJ, Hudmon A, Ginsberg TR , Waxham MN. Identification of domains essential for the assembly of calcium/calmodulin-dependent protein kinase II holoenzymes. J Biol Chem 1998; 273: 31555-64. (Pubitemid 28533179)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.47 , pp. 31555-31564
    • Kolb, S.J.1    Hudmon, A.2    Ginsberg, T.R.3    Waxham, M.N.4
  • 59
    • 0033529559 scopus 로고    scopus 로고
    • Functional implications of the subunit composition of neuronal CaM kinase II
    • Brocke L, Chiang LW, Wagner PD, Schulman H. Functional implications of the subunit composition of neuronal CaM kinase II. J Biol Chem 1999; 274: 22713-22.
    • (1999) J Biol Chem , vol.274 , pp. 22713-22
    • Brocke, L.1    Chiang, L.W.2    Wagner, P.D.3    Schulman, H.4
  • 60
    • 26944451290 scopus 로고    scopus 로고
    • CaMK-II oligomerization potential determined using CFP/YFP FRET
    • DOI 10.1016/j.bbamcr.2005.08.005, PII S0167488905001813
    • Lantsman K, Tombes RM. CaMK-II oligomerization potential determined using CFP/YFP FRET . Biochim Biophys Acta 2005; 1746: 45-54. (Pubitemid 41484085)
    • (2005) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1746 , Issue.1 , pp. 45-54
    • Lantsman, K.1    Tombes, R.M.2
  • 61
    • 0026360042 scopus 로고
    • 2+/calmodulin-dependent protein kinase II revealed by electron microscopy
    • Kanaseki T, Ikeuchi Y, Sugiura H, Yamauchi T. Structural features of Ca2+/calmodulin-dependent protein kinase II revealed by electron microscopy. J Cell Biol 1991; 115: 1049-60. (Pubitemid 21909952)
    • (1991) Journal of Cell Biology , vol.115 , Issue.4 , pp. 1049-1060
    • Kanaseki, T.1    Ikeuchi, Y.2    Sugiura, H.3    Yamauchi, T.4
  • 62
    • 0035917320 scopus 로고    scopus 로고
    • Oligomeric structure of α-calmodulin-dependent protein kinase II
    • DOI 10.1006/jmbi.2001.4584
    • Morris EP, Török K. Oligomeric structure of [alpha]-calmodulindependent protein kinase II. J Mol Biol 2001; 308: 1-8. (Pubitemid 33027621)
    • (2001) Journal of Molecular Biology , vol.308 , Issue.1 , pp. 1-8
    • Morris, E.P.1    Torok, K.2
  • 63
    • 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 1999; 274: 26199-208.
    • (1999) J Biol Chem , vol.274 , pp. 26199-208
    • Yang, E.1    Schulman, H.2
  • 64
    • 0035859082 scopus 로고    scopus 로고
    • Interaction with the NMDA receptor locks CaMKII in an active conformation
    • DOI 10.1038/35081080
    • Bayer KU, De Koninck P, Leonard AS, Hell JW, Schulman H. Interaction with the NMDA receptor locks CaMKII in an active conformation. Nature 2001; 411: 801-5. (Pubitemid 32588103)
    • (2001) Nature , vol.411 , Issue.6839 , pp. 801-805
    • Bayer, K.-U.1    De Koninck, P.2    Leonard, A.S.3    Hell, J.W.4    Schulman, H.5
  • 65
    • 0028306195 scopus 로고
    • Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals
    • DOI 10.1016/0896-6273(94)90306-9
    • Hanson PI, Meyer T, Stryer L, Schulman H. Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals. Neuron 1994; 12: 943-56. (Pubitemid 24178190)
    • (1994) Neuron , vol.12 , Issue.5 , pp. 943-956
    • Hanson, P.I.1    Meyer, T.2    Stryer, L.3    Schulman, H.4
  • 66
    • 0032561201 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II
    • DOI 10.1074/jbc.273.43.28424
    • Rich RC, Schulman H. Substrate-directed function of calmodulin in autophosphorylation of Ca2+/calmodulin-dependent protein kinase II. J Biol Chem 1998; 273: 28424-9. (Pubitemid 28496147)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.43 , pp. 28424-28429
    • Rich, R.C.1    Schulman, H.2
  • 67
    • 77952943036 scopus 로고    scopus 로고
    • CaMKII autonomy is substrate-dependent and further stimulated by Ca2+/ calmodulin
    • Coultrap SJ, Buard I, Kulbe JR, DellAcqua ML, Bayer KU. CaMKII autonomy is substrate-dependent and further stimulated by Ca2+/ calmodulin. J Biol Chem 2010; 285: 17930-7.
    • (2010) J Biol Chem , vol.285 , pp. 17930-7
    • Coultrap, S.J.1    Buard, I.2    Kulbe, J.R.3    Dellacqua, M.L.4    Bayer, K.U.5
  • 68
    • 0032488659 scopus 로고    scopus 로고
    • 286 of the α calcium-calmodulin kinase II in LTP and learning
    • DOI 10.1126/science.279.5352.870
    • Giese KP, Fedorov NB, Filipkowski RK, Silva AJ. Autophosphorylation at Thr286 of the alpha calcium-calmodulin kinase II in LT P and learning. Science 1998; 279: 870-3. (Pubitemid 28106282)
    • (1998) Science , vol.279 , Issue.5352 , pp. 870-873
    • Giese, K.P.1    Fedorov, N.B.2    Filipkowski, R.K.3    Silva, A.J.4
  • 69
    • 0025301783 scopus 로고
    • Calcium/calmodulin-independent autophosphorylation sites of calcium/calmodulin-dependent protein kinase II. Studies on the effect of phosphorylation of threonine 305/306 and serine 314 on calmodulin binding using synthetic peptides
    • Colbran RJ, Soderling TR . Calcium/calmodulin-independent autophosphorylation sites of calcium/calmodulin-dependent protein kinase II. Studies on the effect of phosphorylation of threonine 305/306 and serine 314 on calmodulin binding using synthetic peptides. J Biol Chem 1990; 265: 11213-9.
    • (1990) J Biol Chem , vol.265 , pp. 11213-9
    • Colbran, R.J.1    Soderling, T.R.2
  • 70
    • 0026806967 scopus 로고
    • Inhibitory autophosphorylation of multifunctional Ca2+/calmodulin- dependent protein kinase analyzed by sitedirected mutagenesis
    • Hanson PI, Schulman H. Inhibitory autophosphorylation of multifunctional Ca2+/calmodulin-dependent protein kinase analyzed by sitedirected mutagenesis. J Biol Chem 1992; 267: 17216-24.
    • (1992) J Biol Chem , vol.267 , pp. 17216-24
    • Hanson, P.I.1    Schulman, H.2
  • 71
    • 0027340006 scopus 로고
    • 2+/calmodulin-dependent protein kinase II by basal autophosphorylation
    • Colbran RJ. Inactivation of Ca2+/calmodulin-dependent protein kinase II by basal autophosphorylation. J Biol Chem 1993; 268: 7163-70. (Pubitemid 23105606)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.10 , pp. 7163-7170
    • Colbran, R.J.1
  • 72
    • 0347993183 scopus 로고    scopus 로고
    • 2+/CaM-responsive pool of CaMKII by scaffold-dependent autophosphorylation
    • DOI 10.1016/S0896-6273(03)00786-4
    • Lu CS, Hodge JJ, Mehren J, Sun XX, Griffith LC. Regulation of the Ca2+/CaM-responsive pool of CaMKII by scaffold-dependent autophosphorylation. Neuron 2003; 40: 1185-97. (Pubitemid 38032794)
    • (2003) Neuron , vol.40 , Issue.6 , pp. 1185-1197
    • Lu, C.S.1    Hodge, J.J.L.2    Mehren, J.3    Sun, X.X.4    Griffith, L.C.5
  • 73
    • 0024461379 scopus 로고
    • Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP
    • Malinow R, Schulman H, Tsien RW. Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LT P. Science 1989; 245: 862-6. (Pubitemid 19223665)
    • (1989) Science , vol.245 , Issue.4920 , pp. 862-866
    • Malinow, R.1    Schulman, H.2    Tsien, R.W.3
  • 74
    • 77953798275 scopus 로고    scopus 로고
    • CaMKII "autonomy" is required for initiating but not for maintaining neuronal long-term information storage
    • Buard I, Coultrap SJ, Freund RK, Lee YS, DellAcqua ML, Silva AJ, et al. CaMKII "autonomy" is required for initiating but not for maintaining neuronal long-term information storage. J Neurosci 2010; 30: 8214-20.
    • (2010) J Neurosci , vol.30 , pp. 8214-20
    • Buard, I.1    Coultrap, S.J.2    Freund, R.K.3    Lee, Y.S.4    Dellacqua, M.L.5    Silva, A.J.6
  • 75
    • 58549090329 scopus 로고    scopus 로고
    • The molecular and cellular biology of enhanced cognition
    • Lee YS, Silva AJ. The molecular and cellular biology of enhanced cognition. Nat Rev Neurosci 2009; 10: 126-40.
