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Volumn 67, Issue , 2014, Pages 387-395

Antisense oligonucleotide against GSK-3β in brain of SAMP8 mice improves learning and memory and decreases oxidative stress: Involvement of transcription factor Nrf2 and implications for Alzheimer disease

Author keywords

Alzheimer's disease (AD); Antisense; Glycogen synthase kinase 3 (GSK 3 ); Nuclear factor E2 related factor 2 (Nrf2); Oxidative stress; SAMP8 mice

Indexed keywords

ANTISENSE OLIGONUCLEOTIDE; BETA ACTIN; GLUTATHIONE TRANSFERASE; GLYCOGEN SYNTHASE KINASE 3BETA; HISTONE H2B; TAU PROTEIN; TRANSCRIPTION FACTOR NRF2; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 BETA; NFE2L2 PROTEIN, MOUSE; REACTIVE OXYGEN METABOLITE;

EID: 84891589937     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.11.014     Document Type: Article
Times cited : (120)

References (57)
  • 1
    • 84875354777 scopus 로고    scopus 로고
    • 2013 Alzheimer's disease facts and figures
    • Association A.S.
    • A.S. Association 2013 Alzheimer's disease facts and figures Alzheimer's Dement 9 2013 208 245
    • (2013) Alzheimer's Dement , vol.9 , pp. 208-245
  • 2
    • 77953068390 scopus 로고    scopus 로고
    • Synergistic Interactions between Abeta, tau, and alpha-synuclen: Acceleration of neuropathology and cognitive decline
    • L.K. Clinton, M. Blurton-Jones, K. Myczek, J.Q. Trojanowski, and F.M. LaFerla Synergistic Interactions between Abeta, tau, and alpha-synuclen: acceleration of neuropathology and cognitive decline J. Neurosci. 30 2010 7281 7289
    • (2010) J. Neurosci. , vol.30 , pp. 7281-7289
    • Clinton, L.K.1    Blurton-Jones, M.2    Myczek, K.3    Trojanowski, J.Q.4    Laferla, F.M.5
  • 3
    • 84863697825 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3: A point of integration in Alzheimer's disease and a therapeutic target
    • S. Mondragon-Rodriguez, G. Perry, X. Zhu, P.I. Moreira, and S. Williams Glycogen synthase kinase 3: a point of integration in Alzheimer's disease and a therapeutic target Int. J. Alzheimer's Dis. 2012 2012 1 4
    • (2012) Int. J. Alzheimer's Dis. , vol.2012 , pp. 1-4
    • Mondragon-Rodriguez, S.1    Perry, G.2    Zhu, X.3    Moreira, P.I.4    Williams, S.5
  • 4
    • 0035909112 scopus 로고    scopus 로고
    • Judging a protein by more than its name: GSK-3
    • J.R. Woodgett Judging a protein by more than its name: GSK-3 Sci STKE 2001 2001 re12
    • (2001) Sci STKE , vol.2001 , pp. 12
    • Woodgett, J.R.1
  • 5
    • 0346457015 scopus 로고    scopus 로고
    • Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3β (GSK3β) plays a critical role in regulating tau's ability to bind and stabilize microtubules
    • J.H. Cho, and G.V. Johnson Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules J. Neurochem. 88 2004 349 358 (Pubitemid 38084551)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.2 , pp. 349-358
    • Cho, J.-H.1    Johnson, G.V.W.2
  • 6
    • 33845530335 scopus 로고    scopus 로고
    • Chronic lithium administration to FTDP-17 tau and GSK-3β overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert
    • DOI 10.1111/j.1471-4159.2006.04139.x
    • T. Engel, P. Goni-Oliver, J.J. Lucas, J. Avila, and F. Hernandez Chronic lithium administration to FTDP-17 tau and GSK-3beta overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert J. Neurochem. 99 2006 1445 1455 (Pubitemid 44924224)
    • (2006) Journal of Neurochemistry , vol.99 , Issue.6 , pp. 1445-1455
    • Engel, T.1    Goni-Oliver, P.2    Lucas, J.J.3    Avila, J.4    Hernandez, F.5
  • 7
    • 39849110726 scopus 로고    scopus 로고
