메뉴 건너뛰기




Volumn 48, Issue 1, 2012, Pages 97-110

DENN/MADD/IG20 alternative splicing changes and cell death in alzheimer's disease

Author keywords

Alternative splicing; DENN MADD IG20; Oligomeric A

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; COMPLEMENTARY DNA; ISOPROTEIN; ISOPROTEIN DM SV; ISOPROTEIN IG20; MESSENGER RNA; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84865119349     PISSN: 08958696     EISSN: 15591166     Source Type: Journal    
DOI: 10.1007/s12031-012-9782-9     Document Type: Article
Times cited : (4)

References (50)
  • 1
    • 0035861631 scopus 로고    scopus 로고
    • Contrasting effects of IG20 and its splice isoforms, MADD and DENN-SV, on tumor necrosis factor alpha-induced apoptosis and activation of caspase-8 and -3
    • 11577081 10.1074/jbc.M104835200 1:CAS:528:DC%2BD3MXpt1Gnur4%3D
    • Al-Zoubi AM, Efimova EV, Kaithamana S, Martinez O, El-Idrissi Mel A, Dogan RE, Prabhakar BS (2001) Contrasting effects of IG20 and its splice isoforms, MADD and DENN-SV, on tumor necrosis factor alpha-induced apoptosis and activation of caspase-8 and -3. J Biol Chem 276:47202-47211
    • (2001) J Biol Chem , vol.276 , pp. 47202-47211
    • Al-Zoubi, A.M.1    Efimova, E.V.2    Kaithamana, S.3    Martinez, O.4    El-Idrissi Mel, A.5    Dogan, R.E.6    Prabhakar, B.S.7
  • 2
    • 33745899048 scopus 로고    scopus 로고
    • Alternative Splicing: New Insights from Global Analyses
    • DOI 10.1016/j.cell.2006.06.023, PII S0092867406008178
    • Blencowe BJ (2006) Alternative splicing: new insights from global analyses. Cell 126:37-47 (Pubitemid 44040990)
    • (2006) Cell , vol.126 , Issue.1 , pp. 37-47
    • Blencowe, B.J.1
  • 3
    • 37549022563 scopus 로고    scopus 로고
    • Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology
    • 18056160 10.1093/brain/awm276
    • Berson A, Knobloch M, Hanan M, Diamant S, Sharoni M, Schuppli D, Geyer BC et al (2008) Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology. Brain 131:109-119
    • (2008) Brain , vol.131 , pp. 109-119
    • Berson, A.1    Knobloch, M.2    Hanan, M.3    Diamant, S.4    Sharoni, M.5    Schuppli, D.6    Geyer, B.C.7
  • 6
    • 34249672242 scopus 로고    scopus 로고
    • Aβ oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • DOI 10.1074/jbc.M607483200
    • De Felice FG, Velasco PT, Lambert MP, Viola K, Fernandez SJ, Ferreira ST, Klein WL (2007) Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 282:11590-11601 (Pubitemid 47100810)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 7
    • 1642570212 scopus 로고    scopus 로고
    • Down-regulation of DENN/MADD, a TNF receptor binding protein, correlates with neuronal cell death in Alzheimer's disease brain and hippocampal neurons
    • DOI 10.1073/pnas.0307349101
    • Del Villar K, Miller CA (2004) Down-regulation of DENN/MADD, a TNF receptor binding protein, correlates with neuronal cell death in Alzheimer's disease brain and hippocampal neurons. Proc Natl Acad Sci U S A 101:4210-4215 (Pubitemid 38405908)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.12 , pp. 4210-4215
    • Del Villar, K.1    Miller, C.A.2
  • 8
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • DOI 10.1074/jbc.M500997200
    • Demuro A, Mina E, Kayed R, Milton SC, Parker I, Glabe CG (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280:17294-17300 (Pubitemid 41389198)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 9
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons
    • DOI 10.1523/JNEUROSCI.1189-06.2006
    • Deshpande A, Mina E, Glabe C, Busciglio J (2006) Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons. J Neurosci 26:6011-6018 (Pubitemid 44318367)
    • (2006) Journal of Neuroscience , vol.26 , Issue.22 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 10
    • 1442327641 scopus 로고    scopus 로고