    • (2009) Nat Rev Neurosci , vol.10 , pp. 126-40
    • Lee, Y.S.1    Silva, A.J.2
  • 76
    • 0033515884 scopus 로고    scopus 로고
    • Dynamic control of caMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation
    • DOI 10.1126/science.284.5411.162
    • Shen K, Meyer T. Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation. Science 1999; 284: 162-6. (Pubitemid 29282073)
    • (1999) Science , vol.284 , Issue.5411 , pp. 162-166
    • Shen, K.1    Meyer, T.2
  • 77
    • 7044270772 scopus 로고    scopus 로고
    • Persistent accumulation of calcium/calmodulin-dependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation
    • DOI 10.1523/JNEUROSCI.2350-04.2004
    • Otmakhov N, Tao-Cheng JH, Carpenter S, Asrican B, Dosemeci A, Reese TS, et al. Persistent accumulation of calcium/calmodulindependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation. J Neurosci 2004; 24: 9324-31. (Pubitemid 39426169)
    • (2004) Journal of Neuroscience , vol.24 , Issue.42 , pp. 9324-9331
    • Otmakhov, N.1    Tao-Cheng, J.-H.2    Carpenter, S.3    Asrican, B.4    Dosemeci, A.5    Reese, T.S.6    Lisman, J.7
  • 78
    • 32544447355 scopus 로고    scopus 로고
    • Transition from reversible to persistent binding of CaMKII to postsynaptic sites and NR2B
    • DOI 10.1523/JNEUROSCI.3116-05.2006
    • Bayer KU, LeBel E, McDonald GL, OLeary H, Schulman H, De Koninck H, et al. Transition from reversible to persistent binding of CaMKII to postsynaptic sites and NR2B. J Neurosci 2006; 26: 1164-74. (Pubitemid 43237049)
    • (2006) Journal of Neuroscience , vol.26 , Issue.4 , pp. 1164-1174
    • Bayer, K.U.1    LeBel, E.2    McDonald, G.L.3    O'Leary, H.4    Schulman, H.5    De Koninck, P.6
  • 79
    • 0029882409 scopus 로고    scopus 로고
    • Inactivation and selfassociation of Ca2+/calmodulin-dependent protein kinase II during autophosphorylation
    • Hudmon A, Aronowski J, Kolb SJ, Waxham MN. Inactivation and selfassociation of Ca2+/calmodulin-dependent protein kinase II during autophosphorylation. J Biol Chem 1996; 271: 8800-8.
    • (1996) J Biol Chem , vol.271 , pp. 8800-8
    • Hudmon, A.1    Aronowski, J.2    Kolb, S.J.3    Waxham, M.N.4
  • 81
    • 0035801596 scopus 로고    scopus 로고
    • 2+/calmodulin- dependent protein kinase II clusters in hippocampal neurons
    • DOI 10.1016/S0306-4522(01)00262-7, PII S0306452201002627
    • Tao-Cheng JH, Vinade L, Smith C, Winters CA, Ward R, Brightman MW, et al. Sustained elevation of calcium induces Ca2+/calmodulindependent protein kinase II clusters in hippocampal neurons. Neuroscience 2001; 106: 69-78. (Pubitemid 32831074)
    • (2001) Neuroscience , vol.106 , Issue.1 , pp. 69-78
    • Tao-Cheng, J.-H.1    Vinade, L.2    Smith, C.3    Winters, C.A.4    Ward, R.5    Brightman, M.W.6    Reese, T.S.7    Dosemeci, A.8
  • 82
    • 23044493437 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II clustering at synaptic and nonsynaptic sites based on self-association
    • DOI 10.1523/JNEUROSCI.4698-04.2005
    • Hudmon A, Lebel E, Roy H, Sik A, Schulman H, Waxham MN, et al. A mechanism for Ca2+/calmodulin-dependent protein kinase II clustering at synaptic and nonsynaptic sites based on self-association. J Neurosci 2005; 25: 6971-83. (Pubitemid 41077005)
    • (2005) Journal of Neuroscience , vol.25 , Issue.30 , pp. 6971-6983
    • Hudmon, A.1    LeBel, E.2    Roy, H.3    Sik, A.4    Schulman, H.5    Waxham, M.N.6    De Koninck, P.7
  • 83
    • 26944487610 scopus 로고    scopus 로고
    • NMDA receptor subunit composition controls synaptic plasticity by regulating binding to CaMKII
    • DOI 10.1016/j.neuron.2005.08.034, PII S0896627305007385
    • Barria A, Malinow R. NMDA receptor subunit composition controls synaptic plasticity by regulating binding to CaMKII. Neuron 2005; 48: 289-301. (Pubitemid 41476362)
    • (2005) Neuron , vol.48 , Issue.2 , pp. 289-301
    • Barria, A.1    Malinow, R.2
  • 85
    • 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
    • DOI 10.1074/jbc.273.33.20689
    • Strack S, Colbran RJ. Autophosphorylation-dependent targeting of calcium/calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl-D-aspartate receptor. J Biol Chem 1998; 273: 20689-92. (Pubitemid 28385342)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.33 , pp. 20689-20692
    • Strack, S.1    Colbran, R.J.2
  • 86
    • 2242425422 scopus 로고    scopus 로고
    • Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin and α-actinin
    • DOI 10.1074/jbc.M205164200
    • Leonard AS, Bayer KU, Merrill MA, Lim IA, Shea MA, Schulman H, et al. Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin and alpha-actinin. J Biol Chem 2002; 277: 48441-8. (Pubitemid 35470802)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48441-48448
    • Leonard, A.S.1    Bayer, K.U.2    Merrill, M.A.3    Lim, I.A.4    Shea, M.A.5    Schulman, H.6    Hell, J.W.7
  • 87
    • 0035930919 scopus 로고    scopus 로고
    • Regulation of signal transduction by protein targeting: The case for CaMKII
    • DOI 10.1006/bbrc.2001.6063
    • Bayer KU, Schulman H. Regulation of signal transduction by protein targeting: the case for CaMKII. Biochem Biophys Res Commun 2001; 289: 917-23. (Pubitemid 34076276)
    • (2001) Biochemical and Biophysical Research Communications , vol.289 , Issue.5 , pp. 917-923
    • Bayer K.Ulrich1    Schulman, H.2
  • 88
    • 2942607447 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II and synaptic plasticity
    • DOI 10.1016/j.conb.2004.05.008, PII S0959438804000753
    • Colbran RJ, Brown AM. Calcium/calmodulin-dependent protein kinase II and synaptic plasticity. Curr Opin Neurobiol 2004; 14: 318-27. (Pubitemid 38759862)
    • (2004) Current Opinion in Neurobiology , vol.14 , Issue.3 , pp. 318-327
    • Colbran, R.J.1    Brown, A.M.2
  • 89
    • 27744460701 scopus 로고    scopus 로고
    • Activity-driven postsynaptic translocation of CaMKII
    • DOI 10.1016/j.tips.2005.10.003, PII S0165614705002683
    • Merrill MA, Chen Y, Strack S, Hell JW. Activity-driven postsynaptic translocation of CaMKII. Trends Pharmacol Sci 2005; 26: 645-53. (Pubitemid 41636310)
    • (2005) Trends in Pharmacological Sciences , vol.26 , Issue.12 , pp. 645-653
    • Merrill, M.A.1    Chen, Y.2    Strack, S.3    Hell, J.W.4
  • 90
    • 0035095802 scopus 로고    scopus 로고
    • Light scattering and transmission electron microscopy studies reveal a mechanism for calcium/calmodulin-dependent protein kinase II self-association
    • DOI 10.1046/j.1471-4159.2001.00119.x
    • Hudmon A, Kim SA, Kolb SJ, Stoops JK, Waxham MN. Light scattering and transmission electron microscopy studies reveal a mechanism for calcium/calmodulin-dependent protein kinase II self-association. J Neurochem 2001; 76: 1364-75. (Pubitemid 32198241)
    • (2001) Journal of Neurochemistry , vol.76 , Issue.5 , pp. 1364-1375
    • Hudmon, A.1    Kim, S.A.2    Kolb, S.J.3    Stoops, J.K.4    Neal Waxham, M.5
  • 91
    • 71749112585 scopus 로고    scopus 로고
    • Differential regulation by ATP versus ADP further links CaMKII aggregation to ischemic conditions
    • Vest RS, OLeary H, Bayer KU. Differential regulation by ATP versus ADP further links CaMKII aggregation to ischemic conditions. FEBS Lett 2009; 583: 3577-81.
    • (2009) FEBS Lett , vol.583 , pp. 3577-81
    • Vest, R.S.1    Oleary, H.2    Bayer, K.U.3
  • 92
    • 0034604651 scopus 로고    scopus 로고
    • Mechanism and regulation of calcium/calmodulin-dependent protein kinase II targeting to the NR2B subunit of the N-methyl-D-aspartate receptor
    • DOI 10.1074/jbc.M001471200
    • Strack S, McNeill RB, Colbran RJ. Mechanism and regulation of calcium/calmodulin-dependent protein kinase II targeting to the NR2B subunit of the N-methyl-D-aspartate receptor. J Biol Chem 2000; 275: 23798-806. (Pubitemid 30624665)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.31 , pp. 23798-23806
    • Strack, S.1    McNeill, R.B.2    Colbran, R.J.3
  • 93
    • 0026668149 scopus 로고
    • Ischemia-induced translocation of Ca2+/calmodulin-dependent protein kinase II: Potential role in neuronal damage
    • Aronowski J, Grotta JC, Waxham MN. Ischemia-induced translocation of Ca2+/calmodulin-dependent protein kinase II: potential role in neuronal damage. J Neurochem 1992; 58: 1743-53.
