메뉴 건너뛰기




Volumn 23, Issue 2, 2011, Pages 223-230

Role of calcineurin in neurodegeneration produced by misfolded proteins and endoplasmic reticulum stress

Author keywords

[No Author keywords available]

Indexed keywords

CALCINEURIN; PHOSPHATASE;

EID: 79954425744     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2010.12.006     Document Type: Review
Times cited : (57)

References (78)
  • 1
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat Rev Neurosci 2003, 4:49-60.
    • (2003) Nat Rev Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006, 75:333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 33646175291 scopus 로고    scopus 로고
    • Stressing out the ER: a role of the unfolded protein response in prion-related disorders
    • Hetz C.A., Soto C. Stressing out the ER: a role of the unfolded protein response in prion-related disorders. Curr Mol Med 2006, 6:37-43.
    • (2006) Curr Mol Med , vol.6 , pp. 37-43
    • Hetz, C.A.1    Soto, C.2
  • 5
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder M., Kaufman R.J. ER stress and the unfolded protein response. Mutat Res 2005, 569:29-63.
    • (2005) Mutat Res , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 6
    • 0038004052 scopus 로고    scopus 로고
    • Molecular pathways of endoplasmic reticulum dysfunctions: possible cause of cell death in the nervous system
    • Lehotsky J., Kaplan P., Babusikova E., Strapkova A., Murin R. Molecular pathways of endoplasmic reticulum dysfunctions: possible cause of cell death in the nervous system. Physiol Res 2003, 52:269-274.
    • (2003) Physiol Res , vol.52 , pp. 269-274
    • Lehotsky, J.1    Kaplan, P.2    Babusikova, E.3    Strapkova, A.4    Murin, R.5
  • 7
    • 54949110895 scopus 로고    scopus 로고
    • Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis
    • Pinton P., Giorgi C., Siviero R., Zecchini E., Rizzuto R. Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis. Oncogene 2008, 27:6407-6418.
    • (2008) Oncogene , vol.27 , pp. 6407-6418
    • Pinton, P.1    Giorgi, C.2    Siviero, R.3    Zecchini, E.4    Rizzuto, R.5
  • 8
    • 34548644786 scopus 로고    scopus 로고
    • Modulation of the ryanodine receptor and intracellular calcium
    • Zalk R., Lehnart S.E., Marks A.R. Modulation of the ryanodine receptor and intracellular calcium. Annu Rev Biochem 2007, 76:367-385.
    • (2007) Annu Rev Biochem , vol.76 , pp. 367-385
    • Zalk, R.1    Lehnart, S.E.2    Marks, A.R.3
  • 9
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C., Russelakis-Carneiro M., Maundrell K., Castilla J., Soto C. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J 2003, 22:5435-5445.
    • (2003) EMBO J , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 10
    • 78650843400 scopus 로고    scopus 로고
    • Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress
    • Torres M., Castillo K., Armisen R., Stutzin A., Soto C., Hetz C. Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PLoS One 2010, 5:e15658.
    • (2010) PLoS One , vol.5
    • Torres, M.1    Castillo, K.2    Armisen, R.3    Stutzin, A.4    Soto, C.5    Hetz, C.6
  • 11
    • 0030856223 scopus 로고    scopus 로고
    • Distinct tissue and cellular distribution of two major isoforms of calcineurin
    • Jiang H., Xiong F., Kong S., Ogawa T., Kobayashi M., Liu J.O. Distinct tissue and cellular distribution of two major isoforms of calcineurin. Mol Immunol 1997, 34:663-669.
    • (1997) Mol Immunol , vol.34 , pp. 663-669
    • Jiang, H.1    Xiong, F.2    Kong, S.3    Ogawa, T.4    Kobayashi, M.5    Liu, J.O.6
  • 12
    • 0024792262 scopus 로고
    • Protein phosphatases come of age
    • Cohen P., Cohen P.T. Protein phosphatases come of age. J Biol Chem 1989, 264:21435-21438.
