메뉴 건너뛰기




Volumn 9, Issue 4, 2014, Pages

Amyloid-β and proinflammatory cytokines utilize a prion protein-dependent pathway to activate NADPH oxidase and induce cofilin-actin rods in hippocampal neurons

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; AMYLOID BETA PROTEIN; COFILIN; CYTOKINE; DIMER; INTERLEUKIN 1BETA; INTERLEUKIN 6; PRION PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TUMOR NECROSIS FACTOR ALPHA; ACTIN DEPOLYMERIZING FACTOR; DACTINOMYCIN; GLUTAMIC ACID; TUMOR NECROSIS FACTOR;

EID: 84899730580     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0095995     Document Type: Article
Times cited : (57)

References (95)
  • 1
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide LS, Striegl AM, Boyle JA, Meberg PJ, Bamburg JR (2000) Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat Cell Biol 2: 628-636.
    • (2000) Nat Cell Biol , vol.2 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 3
    • 84863023555 scopus 로고    scopus 로고
    • Cofilin aggregation blocks intracellular trafficking and induces synaptic loss in hippocampal neurons
    • Cichon J, Sun C, Chen B, Jiang M, Chen XA, Sun Y, et al. (2012) Cofilin aggregation blocks intracellular trafficking and induces synaptic loss in hippocampal neurons. J Biol Chem 287: 3919-29.
    • (2012) J Biol Chem , vol.287 , pp. 3919-3929
    • Cichon, J.1    Sun, C.2    Chen, B.3    Jiang, M.4    Chen, X.A.5    Sun, Y.6
  • 4
    • 30544447666 scopus 로고    scopus 로고
    • Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: A feedforward mechanism for alzheimer's disease
    • DOI 10.1523/JNEUROSCI.3711-05.2005
    • Maloney MT, Minamide LS, Kinley AW, Boyle JA, Bamburg JR (2005) Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: a feedforward mechanism for Alzheimer's disease. J Neurosci 25: 11313-11321. Erratum in: J Neurosci 26: 354. (Pubitemid 43083705)
    • (2005) Journal of Neuroscience , vol.25 , Issue.49 , pp. 11313-11321
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 6
    • 84879829589 scopus 로고    scopus 로고
    • Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease
    • 2012
    • Masters CL, Selkoe DJ (2012) Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease. Cold Spring Harbor Perspect Med 2012;2: a006262
    • (2012) Cold Spring Harbor Perspect Med , vol.2
    • Masters, C.L.1    Selkoe, D.J.2
  • 7
    • 78751649794 scopus 로고    scopus 로고
    • Amyloid beta dimers/trimers potently induce cofilin-actin rods that are inhibited by maintaining cofilin phosphorylation
    • Davis RC, Marsden IT, Maloney MT, Minamide LS, Podlisny M, et al. (2011) Amyloid beta dimers/trimers potently induce cofilin-actin rods that are inhibited by maintaining cofilin phosphorylation. Mol Neurodegen 6: 10.
    • (2011) Mol Neurodegen , vol.6 , pp. 10
    • Davis, R.C.1    Marsden, I.T.2    Maloney, M.T.3    Minamide, L.S.4    Podlisny, M.5
  • 8
    • 77957275697 scopus 로고    scopus 로고
    • ADF/cofilin-mediated actin dynamics regulate AMPA receptor trafficking during synaptic plasticity
    • Gu J, Lee CW, Fan Y, Komlos D, Tang X, et al. (2010) ADF/cofilin-mediated actin dynamics regulate AMPA receptor trafficking during synaptic plasticity. Nat Neurosci 13: 1208-1215.
    • (2010) Nat Neurosci , vol.13 , pp. 1208-1215
    • Gu, J.1    Lee, C.W.2    Fan, Y.3    Komlos, D.4    Tang, X.5
  • 9
    • 84894281353 scopus 로고    scopus 로고
    • A genetically encoded reporter for imaging cofilin-actin rods in living neurons
    • Mi J, Shaw AE, Pak CW, Walsh KP, Minamide LS, et al. (2013) A genetically encoded reporter for imaging cofilin-actin rods in living neurons. PLoS One 8(12): e83609.
    • (2013) PLoS One , vol.8 , Issue.12
    • Mi, J.1    Shaw, A.E.2    Pak, C.W.3    Walsh, K.P.4    Minamide, L.S.5
  • 10
    • 77951928742 scopus 로고    scopus 로고
    • The presence of sodium dodecyl sulphate-stable Abeta dimers is strongly associated with Alzheimer-type dementia
    • McDonald JM, Savva GM, Brayne C, Welzel AT, Forster G, et al. (2010) The presence of sodium dodecyl sulphate-stable Abeta dimers is strongly associated with Alzheimer-type dementia. Brain 133: 1328-1341.