    • (1992) J Neurochem , vol.58 , pp. 1743-53
    • Aronowski, J.1    Grotta, J.C.2    Waxham, M.N.3
  • 94
    • 0028173233 scopus 로고
    • Activity of Ca2+/ calmodulin-dependent protein kinase II following ischemia: A comparison between CA1 and dentate gyrus in a hippocampal slice model
    • Westgate SA, Brown J, Aronowski J, Waxham MN. Activity of Ca2+/ calmodulin-dependent protein kinase II following ischemia: a comparison between CA1 and dentate gyrus in a hippocampal slice model. J Neurochem 1994; 63: 2217-24.
    • (1994) J Neurochem , vol.63 , pp. 2217-24
    • Westgate, S.A.1    Brown, J.2    Aronowski, J.3    Waxham, M.N.4
  • 95
    • 0028903333 scopus 로고
    • Excitotoxic activation of the NMDA receptor results in inhibition of calcium/calmodulin kinase II activity in cultured hippocampal neurons
    • Churn S, Limbrick D, Sombati S, DeLorenzo R. Excitotoxic activation of the NMDA receptor results in inhibition of calcium/calmodulin kinase II activity in cultured hippocampal neurons. J Neurosci 1995; 15: 3200-14.
    • (1995) J Neurosci , vol.15 , pp. 3200-14
    • Churn, S.1    Limbrick, D.2    Sombati, S.3    Delorenzo, R.4
  • 96
    • 0025259442 scopus 로고
    • KN-62,1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4- phenylpiperazi ne, a specific inhibitor of Ca2+/calmodulin-dependent protein kinase II
    • Tokumitsu H, Chijiwa T, Hagiwara M, Mizutani A, Terasawa M, Hidaka H. KN-62,1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4- phenylpiperazi ne, a specific inhibitor of Ca2+/calmodulin-dependent protein kinase II. J Biol Chem 1990; 265: 4315-20.
    • (1990) J Biol Chem , vol.265 , pp. 4315-20
    • Tokumitsu, H.1    Chijiwa, T.2    Hagiwara, M.3    Mizutani, A.4    Terasawa, M.5    Hidaka, H.6
  • 97
    • 0026345859 scopus 로고
    • The newly synthesized selective Ca2+/calmodulin dependent protein kinase II inhibitor KN-93 reduces dopamine contents in PC12h cells
    • Sumi M, Kiuchi K, Ishikawa T, Ishii A, Hagiwara M, Nagatsu T, et al. The newly synthesized selective Ca2+/calmodulin dependent protein kinase II inhibitor KN-93 reduces dopamine contents in PC12h cells. Biochem Biophys Res Commun 1991; 181: 968-75.
    • (1991) Biochem Biophys Res Commun , vol.181 , pp. 968-75
    • Sumi, M.1    Kiuchi, K.2    Ishikawa, T.3    Ishii, A.4    Hagiwara, M.5    Nagatsu, T.6
  • 98
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 2000; 351: 95-105.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 99
    • 0028176722 scopus 로고
    • Characterization of Ca2+/calmodulin-dependent protein kinase IV. Role in transcriptional regulation
    • Enslen H, Sun P, Brickey D, Soderling SH, Klamo E, Soderling TR . Characterization of Ca2+/calmodulin-dependent protein kinase IV. Role in transcriptional regulation. J Biol Chem 1994; 269: 15520-7.
    • (1994) J Biol Chem , vol.269 , pp. 15520-7
    • Enslen, H.1    Sun, P.2    Brickey, D.3    Soderling, S.H.4    Klamo, E.5    Soderling, T.R.6
  • 101
    • 79953182338 scopus 로고    scopus 로고
    • CaMKII inhibitors disrupt AKAP79-dependent PKC signaling to GluA1 AMPA receptors
    • Brooks IM, Tavalin SJ. CaMKII inhibitors disrupt AKAP79-dependent PKC signaling to GluA1 AMPA receptors. J Biol Chem 2011; 286: 6697-706.
    • (2011) J Biol Chem , vol.286 , pp. 6697-706
    • Brooks, I.M.1    Tavalin, S.J.2
  • 102
    • 0027050005 scopus 로고
    • Inhibition of voltage-gated Ca2+ channels and insulin secretion in HIT cells by the Ca2+/calmodulindependent protein kinase II inhibitor KN-62: Comparison with antagonists of calmodulin and L-type Ca2+ channels
    • L i G, Hidaka H, Wollheim CB. Inhibition of voltage-gated Ca2+ channels and insulin secretion in HIT cells by the Ca2+/calmodulindependent protein kinase II inhibitor KN-62: comparison with antagonists of calmodulin and L-type Ca2+ channels. Mol Pharmacol 1992; 42: 489-8.
    • (1992) Mol Pharmacol , vol.42 , pp. 489-8
    • Li, G.1    Hidaka, H.2    Wollheim, C.B.3
  • 104
  • 105
    • 0033583175 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent phosphorylation and activation of human Cdc25-C at the G2/M phase transition in HeLa cells
    • Patel R, Holt M, Philipova R, Moss S, Schulman H, Hidaka H, et al. Calcium/calmodulin-dependent phosphorylation and activation of human Cdc25-C at the G2/M phase transition in HeLa cells. J Biol Chem 1999; 274: 7958-68.
    • (1999) J Biol Chem , vol.274 , pp. 7958-68
    • Patel, R.1    Holt, M.2    Philipova, R.3    Moss, S.4    Schulman, H.5    Hidaka, H.6
  • 107
    • 0025088506 scopus 로고
    • Specificities of autoinhibitory domain peptides for four protein kinases. Implications for intact cell studies of protein kinase function
    • Smith MK, Colbran RJ, Soderling TR. Specificities of autoinhibitory domain peptides for four protein kinases. Implications for intact cell studies of protein kinase function. J Biol Chem 1990; 265: 1837-40.
    • (1990) J Biol Chem , vol.265 , pp. 1837-40
    • Smith, M.K.1    Colbran, R.J.2    Soderling, T.R.3
  • 108
    • 60549085044 scopus 로고    scopus 로고
    • The delta isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload
    • Backs J, Backs T, Neef S, Kreusser MM, Lehmann LH , Patrick DM, et al. The delta isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload. Proc Natl Acad Sci U S A 2009; 106: 2342-7.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2342-7
    • Backs, J.1    Backs, T.2    Neef, S.3    Kreusser, M.M.4    Lehmann, L.H.5    Patrick, D.M.6
  • 109
    • 0033583175 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent phosphorylation and activation of human Cdc25-C at the G2/M phase transition in HeLa cells
    • Patel R, Holt M, Philipova R, Moss S, Schulman H, Hidaka H, et al. Calcium/calmodulin-dependent phosphorylation and activation of human Cdc25-C at the G2/M phase transition in HeLa cells. J Biol Chem 1999; 274: 7958-68.
    • (1999) J Biol Chem , vol.274 , pp. 7958-68
    • Patel, R.1    Holt, M.2    Philipova, R.3    Moss, S.4    Schulman, H.5    Hidaka, H.6
  • 110
    • 0035065721 scopus 로고    scopus 로고
    • Is persistent activity of calcium/calmodulin-dependent kinase required for the maintenance of LTP?
