메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Herpes Simplex Virus type-1 infection induces synaptic dysfunction in cultured cortical neurons via GSK-3 activation and intraneuronal amyloid-β protein accumulation

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; GLYCOGEN SYNTHASE KINASE 3; SYNAPSIN; SYNAPTOPHYSIN;

EID: 84944916968     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep15444     Document Type: Article
Times cited : (81)

References (60)
  • 2
    • 84926683321 scopus 로고    scopus 로고
    • Relationship between herpes simplex virus-1-specific antibody titers and cortical brain damage in Alzheimer's disease and amnestic mild cognitive impairment
    • Mancuso, R. et al. Relationship between herpes simplex virus-1-specific antibody titers and cortical brain damage in Alzheimer's disease and amnestic mild cognitive impairment. Front Aging Neurosci 6, 285 (2014).
    • (2014) Front Aging Neurosci , vol.6 , pp. 285
    • Mancuso, R.1
  • 3
    • 84904624887 scopus 로고    scopus 로고
    • HSV-1 and Alzheimer's disease: More than a hypothesis
    • Piacentini, R. et al. HSV-1 and Alzheimer's disease: more than a hypothesis. Front. Pharmacol. 5, 97 (2014).
    • (2014) Front. Pharmacol. , vol.5 , pp. 97
    • Piacentini, R.1
  • 5
    • 80053646131 scopus 로고    scopus 로고
    • HSV-1 promotes Ca2+-mediated APP phosphorylation and A accumulation in rat cortical neurons
    • Piacentini, R. et al. HSV-1 promotes Ca2+-mediated APP phosphorylation and A accumulation in rat cortical neurons. Neurobiol. Aging 32, 2323.e13-26 (2011).
    • (2011) Neurobiol. Aging , vol.32 , pp. 2323e13-26
    • Piacentini, R.1
  • 6
    • 33646862834 scopus 로고    scopus 로고
    • Phosphorylation of amyloid precursor protein (APP) at Thr668 regulates the nuclear translocation of the APP intracellular domain and induces neurodegeneration
    • Chang, K. A. et al. Phosphorylation of amyloid precursor protein (APP) at Thr668 regulates the nuclear translocation of the APP intracellular domain and induces neurodegeneration. Mol. Cell. Biol. 26, 4327-4338 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 4327-4338
    • Chang, K.A.1
  • 7
    • 0034488295 scopus 로고    scopus 로고
    • Generation of an apoptotic intracellular peptide by-secretase cleavage of Alzheimer's amyloid protein precursor
    • Passer, B. et al. Generation of an apoptotic intracellular peptide by-secretase cleavage of Alzheimer's amyloid protein precursor. J. Alzheimer's. Dis. 2, 289-301 (2000).
    • (2000) J. Alzheimer's. Dis. , vol.2 , pp. 289-301
    • Passer, B.1
  • 8
    • 78649757007 scopus 로고    scopus 로고
    • APP processing induced by herpes simplex virus type 1 (HSV-1) yields several APP fragments in human and rat neuronal cells
    • De Chiara, G. et al. APP processing induced by herpes simplex virus type 1 (HSV-1) yields several APP fragments in human and rat neuronal cells. PLoS One 5, e13989 (2010).
    • (2010) PLoS One , vol.5 , pp. e13989
    • De Chiara, G.1
  • 9
    • 0030035749 scopus 로고    scopus 로고
    • In vitro phosphorylation of the cytoplasmic domain of the amyloid precursor protein by glycogen synthase kinase-3
    • Aplin, A. E., Gibb, G. M., Jacobsen, J. S., Gallo, J. M. & Anderton, B. H. In vitro phosphorylation of the cytoplasmic domain of the amyloid precursor protein by glycogen synthase kinase-3. J. Neurochem. 67, 699-707 (1996).