    • The GSK3 hypothesis of Alzheimer's disease
    • DOI 10.1111/j.1471-4159.2007.05194.x
    • C. Hooper, R. Killick, and S. Lovestone The GSK3 hypothesis of Alzheimer's disease J. Neurochem. 104 2008 1433 1439 (Pubitemid 351316776)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.6 , pp. 1433-1439
    • Hooper, C.1    Killick, R.2    Lovestone, S.3
  • 9
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear β-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3β conditional transgenic mice
    • DOI 10.1093/emboj/20.1.27
    • J.J. Lucas, F. Hernandez, P. Gomez-Ramos, M.A. Moran, R. Hen, and J. Avila Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice EMBO J. 20 2001 27 39 (Pubitemid 32099099)
    • (2001) EMBO Journal , vol.20 , Issue.1-2 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 12
    • 0344517353 scopus 로고    scopus 로고
    • Lithium protects cultured neurons against β-amyloid-induced neurodegeneration
    • DOI 10.1016/S0014-5793(99)00685-7, PII S0014579399006857
    • G. Alvarez, J.R. Munoz-Montano, J. Satrustegui, J. Avila, E. Bogonez, and J. Diaz-Nido Lithium protects cultured neurons against beta-amyloid-induced neurodegeneration FEBS Lett. 453 1999 260 264 (Pubitemid 29326659)
    • (1999) FEBS Letters , vol.453 , Issue.3 , pp. 260-264
    • Alvarez, G.1    Munoz-Montano, J.R.2    Satrustegui, J.3    Avila, J.4    Bogonez, E.5    Diaz-Nido, J.6
  • 13
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/factor A
    • J.R. Woodgett Molecular cloning and expression of glycogen synthase kinase-3/factor A EMBO J. 9 1990 2431 2438
    • (1990) EMBO J. , vol.9 , pp. 2431-2438
    • Woodgett, J.R.1
  • 17
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • DOI 10.1038/nature01640
    • C.J. Phiel, C.A. Wilson, V.M. Lee, and P.S. Klein GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides Nature 423 2003 435 439 (Pubitemid 36626994)
    • (2003) Nature , vol.423 , Issue.6938 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.-Y.3    Klein, P.S.4
  • 18
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3alpha regulates production of Alzheimer's disease amyloi-beta peptides
    • C.J. Phiel, C.A. Wilson, V.M. Lee, and P.S. Klein GSK-3alpha regulates production of Alzheimer's disease amyloi-beta peptides Nature 423 2003 435
    • (2003) Nature , vol.423 , pp. 435
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.3    Klein, P.S.4
  • 19
    • 33747425620 scopus 로고    scopus 로고
    • GSK-3 is essential in the pathogenesis of Alzheimer's disease
    • A. Takashima GSK-3 is essential in the pathogenesis of Alzheimer's disease J. Alzheimers Dis. 9 2006 309 317 (Pubitemid 44253325)
    • (2006) Journal of Alzheimer's Disease , vol.9 , Issue.SUPPL. 3 , pp. 309-317
    • Takashima, A.1
  • 21
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase
    • D.P. Hanger, K. Hughes, J.R. Woodgett, J.P. Brion, and B.H. Anderton Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase Neurosci. Lett. 147 1992 58 62
    • (1992) Neurosci. Lett. , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 23
    • 0030868557 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3
    • DOI 10.1074/jbc.272.40.25326
    • M. Hong, D.C. Chen, P.S. Klein, and V.M. Lee Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3 J. Biol. Chem. 272 1997 25326 25332 (Pubitemid 27415724)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.40 , pp. 25326-25332
    • Hong, M.1    Chen, D.C.R.2    Klein, P.S.3    Lee, V.M.-Y.4
  • 24
    • 0037996661 scopus 로고    scopus 로고
    • Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress
    • A.Y. Shih, D.A. Johnson, G. Wong, A.D. Kraft, L. Jiang, H. Erb, J.A. Johnson, and T.H. Murphy Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress J. Neurosci. 23 2003 3394 3406 (Pubitemid 36531981)
    • (2003) Journal of Neuroscience , vol.23 , Issue.8 , pp. 3394-3406
    • Shih, A.Y.1    Johnson, D.A.2    Wong, G.3    Kraft, A.D.4    Jiang, L.5    Erb, H.6    Johnson, J.A.7    Murphy, T.H.8
  • 25
    • 0842304134 scopus 로고    scopus 로고
    • Nuclear Factor E2-Related Factor 2-Dependent Antioxidant Response Element Activation by tert-Butylhydroquinone and Sulforaphane Occurring Preferentially in Astrocytes Conditions Neurons against Oxidative Insult
    • DOI 10.1523/JNEUROSCI.3817-03.2004
    • A.D. Kraft, D.A. Johnson, and J.A. Johnson Nuclear factor E2-related factor 2-dependent antioxidant response element activation by tert-butylhydroquinone and sulforaphane occurring preferentially in astrocytes conditions neurons against oxidative insult J. Neurosci 24 2004 1101 1112 (Pubitemid 38177017)
    • (2004) Journal of Neuroscience , vol.24 , Issue.5 , pp. 1101-1112
    • Kraft, A.D.1    Johnson, D.A.2    Johnson, J.A.3
  • 27
    • 84862808451 scopus 로고    scopus 로고
    • Activation of the Nrf2-ARE pathway by siRNA knockdown of Keap1 reduces oxidative stress and provides partial protection from MPTP-mediated neurotoxicity
    • T.P. Williamson, D.A. Johnson, and J.A. Johnson Activation of the Nrf2-ARE pathway by siRNA knockdown of Keap1 reduces oxidative stress and provides partial protection from MPTP-mediated neurotoxicity Neurotoxicology 33 2012 272 279
    • (2012) Neurotoxicology , vol.33 , pp. 272-279
    • Williamson, T.P.1    Johnson, D.A.2    Johnson, J.A.3
  • 28
    • 33747606306 scopus 로고    scopus 로고
    • Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling
    • DOI 10.1038/sj.emboj.7601243, PII 7601243
    • S.C. Lo, X. Li, M.T. Henzl, L.J. Beamer, and M. Hannink Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling EMBO J. 25 2006 3605 3617 (Pubitemid 44264871)
    • (2006) EMBO Journal , vol.25 , Issue.15 , pp. 3605-3617
    • Lo, S.-C.1    Li, X.2    Henzl, M.T.3    Beamer, L.J.4    Hannink, M.5
  • 29
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • K. Itoh, N. Wakabayashi, Y. Katoh, T. Ishii, K. Igarashi, J.D. Engel, and M. Yamamoto Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain Genes Dev. 13 1999 76 86 (Pubitemid 29045117)
    • (1999) Genes and Development , vol.13 , Issue.1 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 30
    • 0032827002 scopus 로고    scopus 로고
    • Regulatory mechanisms of cellular response to oxidative stress
    • DOI 10.1080/10715769900300881
    • K. Itoh, T. Ishii, N. Wakabayashi, and M. Yamamoto Regulatory mechanisms of cellular response to oxidative stress Free Radic. Res. 31 1999 319 324 (Pubitemid 29452857)
    • (1999) Free Radical Research , vol.31 , Issue.4 , pp. 319-324
    • Itoh, K.1    Ishii, T.2    Wakabayashi, N.3    Yamamoto, M.4
  • 32
    • 0242580049 scopus 로고    scopus 로고
    • Distinct Cysteine Residues in Keap1 Are Required for Keap1-Dependent Ubiquitination of Nrf2 and for Stabilization of Nrf2 by Chemopreventive Agents and Oxidative Stress
    • DOI 10.1128/MCB.23.22.8137-8151.2003
    • D.D. Zhang, and M. Hannink Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress Mol. Cell. Biol. 23 2003 8137 8151 (Pubitemid 37377505)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.22 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 33
    • 0024211998 scopus 로고