    • (1989) J Biol Chem , vol.264 , pp. 21435-21438
    • Cohen, P.1    Cohen, P.T.2
  • 13
    • 0020641117 scopus 로고
    • The protein phosphatases involved in cellular regulation 6. Measurement of type-1 and type-2 protein phosphatases in extracts of mammalian tissues; an assessment of their physiological roles
    • Ingebritsen T.S., Stewart A.A., Cohen P. The protein phosphatases involved in cellular regulation 6. Measurement of type-1 and type-2 protein phosphatases in extracts of mammalian tissues; an assessment of their physiological roles. Eur J Biochem 1983, 132:297-307.
    • (1983) Eur J Biochem , vol.132 , pp. 297-307
    • Ingebritsen, T.S.1    Stewart, A.A.2    Cohen, P.3
  • 14
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem 1989, 58:453-508.
    • (1989) Annu Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 15
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu J., Farmer J.D., Lane W.S., Friedman J., Weissman I., Schreiber S.L. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 1991, 66:807-815.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer, J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 16
    • 0026513446 scopus 로고
    • Solution structure of FK506 bound to FKBP-12
    • Lepre C.A., Thomson J.A., Moore J.M. Solution structure of FK506 bound to FKBP-12. FEBS Lett 1992, 302:89-96.
    • (1992) FEBS Lett , vol.302 , pp. 89-96
    • Lepre, C.A.1    Thomson, J.A.2    Moore, J.M.3
  • 17
    • 0018757118 scopus 로고
    • Mode of action of cyclosporin A: a new immunosuppressive agent
    • White D.J., Calne R.Y., Plumb A. Mode of action of cyclosporin A: a new immunosuppressive agent. Transplant Proc 1979, 11:855-859.
    • (1979) Transplant Proc , vol.11 , pp. 855-859
    • White, D.J.1    Calne, R.Y.2    Plumb, A.3
  • 18
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: form and function
    • Rusnak F., Mertz P. Calcineurin: form and function. Physiol Rev 2000, 80:1483-1521.
    • (2000) Physiol Rev , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 19
    • 0036171986 scopus 로고    scopus 로고
    • Calcineurin as a multifunctional regulator
    • Shibasaki F., Hallin U., Uchino H. Calcineurin as a multifunctional regulator. J Biochem 2002, 131:1-15.
    • (2002) J Biochem , vol.131 , pp. 1-15
    • Shibasaki, F.1    Hallin, U.2    Uchino, H.3
  • 21
    • 0001018554 scopus 로고
    • Calcineurin: a calcium- and calmodulin-binding protein of the nervous system
    • Klee C.B., Crouch T.H., Krinks M.H. Calcineurin: a calcium- and calmodulin-binding protein of the nervous system. Proc Natl Acad Sci U S A 1979, 76:6270-6273.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 6270-6273
    • Klee, C.B.1    Crouch, T.H.2    Krinks, M.H.3
  • 22
    • 0021178719 scopus 로고
    • Activation of brain calcineurin phosphatase towards nonprotein phosphoesters by Ca2+, calmodulin, and Mg2+
    • Li H.C. Activation of brain calcineurin phosphatase towards nonprotein phosphoesters by Ca2+, calmodulin, and Mg2+. J Biol Chem 1984, 259:8801-8807.
    • (1984) J Biol Chem , vol.259 , pp. 8801-8807
    • Li, H.C.1
  • 23
    • 0023758460 scopus 로고
    • Regulatory interactions of calmodulin-binding proteins: phosphorylation of calcineurin by autophosphorylated Ca2+/calmodulin-dependent protein kinase II
    • Hashimoto Y., King M.M., Soderling T.R. Regulatory interactions of calmodulin-binding proteins: phosphorylation of calcineurin by autophosphorylated Ca2+/calmodulin-dependent protein kinase II. Proc Natl Acad Sci U S A 1988, 85:7001-7005.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 7001-7005
    • Hashimoto, Y.1    King, M.M.2    Soderling, T.R.3
  • 24
    • 0034661450 scopus 로고    scopus 로고
    • Caspase-mediated proteolytic activation of calcineurin in thapsigargin-mediated apoptosis in SH-SY5Y neuroblastoma cells
    • Mukerjee N., McGinnis K.M., Park Y.H., Gnegy M.E., Wang K.K. Caspase-mediated proteolytic activation of calcineurin in thapsigargin-mediated apoptosis in SH-SY5Y neuroblastoma cells. Arch Biochem Biophys 2000, 379:337-343.
