메뉴 건너뛰기




Volumn 2012, Issue , 2012, Pages

Synapses and dendritic spines as pathogenic targets in Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

TAU PROTEIN; AMYLOID BETA PROTEIN;

EID: 84858204150     PISSN: 20905904     EISSN: 16875443     Source Type: Journal    
DOI: 10.1155/2012/247150     Document Type: Review
Times cited : (98)

References (97)
  • 1
  • 2
    • 77951531718 scopus 로고    scopus 로고
    • Excitation control: Balancing PSD-95 function at the synapse
    • article 4
    • Keith D., El-Husseini A., Excitation control: balancing PSD-95 function at the synapse Frontiers in Molecular Neuroscience 2008 1, article 4
    • (2008) Frontiers in Molecular Neuroscience , vol.1
    • Keith, D.1    El-Husseini, A.2
  • 3
    • 0742323527 scopus 로고    scopus 로고
    • Homeostatic plasticity in the developing nervous system
    • Turrigiano G. G., Nelson S. B., Homeostatic plasticity in the developing nervous system Nature Reviews Neuroscience 2004 5 2 97 107 (Pubitemid 38160285)
    • (2004) Nature Reviews Neuroscience , vol.5 , Issue.2 , pp. 97-107
    • Turrigiano, G.G.1    Nelson, S.B.2
  • 4
    • 38049152679 scopus 로고    scopus 로고
    • Gephyrin expression and clustering affects the size of glutamatergic synaptic contacts
    • Yu W., Blas A. L. D., Gephyrin expression and clustering affects the size of glutamatergic synaptic contacts Journal of Neurochemistry 2008 104 3 830 845
    • (2008) Journal of Neurochemistry , vol.104 , Issue.3 , pp. 830-845
    • Yu, W.1    Blas, A.L.D.2
  • 5
    • 33847072745 scopus 로고    scopus 로고
    • Enhanced synaptic excitation-inhibition ratio in hippocampal interneurons of rats with temporal lobe epilepsy
    • Stief F., Zuschratter W., Hartmann K., Schmitz D., Draguhn A., Enhanced synaptic excitation-inhibition ratio in hippocampal interneurons of rats with temporal lobe epilepsy European Journal of Neuroscience 2007 25 2 519 528
    • (2007) European Journal of Neuroscience , vol.25 , Issue.2 , pp. 519-528
    • Stief, F.1    Zuschratter, W.2    Hartmann, K.3    Schmitz, D.4    Draguhn, A.5
  • 6
    • 0036308284 scopus 로고    scopus 로고
    • Schizophrenia as a disorder of neurodevelopment
    • DOI 10.1146/annurev.neuro.25.112701.142754
    • Lewis D. A., Levitt P., Schizophrenia as a disorder of neurodevelopment Annual Review of Neuroscience 2002 25 409 432 (Pubitemid 34748023)
    • (2002) Annual Review of Neuroscience , vol.25 , pp. 409-432
    • Lewis, D.A.1    Levitt, P.2
  • 7
    • 4544306641 scopus 로고    scopus 로고
    • Neuropsychiatric symptoms of fragile X syndrome: Pathophysiology and pharmacotherapy
    • DOI 10.2165/00023210-200418110-00001
    • Tsiouris J. A., Brown W. T., Neuropsychiatric symptoms of fragile X syndrome: pathophysiology and pharmacotherapy CNS Drugs 2004 18 11 687 703 (Pubitemid 39243564)
    • (2004) CNS Drugs , vol.18 , Issue.11 , pp. 687-703
    • Tsiouris, J.A.1    Brown, W.T.2
  • 8
    • 33750592733 scopus 로고    scopus 로고
    • Autistic spectrum disorder: Evaluating a possible contributing or causal role of epilepsy
    • DOI 10.1111/j.1528-1167.2006.00697.x
    • Deonna T., Roulet E., Autistic spectrum disorder: evaluating a possible contributing or causal role of epilepsy Epilepsia 2006 47 supplement 2 79 82 (Pubitemid 44684629)
    • (2006) Epilepsia , vol.47 , Issue.SUPPL. 2 , pp. 79-82
    • Deonna, T.1    Roulet, E.2
  • 9
    • 0019917243 scopus 로고
    • Molecular biology of learning: Modulation of transmitter release
    • Kandel E. R., Schwartz J. H., Molecular biology of learning: modulation of transmitter release Science 1982 218 4571 433 443 (Pubitemid 12000895)