    • (2010) Brain , vol.133 , pp. 1328-1341
    • McDonald, J.M.1    Savva, G.M.2    Brayne, C.3    Welzel, A.T.4    Forster, G.5
  • 11
    • 84859434098 scopus 로고    scopus 로고
    • The levels of water-soluble and triton-soluble Aβ are increased in Alzheimer's disease brain
    • McDonald JM, Cairns NJ, Taylor-Reinwald L, Holtzman D, Walsh DM (2012) The levels of water-soluble and triton-soluble Aβ are increased in Alzheimer's disease brain. Brain Res 1450: 138-147.
    • (2012) Brain Res , vol.1450 , pp. 138-147
    • McDonald, J.M.1    Cairns, N.J.2    Taylor-Reinwald, L.3    Holtzman, D.4    Walsh, D.M.5
  • 12
    • 84884635054 scopus 로고    scopus 로고
    • Promiscuous Alzheimer's amyloid: Yet another partner
    • Benilova I, De Strooper B (2013) Promiscuous Alzheimer's amyloid: yet another partner. Science 341: 1354-1355.
    • (2013) Science , vol.341 , pp. 1354-1355
    • Benilova, I.1    De Strooper, B.2
  • 13
    • 58149379613 scopus 로고    scopus 로고
    • SynGAP regulates steady-state and activity-dependent phosphorylation of cofilin
    • Carlisle HJ, Manzerra P, Marcora E, Kennedy MB (2008) SynGAP regulates steady-state and activity-dependent phosphorylation of cofilin. J Neurosci 28: 13673-13683.
    • (2008) J Neurosci , vol.28 , pp. 13673-13683
    • Carlisle, H.J.1    Manzerra, P.2    Marcora, E.3    Kennedy, M.B.4
  • 14
    • 84884630099 scopus 로고    scopus 로고
    • Human LilrB2 is a β-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer's model
    • Kim T, Vidal GS, Djurisic M, William CM, Birnbaum ME, et al. (2013) Human LilrB2 is a β-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer's model. Science 341: 1399-1404.
    • (2013) Science , vol.341 , pp. 1399-1404
    • Kim, T.1    Vidal, G.S.2    Djurisic, M.3    William, C.M.4    Birnbaum, M.E.5
  • 15
    • 84890478683 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and calcium deregulation by RanBP9-cofilin pathway
    • Roh S-E, Woo JA, Lakshmana MK, Uhlar C, Ankala V, et al. (2013) Mitochondrial dysfunction and calcium deregulation by RanBP9-cofilin pathway. FASEB J 27:4776-4789.
    • (2013) FASEB J , vol.27 , pp. 4776-4789
    • Roh, S.-E.1    Woo, J.A.2    Lakshmana, M.K.3    Uhlar, C.4    Ankala, V.5
  • 16
    • 84860657462 scopus 로고    scopus 로고
    • Incorporation of cofilin into rods depends on disulfide intermolecular bonds: Implications for actin regulation and neurodegenerative disease
    • Bernstein BW, Shaw AE, Minamide LS, Pak CW, Bamburg JR (2012) Incorporation of cofilin into rods depends on disulfide intermolecular bonds: implications for actin regulation and neurodegenerative disease. J Neurosci 32: 6670-6681.
    • (2012) J Neurosci , vol.32 , pp. 6670-6681
    • Bernstein, B.W.1    Shaw, A.E.2    Minamide, L.S.3    Pak, C.W.4    Bamburg, J.R.5
  • 17
    • 16844382331 scopus 로고    scopus 로고
    • Evidence of increased oxidative damage in subjects with mild cognitive impairment
    • Keller JN, Schmitt FA, Scheff SW, Ding Q, Chen Q, et al. (2005) Evidence of increased oxidative damage in subjects with mild cognitive impairment. Neurology 64: 1152-1156.
    • (2005) Neurology , vol.64 , pp. 1152-1156
    • Keller, J.N.1    Schmitt, F.A.2    Scheff, S.W.3    Ding, Q.4    Chen, Q.5
  • 18
    • 33645082486 scopus 로고    scopus 로고
    • Potential inflammatory biomarkers in Alzheimer's disease
    • Mrak RE, Griffin WS (2005) Potential inflammatory biomarkers in Alzheimer's disease. J. Alzheimers Dis 8: 369-375.
    • (2005) J. Alzheimers Dis , vol.8 , pp. 369-375
    • Mrak, R.E.1    Griffin, W.S.2
  • 19
    • 84864221504 scopus 로고    scopus 로고
    • Neuroinflammatory cytokines - The common thread in Alzheimer's pathogenesis
    • Griffin WS, Barger SW (2010) Neuroinflammatory cytokines- the common thread in Alzheimer's pathogenesis. US Neurol 6: 19-27.