    • (2000) Arch Biochem Biophys , vol.379 , pp. 337-343
    • Mukerjee, N.1    McGinnis, K.M.2    Park, Y.H.3    Gnegy, M.E.4    Wang, K.K.5
  • 25
    • 34447319392 scopus 로고    scopus 로고
    • Calpain-calcineurin signaling in the pathogenesis of calcium-dependent disorder
    • Wu H.Y., Tomizawa K., Matsui H. Calpain-calcineurin signaling in the pathogenesis of calcium-dependent disorder. Acta Med Okayama 2007, 61:123-137.
    • (2007) Acta Med Okayama , vol.61 , pp. 123-137
    • Wu, H.Y.1    Tomizawa, K.2    Matsui, H.3
  • 26
    • 0020609098 scopus 로고
    • Activation of calcineurin by limited proteolysis
    • Manalan A.S., Klee C.B. Activation of calcineurin by limited proteolysis. Proc Natl Acad Sci U S A 1983, 80:4291-4295.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 4291-4295
    • Manalan, A.S.1    Klee, C.B.2
  • 27
    • 27844553889 scopus 로고    scopus 로고
    • Truncation and activation of calcineurin A by calpain I in Alzheimer disease brain
    • Liu F., Grundke-Iqbal I., Iqbal K., Oda Y., Tomizawa K., Gong C.X. Truncation and activation of calcineurin A by calpain I in Alzheimer disease brain. J Biol Chem 2005, 280:37755-37762.
    • (2005) J Biol Chem , vol.280 , pp. 37755-37762
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Oda, Y.4    Tomizawa, K.5    Gong, C.X.6
  • 28
    • 0242690133 scopus 로고    scopus 로고
    • Calcineurin in memory and bidirectional plasticity
    • Mansuy I.M. Calcineurin in memory and bidirectional plasticity. Biochem Biophys Res Commun 2003, 311:1195-1208.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 1195-1208
    • Mansuy, I.M.1
  • 29
    • 0023261649 scopus 로고
    • Calmodulin binding by calcineurin ligand-induced renaturation of protein immobilized on nitrocellulose
    • Hubbard M.J., Klee C.B. Calmodulin binding by calcineurin ligand-induced renaturation of protein immobilized on nitrocellulose. J Biol Chem 1987, 262:15062-15070.
    • (1987) J Biol Chem , vol.262 , pp. 15062-15070
    • Hubbard, M.J.1    Klee, C.B.2
  • 30
    • 0024503519 scopus 로고
    • Calcium channel regulation by calcineurin, a Ca2+-activated phosphatase in mammalian brain
    • Armstrong D.L. Calcium channel regulation by calcineurin, a Ca2+-activated phosphatase in mammalian brain. Trends Neurosci 1989, 12:117-122.
    • (1989) Trends Neurosci , vol.12 , pp. 117-122
    • Armstrong, D.L.1
  • 31
    • 0033811168 scopus 로고    scopus 로고
    • A modulatory role for protein phosphatase 2B (calcineurin) in the regulation of Ca2+ entry
    • Burley J.R., Sihra T.S. A modulatory role for protein phosphatase 2B (calcineurin) in the regulation of Ca2+ entry. Eur J Neurosci 2000, 12:2881-2891.
    • (2000) Eur J Neurosci , vol.12 , pp. 2881-2891
    • Burley, J.R.1    Sihra, T.S.2
  • 32
    • 0030764597 scopus 로고    scopus 로고
    • Calcineurin modulates G protein-mediated inhibition of N-type calcium channels in rat sympathetic neurons
    • Zhu Y., Yakel J.L. Calcineurin modulates G protein-mediated inhibition of N-type calcium channels in rat sympathetic neurons. J Neurophysiol 1997, 78:1161-1165.