    • (1982) Science , vol.218 , Issue.4571 , pp. 433-443
    • Kandel, E.R.1    Schwartz, J.H.2
  • 10
    • 5344241223 scopus 로고    scopus 로고
    • LTP and LTD: An embarrassment of riches
    • DOI 10.1016/j.neuron.2004.09.012, PII S0896627304006087
    • Malenka R. C., Bear M. F., LTP and LTD: an embarrassment of riches Neuron 2004 44 1 5 21 (Pubitemid 39348827)
    • (2004) Neuron , vol.44 , Issue.1 , pp. 5-21
    • Malenka, R.C.1    Bear, M.F.2
  • 11
    • 0015799240 scopus 로고
    • Long lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path
    • Bliss T. V. P., Lomo T., Long lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path The Journal of Physiology 1973 232 2 331 356
    • (1973) The Journal of Physiology , vol.232 , Issue.2 , pp. 331-356
    • Bliss, T.V.P.1    Lomo, T.2
  • 12
    • 0017329360 scopus 로고
    • Heterosynaptic depression: A postsynaptic correlate of long term potentiation
    • Lynch G. S., Dunwiddie T., Gribkoff V., Heterosynaptic depression: a postsynaptic correlate of long term potentiation Nature 1977 266 5604 737 739 (Pubitemid 8073808)
    • (1977) Nature , vol.266 , Issue.5604 , pp. 737-739
    • Lynch, G.S.1    Dunwiddie, T.2    Gribkoff, V.3
  • 14
    • 0033681557 scopus 로고    scopus 로고
    • Regulation of AMPA receptor-mediated synaptic transmission by clathrin-dependent receptor internalization
    • Man H. Y., Lin J. W., Ju W. H., Ahmadian G., Liu L., Becker L. E., Sheng M., Wang Y. T., Regulation of AMPA receptor-mediated synaptic transmission by clathrin-dependent receptor internalization Neuron 2000 25 3 649 662
    • (2000) Neuron , vol.25 , Issue.3 , pp. 649-662
    • Man, H.Y.1    Lin, J.W.2    Ju, W.H.3    Ahmadian, G.4    Liu, L.5    Becker, L.E.6    Sheng, M.7    Wang, Y.T.8
  • 15
    • 0035708880 scopus 로고    scopus 로고
    • Internalization of ionotropic glutamate receptors in response to mGluR activation
    • DOI 10.1038/nn746
    • Snyder E. M., Philpot B. D., Huber K. M., Dong X., Fallon J. R., Bear M. F., Internalization of ionotropic glutamate receptors in response to mGluR activation Nature Neuroscience 2001 4 11 1079 1085 (Pubitemid 34116552)
    • (2001) Nature Neuroscience , vol.4 , Issue.11 , pp. 1079-1085
    • Snyder, E.M.1    Philpot, B.D.2    Huber, K.M.3    Dong, X.4    Fallon, J.R.5    Bear, M.F.6
  • 16
    • 0034788373 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor activation causes a rapid redistribution of AMPA receptors
    • DOI 10.1016/S0028-3908(01)00134-4, PII S0028390801001344
    • Xiao M. Y., Zhou Q., Nicoll R. A., Metabotropic glutamate receptor activation causes a rapid redistribution of AMPA receptors Neuropharmacology 2001 41 6 664 671 (Pubitemid 32972183)
    • (2001) Neuropharmacology , vol.41 , Issue.6 , pp. 664-671
    • Xiao, M.-Y.1    Zhou, Q.2    Nicoll, R.A.3
  • 17
    • 0037079062 scopus 로고    scopus 로고
    • Clathrin adaptor AP2 and NSF interact with overlapping sites of GluR2 and play distinct roles in AMPA receptor trafficking and hippocampal LTD
    • DOI 10.1016/S0896-6273(02)01024-3
    • Lee S. H., Liu L., Wang Y. T., Sheng M., Clathrin adaptor AP2 and NSF interact with overlapping sites of GluR2 and play distinct roles in AMPA receptor trafficking and hippocampal LTD Neuron 2002 36 4 661 674 (Pubitemid 35346759)
    • (2002) Neuron , vol.36 , Issue.4 , pp. 661-674
    • Lee, S.H.1    Liu, L.2    Wang, Y.T.3    Sheng, M.4
  • 18
    • 9644265305 scopus 로고    scopus 로고
    • Bidirectional activity-dependent morphological plasticity in hippocampal neurons
    • DOI 10.1016/j.neuron.2004.11.016, PII S0896627304007299