    • (2010) US Neurol , vol.6 , pp. 19-27
    • Griffin, W.S.1    Barger, S.W.2
  • 20
    • 84859085370 scopus 로고    scopus 로고
    • Ceramide kinase regulates TNF α-stimulated NADPH oxidase activity and eicosanoid biosynthesis in neuroblastoma cells
    • Barth BM, Gustafson SJ, Hankins JL, Kaiser JM, Haakenson JK, et al. (2012) Ceramide kinase regulates TNF α-stimulated NADPH oxidase activity and eicosanoid biosynthesis in neuroblastoma cells. Cell Signal 24: 1126-1133.
    • (2012) Cell Signal , vol.24 , pp. 1126-1133
    • Barth, B.M.1    Gustafson, S.J.2    Hankins, J.L.3    Kaiser, J.M.4    Haakenson, J.K.5
  • 21
    • 79957935719 scopus 로고    scopus 로고
    • NADPH-oxidase activation and cognition in Alzheimer disease progression
    • Ansari MA, Scheff SW (2011) NADPH-oxidase activation and cognition in Alzheimer disease progression. Free Radic Biol Med 51: 171-178.
    • (2011) Free Radic Biol Med , vol.51 , pp. 171-178
    • Ansari, M.A.1    Scheff, S.W.2
  • 23
    • 84864360749 scopus 로고    scopus 로고
    • Targeting NOX enzymes in the central nervous system: Therapeutic opportunities
    • Sorce S, Krause KH, Jaquet V (2012) Targeting NOX enzymes in the central nervous system: therapeutic opportunities. Cell Mol Life Sci 69: 2387-2407.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 2387-2407
    • Sorce, S.1    Krause, K.H.2    Jaquet, V.3
  • 24
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 457: 1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 26
    • 84884200967 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer Aβ oligomer bound to cellular prion protein
    • Um JW, Kaufman AC, Kostylev M, Heiss JK, Stagi M, et al. (2013) Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer Aβ oligomer bound to cellular prion protein. Neuron 79: 887-902.
    • (2013) Neuron , vol.79 , pp. 887-902
    • Um, J.W.1    Kaufman, A.C.2    Kostylev, M.3    Heiss, J.K.4    Stagi, M.5
  • 27
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzhemier's disease mouse models
    • Ittner LM, Ke YD, Delerue F, Bi M, Gladbach A, et al. (2010) Dendritic function of tau mediates amyloid-beta toxicity in Alzhemier's disease mouse models. Cell 142: 387-397.
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1    Ke, Y.D.2    Delerue, F.3    Bi, M.4    Gladbach, A.5
  • 28
    • 84866065959 scopus 로고    scopus 로고
    • Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
    • Um JW, Nygaard HB, Heiss JK, Kostylev MA, Stagi M, et al. (2012) Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nat Neurosci 15: 1227-1235.
    • (2012) Nat Neurosci , vol.15 , pp. 1227-1235
    • Um, J.W.1    Nygaard, H.B.2    Heiss, J.K.3    Kostylev, M.A.4    Stagi, M.5
  • 29
    • 79956302348 scopus 로고    scopus 로고
    • Alzheimer's disease brain-derived amyloid-β-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein
    • Barry AE, Klyubin I, Mc Donald JM, Mably AJ, Farrell MA, et al. (2011) Alzheimer's disease brain-derived amyloid-β-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein. J Neurosci 31: 7259-7263.
    • (2011) J Neurosci , vol.31 , pp. 7259-7263
    • Barry, A.E.1    Klyubin, I.2    Mc Donald, J.M.3    Mably, A.J.4    Farrell, M.A.5
  • 30
    • 77957778860 scopus 로고    scopus 로고
    • C monoclonal antibody infusion as a novel treatment for cognitive deficits in Alzheimer disease model mouse
    • C monoclonal antibody infusion as a novel treatment for cognitive deficits in Alzheimer disease model mouse. BMC Neurosci 11: 130.
    • (2010) BMC Neurosci , vol.11 , pp. 130
    • Chung, E.1    Ji, Y.2    Sun, Y.3    Kascsak, R.J.4    Kascsak, R.B.5
  • 31
    • 67349164761 scopus 로고    scopus 로고
    • Proinflammatory cytokines provoke oxidative damage to actin in neuronal cells mediated by Rac1 and NADPH oxidase
    • Barth BM, Stewart-Smeets S, Kuhn TB (2009) Proinflammatory cytokines provoke oxidative damage to actin in neuronal cells mediated by Rac1 and NADPH oxidase. Mol Cell Neurosci 41: 274-285.