    • (1997) J Neurophysiol , vol.78 , pp. 1161-1165
    • Zhu, Y.1    Yakel, J.L.2
  • 33
    • 0036086484 scopus 로고    scopus 로고
    • Stimulation of 5-HT(2) receptors in prefrontal pyramidal neurons inhibits Ca(v)1.2 L type Ca(2+) currents via a PLCbeta/IP3/calcineurin signaling cascade
    • Day M., Olson P.A., Platzer J., Striessnig J., Surmeier D.J. Stimulation of 5-HT(2) receptors in prefrontal pyramidal neurons inhibits Ca(v)1.2 L type Ca(2+) currents via a PLCbeta/IP3/calcineurin signaling cascade. J Neurophysiol 2002, 87:2490-2504.
    • (2002) J Neurophysiol , vol.87 , pp. 2490-2504
    • Day, M.1    Olson, P.A.2    Platzer, J.3    Striessnig, J.4    Surmeier, D.J.5
  • 34
    • 0030463470 scopus 로고    scopus 로고
    • CREB phosphorylation and dephosphorylation: a Ca(2+)- and stimulus duration-dependent switch for hippocampal gene expression
    • Bito H., Deisseroth K., Tsien R.W. CREB phosphorylation and dephosphorylation: a Ca(2+)- and stimulus duration-dependent switch for hippocampal gene expression. Cell 1996, 87:1203-1214.
    • (1996) Cell , vol.87 , pp. 1203-1214
    • Bito, H.1    Deisseroth, K.2    Tsien, R.W.3
  • 35
    • 0037806030 scopus 로고    scopus 로고
    • Neurotrophins and netrins require calcineurin/NFAT signaling to stimulate outgrowth of embryonic axons
    • Graef I.A., Wang F., Charron F., Chen L., Neilson J., Tessier-Lavigne M., Crabtree G.R. Neurotrophins and netrins require calcineurin/NFAT signaling to stimulate outgrowth of embryonic axons. Cell 2003, 113:657-670.
    • (2003) Cell , vol.113 , pp. 657-670
    • Graef, I.A.1    Wang, F.2    Charron, F.3    Chen, L.4    Neilson, J.5    Tessier-Lavigne, M.6    Crabtree, G.R.7
  • 36
    • 0041835836 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor activation of NFAT (nuclear factor of activated T-cells)-dependent transcription: a role for the transcription factor NFATc4 in neurotrophin-mediated gene expression
    • Groth R.D., Mermelstein P.G. Brain-derived neurotrophic factor activation of NFAT (nuclear factor of activated T-cells)-dependent transcription: a role for the transcription factor NFATc4 in neurotrophin-mediated gene expression. J Neurosci 2003, 23:8125-8134.
    • (2003) J Neurosci , vol.23 , pp. 8125-8134
    • Groth, R.D.1    Mermelstein, P.G.2
  • 39
    • 0037431130 scopus 로고    scopus 로고
    • Cdk5-mediated inhibition of the protective effects of transcription factor MEF2 in neurotoxicity-induced apoptosis
    • Gong X., Tang X., Wiedmann M., Wang X., Peng J., Zheng D., Blair L.A., Marshall J., Mao Z. Cdk5-mediated inhibition of the protective effects of transcription factor MEF2 in neurotoxicity-induced apoptosis. Neuron 2003, 38:33-46.
    • (2003) Neuron , vol.38 , pp. 33-46
    • Gong, X.1    Tang, X.2    Wiedmann, M.3    Wang, X.4    Peng, J.5    Zheng, D.6    Blair, L.A.7    Marshall, J.8    Mao, Z.9
  • 40
    • 0036667397 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatases in apoptosis
    • Klumpp S., Krieglstein J. Serine/threonine protein phosphatases in apoptosis. Curr Opin Pharmacol 2002, 2:458-462.
    • (2002) Curr Opin Pharmacol , vol.2 , pp. 458-462
    • Klumpp, S.1    Krieglstein, J.2
  • 42
    • 2542564200 scopus 로고    scopus 로고
    • Calcineurin-mediated Bad translocation regulates cyanide-induced neuronal apoptosis
    • Shou Y., Li L., Prabhakaran K., Borowitz J.L., Isom G.E. Calcineurin-mediated Bad translocation regulates cyanide-induced neuronal apoptosis. Biochem J 2004, 379:805-813.