    • Age-related deterioration of ability of acquisition in memory and learning in senescence accelerated mouse: SAM-P/8 as an animal model of disturbances in recent memory
    • DOI 10.1016/0006-8993(88)90671-3
    • H. Yagi, S. Katoh, I. Akiguchi, and T. Takeda Afe-related deterioration of ability of acquisition in memory and learning in senescence accelerated mouse: SAM-P/8 as an animal model of disturbances in recent memory Neurosci. Biobehav. Rev. 474 1988 86 93 (Pubitemid 19001185)
    • (1988) Brain Research , vol.474 , Issue.1 , pp. 86-93
    • Yagi, H.1    Katoh, S.2    Akiguchi, I.3    Takeda, T.4
  • 34
    • 0344653645 scopus 로고    scopus 로고
    • Learning and memory in the SAMP8 mouse
    • DOI 10.1016/S0149-7634(96)00063-2, PII S0149763496000632
    • J.F. Flood, and J.E. Morley Learning and memory in the SAMP8 mouse Neurosci. Biobehav. Rev. 22 1998 1 20 (Pubitemid 28082281)
    • (1998) Neuroscience and Biobehavioral Reviews , vol.22 , Issue.1 , pp. 1-20
    • Flood, J.F.1    Morley, J.E.2
  • 35
    • 0034531444 scopus 로고    scopus 로고
    • β-Amyloid precursor polypeptide in SAMP8 mice affects learning and memory
    • DOI 10.1016/S0196-9781(00)00342-9, PII S0196978100003429
    • J.E. Morley, V.B. Kumar, A.I. Bernardo, S.A. Farr, K. Uezu, N. Tumosa, and J.F. Flood Beta-amyloid precursor polypeptide in SAMP8 mice affects learning and memory Peptides 21 2000 1761 1767 (Pubitemid 32058850)
    • (2000) Peptides , vol.21 , Issue.12 , pp. 1761-1767
    • Morley, J.E.1    Kumar, V.B.2    Bernardo, A.E.3    Farr, S.A.4    Uezu, K.5    Tumosa, N.6    Flood, J.F.7
  • 36
    • 58149380018 scopus 로고    scopus 로고
    • From aging to Alzheimer's disease: Unveiling the switch with the senescence-accelerated mouse model (SAMP8)
    • M. Pallas, A. Camins, M.A. Smith, G. Perry, H.G. Lee, and G. Casadesus From aging to Alzheimer's disease: unveiling the switch with the senescence-accelerated mouse model (SAMP8) J. Alzheimers Dis. 15 2008 615 624
    • (2008) J. Alzheimers Dis. , vol.15 , pp. 615-624
    • Pallas, M.1    Camins, A.2    Smith, M.A.3    Perry, G.4    Lee, H.G.5    Casadesus, G.6
  • 38
    • 2942659505 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of specific protein expression and oxidative modification in aged senescence-accelerated-prone 8 mice brain
    • DOI 10.1016/j.neuroscience.2004.04.046, PII S0306452204003355
    • H.F. Poon, A. Castegna, S.A. Farr, V. Thongboonkerd, B.C. Lynn, W.A. Banks, J.E. Morley, J.B. Klein, and D.A. Butterfield Quantitative proteomics analysis of specific protein expression and oxidative modification in aged senescence-accelerated-prone 8 mice brain Neuroscience 126 2004 915 926 (Pubitemid 38780896)
    • (2004) Neuroscience , vol.126 , Issue.4 , pp. 915-926
    • Poon, H.F.1    Castegna, A.2    Farr, S.A.3    Thongboonkerd, V.4    Lynn, B.C.5    Banks, W.A.6    Morley, J.E.7    Klein, J.B.8    Butterfield, D.A.9
  • 39
    • 84858020530 scopus 로고    scopus 로고
    • Peripheral admininstration of antisense oligonucleotides targeting the amyloid-B protein precursor reverses ABPP and LRP-1 overexpression in the aged SAMP8 mouse brain
    • M.A. Erickson, M.L. Niehoff, S.A. Farr, J.E. Morley, L.A. Dillman, K.M. Lynch, and W.A. Banks Peripheral admininstration of antisense oligonucleotides targeting the amyloid-B protein precursor reverses ABPP and LRP-1 overexpression in the aged SAMP8 mouse brain J. Alzheimers Dis. 28 2012 951 960
    • (2012) J. Alzheimers Dis. , vol.28 , pp. 951-960
    • Erickson, M.A.1    Niehoff, M.L.2    Farr, S.A.3    Morley, J.E.4    Dillman, L.A.5    Lynch, K.M.6    Banks, W.A.7
  • 41