    • (2009) Mol Cell Neurosci , vol.41 , pp. 274-285
    • Barth, B.M.1    Stewart-Smeets, S.2    Kuhn, T.B.3
  • 33
    • 77951876319 scopus 로고    scopus 로고
    • Memory impairment in transgenic Alzheimer mice require cellular prion protein
    • Gimbel DA, Nygaard HB, Coffey EE, Gunther EC, Laurén J, et al. (2010) Memory impairment in transgenic Alzheimer mice require cellular prion protein. J Neurosci 30: 6367-6374.
    • (2010) J Neurosci , vol.30 , pp. 6367-6374
    • Gimbel, D.A.1    Nygaard, H.B.2    Coffey, E.E.3    Gunther, E.C.4    Laurén, J.5
  • 34
    • 34347257042 scopus 로고    scopus 로고
    • Nox enzymes, ROS, and chronic disease: An example of antagonistic pleiotropy
    • Lambeth JD (2007) Nox enzymes, ROS, and chronic disease: an example of antagonistic pleiotropy. Free Radic Biol Med 43: 332-347.
    • (2007) Free Radic Biol Med , vol.43 , pp. 332-347
    • Lambeth, J.D.1
  • 35
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • DOI 10.1152/physrev.00044.2005
    • Bedard K, Krause KH (2007) The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 87: 245-313. (Pubitemid 46209993)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 245-313
    • Bedard, K.1    Krause, K.-H.2
  • 36
  • 37
    • 67651184281 scopus 로고    scopus 로고
    • NOX enzymes in the central nervous system: From signaling to disease
    • Sorce S, Krause KH (2009) NOX enzymes in the central nervous system: from signaling to disease. Antioxid Redox Signal 11: 2481-2504.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2481-2504
    • Sorce, S.1    Krause, K.H.2
  • 38
    • 24744468043 scopus 로고    scopus 로고
    • phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation
    • DOI 10.1074/jbc.M501882200
    • Kawahara T., Ritsick D, Cheng G, Lambeth JD (2005) Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation. J Biol Chem 280: 31859-31869. (Pubitemid 41291936)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 31859-31869
    • Kawahara, T.1    Ritsick, D.2    Cheng, G.3    Lambeth, J.D.4
  • 40
    • 84899750432 scopus 로고    scopus 로고
    • Evolution of NADPH oxidase inhibitors: Selectivity and mechanisms for target engagement
    • 2014 Feb 26 [Epub ahead of print]
    • Altenhofer S, Radermacher KA, Kleikers PW, Wingler K, Schmidt HH (2014) Evolution of NADPH oxidase inhibitors: selectivity and mechanisms for target engagement. Antioxid Redox Signal 2014 Feb 26 [Epub ahead of print].
    • (2014) Antioxid Redox Signal
    • Altenhofer, S.1    Radermacher, K.A.2    Kleikers, P.W.3    Wingler, K.4    Schmidt, H.H.5
  • 41
    • 84898912842 scopus 로고    scopus 로고
    • Isoproterenol induced stressful reactions in the brain are characterized by inflammation due to activation of NADPH oxidase and ER stress: Attenuated by apocyanin, Rehmannia complex and triterpene acids
    • 2014 Feb 26 [Epub ahead of print]
    • Mo G-L, Li Y, Du R-H, Dai D-Z, Cong X-D, et al. (2014) Isoproterenol induced stressful reactions in the brain are characterized by inflammation due to activation of NADPH oxidase and ER stress: attenuated by apocyanin, Rehmannia complex and triterpene acids. Neurochem Res 2014 Feb 26 [Epub ahead of print]
    • (2014) Neurochem Res
    • Mo, G.-L.1    Li, Y.2    Du, R.-H.3    Dai, D.-Z.4    Cong, X.-D.5
  • 42
    • 80055071341 scopus 로고    scopus 로고
    • Amyloid-b-induced synapse damage is mediated via cross-linkage of cellular prion proteins
    • Bate C, Williams A (2011) Amyloid-b-induced synapse damage is mediated via cross-linkage of cellular prion proteins. J Biol Chem 286: 37955-37963.