    • (2004) Biochem J , vol.379 , pp. 805-813
    • Shou, Y.1    Li, L.2    Prabhakaran, K.3    Borowitz, J.L.4    Isom, G.E.5
  • 43
    • 0442323504 scopus 로고    scopus 로고
    • Calcineurin-mediated BAD Ser155 dephosphorylation in ammonia-induced apoptosis of cultured rat hippocampal neurons
    • Yang L., Omori K., Suzukawa J., Inagaki C. Calcineurin-mediated BAD Ser155 dephosphorylation in ammonia-induced apoptosis of cultured rat hippocampal neurons. Neurosci Lett 2004, 357:73-75.
    • (2004) Neurosci Lett , vol.357 , pp. 73-75
    • Yang, L.1    Omori, K.2    Suzukawa, J.3    Inagaki, C.4
  • 45
    • 40949104298 scopus 로고    scopus 로고
    • Overactivation of calcineurin induced by amyloid-beta and prion proteins
    • Agostinho P., Lopes J.P., Velez Z., Oliveira C.R. Overactivation of calcineurin induced by amyloid-beta and prion proteins. Neurochem Int 2008, 52:1226-1233.
    • (2008) Neurochem Int , vol.52 , pp. 1226-1233
    • Agostinho, P.1    Lopes, J.P.2    Velez, Z.3    Oliveira, C.R.4
  • 46
    • 56849091064 scopus 로고    scopus 로고
    • Selective induction of calcineurin activity and signaling by oligomeric amyloid beta
    • Reese L.C., Zhang W., Dineley K.T., Kayed R., Taglialatela G. Selective induction of calcineurin activity and signaling by oligomeric amyloid beta. Aging Cell 2008, 7:824-835.
    • (2008) Aging Cell , vol.7 , pp. 824-835
    • Reese, L.C.1    Zhang, W.2    Dineley, K.T.3    Kayed, R.4    Taglialatela, G.5
  • 47
    • 78449257695 scopus 로고    scopus 로고
    • Calcineurin inhibition at the clinical phase of prion disease reduces neurodegeneration, improves behavioral alterations and increases animal survival
    • Mukherjee A., Morales-Scheihing D., Gonzalez-Romero D., Green K., Taglialatela G., Soto C. Calcineurin inhibition at the clinical phase of prion disease reduces neurodegeneration, improves behavioral alterations and increases animal survival. PLoS Pathog 2010, 6:e1001138.
    • (2010) PLoS Pathog , vol.6
    • Mukherjee, A.1    Morales-Scheihing, D.2    Gonzalez-Romero, D.3    Green, K.4    Taglialatela, G.5    Soto, C.6
  • 48
    • 77249158836 scopus 로고    scopus 로고
    • Amyloid beta induces the morphological neurodegenerative triad of spine loss, dendritic simplification, and neuritic dystrophies through calcineurin activation
    • Wu H.Y., Hudry E., Hashimoto T., Kuchibhotla K., Rozkalne A., Fan Z., Spires-Jones T., Xie H., Arbel-Ornath M., Grosskreutz C.L., et al. Amyloid beta induces the morphological neurodegenerative triad of spine loss, dendritic simplification, and neuritic dystrophies through calcineurin activation. J Neurosci 2010, 30:2636-2649.
    • (2010) J Neurosci , vol.30 , pp. 2636-2649
    • Wu, H.Y.1    Hudry, E.2    Hashimoto, T.3    Kuchibhotla, K.4    Rozkalne, A.5    Fan, Z.6    Spires-Jones, T.7    Xie, H.8    Arbel-Ornath, M.9    Grosskreutz, C.L.10
  • 49
    • 39149105604 scopus 로고    scopus 로고
    • NFAT signaling in neural development and axon growth
    • Nguyen T., Di Giovanni S. NFAT signaling in neural development and axon growth. Int J Dev Neurosci 2008, 26:141-145.
    • (2008) Int J Dev Neurosci , vol.26 , pp. 141-145
    • Nguyen, T.1    Di Giovanni, S.2
  • 50
    • 72949098095 scopus 로고    scopus 로고
    • Genetic and pharmacological inhibition of calcineurin corrects the BDNF transport defect in Huntington's disease
    • Pineda J.R., Pardo R., Zala D., Yu H., Humbert S., Saudou F. Genetic and pharmacological inhibition of calcineurin corrects the BDNF transport defect in Huntington's disease. Mol Brain 2009, 2:33.