    • (1996) J. Neurochem. , vol.67 , pp. 699-707
    • Aplin, A.E.1    Gibb, G.M.2    Jacobsen, J.S.3    Gallo, J.M.4    Anderton, B.H.5
  • 10
    • 33846031988 scopus 로고    scopus 로고
    • Calcium-mediated transient phosphorylation of tau and amyloid precursor protein followed by intraneuronal amyloid accumulation
    • Pierrot, N. et al. Calcium-mediated transient phosphorylation of tau and amyloid precursor protein followed by intraneuronal amyloid accumulation. J. Biol. Chem. 281, 39907-39914 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 39907-39914
    • Pierrot, N.1
  • 11
    • 60849105665 scopus 로고    scopus 로고
    • JNK regulates APP cleavage and degradation in a model of Alzheimer's disease
    • Colombo, A. et al. JNK regulates APP cleavage and degradation in a model of Alzheimer's disease. Neurobiol Dis. 33, 518-525 (2009).
    • (2009) Neurobiol Dis. , vol.33 , pp. 518-525
    • Colombo, A.1
  • 12
    • 0033836219 scopus 로고    scopus 로고
    • Neuron-specific phosphorylation of Alzheimer's-amyloid precursor protein by cyclin-dependent kinase 5
    • Iijima, K. et al. Neuron-specific phosphorylation of Alzheimer's-amyloid precursor protein by cyclin-dependent kinase 5. J. Neurochem. 75, 1085-1091 (2000).
    • (2000) J. Neurochem. , vol.75 , pp. 1085-1091
    • Iijima, K.1
  • 14
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3 regulates production of Alzheimer's disease amyloid peptides
    • Phiel, C. J., Wilson, C. A., Lee, V. M. & Klein, P. S. GSK-3 regulates production of Alzheimer's disease amyloid peptides. Nature 423, 435-439 (2003).
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.3    Klein, P.S.4
  • 15
    • 33747425620 scopus 로고    scopus 로고
    • GSK-3 is essential in the pathogenesis of Alzheimer's disease
    • Takashima, A. GSK-3 is essential in the pathogenesis of Alzheimer's disease. J. Alzheimers Dis. 9 (3 Suppl), 309-317 (2006).
    • (2006) J. Alzheimers Dis. , vol.9 , Issue.3 , pp. 309-317
    • Takashima, A.1
  • 16
    • 33846129434 scopus 로고    scopus 로고
    • Increased level of active GSK-3 in Alzheimer's disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration
    • Leroy, K., Yilmaz, Z. & Brion, J. P. Increased level of active GSK-3 in Alzheimer's disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration. Neuropathol. Appl. Neurobiol. 33, 43-55 (2007).
    • (2007) Neuropathol. Appl. Neurobiol. , vol.33 , pp. 43-55
    • Leroy, K.1    Yilmaz, Z.2    Brion, J.P.3
  • 17
    • 81955167913 scopus 로고    scopus 로고
    • Activation of glycogen synthase kinase-3 beta mediates-amyloid induced neuritic damage in Alzheimer's disease
    • DaRocha-Souto, B. et al. Activation of glycogen synthase kinase-3 beta mediates-amyloid induced neuritic damage in Alzheimer's disease. Neurobiol. Dis. 45, 425-437 (2012).
    • (2012) Neurobiol. Dis. , vol.45 , pp. 425-437
    • DaRocha-Souto, B.1
  • 18
    • 33847214486 scopus 로고    scopus 로고
    • Neuroprotective effects of regulators of the glycogen synthase kinase-3 signaling pathway in a transgenic model of Alzheimer's disease are associated with reduced amyloid precursor protein phosphorylation
    • Rockenstein, E. et al. Neuroprotective effects of regulators of the glycogen synthase kinase-3 signaling pathway in a transgenic model of Alzheimer's disease are associated with reduced amyloid precursor protein phosphorylation. J. Neurosci. 27, 1981-1991 (2007).
    • (2007) J. Neurosci. , vol.27 , pp. 1981-1991
    • Rockenstein, E.1
  • 19
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular A and synaptic dysfunction
    • Oddo, S. et al. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular A and synaptic dysfunction. Neuron 39, 409-421 (2003).