    • (2011) J Biol Chem , vol.286 , pp. 37955-37963
    • Bate, C.1    Williams, A.2
  • 43
    • 24944491725 scopus 로고    scopus 로고
    • Copper binding is the governing determinant of prion protein turnover
    • DOI 10.1016/j.mcn.2005.07.001, PII S1044743105001478
    • Haigh CL, Edwards K, Brown DR (2005) Copper binding is the governing determinant of prion protein turnover. Mol Cell Neurosci 30: 186-196. (Pubitemid 41316562)
    • (2005) Molecular and Cellular Neuroscience , vol.30 , Issue.2 , pp. 186-196
    • Haigh, C.L.1    Edwards, K.2    Brown, D.R.3
  • 45
    • 33751082967 scopus 로고    scopus 로고
    • Formation of actin-ADF/cofilin rods transiently retards decline of mitochondrial potential and ATP in stressed neurons
    • DOI 10.1152/ajpcell.00066.2006
    • Bernstein BW, Chen H, Boyle JA, Bamburg JR (2006) Formation of actin-ADF/cofilin rods transiently retards decline of mitochondrial potential and ATP in stressed neurons. Am J Physiol Cell Physiol 291: C828-839. (Pubitemid 44771802)
    • (2006) American Journal of Physiology - Cell Physiology , vol.291 , Issue.5
    • Bernstein, B.W.1    Chen, H.2    Boyle, J.A.3    Bamburg, J.R.4
  • 46
    • 70450148316 scopus 로고    scopus 로고
    • Mapping cofilin-actin rods in stressed hippocampal slices and the role of cdc42 in amyloid-β-induced rods
    • Davis RC, Maloney MT, Minamide LS, Flynn KC, Stonebraker MA, et al. (2009) Mapping cofilin-actin rods in stressed hippocampal slices and the role of cdc42 in amyloid-β-induced rods. J Alzheimers Dis 18: 35-50
    • (2009) J Alzheimers Dis , vol.18 , pp. 35-50
    • Davis, R.C.1    Maloney, M.T.2    Minamide, L.S.3    Flynn, K.C.4    Stonebraker, M.A.5
  • 47
    • 84864471159 scopus 로고    scopus 로고
    • A mutation in APP protects against Alzheimer's disease and age-related cognitive decline
    • Jonsson T, Atwal JK, Steinberg S, Snaedal J, Jonsson PV, et al. (2012) A mutation in APP protects against Alzheimer's disease and age-related cognitive decline. Nature 488: 96-99.
    • (2012) Nature , vol.488 , pp. 96-99
    • Jonsson, T.1    Atwal, J.K.2    Steinberg, S.3    Snaedal, J.4    Jonsson, P.V.5
  • 48
    • 84872487799 scopus 로고    scopus 로고
    • Brain ischemia activates β- and γ-secretase cleavage of amyloid precursor protein: Significance in sporadic Alzheimer's disease
    • Pluta R, Furmaga-Jablonska W, Maciejewski R, Ulamek-Koziol M, Jablonski M (2013) Brain ischemia activates β- and γ-secretase cleavage of amyloid precursor protein: significance in sporadic Alzheimer's disease. Mol Neurobiol 47: 425-434.
    • (2013) Mol Neurobiol , vol.47 , pp. 425-434
    • Pluta, R.1    Furmaga-Jablonska, W.2    Maciejewski, R.3    Ulamek-Koziol, M.4    Jablonski, M.5
  • 49
    • 84861330645 scopus 로고    scopus 로고
    • Overlapping profiles of Aβ peptides in the Alzheimer's disease and pathological aging brains
    • Moore BD, Chakrabart P, Levites Y, Kukar TL, Baine A-M, et al. (2012) Overlapping profiles of Aβ peptides in the Alzheimer's disease and pathological aging brains. Alz Res Therapy 4: 18.
    • (2012) Alz Res Therapy , vol.4 , pp. 18
    • Moore, B.D.1    Chakrabart, P.2    Levites, Y.3    Kukar, T.L.4    Baine, A.-M.5
  • 50
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, Li S, Mehta TH, Garcia-Munoz A, Shepardson NE, et al. (2008) Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 14: 837-842.
    • (2008) Nat Med , vol.14 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3    Garcia-Munoz, A.4    Shepardson, N.E.5
  • 53
    • 3442893295 scopus 로고    scopus 로고
    • Cytokines in neuroinflammation and Alzheimer's disease
    • DOI 10.2174/1389450043345308
    • Cacquevel M, Lebeurrier N, Chéenne S, Vivien D (2004) Cytokines in neuroinflammation and Alzheimer's disease. Curr Drug Targets 5: 529-534. (Pubitemid 39004427)
    • (2004) Current Drug Targets , vol.5 , Issue.6 , pp. 529-534
    • Cacquevel, M.1    Lebeurrier, N.2    Cheenne, S.3    Vivien, D.4
  • 55
    • 84896324370 scopus 로고    scopus 로고
    • The role of inflammasome in Alzheimer's disease
    • Liu L, Chan C (2014) The role of inflammasome in Alzheimer's disease. Ageing Res Rev 15C: 6-15.
    • (2014) Ageing Res Rev , vol.15 C , pp. 6-15
    • Liu, L.1    Chan, C.2
  • 56
    • 84880117155 scopus 로고    scopus 로고
    • Down's syndrome, neuroinflammation, and Alzheimer neuropathogenesis
    • Wilcock DM, Griffin WS (2013) Down's syndrome, neuroinflammation, and Alzheimer neuropathogenesis. J Neuroinflammation 10: 84.