    • (2009) Mol Brain , vol.2 , pp. 33
    • Pineda, J.R.1    Pardo, R.2    Zala, D.3    Yu, H.4    Humbert, S.5    Saudou, F.6
  • 51
    • 33645065612 scopus 로고    scopus 로고
    • Huntington's disease: intracellular signaling pathways and neuronal death
    • Humbert S., Saudou F. Huntington's disease: intracellular signaling pathways and neuronal death. J Soc Biol 2005, 199:247-251.
    • (2005) J Soc Biol , vol.199 , pp. 247-251
    • Humbert, S.1    Saudou, F.2
  • 52
    • 32544432052 scopus 로고    scopus 로고
    • Inhibition of calcineurin by FK506 protects against polyglutamine-huntingtin toxicity through an increase of huntingtin phosphorylation at S421
    • Pardo R., Colin E., Regulier E., Aebischer P., Deglon N., Humbert S., Saudou F. Inhibition of calcineurin by FK506 protects against polyglutamine-huntingtin toxicity through an increase of huntingtin phosphorylation at S421. J Neurosci 2006, 26:1635-1645.
    • (2006) J Neurosci , vol.26 , pp. 1635-1645
    • Pardo, R.1    Colin, E.2    Regulier, E.3    Aebischer, P.4    Deglon, N.5    Humbert, S.6    Saudou, F.7
  • 53
    • 66449104770 scopus 로고    scopus 로고
    • Regulator of calcineurin (RCAN1-1L) is deficient in Huntington disease and protective against mutant huntingtin toxicity in vitro
    • Ermak G., Hench K.J., Chang K.T., Sachdev S., Davies K.J. Regulator of calcineurin (RCAN1-1L) is deficient in Huntington disease and protective against mutant huntingtin toxicity in vitro. J Biol Chem 2009, 284:11845-11853.
    • (2009) J Biol Chem , vol.284 , pp. 11845-11853
    • Ermak, G.1    Hench, K.J.2    Chang, K.T.3    Sachdev, S.4    Davies, K.J.5
  • 54
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe D.J. Alzheimer's disease is a synaptic failure. Science 2002, 298:789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 55
    • 74249085705 scopus 로고    scopus 로고
    • Prion neurodegeneration: starts and stops at the synapse
    • Mallucci G.R. Prion neurodegeneration: starts and stops at the synapse. Prion 2009, 3:195-201.
    • (2009) Prion , vol.3 , pp. 195-201
    • Mallucci, G.R.1
  • 58
    • 0032498227 scopus 로고    scopus 로고
    • Restricted and regulated overexpression reveals calcineurin as a key component in the transition from short-term to long-term memory
    • Mansuy I.M., Mayford M., Jacob B., Kandel E.R., Bach M.E. Restricted and regulated overexpression reveals calcineurin as a key component in the transition from short-term to long-term memory. Cell 1998, 92:39-49.
    • (1998) Cell , vol.92 , pp. 39-49
    • Mansuy, I.M.1    Mayford, M.2    Jacob, B.3    Kandel, E.R.4    Bach, M.E.5
  • 60
    • 0035977139 scopus 로고    scopus 로고
    • Forebrain-specific calcineurin knockout selectively impairs bidirectional synaptic plasticity and working/episodic-like memory
    • Zeng H., Chattarji S., Barbarosie M., Rondi-Reig L., Philpot B.D., Miyakawa T., Bear M.F., Tonegawa S. Forebrain-specific calcineurin knockout selectively impairs bidirectional synaptic plasticity and working/episodic-like memory. Cell 2001, 107:617-629.