    • Chen HX, Otmakhov N, Strack S, Colbran RJ, Lisman JE. Is persistent activity of calcium/calmodulin-dependent kinase required for the maintenance of LT P? J Neurophysiol 2001; 85: 1368-76. (Pubitemid 32280578)
    • (2001) Journal of Neurophysiology , vol.85 , Issue.4 , pp. 1368-1376
    • Chen, H.-X.1    Otmakhov, N.2    Strack, S.3    Colbran, R.J.4    Lisman, J.E.5
  • 115
    • 1542609485 scopus 로고    scopus 로고
    • Transduction peptides: From technology to physiology
    • DOI 10.1038/ncb0304-189
    • Joliot A, Prochiantz A. Transduction peptides: from technology to physiology. Nat Cell Biol 2004; 6: 189-96. (Pubitemid 38344356)
    • (2004) Nature Cell Biology , vol.6 , Issue.3 , pp. 189-196
    • Joliot, A.1    Prochiantz, A.2
  • 116
    • 0042347897 scopus 로고    scopus 로고
    • Selective regulation of neurite extension and synapse formation by the β but not the α isoform of CaMKII
    • DOI 10.1016/S0896-6273(03)00428-8
    • Fink CC, Bayer KU, Myers JW, Ferrell JE Jr, Schulman H, Meyer T. Selective regulation of neurite extension and synapse formation by the beta but not the alpha isoform of CaMKII. Neuron 2003; 39: 283-97. (Pubitemid 36897550)
    • (2003) Neuron , vol.39 , Issue.2 , pp. 283-297
    • Fink, C.C.1    Bayer, K.-U.2    Myers, J.W.3    Ferrell Jr., J.E.4    Schulman, H.5    Meyer, T.6
  • 117
    • 0242413666 scopus 로고    scopus 로고
    • Calcium/Calmodulin-dependent Protein Kinase II Binds to Raf-1 and Modulates Integrin-stimulated ERK Activation
    • DOI 10.1074/jbc.M305355200
    • Illario M, Cavallo AL, Bayer KU, Di Matola T, Fenzi G, Rossi G, et al. Calcium/calmodulin-dependent protein kinase II binds to Raf-1 and modulates integrin-stimulated ER K activation. J Biol Chem 2003; 278: 45101-8. (Pubitemid 37432642)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45101-45108
    • Illario, M.1    Cavallo, A.L.2    Bayer, K.U.3    Di Matola, T.4    Fenzi, G.5    Rossi, G.6    Vitale, M.7
  • 118
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • DOI 10.1126/science.285.5433.1569
    • Schwarze SR, Ho A, Vocero-Akbani A, Dowdy SF. In vivo protein transduction: delivery of a biologically active protein into the mouse. Science 1999; 285: 1569-72. (Pubitemid 29420581)
    • (1999) Science , vol.285 , Issue.5433 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 119
    • 0029040992 scopus 로고
    • A specific inhibitor of calcium/ calmodulin-dependent protein kinase-II provides neuroprotection against NMDA- and hypoxia/hypoglycemia-induced cell death
    • H ajimohammadreza I, Probert AW, Coughenour LL , Borosky SA, Marcoux FW, Boxer PA, et al. A specific inhibitor of calcium/ calmodulin-dependent protein kinase-II provides neuroprotection against NMDA- and hypoxia/hypoglycemia- induced cell death. J Neurosci 1995; 15: 4093-101.
    • (1995) J Neurosci , vol.15 , pp. 4093-101
    • Hajimohammadreza, I.1    Probert, A.W.2    Coughenour, L.L.3    Borosky, S.A.4    Marcoux, F.W.5    Boxer, P.A.6
  • 120
    • 0034727899 scopus 로고    scopus 로고
    • Neuroprotective effect of AIP on N-methyl-D-aspartate-induced cell death in retinal neurons
    • DOI 10.1016/S0169-328X(00)00226-6, PII S0169328X00002266
    • L aabich A, Cooper NG. Neuroprotective effect of AIP on N-methyl-Daspartate- induced cell death in retinal neurons. Brain Res Mol Brain Res 2000; 85: 32-40. (Pubitemid 32063059)
    • (2000) Molecular Brain Research , vol.85 , Issue.1-2 , pp. 32-40
    • Laabich, A.1    Cooper, N.G.F.2
  • 121
    • 0037423008 scopus 로고    scopus 로고
    • Calmodulin and calmodulin-dependent kinase II mediate neuronal cell death induced by depolarization
    • DOI 10.1016/S0006-8993(02)03932-X, PII S000689930203932X
    • Takano H, Fukushi H, Morishima Y, Shirasaki Y. Calmodulin and calmodulin-dependent kinase II mediate neuronal cell death induced by depolarization. Brain Res 2003 962 41-7. (Pubitemid 36126320)
    • (2003) Brain Research , vol.962 , Issue.1-2 , pp. 41-47
    • Takano, H.1    Fukushi, H.2    Morishima, Y.3    Shirasaki, Y.4
  • 122
    • 31144456872 scopus 로고    scopus 로고
    • The role of CaMKII in BDNF-mediated neuroprotection of retinal ganglion cells (RGC-5)
    • DOI 10.1016/j.brainres.2005.10.030, PII S0006899305014320
    • Fan W, Agarwal N, Cooper NG. The role of CaMKII in BDNF-mediated neuroprotection of retinal ganglion cells (RGC-5). Brain Res 2006; 1067: 48-57. (Pubitemid 43133073)
    • (2006) Brain Research , vol.1067 , Issue.1 , pp. 48-57
    • Fan, W.1    Agarwal, N.2    Cooper, N.G.F.3
  • 123
    • 27844502151 scopus 로고    scopus 로고
    • Coupling between NMDA receptor and acid-sensing ion channel contributes to ischemic neuronal death
    • DOI 10.1016/j.neuron.2005.10.011, PII S0896627305008342
    • Gao J, Duan B, Wang DG, Deng XH, Zhang GY, Xu L, et al. Coupling between NMDA receptor and acid-sensing ion channel contributes to ischemic neuronal death. Neuron 2005; 48: 635-46. (Pubitemid 41654684)
    • (2005) Neuron , vol.48 , Issue.4 , pp. 635-646
    • Gao, J.1    Duan, B.2    Wang, D.-G.3    Deng, X.-H.4    Zhang, G.-Y.5    Xu, L.6    Xu, T.-L.7
  • 126
    • 0142135022 scopus 로고    scopus 로고
    • 2+/Calmodulin-dependent Kinase II Promotes Depolarization-mediated Cerebellar Granule Neuron Survival
    • DOI 10.1074/jbc.M307245200
    • L inseman DA, Bartley CM, Le SS, Laessig TA, Bouchard RJ, Meintzer MK, et al. Inactivation of the myocyte enhancer factor-2 repressor histone deacetylase-5 by endogenous Ca2+/calmodulin-dependent kinase II promotes depolarization-mediated cerebellar granule neuron survival. J Biol Chem 2003; 278: 41472-81. (Pubitemid 37280976)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.42 , pp. 41472-41481
    • Linseman, D.A.1    Bartley, C.M.2    Le, S.S.3    Laessig, T.A.4    Bouchard, R.J.5    Meintzer, M.K.6    Li, M.7    Heidenreich, K.A.8
  • 127
    • 34548514227 scopus 로고    scopus 로고
    • CaMKII and CaMKIV mediate distinct prosurvival signaling pathways in response to depolarization in neurons
    • DOI 10.1016/j.mcn.2007.05.008, PII S1044743107001297
    • Bok J, Wang Q, Huang J, Green SH. CaMKII and CaMKIV mediate distinct prosurvival signaling pathways in response to depolarization in neurons. Mol Cell Neurosci 2007; 36: 13-26. (Pubitemid 47379552)
    • (2007) Molecular and Cellular Neuroscience , vol.36 , Issue.1 , pp. 13-26
    • Bok, J.1    Wang, Q.2    Huang, J.3    Green, S.H.4
  • 128
    • 0037446081 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinases II and IV both promote survival but differ in their effects on axon growth in spiral ganglion neurons
    • DOI 10.1002/jnr.10551
    • H ansen MR, Bok J, Devaiah AK, Zha XM, Green SH. Ca2+/calmodulindependent protein kinases II and IV both promote survival but differ in their effects on axon growth in spiral ganglion neurons. J Neurosci Res 2003; 72: 169-84. (Pubitemid 36389883)
    • (2003) Journal of Neuroscience Research , vol.72 , Issue.2 , pp. 169-184
    • Hansen, M.R.1    Bok, J.2    Devaiah, A.K.3    Zha, X.-M.4    Green, S.H.5
  • 130
    • 67049162108 scopus 로고    scopus 로고
    • Kinase-dead knock-in mouse reveals an essential role of kinase activity of Ca2+/calmodulin-dependent protein kinase II{alpha} in dendritic spine enlargement, long-term potentiation, and learning
    • Y amagata Y, Kobayashi S, Umeda T, Inoue A, Sakagami H, Fukaya M, et al. Kinase-dead knock-in mouse reveals an essential role of kinase activity of Ca2+/calmodulin-dependent protein kinase II{alpha} in dendritic spine enlargement, long-term potentiation, and learning. J Neurosci 2009; 29: 7607-18.