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1
  • 20
    • 34547110577 scopus 로고    scopus 로고
    • Internalized antibodies to the A domain of APP reduce neuronal A and protect against synaptic alterations
    • Tampellini, D. et al. Internalized antibodies to the A domain of APP reduce neuronal A and protect against synaptic alterations. J. Biol. Chem. 282, 18895-18906 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 18895-18906
    • Tampellini, D.1
  • 21
    • 65249174019 scopus 로고    scopus 로고
    • Synaptic transmission block by presynaptic injection of oligomeric amyloid
    • Moreno, H. et al. Synaptic transmission block by presynaptic injection of oligomeric amyloid. Proc. Natl. Acad. Sci. USA 106, 5901-5906 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5901-5906
    • Moreno, H.1
  • 22
    • 84899571989 scopus 로고    scopus 로고
    • Intracellular accumulation of amyloid-a predictor for synaptic dysfunction and neuron loss in Alzheimer's disease
    • Bayer, T. A. & Wirths, O. Intracellular accumulation of amyloid-a predictor for synaptic dysfunction and neuron loss in Alzheimer's disease. Front. Aging Neurosci. 2, 8 (2010).
    • (2010) Front. Aging Neurosci. , vol.2 , pp. 8
    • Bayer, T.A.1    Wirths, O.2
  • 23
    • 84872281213 scopus 로고    scopus 로고
    • Effects of different amyloid-protein analogues on synaptic function
    • Ripoli, C. et al. Effects of different amyloid-protein analogues on synaptic function. Neurobiol. Aging 34, 1032-1044 (2013).
    • (2013) Neurobiol. Aging , vol.34 , pp. 1032-1044
    • Ripoli, C.1
  • 24
    • 84907149261 scopus 로고    scopus 로고
    • Intracellular accumulation of amyloid (A) protein plays a major role in A-induced alterations of glutamatergic synaptic transmission and plasticity
    • Ripoli, C. et al. Intracellular accumulation of amyloid (A) protein plays a major role in A-induced alterations of glutamatergic synaptic transmission and plasticity. J. Neurosci. 34, 12893-12903 (2014).
    • (2014) J. Neurosci. , vol.34 , pp. 12893-12903
    • Ripoli, C.1
  • 25
    • 79955484857 scopus 로고    scopus 로고
    • A (1-42) inhibition of LTP is mediated by a signaling pathway involving caspase-3, Akt1 and GSK-3
    • Jo, J. et al. A (1-42) inhibition of LTP is mediated by a signaling pathway involving caspase-3, Akt1 and GSK-3. Nat. Neurosci. 14, 545-547 (2010).
    • (2010) Nat. Neurosci. , vol.14 , pp. 545-547
    • Jo, J.1
  • 26
    • 84863063951 scopus 로고    scopus 로고
    • A pivotal role of GSK-3 in synaptic plasticity
    • Bradley, C. A. et al. A pivotal role of GSK-3 in synaptic plasticity. Front. Mol. Neurosci. 5, 13 (2012).
    • (2012) Front. Mol. Neurosci. , vol.5 , pp. 13
    • Bradley, C.A.1
  • 27
    • 79955385225 scopus 로고    scopus 로고
    • The Role of GSK3 in Presynaptic Function
    • Smillie, K. J., Cousin, M. A. The Role of GSK3 in Presynaptic Function. Int. J. Alzheimers Dis. 2011, 263673 (2011).
    • (2011) Int. J. Alzheimers Dis. , vol.2011 , pp. 263673
    • Smillie, K.J.1    Cousin, M.A.2
  • 28
    • 84945482050 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 infection in neurons leads to production and nuclear localization of APP intracellular domain (AICD): Implications for Alzheimers disease pathogenesis
    • In Press
    • Civitelli, L. et al. Herpes simplex virus type 1 infection in neurons leads to production and nuclear localization of APP intracellular domain (AICD): implications for Alzheimers disease pathogenesis. J. Neurovirology In Press (2015).