    • (2001) Cell , vol.107 , pp. 617-629
    • Zeng, H.1    Chattarji, S.2    Barbarosie, M.3    Rondi-Reig, L.4    Philpot, B.D.5    Miyakawa, T.6    Bear, M.F.7    Tonegawa, S.8
  • 61
    • 77951246736 scopus 로고    scopus 로고
    • Inhibition of calcineurin-mediated endocytosis and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors prevents amyloid beta oligomer-induced synaptic disruption
    • Zhao W.Q., Santini F., Breese R., Ross D., Zhang X.D., Stone D.J., Ferrer M., Townsend M., Wolfe A.L., Seager M.A., et al. Inhibition of calcineurin-mediated endocytosis and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors prevents amyloid beta oligomer-induced synaptic disruption. J Biol Chem 2010, 285:7619-7632.
    • (2010) J Biol Chem , vol.285 , pp. 7619-7632
    • Zhao, W.Q.1    Santini, F.2    Breese, R.3    Ross, D.4    Zhang, X.D.5    Stone, D.J.6    Ferrer, M.7    Townsend, M.8    Wolfe, A.L.9    Seager, M.A.10
  • 62
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar G.M., Bloodgood B.L., Townsend M., Walsh D.M., Selkoe D.J., Sabatini B.L. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J Neurosci 2007, 27:2866-2875.
    • (2007) J Neurosci , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 63
    • 62649147319 scopus 로고    scopus 로고
    • Intermediate- and long-term recognition memory deficits in Tg2576 mice are reversed with acute calcineurin inhibition
    • Taglialatela G., Hogan D., Zhang W.R., Dineley K.T. Intermediate- and long-term recognition memory deficits in Tg2576 mice are reversed with acute calcineurin inhibition. Behav Brain Res 2009, 200:95-99.
    • (2009) Behav Brain Res , vol.200 , pp. 95-99
    • Taglialatela, G.1    Hogan, D.2    Zhang, W.R.3    Dineley, K.T.4
  • 64
    • 0037101970 scopus 로고    scopus 로고
    • Function and regulation of CREB family transcription factors in the nervous system
    • Lonze B.E., Ginty D.D. Function and regulation of CREB family transcription factors in the nervous system. Neuron 2002, 35:605-623.
    • (2002) Neuron , vol.35 , pp. 605-623
    • Lonze, B.E.1    Ginty, D.D.2
  • 65
    • 0032852479 scopus 로고    scopus 로고
    • CREB: a stimulus-induced transcription factor activated by a diverse array of extracellular signals
    • Shaywitz A.J., Greenberg M.E. CREB: a stimulus-induced transcription factor activated by a diverse array of extracellular signals. Annu Rev Biochem 1999, 68:821-861.
    • (1999) Annu Rev Biochem , vol.68 , pp. 821-861
    • Shaywitz, A.J.1    Greenberg, M.E.2
  • 66
    • 77952889956 scopus 로고    scopus 로고
    • CREB's control of intrinsic and synaptic plasticity: implications for CREB-dependent memory models
    • Benito E., Barco A. CREB's control of intrinsic and synaptic plasticity: implications for CREB-dependent memory models. Trends Neurosci 2010, 33:230-240.
    • (2010) Trends Neurosci , vol.33 , pp. 230-240
    • Benito, E.1    Barco, A.2
  • 67
    • 0032034262 scopus 로고    scopus 로고
    • Ca2+ influx regulates BDNF transcription by a CREB family transcription factor-dependent mechanism
    • Tao X., Finkbeiner S., Arnold D.B., Shaywitz A.J., Greenberg M.E. Ca2+ influx regulates BDNF transcription by a CREB family transcription factor-dependent mechanism. Neuron 1998, 20:709-726.
    • (1998) Neuron , vol.20 , pp. 709-726
    • Tao, X.1    Finkbeiner, S.2    Arnold, D.B.3    Shaywitz, A.J.4    Greenberg, M.E.5
  • 68
    • 0041488911 scopus 로고    scopus 로고
    • Trk receptors: roles in neuronal signal transduction
    • Huang E.J., Reichardt L.F. Trk receptors: roles in neuronal signal transduction. Annu Rev Biochem 2003, 72:609-642.