    • Ngerl U. V., Eberhorn N., Cambridge S. B., Bonhoeffer T., Bidirectional activity-dependent morphological plasticity in hippocampal neurons Neuron 2004 44 5 759 767 (Pubitemid 39575630)
    • (2004) Neuron , vol.44 , Issue.5 , pp. 759-767
    • Nagerl, U.V.1    Eberhorn, N.2    Cambridge, S.B.3    Bonhoeffer, T.4
  • 19
    • 9644278075 scopus 로고    scopus 로고
    • Shrinkage of dendritic spines associated with long-term depression of hippocampal synapses
    • DOI 10.1016/j.neuron.2004.11.011, PII S0896627304007226
    • Zhou Q., Homma K. J., Poo M. M., Shrinkage of dendritic spines associated with long-term depression of hippocampal synapses Neuron 2004 44 5 749 757 (Pubitemid 39575629)
    • (2004) Neuron , vol.44 , Issue.5 , pp. 749-757
    • Zhou, Q.1    Homma, K.J.2    Poo, M.-M.3
  • 20
    • 43449117577 scopus 로고    scopus 로고
    • Balancing structure and function at hippocampal dendritic spines
    • Bourne J. N., Harris K. M., Balancing structure and function at hippocampal dendritic spines Annual Review of Neuroscience 2008 31 47 67
    • (2008) Annual Review of Neuroscience , vol.31 , pp. 47-67
    • Bourne, J.N.1    Harris, K.M.2
  • 21
    • 0036082812 scopus 로고    scopus 로고
    • Dendritic spine pathology: Cause or consequence of neurological disorders?
    • DOI 10.1016/S0165-0173(02)00158-3, PII S0165017302001583
    • Fiala J. C., Spacek J., Harris K. M., Dendritic spine pathology: cause or consequence of neurological disorders? Brain Research Reviews 2002 39 1 29 54 (Pubitemid 34666985)
    • (2002) Brain Research Reviews , vol.39 , Issue.1 , pp. 29-54
    • Fiala, J.C.1    Spacek, J.2    Harris, K.M.3
  • 22
    • 77957264418 scopus 로고    scopus 로고
    • The synaptic pathology of -synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementia
    • Schulz-Schaeffer W. J., The synaptic pathology of -synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementia Acta Neuropathologica 2010 120 2 131 143
    • (2010) Acta Neuropathologica , vol.120 , Issue.2 , pp. 131-143
    • Schulz-Schaeffer, W.J.1
  • 26
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics
    • DOI 10.1146/annurev.pharmtox.43.100901.140248
    • Selkoe D. J., Schenk D., Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics Annual Review of Pharmacology and Toxicology 2003 43 545 584 (Pubitemid 37372653)
    • (2003) Annual Review of Pharmacology and Toxicology , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 28
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • DOI 10.1126/science.1074069
    • Selkoe D. J., Alzheimer's disease is a synaptic failure Science 2002 298 5594 789 791 (Pubitemid 35231524)
    • (2002) Science , vol.298 , Issue.5594 , pp. 789-791
    • Selkoe, D.J.1
  • 29
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • DeKosky S. T., Scheff S. W., Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity Annals of Neurology 1990 27 5 457 464 (Pubitemid 20149963)
    • (1990) Annals of Neurology , vol.27 , Issue.5 , pp. 457-464
    • DeKosky, S.T.1    Scheff, S.W.2
  • 30
    • 0024314702 scopus 로고
    • Amyloid protein precursor and the pathogenesis of Alzheimer's disease
    • DOI 10.1016/0092-8674(89)90093-7
    • Selkoe D. J., Amyloid protein precursor and the pathogenesis of Alzheimer's disease Cell 1989 58 4 611 612 (Pubitemid 19210954)
    • (1989) Cell , vol.58 , Issue.4 , pp. 611-612
    • Selkoe, D.J.1
  • 31
    • 7044220336 scopus 로고    scopus 로고
    • Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches
    • DOI 10.1038/nn1335
    • Tsai J., Grutzendler J., Duff K., Gan W. B., Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches Nature Neuroscience 2004 7 11 1181 1183 (Pubitemid 39426234)