    • (2009) J Neurosci , vol.29 , pp. 7607-18
    • Yamagata, Y.1    Kobayashi, S.2    Umeda, T.3    Inoue, A.4    Sakagami, H.5    Fukaya, M.6
  • 132
    • 0035175495 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase type IV (CaMKIV) inhibits apoptosis induced by potassium deprivation in cerebellar granule neurons
    • DOI 10.1096/fj.00-0106com
    • See V, Boutillier AL, Bito H, Loeffler JP. Calcium/calmodulindependent protein kinase type IV (CaMKIV) inhibits apoptosis induced by potassium deprivation in cerebellar granule neurons. FASEB J 2001; 15: 134-44. (Pubitemid 32061664)
    • (2001) FASEB Journal , vol.15 , Issue.1 , pp. 134-144
    • See, V.1    Boutillier, A.-L.2    Bito, H.3    Loeffler, J.-P.4
  • 133
    • 0035956978 scopus 로고    scopus 로고
    • Activity-dependent CREB phosphorylation: Convergence of a fast, sensitive calmodulin kinase pathway and a slow, less sensitive mitogen-activated protein kinase pathway
    • DOI 10.1073/pnas.051634198
    • Wu GY, Deisseroth K, Tsien RW. Activity-dependent CRE B phosphorylation: convergence of a fast, sensitive calmodulin kinase pathway and a slow, less sensitive mitogen-activated protein kinase pathway. Proc Natl Acad Sci U S A 2001; 98: 2808-13. (Pubitemid 32209565)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.5 , pp. 2808-2813
    • Wu, G.-Y.1    Deisseroth, K.2    Tsien, R.W.3
  • 134
    • 33744900895 scopus 로고    scopus 로고
    • Activity-Dependent Dendritic Arborization Mediated by CaM-Kinase I Activation and Enhanced CREB-Dependent Transcription of Wnt-2
    • DOI 10.1016/j.neuron.2006.05.008, PII S0896627306003746
    • Wayman GA, Impey S, Marks D, Saneyoshi T, Grant WF, Derkach V, et al. Activity-dependent dendritic arborization mediated by CaM-kinase I activation and enhanced CRE B-dependent transcription of Wnt-2. Neuron 2006; 50: 897-909. (Pubitemid 43850689)
    • (2006) Neuron , vol.50 , Issue.6 , pp. 897-909
    • Wayman, G.A.1    Impey, S.2    Marks, D.3    Saneyoshi, T.4    Grant, W.F.5    Derkach, V.6    Soderling, T.R.7
  • 136
    • 0032506514 scopus 로고    scopus 로고
    • Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway
    • DOI 10.1038/25147
    • Yano S, Tokumitsu H, Soderling TR. Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway. Nature 1998 396 584-7. (Pubitemid 28563720)
    • (1998) Nature , vol.396 , Issue.6711 , pp. 584-587
    • Yano, S.1    Tokumitsu, H.2    Soderling, T.R.3
  • 138
    • 77649271004 scopus 로고    scopus 로고
    • Effects of AMP-activated protein kinase in cerebral ischemia
    • Li J, McCullough LD . Effects of AMP-activated protein kinase in cerebral ischemia. J Cereb Blood Flow Metab 2010 30 480-92.
    • (2010) J Cereb Blood Flow Metab , vol.30 , pp. 480-92
    • Li, J.1    McCullough, L.D.2
  • 140
    • 0022542884 scopus 로고
    • Adaptation of adult brain tissue to anoxia and hypoxia in vitro
    • DOI 10.1016/0006-8993(86)90418-X
    • Schurr A, Reid KH, Tseng MT, West C, Rigor BM. Adaptation of adult brain tissue to anoxia and hypoxia in vitro. Brain Res 1986; 374: 244-8. (Pubitemid 16077975)
    • (1986) Brain Research , vol.374 , Issue.2 , pp. 244-248
    • Schurr, A.1    Reid, K.H.2    Tseng, M.T.3
  • 142
    • 0026702946 scopus 로고
    • Protection of rat hippocampus against ischemic neuronal damage by pretreatment with sublethal ischemia
    • Liu Y, Kato H, Nakata N, Kogure K. Protection of rat hippocampus against ischemic neuronal damage by pretreatment with sublethal ischemia. Brain Research 1992 586 121-4.
    • (1992) Brain Research , vol.586 , pp. 121-4
    • Liu, Y.1    Kato, H.2    Nakata, N.3    Kogure, K.4
  • 144
    • 20144368904 scopus 로고    scopus 로고
    • Pharmacological inhibition of AMP-activated protein kinase provides neuroprotection in stroke
    • DOI 10.1074/jbc.M409985200
    • McCullough LD, Zeng Z, Li H, Landree LE, McFadden J, Ronnett GV. Pharmacological inhibition of AMP-activated protein kinase provides neuroprotection in stroke. J Biol Chem 2005; 280: 20493-502. (Pubitemid 40776749)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.21 , pp. 20493-20502
    • McCullough, L.D.1    Zeng, Z.2    Li, H.3    Landree, L.E.4    McFadden, J.5    Ronnett, G.V.6
  • 145
    • 74549173438 scopus 로고    scopus 로고
    • DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke
    • T u W, Xu X, Peng L, Zhong X, Zhang W, Soundarapandian MM, et al. DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage in stroke. Cell 2010; 140: 222-34.
    • (2010) Cell , vol.140 , pp. 222-34
    • Tu, W.1    Xu, X.2    Peng, L.3    Zhong, X.4    Zhang, W.5    Soundarapandian, M.M.6
  • 146
    • 78649983743 scopus 로고    scopus 로고
    • Treatment of cerebral ischemia by disrupting ischemia-induced interaction of nNOS with PSD-95
    • Zhou L, Li F, Xu HB, Luo CX, Wu HY , Zhu MM, et al. Treatment of cerebral ischemia by disrupting ischemia-induced interaction of nNOS with PSD-95. Nat Med 2010; 16: 1439-43.
    • (2010) Nat Med , vol.16 , pp. 1439-43
    • Zhou, L.1    Li, F.2    Xu, H.B.3    Luo, C.X.4    Wu, H.Y.5    Zhu, M.M.6
  • 148
    • 0030744875 scopus 로고    scopus 로고
    • Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
    • DOI 10.1126/science.276.5321.2042
    • Barria A, Muller D, Derkach V, Griffith LC, Soderling TR. Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation. Science 1997; 276: 2042-5. (Pubitemid 27443609)
    • (1997) Science , vol.276 , Issue.5321 , pp. 2042-2045
    • Barria, A.1    Muller, D.2    Derkach, V.3    Griffith, L.C.4    Soderling, T.R.5
  • 149
    • 24944528380 scopus 로고    scopus 로고
    • Dominant role of the GluR2 subunit in regulation of AMPA receptors by CaMKII
    • Oh MC, Derkach VA. Dominant role of the GluR2 subunit in regulation of AMPA receptors by CaMKII. Nat Neurosci 2005 8 853-4.
    • (2005) Nat Neurosci , vol.8 , pp. 853-4
    • Oh, M.C.1    Derkach, V.A.2
  • 150
    • 0025923461 scopus 로고
    • 2+ permeability of KA-AMPA - gated glutamate receptor channels depends on subunit composition
    • H ollmann M, Hartley M, Heinemann S. Ca2+ permeability of KAAMPA- gated glutamate receptor channels depends on subunit composition. Science 1991; 252: 851-3. (Pubitemid 121000528)
    • (1991) Science , vol.252 , Issue.5007 , pp. 851-853
    • Hollmann, M.1    Hartley, M.2    Heinemann, S.3
  • 151
    • 0025879427 scopus 로고
    • Structural determinants of ion flow through recombinant glutamate receptor channels
    • Verdoorn T, Burnashev N, Monyer H, Seeburg P, Sakmann, B. Structural determinants of ion flow through recombinant glutamate receptor channels. Science 1991; 252: 1715-8. (Pubitemid 21917095)
    • (1991) Science , vol.252 , Issue.5013 , pp. 1715-1718
    • Verdoorn, T.A.1    Burnashev, N.2    Monyer, H.3    Seeburg, P.H.4    Sakmann, B.5
  • 152
    • 33847125205 scopus 로고    scopus 로고
    • 2+-permeable AMPA receptors in synaptic plasticity and neuronal death
    • DOI 10.1016/j.tins.2007.01.006, PII S0166223607000203
    • Liu SJ, Zukin RS. Ca2+-permeable AMPA receptors in synaptic plasticity and neuronal death. Trends Neurosci 2007 30 126-34. (Pubitemid 46283597)
    • (2007) Trends in Neurosciences , vol.30 , Issue.3 , pp. 126-134
    • Liu, S.J.1    Zukin, R.S.2
  • 153
    • 27744483468 scopus 로고    scopus 로고
    • 2+ signals for facilitation
    • DOI 10.1083/jcb.200505155
    • Hudmon A, Schulman H, Kim J, Maltez JM, Tsien RW, Pitt GS. CaMKII tethers to L-type Ca2+ channels, establishing a local and dedicated integrator of Ca2+ signals for facilitation. J Cell Biol 2005 171 537-47. (Pubitemid 41586942)
    • (2005) Journal of Cell Biology , vol.171 , Issue.3 , pp. 537-547
    • Hudmon, A.1    Schulman, H.2    Kim, J.3    Maltez, J.M.4    Tsien, R.W.5    Pitt, G.S.6
  • 155
    • 58549118713 scopus 로고    scopus 로고
    • The neuronal connexin36 interacts with and is phosphorylated by CaMKII in a way similar to CaMKII interaction with glutamate receptors
    • Alev C, Urschel S, Sonntag S, Zoidl G, Fort AG, Hoher T, et al. The neuronal connexin36 interacts with and is phosphorylated by CaMKII in a way similar to CaMKII interaction with glutamate receptors. Proc Natl Acad Sci U S A 2008; 105: 20964-9.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 20964-9
    • Alev, C.1    Urschel, S.2    Sonntag, S.3    Zoidl, G.4    Fort, A.G.5    Hoher, T.6
  • 156
    • 0035478279 scopus 로고    scopus 로고
    • Global Ischemia-induced Increases in the Gap Junctional Proteins Connexin (Cx32) and Cx36 in Hippocampus and Enhanced Vulnerability of Cx32 Knock-out Mice
    • O guro K, Jover T, Tanaka H, Lin Y, Kojima T, Oguro N, et al. Global ischemia-induced increases in the gap junctional proteins connexin (Cx32) and Cx36 in hippocampus and enhanced vulnerability of Cx32 knock-out mice. J Neurosci 2001; 21: 7534-42.