    • (2003) Annu Rev Biochem , vol.72 , pp. 609-642
    • Huang, E.J.1    Reichardt, L.F.2
  • 69
  • 70
    • 78650518914 scopus 로고    scopus 로고
    • Calcineurin inhibition with systemic FK506 treatment increases dendritic branching and dendritic spine density in healthy adult mouse brain
    • Spires-Jones T.L., Kay K., Matsouka R., Rozkalne A., Betensky R.A., Hyman B.T. Calcineurin inhibition with systemic FK506 treatment increases dendritic branching and dendritic spine density in healthy adult mouse brain. Neurosci Lett 2011, 487:260-263.
    • (2011) Neurosci Lett , vol.487 , pp. 260-263
    • Spires-Jones, T.L.1    Kay, K.2    Matsouka, R.3    Rozkalne, A.4    Betensky, R.A.5    Hyman, B.T.6
  • 71
    • 34848895216 scopus 로고    scopus 로고
    • Calcineurin activity is required for depolarization-induced CREB-dependent gene transcription in cortical neurons
    • Kingsbury T.J., Bambrick L.L., Roby C.D., Krueger B.K. Calcineurin activity is required for depolarization-induced CREB-dependent gene transcription in cortical neurons. J Neurochem 2007, 103:761-770.
    • (2007) J Neurochem , vol.103 , pp. 761-770
    • Kingsbury, T.J.1    Bambrick, L.L.2    Roby, C.D.3    Krueger, B.K.4
  • 72
    • 66449112294 scopus 로고    scopus 로고
    • Inverse regulation of plasticity-related immediate early genes by calcineurin in hippocampal neurons
    • Lam B.Y., Zhang W., Enticknap N., Haggis E., Cader M.Z., Chawla S. Inverse regulation of plasticity-related immediate early genes by calcineurin in hippocampal neurons. J Biol Chem 2009, 284:12562-12571.
    • (2009) J Biol Chem , vol.284 , pp. 12562-12571
    • Lam, B.Y.1    Zhang, W.2    Enticknap, N.3    Haggis, E.4    Cader, M.Z.5    Chawla, S.6
  • 73
    • 47749113650 scopus 로고    scopus 로고
    • Abeta plaques lead to aberrant regulation of calcium homeostasis in vivo resulting in structural and functional disruption of neuronal networks
    • Kuchibhotla K.V., Goldman S.T., Lattarulo C.R., Wu H.Y., Hyman B.T., Bacskai B.J. Abeta plaques lead to aberrant regulation of calcium homeostasis in vivo resulting in structural and functional disruption of neuronal networks. Neuron 2008, 59:214-225.
    • (2008) Neuron , vol.59 , pp. 214-225
    • Kuchibhotla, K.V.1    Goldman, S.T.2    Lattarulo, C.R.3    Wu, H.Y.4    Hyman, B.T.5    Bacskai, B.J.6
  • 74
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard P., Valtorta F., Czernik A.J., Benfenati F. Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 1993, 259:780-785.
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 75
    • 0033213603 scopus 로고    scopus 로고
    • A phospho-switch controls the dynamic association of synapsins with synaptic vesicles
    • Hosaka M., Hammer R.E., Sudhof T.C. A phospho-switch controls the dynamic association of synapsins with synaptic vesicles. Neuron 1999, 24:377-387.
    • (1999) Neuron , vol.24 , pp. 377-387
    • Hosaka, M.1    Hammer, R.E.2    Sudhof, T.C.3
  • 76
    • 0035887768 scopus 로고    scopus 로고
    • Opposing changes in phosphorylation of specific sites in synapsin I during Ca2+-dependent glutamate release in isolated nerve terminals
    • Jovanovic J.N., Sihra T.S., Nairn A.C., Hemmings H.C., Greengard P., Czernik A.J. Opposing changes in phosphorylation of specific sites in synapsin I during Ca2+-dependent glutamate release in isolated nerve terminals. J Neurosci 2001, 21:7944-7953.
    • (2001) J Neurosci , vol.21 , pp. 7944-7953
    • Jovanovic, J.N.1    Sihra, T.S.2    Nairn, A.C.3    Hemmings, H.C.4    Greengard, P.5    Czernik, A.J.6
  • 77
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra J.D., Kaufman R.J. The endoplasmic reticulum and the unfolded protein response. Semin Cell Dev Biol 2007, 18:716-731.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 78
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007, 8:519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.