    • (2013) J Neuroinflammation , vol.10 , pp. 84
    • Wilcock, D.M.1    Griffin, W.S.2
  • 57
    • 84858742061 scopus 로고    scopus 로고
    • Traumatic brain injury: A risk factor for Alzheimer's disease
    • Sivanandam TM, Thakur MK (2012) Traumatic brain injury: A risk factor for Alzheimer's disease. Neurosci Biobehav Rev 36: 1376-1381.
    • (2012) Neurosci Biobehav Rev , vol.36 , pp. 1376-1381
    • Sivanandam, T.M.1    Thakur, M.K.2
  • 60
    • 84873033865 scopus 로고    scopus 로고
    • Vascular factors and mitochondrial dysfunction: A central role in the pathogenesis of Alzheimer's disease
    • Orsucci D, Mancuso M, Ienco EC, Simoncini C, Siciliano G, et al. (2013) Vascular factors and mitochondrial dysfunction: a central role in the pathogenesis of Alzheimer's disease. Curr Neurovasc Res. 10: 76-80.
    • (2013) Curr Neurovasc Res , vol.10 , pp. 76-80
    • Orsucci, D.1    Mancuso, M.2    Ienco, E.C.3    Simoncini, C.4    Siciliano, G.5
  • 62
    • 69349088255 scopus 로고    scopus 로고
    • Riboflavin kinase couples TNF receptor 1 to NADPH oxidase
    • Yazdanpanah B, Wiegmann K, Tchikov V, Krut O, Pongratz C, et al. (2009) Riboflavin kinase couples TNF receptor 1 to NADPH oxidase. Nature 460: 1159-1163.
    • (2009) Nature , vol.460 , pp. 1159-1163
    • Yazdanpanah, B.1    Wiegmann, K.2    Tchikov, V.3    Krut, O.4    Pongratz, C.5
  • 63
    • 72849147328 scopus 로고    scopus 로고
    • The combinations of TNFalpha-308 and IL-6-174 or IL-10-1082 genes polymorphisms suggest an association with susceptibility to sporadic late-onset Alzheimer's disease
    • Vural P, Degirmencioglu S, Parildar-Karpuzoglu, Dogru-Abbasoglu S, Hanagasi HA, et al. (2009) The combinations of TNFalpha-308 and IL-6-174 or IL-10-1082 genes polymorphisms suggest an association with susceptibility to sporadic late-onset Alzheimer's disease. Acta Neurol Scand 120: 396-401.
    • (2009) Acta Neurol Scand , vol.120 , pp. 396-401
    • Vural, P.1    Degirmencioglu, S.2    Parildar-Karpuzoglu3    Dogru-Abbasoglu, S.4    Hanagasi, H.A.5
  • 65
    • 79952180064 scopus 로고    scopus 로고
    • Lipid rafts: Linking Alzheimer's amyloid-b production, aggregation, and toxicity at neuronal membranes
    • doi:10.4061/2011/603052
    • Rushworth JV, Hooper NM (2011) Lipid rafts: linking Alzheimer's amyloid-b production, aggregation, and toxicity at neuronal membranes. Int J Alz Dis doi:10.4061/2011/603052
    • (2011) Int J Alz Dis
    • Rushworth, J.V.1    Hooper, N.M.2
  • 66
    • 84858061475 scopus 로고    scopus 로고
    • Neurodegeneration induced by clustering of sialylated glycosylphosphatidylinositols of prion proteins
    • Bate C, Williams A (2012) Neurodegeneration induced by clustering of sialylated glycosylphosphatidylinositols of prion proteins. J Biol Chem 287: 7935-7944.
    • (2012) J Biol Chem , vol.287 , pp. 7935-7944
    • Bate, C.1    Williams, A.2
  • 69
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: A functional node in cell biology
    • Bernstein BW, Bamburg JR (2010) ADF/cofilin: a functional node in cell biology. Trends Cell Biol 20: 187-195.
    • (2010) Trends Cell Biol , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 70
    • 70349651926 scopus 로고    scopus 로고
    • Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin
    • Klamt F, Zdanov S, Levine RL, Pariser A, Zhang Y, et al. (2009) Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin. Nat Cell Biol 11: 1241-1246.
    • (2009) Nat Cell Biol , vol.11 , pp. 1241-1246
    • Klamt, F.1    Zdanov, S.2    Levine, R.L.3    Pariser, A.4    Zhang, Y.5
  • 71
    • 84865175287 scopus 로고    scopus 로고
    • Pivotal role of the RanBP9-cofilin pathway in Aβ-induced apoptosis and neurodegeneration
    • Woo JA, Jung AR, Lakshmana MK, Bedrossian A, Lim Y, et al. (2012) Pivotal role of the RanBP9-cofilin pathway in Aβ-induced apoptosis and neurodegeneration. Cell Death Differ 19: 1413-1423.