    • (2004) Nature Neuroscience , vol.7 , Issue.11 , pp. 1181-1183
    • Tsai, J.1    Grutzendler, J.2    Duff, K.3    Gan, W.-B.4
  • 32
    • 23444448170 scopus 로고    scopus 로고
    • Dendritic spine abnormalities in amyloid precursor protein transgenic mice demonstrated by gene transfer and intravital multiphoton microscopy
    • DOI 10.1523/JNEUROSCI.1879-05.2005
    • Spires T. L., Meyer-Luehmann M., Stern E. A., McLean P. J., Skoch J., Nguyen P. T., Bacskai B. J., Hyman B. T., Dendritic spine abnormalities in amyloid precursor protein transgenic mice demonstrated by gene transfer and intravital multiphoton microscopy Journal of Neuroscience 2005 25 31 7278 7287 (Pubitemid 41113944)
    • (2005) Journal of Neuroscience , vol.25 , Issue.31 , pp. 7278-7287
    • Spires, T.L.1    Meyer-Luehmann, M.2    Stern, E.A.3    McLean, P.J.4    Skoch, J.5    Nguyen, P.T.6    Bacskai, B.J.7    Hyman, B.T.8
  • 34
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid -protein impair synaptic plasticity and behavior
    • Selkoe D. J., Soluble oligomers of the amyloid -protein impair synaptic plasticity and behavior Behavioural Brain Research 2008 192 1 106 113
    • (2008) Behavioural Brain Research , vol.192 , Issue.1 , pp. 106-113
    • Selkoe, D.J.1
  • 35
    • 0028985799 scopus 로고
    • Role of the -amyloid protein in Alzheimer's disease
    • Sisodia S. S., Price D. L., Role of the -amyloid protein in Alzheimer's disease The FASEB Journal 1995 9 5 366 370
    • (1995) The FASEB Journal , vol.9 , Issue.5 , pp. 366-370
    • Sisodia, S.S.1    Price, D.L.2
  • 37
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy J., Selkoe D. J., The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 2002 297 5580 353 356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 38
    • 0024472693 scopus 로고
    • Neurotixicity of a fragment of the amyloid precursor associated with Alzheimer's disease
    • Yankner B. A., Dawes L. R., Fisher S., Villa-Komaroff L., Oster-Granite M. L., Neve R. L., Neurotixicity of a fragment of the amyloid precursor associated with Alzheimer's disease Science 1989 245 4916 417 420 (Pubitemid 19203368)
    • (1989) Science , vol.245 , Issue.4916 , pp. 417-420
    • Yankner, B.A.1    Dawes, L.R.2    Fisher, S.3    Villa-Komaroff, L.4    Oster-Granite, M.L.5    Neve, R.L.6
  • 39
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh D. M., Klyubin I., Fadeeva J. V., Cullen W. K., Anwyl R., Wolfe M. S., Rowan M. J., Selkoe D. J., Naturally secreted oligomers of amyloid protein potently inhibit hippocampal long-term potentiation in vivo Nature 2002 416 6880 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
  • 42
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal A causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • DOI 10.1016/j.neuron.2005.01.040
    • Billings L. M., Oddo S., Green K. N., McGaugh J. L., LaFerla F. M., Intraneuronal A causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice Neuron 2005 45 5 675 688 (Pubitemid 40320703)
    • (2005) Neuron , vol.45 , Issue.5 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 43
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • DOI 10.1073/pnas.90.2.567
    • Arispe N., Rojas E., Pollard H. B., Alzheimer disease amyloid protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum Proceedings of the National Academy of Sciences of the United States of America 1993 90 2 567 571 (Pubitemid 23028904)
    • (1993) Proceedings of the National Academy of Sciences of the United States of America , vol.90 , Issue.2 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 44