    • (2001) J Neurosci , vol.21 , pp. 7534-42
    • Oguro, K.1    Jover, T.2    Tanaka, H.3    Lin, Y.4    Kojima, T.5    Oguro, N.6
  • 158
    • 9644302728 scopus 로고    scopus 로고
    • Role of connexin-based gap junction channels and hemichannels in ischemia-induced cell death in nervous tissue
    • DOI 10.1016/j.brainresrev.2004.08.002, PII S0165017304001201, Chemical and Electrical Synapses
    • Contreras JE, Sanchez HA, Veliz LP, Bukauskas FF, Bennett MV, Saez JC. Role of connexin-based gap junction channels and hemichannels in ischemia-induced cell death in nervous tissue. Brain Res Brain Res Rev 2004; 47: 290-303. (Pubitemid 39574326)
    • (2004) Brain Research Reviews , vol.47 , Issue.1-3 , pp. 290-303
    • Contreras, J.E.1    Sanchez, H.A.2    Veliz, L.P.3    Bukauskas, F.F.4    Bennett, M.V.L.5    Saez, J.C.6
  • 160
    • 33746233388 scopus 로고    scopus 로고
    • RNA-binding proteins: A lesson in repression
    • Wells DG. RNA-binding proteins: a lesson in repression. J Neurosci 2006; 26: 7135-8.
    • (2006) J Neurosci , vol.26 , pp. 7135-8
    • Wells, D.G.1
  • 161
    • 34249908103 scopus 로고    scopus 로고
    • CPEB: A life in translation
    • DOI 10.1016/j.tibs.2007.04.004, PII S0968000407000928
    • R ichter JD. CPEB: a life in translation. Trends Biochem Sci 2007; 32: 279-85. (Pubitemid 46874928)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.6 , pp. 279-285
    • Richter, J.D.1
  • 162
    • 0032215079 scopus 로고    scopus 로고
    • CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of α-CaMKII mRNA at synapses
    • DOI 10.1016/S0896-6273(00)80630-3
    • Wu L, Wells D, Tay J, Mendis D, Abbott MA, Barnitt A, et al. CPEBmediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of [alpha]-camkii mrna at synapses. Neuron 1998; 21: 1129-39. (Pubitemid 29018082)
    • (1998) Neuron , vol.21 , Issue.5 , pp. 1129-1139
    • Wu, L.1    Wells, D.2    Tay, J.3    Mendis, D.4    Abbott, M.-A.5    Barnitt, A.6    Quinlan, E.7    Heynen, A.8    Fallon, J.R.9    Richter, J.D.10
  • 163
    • 70350539645 scopus 로고    scopus 로고
    • Cytoplasmic polyadenylation element-binding protein regulates neurotrophin-3-dependent {beta}- catenin mrna translation in developing hippocampal neurons
    • Kundel M, Jones KJ, Shin CY, Wells DG. Cytoplasmic polyadenylation element-binding protein regulates neurotrophin-3-dependent {beta}- catenin mrna translation in developing hippocampal neurons. J Neurosci 2009; 29: 13630-9.
    • (2009) J Neurosci , vol.29 , pp. 13630-9
    • Kundel, M.1    Jones, K.J.2    Shin, C.Y.3    Wells, D.G.4
  • 164
    • 77950921560 scopus 로고    scopus 로고
    • Contributions of poly(ADP-ribose) polymerase-1 and -2 to nuclear translocation of apoptosis-inducing factor and injury from focal cerebral ischemia
    • L i X, Klaus JA, Zhang J, Xu Z, Kibler KK, Andrabi SA, et al. Contributions of poly(ADP-ribose) polymerase-1 and -2 to nuclear translocation of apoptosis-inducing factor and injury from focal cerebral ischemia. J Neurochem 2010; 113: 1012-22.
    • (2010) J Neurochem , vol.113 , pp. 1012-22
    • Li, X.1    Klaus, J.A.2    Zhang, J.3    Xu, Z.4    Kibler, K.K.5    Andrabi, S.A.6
  • 165
    • 0034623146 scopus 로고    scopus 로고
    • Inhibition of neuronal nitric-oxide synthase by calcium/calmodulin- dependent protein kinase II through Ser847 phosphorylation in NG108-15 neuronal cells
    • Komeima K, Hayashi Y, Naito Y, Watanabe Y. Inhibition of neuronal nitric-oxide synthase by calcium/calmodulin-dependent protein kinase II through Ser847 phosphorylation in NG108-15 neuronal cells. J Biol Chem 2000; 275: 28139-43.
    • (2000) J Biol Chem , vol.275 , pp. 28139-43
    • Komeima, K.1    Hayashi, Y.2    Naito, Y.3    Watanabe, Y.4
  • 167
    • 1842790618 scopus 로고    scopus 로고
    • Bidirectional Regulation of Neuronal Nitric-oxide Synthase Phosphorylation at Serine 847 by the N-Methyl-D-aspartate Receptor
    • DOI 10.1074/jbc.M311103200
    • R ameau GA, Chiu LY , Ziff EB. Bidirectional regulation of neuronal nitric-oxide synthase phosphorylation at Serine 847 by the N-methyl- D-aspartate receptor . J Biol Chem 2004; 279: 14307-14. (Pubitemid 38468971)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 14307-14314
    • Rameaut, G.A.1    Chiu, L.-Y.2    Ziff, E.B.3
  • 168
    • 34047148363 scopus 로고    scopus 로고
    • Biphasic coupling of neuronal nitric oxide synthase phosphorylation to the NMDA receptor regulates AMPA receptor trafficking and neuronal cell death
    • DOI 10.1523/JNEUROSCI.4799-06.2007
    • R ameau GA, Tukey DS, Garcin-Hosfield ED , Titcombe RF, Misra C, Khatri L, et al. Biphasic coupling of neuronal nitric oxide synthase phosphorylation to the NMDA receptor regulates AMPA receptor trafficking and neuronal cell death. J Neurosci 2007; 27: 3445-55. (Pubitemid 46515122)
    • (2007) Journal of Neuroscience , vol.27 , Issue.13 , pp. 3445-3455
    • Rameau, G.A.1    Tukey, D.S.2    Garcin-Hosfield, E.D.3    Titcombe, R.F.4    Misra, C.5    Khatri, L.6    Getzoff, E.D.7    Ziff, E.B.8
  • 169
    • 0029927787 scopus 로고    scopus 로고
    • Resistance to neurotoxicity in cortical cultures from neuronal nitric oxide synthase-deficient mice
    • D awson V, Kizushi V, Huang P, Snyder S, Dawson T. Resistance to neurotoxicity in cortical cultures from neuronal nitric oxide synthasedeficient mice. J Neurosci 1996; 16: 2479-87. (Pubitemid 26122672)
    • (1996) Journal of Neuroscience , vol.16 , Issue.8 , pp. 2479-2487
    • Dawson, V.L.1    Kizushi, V.M.2    Huang, P.L.3    Snyder, S.H.4    Dawson, T.M.5
  • 171
    • 0034097511 scopus 로고    scopus 로고
    • Involvement of peroxynitrite and hydroxyradical generated from nitric oxide in hypoxia/reoxygenation injury in rat cerebrocortical slices
    • DOI 10.1016/S0028-3908(99)00197-5, PII S0028390899001975
    • Oka M, Hirouchi M, Itoh Y, Ukai Y. Involvement of peroxynitrite and hydroxyradical generated from nitric oxide in hypoxia/reoxygenation injury in rat cerebrocortical slices. Neuropharmacology 2000 39 1319-30. (Pubitemid 30173196)
    • (2000) Neuropharmacology , vol.39 , Issue.7 , pp. 1319-1330
    • Oka, M.1    Hirouchi, M.2    Itoh, Y.3    Ukai, Y.4
  • 172
    • 67349230279 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase: Structure, subcellular localization, regulation, and clinical implications
    • Zhou L, Zhu DY . Neuronal nitric oxide synthase: structure, subcellular localization, regulation, and clinical implications. Nitric Oxide 2009; 20: 223-30.
    • (2009) Nitric Oxide , vol.20 , pp. 223-30
    • Zhou, L.1    Zhu, D.Y.2
  • 173
    • 18044378434 scopus 로고    scopus 로고
    • CaMKIIα enhances the desensitization of NR2B-containing NMDA receptors by an autophosphorylation-dependent mechanism
    • DOI 10.1016/j.mcn.2005.01.006
    • Sessoms-Sikes S, Honse Y, Lovinger DM, Colbran RJ. CaMKIIalpha enhances the desensitization of NR2B-containing NMDA receptors by an autophosphorylation- dependent mechanism. Mol Cell Neurosci 2005; 29: 139-47. (Pubitemid 40603887)
    • (2005) Molecular and Cellular Neuroscience , vol.29 , Issue.1 , pp. 139-147
    • Sessoms-Sikes, S.1    Honse, Y.2    Lovinger, D.M.3    Colbran, R.J.4
  • 174
    • 37549067018 scopus 로고    scopus 로고
    • NMDA receptor activation potentiates inhibitory transmission through GABA receptorassociated protein-dependent exocytosis of GABAA receptors
    • Marsden KC, Beattie JB, Friedenthal J, Carroll RC. NMDA receptor activation potentiates inhibitory transmission through GABA receptorassociated protein-dependent exocytosis of GABAA receptors. J Neurosci 2007; 27: 14326-37.