    • (2012) Cell Death Differ , vol.19 , pp. 1413-1423
    • Woo, J.A.1    Jung, A.R.2    Lakshmana, M.K.3    Bedrossian, A.4    Lim, Y.5
  • 72
    • 84880759156 scopus 로고    scopus 로고
    • Neurotoxicity of amyloid β-protein: Synaptic and network dysfunction
    • doi: 10.110/cshperspect.a006338
    • Mucke L, Selkoe DJ (2012) Neurotoxicity of amyloid β-protein: synaptic and network dysfunction. Cold Spring Harbor Perspect Med 2012 doi: 10.110/cshperspect.a006338
    • (2012) Cold Spring Harbor Perspect Med , vol.2012
    • Mucke, L.1    Selkoe, D.J.2
  • 73
    • 55549091059 scopus 로고    scopus 로고
    • Chronophin serves as an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation
    • Huang TY, Minamide LS, Bamburg JR, Bokoch GM (2008) Chronophin serves as an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation. Develop Cell 15: 691-703.
    • (2008) Develop Cell , vol.15 , pp. 691-703
    • Huang, T.Y.1    Minamide, L.S.2    Bamburg, J.R.3    Bokoch, G.M.4
  • 74
    • 84881587735 scopus 로고    scopus 로고
    • Oxidative stress response elicted by mitochondrial dysfunction: Implication in the pathophysiology of aging
    • Maywood
    • Wang CH, Wu SB, Wu YT, Wei YH (2013) Oxidative stress response elicted by mitochondrial dysfunction: implication in the pathophysiology of aging. Exp Biol Med (Maywood) 238: 450-460.
    • (2013) Exp Biol Med , vol.238 , pp. 450-460
    • Wang, C.H.1    Wu, S.B.2    Wu, Y.T.3    Wei, Y.H.4
  • 75
    • 0036794093 scopus 로고    scopus 로고
    • 14-3-3 Regulates actin dynamics by stabilizing phosphorylated cofilin
    • DOI 10.1016/S0960-9822(02)01184-3, PII S0960982202011843
    • Gohla A, Bokoch GM (2002) 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. Curr Biol 12: 1704-1710. (Pubitemid 35161927)
    • (2002) Current Biology , vol.12 , Issue.19 , pp. 1704-1710
    • Gohla, A.1    Bokoch, G.M.2
  • 77
    • 66349108700 scopus 로고    scopus 로고
    • Reactive oxygen species regulate a slingshot-cofilin activation pathway
    • Kim JS, Huang TY, Bokoch GM (2009) Reactive oxygen species regulate a slingshot-cofilin activation pathway. Mol Biol Cell 20: 2650-2660.
    • (2009) Mol Biol Cell , vol.20 , pp. 2650-2660
    • Kim, J.S.1    Huang, T.Y.2    Bokoch, G.M.3
  • 80
    • 3242661985 scopus 로고    scopus 로고
    • GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice
    • DOI 10.1016/j.nbd.2004.05.005, PII S096999610400110X
    • Barmada S, Piccardo P,Yamaguchi K, Ghetti B, Harris DA (2004) GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice. Neurobiol Dis 16: 527-537. (Pubitemid 38942985)
    • (2004) Neurobiology of Disease , vol.16 , Issue.3 , pp. 527-537
    • Barmada, S.1    Piccardo, P.2    Yamaguchi, K.3    Ghetti, B.4    Harris, D.A.5
  • 81
    • 0034711176 scopus 로고    scopus 로고
    • Iatrogenic Creutzfeldt-Jakob disease at the millenium
    • Brown P, Preece M, Brandel JP, Sato T, McShane L, et al. (2000) Iatrogenic Creutzfeldt-Jakob disease at the millenium. Neurology 55: 1075-1081.
    • (2000) Neurology , vol.55 , pp. 1075-1081
    • Brown, P.1    Preece, M.2    Brandel, J.P.3    Sato, T.4    McShane, L.5
  • 82
    • 1642416427 scopus 로고    scopus 로고
    • Neuropathology and Molecular Biology of Variant Creutzfeldt-Jakob Disease
    • Ironside JW, Head MW (2004) Neuropathology and molecular biology of variant Creutzfeldt-Jakob disease. Curr Top Microbiol Immunol 284: 133-159. (Pubitemid 38391551)
    • (2004) Current Topics in Microbiology and Immunology , vol.284 , pp. 133-159
    • Ironside, J.W.1    Head, M.W.2
  • 83
    • 84875415784 scopus 로고    scopus 로고
    • The association between the methionine/valine (M/V) polymorphism (rs1799990) in the PRNP gene and the risk of Alzheimer disease: An update by meta-analysis
    • He J, Li X, Yang J, Huang J, Fu X, et al. (2013) The association between the methionine/valine (M/V) polymorphism (rs1799990) in the PRNP gene and the risk of Alzheimer disease: An update by meta-analysis. J Neurol Sci 326: 89-95.