    • (2015) J. Neurovirology
    • Civitelli, L.1
  • 29
    • 84887273908 scopus 로고    scopus 로고
    • Plus-end tracking proteins, CLASPs, and a viral Akt mimic regulate herpesvirusinduced stable microtubule formation and virus spread
    • Naghavi, M. H., Gundersen G. G. & Walsh D. Plus-end tracking proteins, CLASPs, and a viral Akt mimic regulate herpesvirusinduced stable microtubule formation and virus spread. Proc. Natl. Acad. Sci. USA 110, 18268-18273 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 18268-18273
    • Naghavi, M.H.1    Gundersen, G.G.2    Walsh, D.3
  • 30
    • 77956226596 scopus 로고    scopus 로고
    • PI3K/Akt signaling mediated apoptosis blockage and viral gene expression in oral epithelial cells during herpes simplex virus infection
    • Hsu, M. J., Wu, C. Y., Chiang, H. H., Lai, Y. L. & Hung, S. L. PI3K/Akt signaling mediated apoptosis blockage and viral gene expression in oral epithelial cells during herpes simplex virus infection. Virus Res. 153, 36-43 (2010).
    • (2010) Virus Res. , vol.153 , pp. 36-43
    • Hsu, M.J.1    Wu, C.Y.2    Chiang, H.H.3    Lai, Y.L.4    Hung, S.L.5
  • 31
    • 84928923376 scopus 로고    scopus 로고
    • GSK3 Inhibition Promotes Synaptogenesis in Drosophila and Mammalian Neurons
    • Cuesto, G. et al. GSK3 Inhibition Promotes Synaptogenesis in Drosophila and Mammalian Neurons. PLoS One 10, e0118475 (2015).
    • (2015) PLoS One , vol.10 , pp. e0118475
    • Cuesto, G.1
  • 32
    • 84896131461 scopus 로고    scopus 로고
    • GSK-3/CREB pathway involved in the gx-50's effect on Alzheimer's disease
    • Tang, M. et al. GSK-3/CREB pathway involved in the gx-50's effect on Alzheimer's disease. Neuropharmacology 81, 256-266 (2014).
    • (2014) Neuropharmacology , vol.81 , pp. 256-266
    • Tang, M.1
  • 33
    • 0028670773 scopus 로고
    • A secondary phosphorylation of CREB341 at Ser129 is required for the cAMP-mediated control of gene expression. A role for glycogen synthase kinase-3 in the control of gene expression
    • Fiol, C. J. et al. A secondary phosphorylation of CREB341 at Ser129 is required for the cAMP-mediated control of gene expression. A role for glycogen synthase kinase-3 in the control of gene expression. J. Biol. Chem. 269, 32187-32193 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 32187-32193
    • Fiol, C.J.1
  • 34
    • 0033558270 scopus 로고    scopus 로고
    • Cell-cycle-regulated phosphorylation of cAMP response element-binding protein: Identification of novel phosphorylation sites
    • Saeki, K., Yuo, A. & Takaku, F. Cell-cycle-regulated phosphorylation of cAMP response element-binding protein: identification of novel phosphorylation sites. Biochem. J. 338, 49-54 (1999).
    • (1999) Biochem. J. , vol.338 , pp. 49-54
    • Saeki, K.1    Yuo, A.2    Takaku, F.3
  • 35
    • 0142123260 scopus 로고    scopus 로고
    • APP processing is regulated by cytoplasmic phosphorylation
    • Lee, M. S. et al. APP processing is regulated by cytoplasmic phosphorylation. J. Cell. Biol. 16, 83-95 (2003).
    • (2003) J. Cell. Biol. , vol.16 , pp. 83-95
    • Lee, M.S.1
  • 36
    • 84858199215 scopus 로고    scopus 로고
    • The amyloid precursor protein intracellular domain-fe65 multiprotein complexes: A challenge to the amyloid hypothesis for Alzheimer's disease
    • Bárquez, D. A. & González-Billault, C. The amyloid precursor protein intracellular domain-fe65 multiprotein complexes: a challenge to the amyloid hypothesis for Alzheimer's disease Int. J. Alzheimer's Dis. 2012, 353145 (2012).