    • 2942555108 scopus 로고    scopus 로고
    • On the delay-dependent involvement of the hippocampus in object recognition memory
    • DOI 10.1016/j.nlm.2004.03.005, PII S1074742704000449
    • R.S. Hammond, L.E. Tull., and R.W. Stackman On the delay-dependent involvement of the hippocampus in object recognition memory Neurobiol. Learn. Mem. 82 2004 26 34 (Pubitemid 38737427)
    • (2004) Neurobiology of Learning and Memory , vol.82 , Issue.1 , pp. 26-34
    • Hammond, R.S.1    Tull, L.E.2    Stackman, R.W.3
  • 42
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • DOI 10.1016/0003-2697(85)90442-7
    • P.K. Smith, R.I. Krohn, G.T. Hermanson, A.K. Mallia, F.H. Gartner, M.D. Provenzano, E.K. Fujimoto, N.M. Goeke, B.J. Olson, and D.C. Klenk Measurement of protein using bicichoninic acid Anal. Biochem. 150 1985 76 85 (Pubitemid 16258399)
    • (1985) Analytical Biochemistry , vol.150 , Issue.1 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 43
    • 84884901013 scopus 로고    scopus 로고
    • Lipid peroxidation triggers neurodegeneration: A redox prloteomics view into the Alzheimer disease brain
    • R. Sultana, M. Perluigi, and D.A. Butterfield Lipid peroxidation triggers neurodegeneration: a redox prloteomics view into the Alzheimer disease brain Free Radic. Biol. Med. 2012
    • (2012) Free Radic. Biol. Med.
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 44
    • 33645384663 scopus 로고    scopus 로고
    • Preproenkephalin targeted antisenses cross the blood-brain barrier to reduce brain methionine enkephalin levels and increase voluntary ethanol drinking
    • W.A. Banks, L.B. Jaeger, A. Urayama, V.B. Kumar, S.M. Hileman, F.S. Gaskin, N.V. Llanza, S.A. Farr, and J.E. Morley Preproenkephalin targeted antisenses cross the blood-brain barrier to reduce brain methionine enkephalin levels and increase voluntary ethanol drinking Peptides 27 2006 784 796
    • (2006) Peptides , vol.27 , pp. 784-796
    • Banks, W.A.1    Jaeger, L.B.2    Urayama, A.3    Kumar, V.B.4    Hileman, S.M.5    Gaskin, F.S.6    Llanza, N.V.7    Farr, S.A.8    Morley, J.E.9
  • 46
    • 0029737421 scopus 로고    scopus 로고
    • Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3β and cyclin-dependent kinase 5, a component of TPK II
    • DOI 10.1007/s004010050513
    • H. Yamaguchi, K. Ishiguro, T. Uchida, A. Takashima, C.A. Lemere, and K. Imahori Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 beta and cyclin-dependent kinase 5, a component of TPK II Acta Neuropathol. 92 1996 232 241 (Pubitemid 26278953)
    • (1996) Acta Neuropathologica , vol.92 , Issue.3 , pp. 232-241
    • Yamaguchi, H.1    Ishiguro, K.2    Uchida, T.3    Takashima, A.4    Lemere, C.A.5    Imahori, K.6
  • 48
    • 33846129434 scopus 로고    scopus 로고
    • Increased level of active GSK-3β in Alzheimer's disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration
    • DOI 10.1111/j.1365-2990.2006.00795.x
    • K. Leroy, Z. Yilmaz, and J.P. Brion Increased level of active GSK-3beta in Alzheimer's disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration Neuropathol. Appl. Neurobiol. 33 2007 43 55 (Pubitemid 46090309)
    • (2007) Neuropathology and Applied Neurobiology , vol.33 , Issue.1 , pp. 43-55
    • Leroy, K.1    Yilmaz, Z.2    Brion, J.-P.3
  • 49
    • 33947597084 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 (GSK3): Inflammation, diseases, and therapeutics
    • DOI 10.1007/s11064-006-9128-5
    • R.S. Jope, C.J. Yukaitis, and E. Beurel Glycogen synthase kinase-3 (GSK3): Inflammation, diseases, and therapeutics Neurochem. Res. 32 2007 577 595 (Pubitemid 46481289)