    • IG20, in contrast to DENN-SV, (MADD splice variants) suppresses tumor cell survival, and enhances their susceptibility to apoptosis and cancer drugs
    • DOI 10.1038/sj.onc.1207210
    • Efimova EV, Al-Zoubi AM, Martinez O, Kaithamana S, Lu S, Arima T, Prabhakar BS (2004) IG20, in contrast to DENN-SV, (MADD splice variants) suppresses tumor cell survival, and enhances their susceptibility to apoptosis and cancer drugs. Oncogene 23:1076-1087 (Pubitemid 38269961)
    • (2004) Oncogene , vol.23 , Issue.5 , pp. 1076-1087
    • Efimova, E.V.1    Al-Zoubi, A.M.2    Martinez, O.3    Kaithamana, S.4    Lu, S.5    Arima, T.6    Prabhakar, B.S.7
  • 11
    • 0033844835 scopus 로고    scopus 로고
    • Sequential treatment of SH-SY5Y cells with retinoic acid and brain-derived neurotrophic factor gives rise to fully differentiated, neurotrophic factor-dependent, human neuron-like cells
    • DOI 10.1046/j.1471-4159.2000.0750991.x
    • Encinas M, Iglesias M, Liu Y, Wang H, Muhaisen A, Cena V, Gallego C, Comella JX (2000) Sequential treatment of SH-SY5Y cells with retinoic acid and brain-derived neurotrophic factor gives rise to fully differentiated, neurotrophic factor-dependent, human neuron-like cells. J Neurochem 75:991-1003 (Pubitemid 30660487)
    • (2000) Journal of Neurochemistry , vol.75 , Issue.3 , pp. 991-1003
    • Encinas, M.1    Iglesias, M.2    Liu, Y.3    Wang, H.4    Muhaisen, A.5    Cena, V.6    Gallego, C.7    Comella, J.X.8
  • 13
    • 0034906754 scopus 로고    scopus 로고
    • Alternative RNA splicing in the nervous system
    • DOI 10.1016/S0301-0082(01)00007-7, PII S0301008201000077
    • Grabowski PJ, Black DL (2001) Alternative RNA splicing in the nervous system. Prog Neurobiol 65:289-308 (Pubitemid 32709987)
    • (2001) Progress in Neurobiology , vol.65 , Issue.3 , pp. 289-308
    • Grabowski, P.J.1    Black, D.L.2
  • 14
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8:101-112 (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 15
    • 2942623972 scopus 로고    scopus 로고
    • The retinoic acid and brain-derived neurotrophic factor differentiated SH-SY5Y cell line as a model for Alzheimer's disease-like tau phosphorylation
    • DOI 10.1016/j.bbrc.2004.05.075, PII S0006291X04010253
    • Jamsa A, Hasslund K, Cowburn RF, Backstrom A, Vasange M (2004) The retinoic acid and brain-derived neurotrophic factor differentiated SH-SY5Y cell line as a model for Alzheimer's disease-like tau phosphorylation. Biochem Biophys Res Commun 319:993-1000 (Pubitemid 38739418)
    • (2004) Biochemical and Biophysical Research Communications , vol.319 , Issue.3 , pp. 993-1000
    • Jamsa, A.1    Hasslund, K.2    Cowburn, R.F.3    Backstrom, A.4    Vasange, M.5
  • 16
    • 79955044494 scopus 로고    scopus 로고
    • Soluble amyloid β-protein dimers isolated from Alzheimer's cortex directly induce Tau hyperphosphorylation and neuritic degeneration
    • 21421841 10.1073/pnas.1017033108 1:CAS:528:DC%2BC3MXkvVCnu7o%3D
    • Jin M, Shepardson N, Yang T, Chen G, Walsh D, Selkoe DJ (2011) Soluble amyloid β-protein dimers isolated from Alzheimer's cortex directly induce Tau hyperphosphorylation and neuritic degeneration. Proc Natl Acad Sci USA 108(14):5819-5824
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.14 , pp. 5819-5824
    • Jin, M.1    Shepardson, N.2    Yang, T.3    Chen, G.4    Walsh, D.5    Selkoe, D.J.6
  • 17
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • DOI 10.1074/jbc.C400260200
    • Kayed R, Sokolov Y, Edmonds B, McIntire TM, Milton SC, Hall JE, Glabe CG (2004) Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 279:46363-46366 (Pubitemid 39518276)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 18
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small A β oligomers: The solution to an Alzheimer's disease conundrum?