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel H. A., Hartley D., Petre B. M., Walz T., Lansbury P. T., Neurodegenerative disease: amyloid pores from pathogenic mutations Nature 2002 418 6895, article 291 291 (Pubitemid 34790672)
    • (2002) Nature , vol.418 , Issue.6895 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 45
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR Removal Underlies A-Induced Synaptic Depression and Dendritic Spine Loss
    • DOI 10.1016/j.neuron.2006.10.035, PII S0896627306008725
    • Hsieh H., Boehm J., Sato C., Iwatsubo T., Tomita T., Sisodia S., Malinow R., AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss Neuron 2006 52 5 831 843 (Pubitemid 44828454)
    • (2006) Neuron , vol.52 , Issue.5 , pp. 831-843
    • Hsieh, H.1    Boehm, J.2    Sato, C.3    Iwatsubo, T.4    Tomita, T.5    Sisodia, S.6    Malinow, R.7
  • 46
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid- protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • DOI 10.1523/JNEUROSCI.4970-06.2007
    • Shankar G. M., Bloodgood B. L., Townsend M., Walsh D. M., Selkoe D. J., Sabatini B. L., Natural oligomers of the Alzheimer amyloid- protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway Journal of Neuroscience 2007 27 11 2866 2875 (Pubitemid 46438992)
    • (2007) Journal of Neuroscience , vol.27 , Issue.11 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 47
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid Beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • Li S., Hong S., Shepardson N. E., Walsh D. M., Shankar G. M., Selkoe D., Soluble oligomers of amyloid Beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake Neuron 2009 62 6 788 801
    • (2009) Neuron , vol.62 , Issue.6 , pp. 788-801
    • Li, S.1    Hong, S.2    Shepardson, N.E.3    Walsh, D.M.4    Shankar, G.M.5    Selkoe, D.6
  • 48
    • 34548264782 scopus 로고    scopus 로고
    • Aberrant Excitatory Neuronal Activity and Compensatory Remodeling of Inhibitory Hippocampal Circuits in Mouse Models of Alzheimer's Disease
    • DOI 10.1016/j.neuron.2007.07.025, PII S0896627307005703
    • Palop J. J., Chin J., Roberson E. D., Wang J., Thwin M. T., Bien-Ly N., Yoo J., Ho K. O., Yu G. Q., Kreitzer A., Finkbeiner S., Noebels J. L., Mucke L., Aberrant excitatory neuronal activity and compensatory remodeling of inhibitory hippocampal circuits in mouse models of Alzheimer's disease Neuron 2007 55 5 697 711 (Pubitemid 47321079)
    • (2007) Neuron , vol.55 , Issue.5 , pp. 697-711
    • Palop, J.J.1    Chin, J.2    Roberson, E.D.3    Wang, J.4    Thwin, M.T.5    Bien-Ly, N.6    Yoo, J.7    Ho, K.O.8    Yu, G.-Q.9    Kreitzer, A.10    Finkbeiner, S.11    Noebels, J.L.12    Mucke, L.13
  • 49
    • 33750683018 scopus 로고    scopus 로고
    • Alzheimer's APP mangles mitochondria
    • DOI 10.1038/nm1106-1241, PII NM11061241
    • Lin M. T., Beal M. F., Alzheimer's APP mangles mitochondria Nature Medicine 2006 12 11 1241 1243 (Pubitemid 44706922)
    • (2006) Nature Medicine , vol.12 , Issue.11 , pp. 1241-1243
    • Lin, M.T.1    Beal, M.F.2
  • 50
    • 33747388358 scopus 로고    scopus 로고
    • Lysosomal system pathways: Genes to neurodegeneration in Alzheimer's disease
    • Nixon R. A., Cataldo A. M., Lysosomal system pathways: genes to neurodegeneration in Alzheimer's disease Journal of Alzheimer's Disease 2006 9 supplement 3 277 289 (Pubitemid 44253321)
    • (2006) Journal of Alzheimer's Disease , vol.9 , Issue.SUPPL. 3 , pp. 277-289
    • Nixon, R.A.1    Cataldo, A.M.2
  • 51
    • 26944467176 scopus 로고    scopus 로고
    • Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses
    • DOI 10.1016/j.nbd.2005.02.008, PII S0969996105000720
    • Almeida C. G., Tampellini D., Takahashi R. H., Greengard P., Lin M. T., Snyder E. M., Gouras G. K., Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses Neurobiology of Disease 2005 20 2 187 198 (Pubitemid 41476246)
    • (2005) Neurobiology of Disease , vol.20 , Issue.2 , pp. 187-198
    • Almeida, C.G.1    Tampellini, D.2    Takahashi, R.H.3    Greengard, P.4    Lin, M.T.5    Snyder, E.M.6    Gouras, G.K.7
  • 52
    • 5044224260 scopus 로고    scopus 로고
    • PDZ domain proteins of synapses
    • DOI 10.1038/nrn1517
    • Kim E., Sheng M., PDZ domain proteins of synapses Nature Reviews Neuroscience 2004 5 10 771 781 (Pubitemid 39336214)
    • (2004) Nature Reviews Neuroscience , vol.5 , Issue.10 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 53
    • 7244223228 scopus 로고    scopus 로고
    • Snaptic changes in alzheimer's disease: Increased amyloid- and gliosis in surviving terminals is accompanied by decreased PSD-95 fluorescence
    • Gylys K. H., Fein J. A., Yang F., Wiley D. J., Miller C. A., Cole G. M., Snaptic changes in alzheimer's disease: increased amyloid- and gliosis in surviving terminals is accompanied by decreased PSD-95 fluorescence The American Journal of Pathology 2004 165 5 1809 1817 (Pubitemid 39435178)
    • (2004) American Journal of Pathology , vol.165 , Issue.5 , pp. 1809-1817
    • Gylys, K.H.1    Fein, J.A.2    Yang, F.3    Wiley, D.J.4    Miller, C.A.5    Cole, G.M.6
  • 54
    • 33846075630 scopus 로고    scopus 로고
    • PAR-1 Kinase Phosphorylates Dlg and Regulates Its Postsynaptic Targeting at the Drosophila Neuromuscular Junction
    • DOI 10.1016/j.neuron.2006.12.016, PII S089662730601021X
    • Zhang Y., Guo H., Kwan H., Wang J. W., Kosek J., Lu B., PAR-1 kinase phosphorylates Dlg and regulates its postsynaptic targeting at the Drosophila neuromuscular junction Neuron 2007 53 2 201 215 (Pubitemid 46074401)
    • (2007) Neuron , vol.53 , Issue.2 , pp. 201-215
    • Zhang, Y.1    Guo, H.2    Kwan, H.3    Wang, J.-W.4    Kosek, J.5    Lu, B.6
  • 55
    • 33846448743 scopus 로고    scopus 로고
    • Activation of PAR-1 kinase and stimulation of tau phosphorylation by diverse signals require the tumor suppressor protein LKB1
    • DOI 10.1523/JNEUROSCI.5094-06.2007
    • Wang J. W., Imai Y., Lu B., Activation of PAR-1 kinase and stimulation of tau phosphorylation by diverse signals require the tumor suppressor protein LKB1 The Journal of Neuroscience 2007 27 3 574 581 (Pubitemid 46143761)
    • (2007) Journal of Neuroscience , vol.27 , Issue.3 , pp. 574-581
    • Wang, J.-W.1    Imai, Y.2    Lu, B.3
  • 56
    • 77956587739 scopus 로고    scopus 로고
    • A oligomers cause localized Ca 2+ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines
    • Zempel H., Thies E., Mandelkow E., Mandelkow E. M., A oligomers cause localized Ca 2+ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines The Journal of Neuroscience 2010 30 36 11938 11950
    • (2010) The Journal of Neuroscience , vol.30 , Issue.36 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 59
    • 0034509448 scopus 로고    scopus 로고
    • A very incomplete comprehensive theory of Alzheimer's disease
    • Davies P., A very incomplete comprehensive theory of Alzheimer's disease Annals of the New York Academy of Sciences 2000 924 8 16 (Pubitemid 32050176)
    • (2000) Annals of the New York Academy of Sciences , vol.924 , pp. 8-16
    • Davies, P.1
  • 60
    • 0035943213 scopus 로고    scopus 로고
    • Biomedicine: Tauists and aptists unitedwell almost!