    • (2007) J Neurosci , vol.27 , pp. 14326-37
    • Marsden, K.C.1    Beattie, J.B.2    Friedenthal, J.3    Carroll, R.C.4
  • 175
    • 78650577766 scopus 로고    scopus 로고
    • Selective translocation of Ca2+/calmodulin protein kinase IIalpha (CaMKIIalpha) to inhibitory synapses
    • Marsden KC, Shemesh A, Bayer KU, Carroll RC. Selective translocation of Ca2+/calmodulin protein kinase IIalpha (CaMKIIalpha) to inhibitory synapses. Proc Natl Acad Sci U S A 2010; 107: 20559-64.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 20559-64
    • Marsden, K.C.1    Shemesh, A.2    Bayer, K.U.3    Carroll, R.C.4
  • 176
    • 4143128938 scopus 로고    scopus 로고
    • Role of CaMKII in hydrogen peroxide activation of ERK1/2, p38 MAPK, HSP27 and actin reorganization in endothelial cells
    • DOI 10.1016/j.febslet.2004.06.061, PII S001457930400818X
    • Nguyen A, Chen P, Cai H. Role of CaMKII in hydrogen peroxide activation of ERK1/2, p38 MAPK, HSP27 and actin reorganization in endothelial cells. FEBS Lett 2004; 572: 307-13. (Pubitemid 39092554)
    • (2004) FEBS Letters , vol.572 , Issue.1-3 , pp. 307-313
    • Nguyen, A.1    Chen, P.2    Cai, H.3
  • 177
    • 58149302821 scopus 로고    scopus 로고
    • CaMKII locally encodes L-type channel activity to signal to nuclear CREB in excitation-transcription coupling
    • Wheeler DG, Barrett CF, Groth RD , Safa P, Tsien RW. CaMKII locally encodes L-type channel activity to signal to nuclear CREB in excitation-transcription coupling. J Cell Biol 2008; 183: 849-63.
    • (2008) J Cell Biol , vol.183 , pp. 849-63
    • Wheeler, D.G.1    Barrett, C.F.2    Groth, R.D.3    Safa, P.4    Tsien, R.W.5
  • 178
    • 78650367828 scopus 로고    scopus 로고
    • Inhibitory phosphorylation of GSK-3 by CaMKII couples depolarization to neuronal survival
    • Song B, Lai B, Zheng Z, Zhang Y, Luo J, Wang C, et al. Inhibitory phosphorylation of GSK-3 by CaMKII couples depolarization to neuronal survival. J Biol Chem 2010; 285: 41122-34.
    • (2010) J Biol Chem , vol.285 , pp. 41122-34
    • Song, B.1    Lai, B.2    Zheng, Z.3    Zhang, Y.4    Luo, J.5    Wang, C.6
  • 179
    • 0033595764 scopus 로고    scopus 로고
    • Neuronal activity-dependent cell survival mediated by transcription factor MEF2
    • Mao Z, Bonni A, Xia F, Nadal-Vicens M, Greenberg ME. Neuronal activity-dependent cell survival mediated by transcription factor MEF2. Science 1999; 286: 785-90.
    • (1999) Science , vol.286 , pp. 785-90
    • Mao, Z.1    Bonni, A.2    Xia, F.3    Nadal-Vicens, M.4    Greenberg, M.E.5
  • 180
    • 0031046848 scopus 로고    scopus 로고
    • Apoptosis and disease: Regulation and clinical relevance of programmed cell death
    • DOI 10.1146/annurev.med.48.1.267
    • Rudin CM, Thompson CB. Apoptosis and disease: regulation and clinical relevance of programmed cell death. Annu Rev Med 1997 48 267-81. (Pubitemid 27101830)
    • (1997) Annual Review of Medicine , vol.48 , pp. 267-281
    • Rudin, C.M.1    Thompson, C.B.2
  • 182
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • H engartner MO. The biochemistry of apoptosis. Nature 2000; 407: 770-6.
    • (2000) Nature , vol.407 , pp. 770-6
    • Hengartner, M.O.1
  • 184
    • 0030817142 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase II mediates signal transduction in apoptosis
    • Wright S, Schellenberger U, Ji L, Wang H, Larrick J. Calmodulindependent protein kinase II mediates signal transduction in apoptosis. FASEB J 1997; 11: 843-9. (Pubitemid 27371893)
    • (1997) FASEB Journal , vol.11 , Issue.11 , pp. 843-849
    • Wright, S.C.1    Schellenberger, U.2    Ji, L.3    Wang, H.4    Larrick, J.W.5
  • 186
    • 33745209195 scopus 로고    scopus 로고
    • CaM-kinaseII-dependent commitment to microcystin-induced apoptosis is coupled to cell budding, but not to shrinkage or chromatin hypercondensation
    • DOI 10.1038/sj.cdd.4401798, PII 4401798
    • Krakstad C, Herfindal L, Gjertsen BT, Boe R, Vintermyr OK, Fladmark KE, et al. CaM-kinaseII-dependent commitment to microcystininduced apoptosis is coupled to cell budding, but not to shrinkage or chromatin hypercondensation. Cell Death Differ 2005; 13: 1191-202. (Pubitemid 43905599)
    • (2006) Cell Death and Differentiation , vol.13 , Issue.7 , pp. 1191-1202
    • Krakstad, C.1    Herfindal, L.2    Gjertsen, B.T.3    Boe, R.4    Vintermyr, O.K.5    Fladmark, K.E.6    Doskeland, S.O.7
  • 187
    • 77958490962 scopus 로고    scopus 로고
    • The role of CaMKII in calcium-activated death pathways in bone marrow B cells
    • Bissonnette SL, Haas A, Mann KK, Schlezinger JJ. The role of CaMKII in calcium-activated death pathways in bone marrow B cells. Toxicol Sci 2010; 118: 108-18.
    • (2010) Toxicol Sci , vol.118 , pp. 108-18
    • Bissonnette, S.L.1    Haas, A.2    Mann, K.K.3    Schlezinger, J.J.4
  • 188
    • 70349696241 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II links ER stress with Fas and mitochondrial apoptosis pathways
    • Timmins JM, Ozcan L, Seimon TA, Li G, Malagelada C, Backs J, et al. Calcium/calmodulin-dependent protein kinase II links ER stress with Fas and mitochondrial apoptosis pathways. J Clin Invest 2009; 119: 2925-41.
    • (2009) J Clin Invest , vol.119 , pp. 2925-41
    • Timmins, J.M.1    Ozcan, L.2    Seimon, T.A.3    Li, G.4    Malagelada, C.5    Backs, J.6
  • 189
    • 76649084540 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II (CaMKII) regulates tumour necrosis factor-related apoptosis inducing ligand (TRAIL)-mediated apoptosis of fibroblast-like synovial cells (FLS) by phosphorylation of Akt
    • Fujikawa K, Kawakami A, Tanaka F, Iwamoto N, Tamai M, Eguchi K. Calcium/calmodulin-dependent protein kinase II (CaMKII) regulates tumour necrosis factor-related apoptosis inducing ligand (TRAIL)-mediated apoptosis of fibroblast-like synovial cells (FLS) by phosphorylation of Akt. Clin Exp Rheumatol 2009; 27: 952-7.
    • (2009) Clin Exp Rheumatol , vol.27 , pp. 952-7
    • Fujikawa, K.1    Kawakami, A.2    Tanaka, F.3    Iwamoto, N.4    Tamai, M.5    Eguchi, K.6
  • 192
    • 77955269637 scopus 로고    scopus 로고
    • Na+/K+-ATPase inhibition by ouabain induces CaMKII-dependent apoptosis in adult rat cardiac myocytes
    • Sapia L, Palomeque J, Mattiazzi A, Petroff MV. Na+/K+-ATPase inhibition by ouabain induces CaMKII-dependent apoptosis in adult rat cardiac myocytes. J Mol Cell Cardiol 2010; 49: 459-68.
    • (2010) J Mol Cell Cardiol , vol.49 , pp. 459-68
    • Sapia, L.1    Palomeque, J.2    Mattiazzi, A.3    Petroff, M.V.4
  • 193
    • 73349084993 scopus 로고    scopus 로고
    • Angiotensin II-induced oxidative stress resets the ca2+ dependence of Ca2+-calmodulin protein kinase ii and promotes a death pathway conserved across different species
    • Palomeque J, Rueda OV, Sapia L, Valverde CA, Salas M, Petroff MV, et al. Angiotensin II-induced oxidative stress resets the ca2+ dependence of Ca2+-calmodulin protein kinase ii and promotes a death pathway conserved across different species. Circ Res 2009; 105: 1204-12.