    • DOI 10.1016/S0166-2236(00)01749-5, PII S0166223600017495
    • Klein WL, Krafft GA, Finch CE (2001) Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci 24:219-224 (Pubitemid 32204378)
    • (2001) Trends in Neurosciences , vol.24 , Issue.4 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 19
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease
    • DOI 10.1016/j.neurobiolaging.2004.02.010, PII S0197458004000892
    • Klein WL, Stine WB Jr, Teplow DB (2004) Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging 25:569-580 (Pubitemid 38686476)
    • (2004) Neurobiology of Aging , vol.25 , Issue.5 , pp. 569-580
    • Klein, W.L.1    Stine Jr., W.B.2    Teplow, D.B.3
  • 20
    • 27844495164 scopus 로고    scopus 로고
    • Molecular basis of programmed cell death involved in neurodegeneration
    • DOI 10.1016/j.tins.2005.09.011, PII S0166223605002596
    • Krantic S, Mechawar N, Reix S, Quirion R (2005) Molecular basis of programmed cell death involved in neurodegeneration. Trends Neurosci 28:670-676 (Pubitemid 41654391)
    • (2005) Trends in Neurosciences , vol.28 , Issue.12 , pp. 670-676
    • Krantic, S.1    Mechawar, N.2    Reix, S.3    Quirion, R.4
  • 23
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • DOI 10.1038/35085008
    • Leist M, Jaattela M (2001) Four deaths and a funeral: from caspases to alternative mechanisms. Nat Rev Mol Cell Biol 2:589-598 (Pubitemid 33674010)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.8 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 24
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • 16541076 10.1038/nature04533 1:CAS:528:DC%2BD28XitlKgurg%3D
    • Lesne S, Koh MT, Kotilinek L, Kayed R, Glabe CG, Yang A, Gallagher M, Ashe KH (2006) A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440:352-357
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3    Kayed, R.4    Glabe, C.G.5    Yang, A.6    Gallagher, M.7    Ashe, K.H.8
  • 25
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid Beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • 19555648 10.1016/j.neuron.2009.05.012 1:CAS:528:DC%2BD1MXpsFOnsro%3D
    • Li S, Hong S, Shepardson NE, Walsh DM, Shankar GM, Selkoe D (2009) Soluble oligomers of amyloid Beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron 62:788-801
    • (2009) Neuron , vol.62 , pp. 788-801
    • Li, S.1    Hong, S.2    Shepardson, N.E.3    Walsh, D.M.4    Shankar, G.M.5    Selkoe, D.6
  • 26
    • 33749054403 scopus 로고    scopus 로고
    • Splicing Regulation in Neurologic Disease
    • DOI 10.1016/j.neuron.2006.09.017, PII S0896627306007240
    • Licatalosi DD, Darnell RB (2006) Splicing regulation in neurologic disease. Neuron 52:93-101 (Pubitemid 44466357)
    • (2006) Neuron , vol.52 , Issue.1 , pp. 93-101
    • Licatalosi, D.D.1    Darnell, R.B.2
  • 27
    • 0036843904 scopus 로고    scopus 로고
    • Induction of marked apoptosis in mammalian cancer cell lines by antisense DNA treatment to abolish expression of DENN (Differentially Expressed in Normal and Neoplastic Cells)
    • DOI 10.1002/mc.10082
    • Lim KM, Chow VT (2002) Induction of marked apoptosis in mammalian cancer cell lines by antisense DNA treatment to abolish expression of DENN (differentially expressed in normal and neoplastic cells). Mol Carcinog 35:110-126 (Pubitemid 35266058)
    • (2002) Molecular Carcinogenesis , vol.35 , Issue.3 , pp. 110-126
    • Lim, K.M.1    Chow, V.T.K.2
  • 28
    • 0742305154 scopus 로고    scopus 로고
    • Antisense abrogation of DENN expression induces apoptosis of leukemia cells in vitro, causes tumor regression in vivo and alters the transcription of genes involved in apoptosis and the cell cycle
    • DOI 10.1002/ijc.11660
    • Lim KM, Yeo WS, Chow VT (2004) Antisense abrogation of DENN expression induces apoptosis of leukemia cells in vitro, causes tumor regression in vivo and alters the transcription of genes involved in apoptosis and the cell cycle. Int J Cancer 109:24-37 (Pubitemid 38160658)
    • (2004) International Journal of Cancer , vol.109 , Issue.1 , pp. 24-37
    • Lim, K.M.1    Yeo, W.S.2    Chow, V.T.K.3