    • (2013) J Neurol Sci , vol.326 , pp. 89-95
    • He, J.1    Li, X.2    Yang, J.3    Huang, J.4    Fu, X.5
  • 86
    • 84872498729 scopus 로고    scopus 로고
    • Role of cholesterol in APP metabolism and its significance in Alzheimer's disease pathogenesis
    • Maulik M, Westaway D, Jhamandas JH, Kar S (2013) Role of cholesterol in APP metabolism and its significance in Alzheimer's disease pathogenesis. Mol Neurobiol 47: 37-63.
    • (2013) Mol Neurobiol , vol.47 , pp. 37-63
    • Maulik, M.1    Westaway, D.2    Jhamandas, J.H.3    Kar, S.4
  • 87
    • 84867210725 scopus 로고    scopus 로고
    • L-threo-C6-pyridoniumceramide bromide, a novel cationic ceramide, induces NADPH oxidase activation, mitochondrial dysfunction and loss in cell viability in INS 832/13 β-cells
    • Syed I, Szulc ZM, Ogretmen B, Kowluru A (2012) L-threo-C6- pyridoniumceramide bromide, a novel cationic ceramide, induces NADPH oxidase activation, mitochondrial dysfunction and loss in cell viability in INS 832/13 β-cells. Cell Physiol Biochem 30: 1051-1058.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 1051-1058
    • Syed, I.1    Szulc, Z.M.2    Ogretmen, B.3    Kowluru, A.4
  • 88
    • 84885440280 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2α upregulation mediates apoptotic neuronal death induced by aggregated amyloid-β peptide 1-42
    • Sagy-Bross C, Hadad N, Levy R (2013) Cytosolic phospholipase A2α upregulation mediates apoptotic neuronal death induced by aggregated amyloid-β peptide 1-42. Neurochem Int 63: 541-550.
    • (2013) Neurochem Int , vol.63 , pp. 541-550
    • Sagy-Bross, C.1    Hadad, N.2    Levy, R.3
  • 89
    • 84888015942 scopus 로고    scopus 로고
    • Sporadic Alzheimer's disease begins as episodes of brain ischemia and ischemically dysregulated Alzheimer's disease genes
    • Pluta R, Jablonski M, Ulamek-Koziol M, Kocki J, Brzozowska J, et al. (2013) Sporadic Alzheimer's disease begins as episodes of brain ischemia and ischemically dysregulated Alzheimer's disease genes. Mol Neurobiol 48: 500-515.
    • (2013) Mol Neurobiol , vol.48 , pp. 500-515
    • Pluta, R.1    Jablonski, M.2    Ulamek-Koziol, M.3    Kocki, J.4    Brzozowska, J.5
  • 90
    • 0347249826 scopus 로고    scopus 로고
    • Production and use of replication-deficient adenoviruses for transgene expression in neurons
    • Minamide LS, Shaw AE, Sarmiere PD, Wiggan O, Maloney MT, et al. (2003) Production and use of replication-deficient adenoviruses for transgene expression in neurons. Methods Cell Biol 71: 387-416.
    • (2003) Methods Cell Biol , vol.71 , pp. 387-416
    • Minamide, L.S.1    Shaw, A.E.2    Sarmiere, P.D.3    Wiggan, O.4    Maloney, M.T.5
  • 93
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, et al. (2002) Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416: 535-539. (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 94
    • 4444267190 scopus 로고    scopus 로고
    • Cross-reactivity of antibodies to actin-depolymerizing factor/cofilin family proteins and identification of the major epitope recognized by a mammalian actin-depolymerizing factor/cofilin antibody
    • DOI 10.1002/elps.200406017
    • Shaw AE, Minamide LS, Bill C, Funk JD, Maiti S, et al. (2004) Cross-reactivity of antibodies to ADF/cofilin family proteins and identification of the major epitope recognized by a mammalian ADF/cofilin antibody. Electrophoresis 25: 2611-2620. (Pubitemid 39193672)
    • (2004) Electrophoresis , vol.25 , Issue.15 , pp. 2611-2620
    • Shaw, A.E.1    Minamide, L.S.2    Bill, C.L.3    Funk, J.D.4    Maiti, S.5    Bamburg, J.R.6
  • 95
    • 0024468554 scopus 로고
    • A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle
    • Abe H, Oshima S, Obinata T (1989) A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle. J Biochem (Tokyo) 106: 696-702. (Pubitemid 19241841)
    • (1989) Journal of Biochemistry , vol.106 , Issue.4 , pp. 696-702
    • Abe, H.1    Ohshima, S.2    Obinata, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.