    • Lee V. M. Y., Biomedicine: tauists and aptists unitedwell almost! Science 2001 293 5534 1446 1447
    • (2001) Science , vol.293 , Issue.5534 , pp. 1446-1447
    • Lee, V.M.Y.1
  • 62
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301L tau transgenic mice induced by A42 fibrils
    • DOI 10.1126/science.1062097
    • Gtz J., Chen F., van Dorpe J., Nitsch R. M., Formation of neurofibrillary tangles in P301L tau transgenic mice induced by A 42 fibrils Science 2001 293 5534 1491 1495 (Pubitemid 32807681)
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 63
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's Disease with plaques and tangles: Intracellular A and synaptic dysfunction
    • DOI 10.1016/S0896-6273(03)00434-3
    • Oddo S., Caccamo A., Shepherd J. D., Murphy M. P., Golde T. E., Kayed R., Metherate R., Mattson M. P., Akbari Y., LaFerla F. M., Triple-transgenic model of Alzheimer's Disease with plaques and tangles: intracellular A and synaptic dysfunction Neuron 2003 39 3 409 421 (Pubitemid 36937044)
    • (2003) Neuron , vol.39 , Issue.3 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6    Metherate, R.7    Mattson, M.P.8    Akbari, Y.9    LaFerla, F.M.10
  • 64
    • 4043167747 scopus 로고    scopus 로고
    • A immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • DOI 10.1016/j.neuron.2004.07.003, PII S0896627304004246
    • Oddo S., Billings L., Kesslak J. P., Cribbs D. H., LaFerla F. M., A immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome Neuron 2004 43 3 321 332 (Pubitemid 39061125)
    • (2004) Neuron , vol.43 , Issue.3 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 66
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • Patrick G. N., Zukerberg L., Nikolic M., De La Monte S., Dikkes P., Tsai L. H., Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration Nature 1999 402 6762 615 622 (Pubitemid 129516324)
    • (1999) Nature , vol.402 , Issue.6762 , pp. 615-622
    • Patrick, G.N.1    Zukerberg, L.2    Nikolic, M.3    De La Monte, S.4    Dikkes, P.5    Tsai, L.-H.6
  • 67
    • 33749826587 scopus 로고    scopus 로고
    • P25/cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid in vivo
    • DOI 10.1523/JNEUROSCI.3133-06.2006
    • Cruz J. C., Kim D., Moy L. Y., Dobbin M. M., Sun X., Bronson R. T., Tsai L. H., p25/cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid in vivo The Journal of Neuroscience 2006 26 41 10536 10541 (Pubitemid 44564604)
    • (2006) Journal of Neuroscience , vol.26 , Issue.41 , pp. 10536-10541
    • Cruz, J.C.1    Kim, D.2    Moy, L.Y.3    Dobbin, M.M.4    Sun, X.5    Bronson, R.T.6    Tsai, L.-H.7
  • 68
    • 0030604667 scopus 로고    scopus 로고
    • A peptide enhances focal adhesion kinase/Fyn association in a rat CNS nerve cell line
    • DOI 10.1016/0304-3940(96)12761-0
    • Zhang C., Qiu H. E., Krafft G. A., Klein W. L., A peptide enhances focal adhesion kinase/Fyn association in a rat CNS nerve cell line Neuroscience Letters 1996 211 3 187 190 (Pubitemid 26290891)
    • (1996) Neuroscience Letters , vol.211 , Issue.3 , pp. 187-190
    • Zhang, C.1    Qiu, H.E.2    Krafft, G.A.3    Klein, W.L.4
  • 69
    • 2442711560 scopus 로고    scopus 로고
    • Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice
    • DOI 10.1523/JNEUROSCI.0277-04.2004
    • Chin J., Palop J. J., Yu G. Q., Kojima N., Masliah E., Mucke L., Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice The Journal of Neuroscience 2004 24 19 4692 4697 (Pubitemid 38656624)
    • (2004) Journal of Neuroscience , vol.24 , Issue.19 , pp. 4692-4697
    • Chin, J.1    Palop, J.J.2    Yu, G.-Q.3    Kojima, N.4    Masliah, E.5    Mucke, L.6
  • 70
    • 0030458524 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 alteration in Alzheimer disease is related to neurofibrillary tangle formation
    • Baum L., Hansen L., Masliah E., Saitoh T., Glycogen synthase kinase 3 alteration in Alzheimer disease is related to neurofibrillary tangle formation Molecular and Chemical Neuropathology 1996 29 2-3 253 261 (Pubitemid 27016933)