    • (2007) Neurochemical Research , vol.32 , Issue.4-5 , pp. 577-595
    • Jope, R.S.1    Yuskaitis, C.J.2    Beurel, E.3
  • 50
    • 0033584867 scopus 로고    scopus 로고
    • Regulation of γ-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2
    • A.C. Wild, H.R. Moinova, and R.T. Mulcahy Regulation of gamma-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2 J. Biol. Chem. 274 1999 33627 33636 (Pubitemid 129511675)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.47 , pp. 33627-33636
    • Wild, A.C.1    Moinova, H.R.2    Mulcahy, R.T.3
  • 52
    • 79955453676 scopus 로고    scopus 로고
    • Making sense of therapeutics using antisense technology
    • R. Malik, and I. Roy Making sense of therapeutics using antisense technology Expert Opin. Drug Discov. 6 2011 507 526
    • (2011) Expert Opin. Drug Discov. , vol.6 , pp. 507-526
    • Malik, R.1    Roy, I.2
  • 53
    • 44649097840 scopus 로고    scopus 로고
    • AEG-35156, an antisense oligonucleotide against X-linked inhibitor of apoptosis for the potential treatment of cancer
    • I. Tamm AEG-35156, an antisense oligonucleotide against X-linked inhibitor of apoptosis for potential tretment of cancer Curr. Opin. Investig. Drugs 9 2008 638 646 (Pubitemid 351777167)
    • (2008) Current Opinion in Investigational Drugs , vol.9 , Issue.6 , pp. 638-646
    • Tamm, I.1
  • 55
    • 3242715959 scopus 로고    scopus 로고
    • Antisense directed at the Aβ region of APP decreases brain oxidative markers in aged senescence accelerated mice
    • DOI 10.1016/j.brainres.2004.05.048, PII S0006899304008157
    • H.F. Poon, G. Joshi, R. Sultana, S.A. Farr, W.A. Banks, J.E. Morley, V. Calabrese, and D.A. Butterfield Antisense directed at the Abeta region of the APP decreases brain oxidative maarkers in aged senescence accelerated mice Brain Res. 1018 2004 86 96 (Pubitemid 38942865)
    • (2004) Brain Research , vol.1018 , Issue.1 , pp. 86-96
    • Poon, H.F.1    Joshi, G.2    Sultana, R.3    Farr, S.A.4    Banks, W.A.5    Morley, J.E.6    Calabrese, V.7    Butterfield, D.A.8
  • 56
    • 0035015218 scopus 로고    scopus 로고
    • Delivery across the blood-brain barrier of antisense directed against amyloid β: Reversal of learning and memory deficits in mice overexpressing amyloid precursor protein
    • W.A. Banks, S.A. Farr, W. Butt, V.B. Kumar, M.W. Franko, and J.E. Morley Delivery across the blood-brain barrier of antisense directed against amyloid beta: reversal of learning and memory deficits in mice overexpressing amyloid precursor protein J. Pharmacol. Exp. Ther. 297 2001 1113 1121 (Pubitemid 32472511)
    • (2001) Journal of Pharmacology and Experimental Therapeutics , vol.297 , Issue.3 , pp. 1113-1121
    • Banks, W.A.1    Farr, S.A.2    Butt, W.3    Kumar, V.B.4    Franko, M.W.5    Morley, J.E.6
  • 57
    • 0034867485 scopus 로고    scopus 로고
    • Site-directed antisense oligonucleotide decreases the expression of amyloid precursor protein and reverses deficits in learning and memory in aged SAMP8 mice
    • DOI 10.1016/S0196-9781(00)00339-9, PII S0196978100003399
    • V.B. Kumar, S.A. Farr, J.F. Flood, V. Kamlesh, M. Franko, W.A. Banks, and J.E. Morley Site-directed antisense oligonucleotide decreases the expression of amyloid precursor protein and reverses deficits in learning and memory in aged SAMP8 mice Peptides 21 2000 1769 1775 (Pubitemid 32058851)
    • (2000) Peptides , vol.21 , Issue.12 , pp. 1769-1775
    • Kumar, V.B.1    Farr, S.A.2    Flood, J.F.3    Kamlesh, V.4    Franko, M.5    Banks, W.A.6    Morley, J.E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.