  • 29
    • 20444368053 scopus 로고    scopus 로고
    • Neuronal proteins custom designed by alternative splicing
    • DOI 10.1016/j.conb.2005.04.002, PII S0959438805000656
    • Lipscombe D (2005) Neuronal proteins custom designed by alternative splicing. Curr Opin Neurobiol 15:358-363 (Pubitemid 40806449)
    • (2005) Current Opinion in Neurobiology , vol.15 , Issue.3 SPEC. ISS. , pp. 358-363
    • Lipscombe, D.1
  • 30
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • 10589538 10.1002/1531-8249(199912)46:6<860::AID-ANA8>3.0.CO;2-M 1:CAS:528:DC%2BD3cXhsFyrug%3D%3D
    • McLean CA, Cherny RA, Fraser FW, Fuller SJ, Smith MJ, Beyreuther K, Bush AI, Masters CL (1999) Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann Neurol 46:860-866
    • (1999) Ann Neurol , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3    Fuller, S.J.4    Smith, M.J.5    Beyreuther, K.6    Bush, A.I.7    Masters, C.L.8
  • 31
    • 33749825177 scopus 로고    scopus 로고
    • MADD/DENN splice variant of the IG20 gene is necessary and sufficient for cancer cell survival
    • DOI 10.1038/sj.onc.1209650, PII 1209650
    • Mulherkar N, Ramaswamy M, Mordi DC, Prabhakar BS (2006) MADD/DENN splice variant of the IG20 gene is necessary and sufficient for cancer cell survival. Oncogene 25:6252-6261 (Pubitemid 44564742)
    • (2006) Oncogene , vol.25 , Issue.47 , pp. 6252-6261
    • Mulherkar, N.1    Ramaswamy, M.2    Mordi, D.C.3    Prabhakar, B.S.4
  • 32
    • 55549134618 scopus 로고    scopus 로고
    • KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator Rab3 occurs in a GTP-dependent manner through DENN/MADD
    • 18849981 10.1038/ncb1785 1:CAS:528:DC%2BD1cXhtlais7vM
    • Niwa S, Tanaka Y, Hirokawa N (2008) KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator Rab3 occurs in a GTP-dependent manner through DENN/MADD. Nat Cell Biol 10:1269-1279
    • (2008) Nat Cell Biol , vol.10 , pp. 1269-1279
    • Niwa, S.1    Tanaka, Y.2    Hirokawa, N.3
  • 33
    • 77954927651 scopus 로고    scopus 로고
    • Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid beta-protein assembly and toxicity
    • 20452980 10.1074/jbc.M109.086496 1:CAS:528:DC%2BC3cXovFels70%3D
    • Ono K, Condron MM, Teplow DB (2010) Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid beta-protein assembly and toxicity. J Biol Chem 285:23186-23197
    • (2010) J Biol Chem , vol.285 , pp. 23186-23197
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 35
    • 63849197629 scopus 로고    scopus 로고
    • Amyloid beta-protein assembly and Alzheimer disease
    • 18845536 10.1074/jbc.R800036200 1:CAS:528:DC%2BD1MXhvVSgtb0%3D
    • Roychaudhuri R, Yang M, Hoshi MM, Teplow DB (2009) Amyloid beta-protein assembly and Alzheimer disease. J Biol Chem 284:4749-4753
    • (2009) J Biol Chem , vol.284 , pp. 4749-4753
    • Roychaudhuri, R.1    Yang, M.2    Hoshi, M.M.3    Teplow, D.B.4
  • 37
    • 4444272979 scopus 로고    scopus 로고
    • Cell signalling and the control of pre-mRNA splicing
    • DOI 10.1038/nrm1467
    • Shin C, Manley JL (2004) Cell signalling and the control of pre-mRNA splicing. Nat Rev Mol Cell Biol 5:727-738 (Pubitemid 39208182)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.9 , pp. 727-738
    • Shin, C.1    Manley, J.L.2
  • 40
    • 22744449772 scopus 로고    scopus 로고
    • The spliceosome: A novel multi-faceted target for therapy
    • DOI 10.1016/j.tibs.2005.06.002, PII S0968000405001817
    • Tazi J, Durand S, Jeanteur P (2005) The spliceosome: a novel multi-faceted target for therapy. Trends Biochem Sci 30:469-478 (Pubitemid 41033243)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.8 , pp. 469-478
    • Tazi, J.1    Durand, S.2    Jeanteur, P.3
  • 41
    • 80053529549 scopus 로고    scopus 로고
    • Analysis of alternative splicing associated with aging and neurodegeneration in the human brain
    • 21846794 10.1101/gr.122226.111 1:CAS:528:DC%2BC3MXhtlSrurfF
    • Tollervey JR, Wang Z, Hortobagyi T, Witten JT, Zarnack K, Kayikci M, Clark TA, Schweitzer AC et al (2011) Analysis of alternative splicing associated with aging and neurodegeneration in the human brain. Genome Res 21:1572-1582