    • (2009) Circ Res , vol.105 , pp. 1204-12
    • Palomeque, J.1    Rueda, O.V.2    Sapia, L.3    Valverde, C.A.4    Salas, M.5    Petroff, M.V.6
  • 194
    • 74049097964 scopus 로고    scopus 로고
    • Cardioprotection by CaMKII-{delta}B is mediated by phosphorylation of heat shock factor 1 and subsequent expression of inducible heat shock protein 70
    • Peng W, Zhang Y, Zheng M, Cheng H, Zhu W, Cao CM, et al. Cardioprotection by CaMKII-{delta}B is mediated by phosphorylation of heat shock factor 1 and subsequent expression of inducible heat shock protein 70. Circ Res 2010; 106: 102-10.
    • (2010) Circ Res , vol.106 , pp. 102-10
    • Peng, W.1    Zhang, Y.2    Zheng, M.3    Cheng, H.4    Zhu, W.5    Cao, C.M.6
  • 197
    • 77952669275 scopus 로고    scopus 로고
    • The signalling pathway of CaMKII-mediated apoptosis and necrosis in the ischemia/reperfusion injury
    • Salas MA, Valverde CA, Sánchez G, Said M, Rodriguez JS, Portiansky EL, et al. The signalling pathway of CaMKII-mediated apoptosis and necrosis in the ischemia/reperfusion injury. J Mol Cell Cardiol 2010; 48: 1298-306.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 1298-306
    • Ma, S.1    Valverde, C.A.2    Sánchez, G.3    Said, M.4    Rodriguez, J.S.5    Portiansky, E.L.6
  • 198
    • 78751647632 scopus 로고    scopus 로고
    • Cardiac hypertrophy and heart failure development through Gq and Cam kinase II signaling
    • Mishra S, Ling H, Grimm M, Zhang T, Bers DM, Brown JH. Cardiac hypertrophy and heart failure development through Gq and Cam kinase II signaling. J Cardiovasc Pharmacol 2010; 56: 598-603.
    • (2010) J Cardiovasc Pharmacol , vol.56 , pp. 598-603
    • Mishra, S.1    Ling, H.2    Grimm, M.3    Zhang, T.4    Bers, D.M.5    Brown, J.H.6
  • 199
    • 26244453715 scopus 로고    scopus 로고
    • Metabolic regulation of oocyte cell death through the CaMKII-mediated phosphorylation of caspase-2
    • DOI 10.1016/j.cell.2005.07.032, PII S0092867405008020
    • Nutt LK, Margolis SS, Jensen M, Herman CE, Dunphy WG, Rathmell JC, et al. Metabolic regulation of oocyte cell death through the CaMKII-mediated phosphorylation of caspase-2. Cell 2005; 123: 89-103. (Pubitemid 41414531)
    • (2005) Cell , vol.123 , Issue.1 , pp. 89-103
    • Nutt, L.K.1    Margolis, S.S.2    Jensen, M.3    Herman, C.E.4    Dunphy, W.G.5    Rathmell, J.C.6    Kornbluth, S.7
  • 201
    • 69949183196 scopus 로고    scopus 로고
    • Endogenous human CaMKII inhibitory protein suppresses tumor growth by inducing cell cycle arrest and apoptosis through down-regulation of the phosphatidylinositide 3-kinase/Akt/HDM2 pathway
    • Ma S, Yang Y, Wang C, Hui N, Gu L, Zhong H, et al. Endogenous human CaMKII inhibitory protein suppresses tumor growth by inducing cell cycle arrest and apoptosis through down-regulation of the phosphatidylinositide 3-kinase/Akt/HDM2 pathway. J Biol Chem 2009; 284: 24773-82.
    • (2009) J Biol Chem , vol.284 , pp. 24773-82
    • Ma, S.1    Yang, Y.2    Wang, C.3    Hui, N.4    Gu, L.5    Zhong, H.6
  • 202
    • 77956880563 scopus 로고    scopus 로고
    • Metabolic regulation of Drosophila apoptosis through inhibitory phosphorylation of Dronc
    • Y ang CS, Thomenius MJ, Gan EC, Tang W, Freel CD, Merritt TJS, et al. Metabolic regulation of Drosophila apoptosis through inhibitory phosphorylation of Dronc. EMBO J 2010; 29: 3196-207.
    • (2010) EMBO J , vol.29 , pp. 3196-3207
    • Yang, C.S.1    Thomenius, M.J.2    Gan, E.C.3    Tang, W.4    Freel, C.D.5    Tjs, M.6
  • 204
    • 79953673530 scopus 로고    scopus 로고
    • Requirement for non-regulated, constitutive calcium influx in macrophage survival signaling
    • T ano JY, Vazquez G. Requirement for non-regulated, constitutive calcium influx in macrophage survival signaling. Biochem Biophys Res Commun 2011; 407: 432-7.
    • (2011) Biochem Biophys Res Commun , vol.407 , pp. 432-7
    • Tano, J.Y.1    Vazquez, G.2
  • 205
    • 79960044552 scopus 로고    scopus 로고
    • CaMKII in myocardial hypertrophy and hear t failure
    • doi: 10.1016/ j.yjmcc.2011.01.012
    • Anderson ME, Brown JH, Bers DM. CaMKII in myocardial hypertrophy and hear t failure. J Mol Cell Cardiol 2011. doi: 10.1016/ j.yjmcc.2011.01.012.
    • (2011) J Mol Cell Cardiol
    • Anderson, M.E.1    Brown, J.H.2    Bers, D.M.3
  • 206
    • 0028085454 scopus 로고
    • Alternative splicing introduces a nuclear localization signal that targets multifunctional CaM kinase to the nucleus
    • DOI 10.1083/jcb.126.4.839
    • Srinivasan M, Edman CF, Schulman H. Alternative splicing introduces a nuclear localization signal that targets multifunctional CaM kinase to the nucleus. J Cell Biol 1994; 126: 839-52. (Pubitemid 24252133)
    • (1994) Journal of Cell Biology , vol.126 , Issue.4 , pp. 839-852
    • Srinivasan, M.1    Edman, C.F.2    Schulman, H.3
  • 207
    • 69949120824 scopus 로고    scopus 로고
    • Critical role of nuclear calcium/calmodulin-dependent protein kinase iideltab in cardiomyocyte survival in cardiomyopathy
    • L ittle GH, Saw A, Bai Y, Dow J, Marjoram P, Simkhovich B, et al. Critical role of nuclear calcium/calmodulin-dependent protein kinase iideltab in cardiomyocyte survival in cardiomyopathy. J Biol Chem 2009; 284: 24857-68.
    • (2009) J Biol Chem , vol.284 , pp. 24857-68
    • Little, G.H.1    Saw, A.2    Bai, Y.3    Dow, J.4    Marjoram, P.5    Simkhovich, B.6
  • 208
    • 0028987937 scopus 로고
    • Calcium signaling in neurons: Molecular mechanisms and cellular consequences
    • Ghosh A, Greenberg M. Calcium signaling in neurons: molecular mechanisms and cellular consequences. Science 1995; 268: 239-47.
    • (1995) Science , vol.268 , pp. 239-47
    • Ghosh, A.1    Greenberg, M.2
  • 209
    • 0042536473 scopus 로고    scopus 로고
    • Molecular mechanisms of calcium-dependent neurodegeneration in excitotoxicity
    • DOI 10.1016/S0143-4160(03)00141-6
    • Arundine M, Tymianski M. Molecular mechanisms of calciumdependent neurodegeneration in excitotoxicity. Cell Calcium 2003; 34: 325-37. (Pubitemid 37021228)
    • (2003) Cell Calcium , vol.34 , Issue.4-5 , pp. 325-337
    • Arundine, M.1    Tymianski, M.2
  • 210
    • 0036241207 scopus 로고    scopus 로고
    • Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
    • DOI 10.1038/nn835
    • Hardingham GE, Fukunaga Y, Bading H Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways. Nat Neurosci 2002 5 405-14. (Pubitemid 34454245)
    • (2002) Nature Neuroscience , vol.5 , Issue.5 , pp. 405-414
    • Hardingham, G.E.1    Fukunaga, Y.2    Bading, H.3
  • 211
    • 79955721239 scopus 로고    scopus 로고
    • A Signaling cascade of nuclear calcium-CREB-ATF3 activated by synaptic NMDA receptors defines a gene repression module that protects against extrasynaptic NMDA receptor-induced neuronal cell death and ischemic brain damage
    • Zhang SJ, Buchthal B, Lau D, Hayer S, Dick O, Schwaninger M, et al. A Signaling cascade of nuclear calcium-CREB-ATF3 activated by synaptic NMDA receptors defines a gene repression module that protects against extrasynaptic NMDA receptor-induced neuronal cell death and ischemic brain damage. J Neurosci 2011; 31: 4978-90.
    • (2011) J Neurosci , vol.31 , pp. 4978-90
    • Zhang, S.J.1    Buchthal, B.2    Lau, D.3    Hayer, S.4    Dick, O.5    Schwaninger, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.