    • (2012) Int. J. Alzheimer's Dis. , vol.2012 , pp. 353145
    • Bárquez, D.A.1    González-Billault, C.2
  • 37
    • 84904631001 scopus 로고    scopus 로고
    • The A-clearance protein transthyretin, like neprilysin, is epigenetically regulated by the amyloid precursor protein intracellular domain
    • Kerridge, C., Belyaev, N. D., Nalivaeva, N. N. & Turner, A. J. The A-clearance protein transthyretin, like neprilysin, is epigenetically regulated by the amyloid precursor protein intracellular domain. J. Neurochem. 130, 419-431 (2014).
    • (2014) J. Neurochem. , vol.130 , pp. 419-431
    • Kerridge, C.1    Belyaev, N.D.2    Nalivaeva, N.N.3    Turner, A.J.4
  • 38
    • 51449088620 scopus 로고    scopus 로고
    • Inhibitors of GSK-3 prevent corticosterone from inducing COX-1 expression in cardiomyocytes
    • Sun, H. & Chen, Q. M. Inhibitors of GSK-3 prevent corticosterone from inducing COX-1 expression in cardiomyocytes. Cardiovasc. Toxicol. 8, 93-100 (2008).
    • (2008) Cardiovasc. Toxicol. , vol.8 , pp. 93-100
    • Sun, H.1    Chen, Q.M.2
  • 39
    • 0033597936 scopus 로고    scopus 로고
    • Transient increases in intracellular calcium result in prolonged site-selective increases in Tau phosphorylation through a glycogen synthase kinase 3-dependent pathway
    • Hartigan, J. A. & Johnson, G. V. Transient increases in intracellular calcium result in prolonged site-selective increases in Tau phosphorylation through a glycogen synthase kinase 3-dependent pathway. J. Biol. Chem. 274, 21395-21401 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 21395-21401
    • Hartigan, J.A.1    Johnson, G.V.2
  • 40
    • 84865415419 scopus 로고    scopus 로고
    • Roles of glycogen synthase kinase 3 in Alzheimer's disease
    • Cai, Z., Zhao, Y. & Zhao, B. Roles of glycogen synthase kinase 3 in Alzheimer's disease. Curr. Alzheimer Res. 9, 864-879 (2012).
    • (2012) Curr. Alzheimer Res. , vol.9 , pp. 864-879
    • Cai, Z.1    Zhao, Y.2    Zhao, B.3
  • 41
    • 83055188883 scopus 로고    scopus 로고
    • GSK-3 / kinases and amyloid production in vivo
    • Jaworski, T. et al. GSK-3 / kinases and amyloid production in vivo. Nature 480, E4-5 (2011).
    • (2011) Nature , vol.480 , pp. E4-5
    • Jaworski, T.1
  • 42
    • 78049427560 scopus 로고    scopus 로고
    • Inhibition of GSK-3 ameliorates A pathology in an adult-onset Drosophila model of Alzheimer's disease
    • Sofola, O. et al. Inhibition of GSK-3 ameliorates A? pathology in an adult-onset Drosophila model of Alzheimer's disease. PLoS Genet 6, e1001087 (2010).
    • (2010) PLoS Genet , vol.6 , pp. e1001087
    • Sofola, O.1
  • 43
    • 77949381494 scopus 로고    scopus 로고
    • GSK-3 inhibits presynaptic vesicle exocytosis by phosphorylating P/Q-type calcium channel and interrupting SNARE complex formation
    • Zhu, L. Q. et al. GSK-3 inhibits presynaptic vesicle exocytosis by phosphorylating P/Q-type calcium channel and interrupting SNARE complex formation. J. Neurosci. 30, 3624-3633 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 3624-3633
    • Zhu, L.Q.1
  • 44
    • 77954144968 scopus 로고    scopus 로고
    • Dynamin i phosphorylation by GSK3 controls activity-dependent bulk endocytosis of synaptic vesicles
    • Clayton, E. L. et al. Dynamin I phosphorylation by GSK3 controls activity-dependent bulk endocytosis of synaptic vesicles. Nat. Neurosci. 13, 845-851 (2010).