    • (2011) Genome Res , vol.21 , pp. 1572-1582
    • Tollervey, J.R.1    Wang, Z.2    Hortobagyi, T.3    Witten, J.T.4    Zarnack, K.5    Kayikci, M.6    Clark, T.A.7    Schweitzer, A.C.8
  • 42
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid beta-protein on hippocampal synaptic plasticity: A potent role for trimers
    • 16469784 10.1113/jphysiol.2005.103754 1:CAS:528:DC%2BD28XksV2jtrc%3D
    • Townsend M, Shankar GM, Mehta T, Walsh DM, Selkoe DJ (2006) Effects of secreted oligomers of amyloid beta-protein on hippocampal synaptic plasticity: a potent role for trimers. J Physiol 572:477-492
    • (2006) J Physiol , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 43
    • 0031041373 scopus 로고    scopus 로고
    • Isolation and characterization of a GDP/GTP exchange protein specific for the RAB3 subfamily small G proteins
    • DOI 10.1074/jbc.272.7.3875
    • Wada M, Nakanishi H, Satoh A, Hirano H, Obaishi H, Matsuura Y, Takai Y (1997) Isolation and characterization of a GDP/GTP exchange protein specific for the Rab3 subfamily small G proteins. J Biol Chem 272:3875-3878 (Pubitemid 27078440)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.7 , pp. 3875-3878
    • Wada, M.1    Nakanishi, H.2    Satoh, A.3    Hirano, H.4    Obaishi, H.5    Matsuura, Y.6    Takai, Y.7
  • 44
    • 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, Wolfe MS, Rowan MJ, Selkoe DJ (2002) Naturally secreted oligomers of amyloid beta 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
  • 45
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • DOI 10.1016/j.neuron.2004.09.010, PII S0896627304006038
    • Walsh DM, Selkoe DJ (2004) Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44:181-193 (Pubitemid 39348839)
    • (2004) Neuron , vol.44 , Issue.1 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 46
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers - A decade of discovery
    • DOI 10.1111/j.1471-4159.2006.04426.x
    • Walsh DM, Selkoe DJ (2007) A beta oligomers-a decade of discovery. J Neurochem 101:1172-1184 (Pubitemid 46718812)
    • (2007) Journal of Neurochemistry , vol.101 , Issue.5 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 47
    • 63349107477 scopus 로고    scopus 로고
    • Transcriptome analysis of synaptoneurosomes identifies neuroplasticity genes overexpressed in incipient Alzheimer's disease
    • 19295912 10.1371/journal.pone.0004936
    • Williams C, Mehrian Shai R, Wu Y, Hsu YH, Sitzer T, Spann B, McCleary C, Mo Y, Miller CA (2009) Transcriptome analysis of synaptoneurosomes identifies neuroplasticity genes overexpressed in incipient Alzheimer's disease. PLoS One 4:e4936
    • (2009) PLoS One , vol.4 , pp. 4936
    • Williams, C.1    Mehrian Shai, R.2    Wu, Y.3    Hsu, Y.H.4    Sitzer, T.5    Spann, B.6    McCleary, C.7    Mo, Y.8    Miller, C.A.9
  • 48
    • 18944407388 scopus 로고    scopus 로고
    • Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death
    • DOI 10.1523/JNEUROSCI.2381-04.2005
    • Wogulis M, Wright S, Cunningham D, Chilcote T, Powell K, Rydel RE (2005) Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death. J Neurosci 25:1071-1080 (Pubitemid 41741352)
    • (2005) Journal of Neuroscience , vol.25 , Issue.5 , pp. 1071-1080
    • Wogulis, M.1    Wright, S.2    Cunningham, D.3    Chilcote, T.4    Powell, K.5    Rydel, R.E.6
  • 50
    • 0032478078 scopus 로고    scopus 로고
    • A splicing variant of a death domain protein that is regulated by a mitogen-activated kinase is a substrate for c-Jun N-terminal kinase in the human central nervous system
    • DOI 10.1073/pnas.95.5.2586
    • Zhang Y, Zhou L, Miller CA (1998) A splicing variant of a death domain protein that is regulated by a mitogen-activated kinase is a substrate for c-Jun N-terminal kinase in the human central nervous system. Proc Natl Acad Sci U S A 95:2586-2591 (Pubitemid 28145986)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.5 , pp. 2586-2591
    • Zhang, Y.1    Zhou, L.2    Miller, C.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.