    • (2010) Nat. Neurosci. , vol.13 , pp. 845-851
    • Clayton, E.L.1
  • 45
    • 84880055131 scopus 로고    scopus 로고
    • The Fibroblast Growth Factor 14: Voltage-gated Sodium Channel Complex Is a New Target of Glycogen Synthase Kinase 3 (GSK3)
    • Shavkunov, A. S. et al. The Fibroblast Growth Factor 14: Voltage-gated Sodium Channel Complex Is a New Target of Glycogen Synthase Kinase 3 (GSK3). J Biol. Chem. 288, 19370-19385 (2013).
    • (2013) J Biol. Chem. , vol.288 , pp. 19370-19385
    • Shavkunov, A.S.1
  • 46
    • 84922572433 scopus 로고    scopus 로고
    • Identifying a kinase network regulating FGF14:Nav1. 6 complex assembly using split-luciferase complementation
    • Hsu, W. C. et al. Identifying a kinase network regulating FGF14:Nav1.6 complex assembly using split-luciferase complementation. PLoS One 10, e0117246 (2015).
    • (2015) PLoS One , vol.10 , pp. e0117246
    • Hsu, W.C.1
  • 47
    • 84922289434 scopus 로고    scopus 로고
    • The Na1. 2 channel is regulated by GSK3
    • James, T. F. et al. The Na1.2 channel is regulated by GSK3. Biochim. Biophys. Acta 1850, 832-844 (2015).
    • (2015) Biochim. Biophys. Acta. , vol.1850 , pp. 832-844
    • James, T.F.1
  • 48
    • 84863993414 scopus 로고    scopus 로고
    • Control of neuronal ion channel function by glycogen synthase kinase-3: New prospective for an old kinase
    • Wildburger, N. C. & Laezza, F. Control of neuronal ion channel function by glycogen synthase kinase-3: new prospective for an old kinase. Front. Mol. Neurosci. 5, 80 (2012).
    • (2012) Front. Mol. Neurosci. , vol.5 , pp. 80
    • Wildburger, N.C.1    Laezza, F.2
  • 49
    • 84901604890 scopus 로고    scopus 로고
    • Differential regulation of collapsin response mediator protein 2 (CRMP2) phosphorylation by GSK3 and CDK5 following traumatic brain injury
    • Wilson S. M., Ki Yeon S., Yang X. F., Park K. D. & Khanna R. Differential regulation of collapsin response mediator protein 2 (CRMP2) phosphorylation by GSK3 and CDK5 following traumatic brain injury. Front. Cell. Neurosci. 8, 135 (2014).
    • (2014) Front. Cell. Neurosci. , vol.8 , pp. 135
    • Wilson, S.M.1    Ki Yeon, S.2    Yang, X.F.3    Park, K.D.4    Khanna, R.5
  • 50
    • 36048937547 scopus 로고    scopus 로고
    • Activation of glycogen synthase kinase-3 inhibits long-term potentiation with synapse-associated impairments
    • Zhu, L. Q. et al. Activation of glycogen synthase kinase-3 inhibits long-term potentiation with synapse-associated impairments. J. Neurosci. 27, 12211-12220 (2007).
    • (2007) J. Neurosci. , vol.27 , pp. 12211-12220
    • Zhu, L.Q.1
  • 51
    • 60349092194 scopus 로고    scopus 로고
    • Alzheimer's disease specific tau phosphorylation is induced by herpes simplex virus type 1
    • Wozniak, M. A., Frost, A. L. & Itzhaki, R. F. Alzheimer's disease specific tau phosphorylation is induced by herpes simplex virus type 1. J. Alzheimer's Dis. 16, 341-350 (2009).
    • (2009) J. Alzheimer's Dis. , vol.16 , pp. 341-350
    • Wozniak, M.A.1    Frost, A.L.2    Itzhaki, R.F.3
  • 52
    • 79957913270 scopus 로고    scopus 로고
    • Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
    • Lasagna-Reeves, C. A. et al. Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice. Mol. Neurodegener. 6, 39 (2011).
    • (2011) Mol. Neurodegener. , vol.6 , pp. 39
    • Lasagna-Reeves, C.A.1
  • 53
    • 84868269943 scopus 로고    scopus 로고
    • Alzheimer brain-derived tau oligomers propagate pathology from endogenous tau
    • Lasagna-Reeves, C. A. et al. Alzheimer brain-derived tau oligomers propagate pathology from endogenous tau. Sci. Rep. 2, 700 (2012).
    • (2012) Sci. Rep. , vol.2 , pp. 700
    • Lasagna-Reeves, C.A.1
  • 54
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3 in cellular signaling
    • Grimes, C. A. & Jope, R. S. The multifaceted roles of glycogen synthase kinase 3 in cellular signaling. Prog. Neurobiol. 65, 391-426 (2001).
    • (2001) Prog. Neurobiol. , vol.65 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 55
    • 58249118862 scopus 로고    scopus 로고
    • Transcription factors in long-term memory and synaptic plasticity
    • Alberini, C. M. Transcription factors in long-term memory and synaptic plasticity. Physiol. Rev. 89, 121-145 (2009).
    • (2009) Physiol. Rev. , vol.89 , pp. 121-145
    • Alberini, C.M.1
  • 56
    • 84855994224 scopus 로고    scopus 로고
    • A role for neuronal cAMP responsive-element binding (CREB)-1 in brain responses to calorie restriction
    • Fusco, S. et al. A role for neuronal cAMP responsive-element binding (CREB)-1 in brain responses to calorie restriction. Proc. Natl. Acad. Sci. USA 109, 621-626 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 621-626
    • Fusco, S.1
  • 57
    • 36348931527 scopus 로고    scopus 로고
    • Herpes simplex virus infection causes cellular-amyloid accumulation and secretase upregulation
    • Wozniak, M. A., Itzhaki, R. F., Shipley, S. J. & Dobson, C. B. Herpes simplex virus infection causes cellular-amyloid accumulation and secretase upregulation. Neurosci. Lett. 429, 95-100 (2007).
    • (2007) Neurosci. Lett. , vol.429 , pp. 95-100
    • Wozniak, M.A.1    Itzhaki, R.F.2    Shipley, S.J.3    Dobson, C.B.4
  • 58
    • 0001997084 scopus 로고
    • Growth, assay and purification of Herpes viruses
    • ed. B. W. J. Mahy Oxford IRL press
    • Killington, R. A. & Powell, K. L. Growth, assay and purification of Herpes viruses. In: Virology A Practical Approach (ed. B. W. J. Mahy), pp. 207-236 (Oxford IRL press, 1991).
    • (1991) Virology A Practical Approach , pp. 207-236
    • Killington, R.A.1    Powell, K.L.2
  • 59
    • 0027971849 scopus 로고
    • Inhibition of low-and high-threshold Ca2+ channels of human neuroblastoma IMR32 cells by Lambert-Eaton myasthenic syndrome (LEMS) IgGs
    • Grassi, C., Magnelli, V., Carabelli, V., Sher, E. & Carbone, E. Inhibition of low-and high-threshold Ca2+ channels of human neuroblastoma IMR32 cells by Lambert-Eaton myasthenic syndrome (LEMS) IgGs. Neurosci Lett. 181, 50-56 (1994).
    • (1994) Neurosci Lett , vol.181 , pp. 50-56
    • Grassi, C.1    Magnelli, V.2    Carabelli, V.3    Sher, E.4    Carbone, E.5
  • 60
    • 84871733093 scopus 로고    scopus 로고
    • Protection of primary neurons and mouse brain from Alzheimer's pathology by molecular tweezers
    • Attar, A. et al. Protection of primary neurons and mouse brain from Alzheimer's pathology by molecular tweezers. Brain 135, 3735-3748 (2012).
    • (2012) Brain , vol.135 , pp. 3735-3748
    • Attar, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.