    • (1996) Molecular and Chemical Neuropathology , vol.29 , Issue.2-3 , pp. 253-261
    • Baum, L.1    Hansen, L.2    Masliah, E.3    Saitoh, T.4
  • 71
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule- associated proteins and trigger microtubule disruption
    • Drewes G., Ebneth A., Preuss U., Mandelkow E. M., Mandelkow E., MARK, a novel family of protein kinases that phosphorylate microtubule- associated proteins and trigger microtubule disruption Cell 1997 89 2 297 308 (Pubitemid 27199901)
    • (1997) Cell , vol.89 , Issue.2 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 72
    • 1542358895 scopus 로고    scopus 로고
    • PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila
    • DOI 10.1016/S0092-8674(04)00170-9, PII S0092867404001709
    • Nishimura I., Yang Y., Lu B., PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila Cell 2004 116 5 671 682 (Pubitemid 38326726)
    • (2004) Cell , vol.116 , Issue.5 , pp. 671-682
    • Nishimura, I.1    Yang, Y.2    Lu, B.3
  • 73
    • 0033758105 scopus 로고    scopus 로고
    • Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: A fluorescence resonance energy transfer study
    • Chin J. Y., Knowles R. B., Schneider A., Drewes G., Mandelkow E. M., Hyman B. T., Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: a fluorescence resonance energy transfer study Journal of Neuropathology and Experimental Neurology 2000 59 11 966 971
    • (2000) Journal of Neuropathology and Experimental Neurology , vol.59 , Issue.11 , pp. 966-971
    • Chin, J.Y.1    Knowles, R.B.2    Schneider, A.3    Drewes, G.4    Mandelkow, E.M.5    Hyman, B.T.6
  • 74
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid -induced deficits in an Alzheimer's disease mouse model
    • DOI 10.1126/science.1141736
    • Roberson E. D., Scearce-Levie K., Palop J. J., Yan F., Cheng I. H., Wu T., Gerstein H., Yu G. Q., Mucke L., Reducing endogenous tau ameliorates amyloid -induced deficits in an Alzheimer's disease mouse model Science 2007 316 5825 750 754 (Pubitemid 46717684)
    • (2007) Science , vol.316 , Issue.5825 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6    Gerstein, H.7    Yu, G.-Q.8    Mucke, L.9
  • 78
    • 0027447602 scopus 로고
    • The protein tyrosine kinase, fyn, in Alzheimer's disease pathology
    • Shirazi S. K., Wood J. G., The protein tyrosine kinase, fyn, in Alzheimer's disease pathology NeuroReport 1993 4 4 435 437 (Pubitemid 23116742)
    • (1993) NeuroReport , vol.4 , Issue.4 , pp. 435-437
    • Shirazi, S.K.1    Wood, J.G.2
  • 79
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid- and taua toxic pas de deux in Alzheimer's disease
    • Ittner L. M., Gtz J., Amyloid- and taua toxic pas de deux in Alzheimer's disease Nature Reviews Neuroscience 2011 12 2 65 72
    • (2011) Nature Reviews Neuroscience , vol.12 , Issue.2 , pp. 65-72
    • Ittner, L.M.1    Gtz, J.2
  • 80
    • 70450212390 scopus 로고    scopus 로고
    • Look who is weaving the neural web: Glial control of synapse formation
    • Bolton M. M., Eroglu C., Look who is weaving the neural web: glial control of synapse formation Current Opinion in Neurobiology 2009 19 5 491 497
    • (2009) Current Opinion in Neurobiology , vol.19 , Issue.5 , pp. 491-497
    • Bolton, M.M.1    Eroglu, C.2
  • 83
    • 55049084760 scopus 로고    scopus 로고
    • The mystery and magic of glia: A perspective on their roles in health and disease
    • Barres B. A., The mystery and magic of glia: a perspective on their roles in health and disease Neuron 2008 60 3 430 440
    • (2008) Neuron , vol.60 , Issue.3 , pp. 430-440
    • Barres, B.A.1
  • 87
    • 33748471099 scopus 로고    scopus 로고
    • Inflammation in Alzheimer disease: Driving force, bystander or beneficial response?
    • DOI 10.1038/nm1484, PII NM1484
    • Wyss-Coray T., Inflammation in Alzheimer disease: driving force, bystander or beneficial response? Nature Medicine 2006 12 9 1005 1015 (Pubitemid 44353380)
    • (2006) Nature Medicine , vol.12 , Issue.9 , pp. 1005-1015
    • Wyss-Coray, T.1
  • 88
    • 77957970155 scopus 로고    scopus 로고
    • Neuroinflammation, oxidative stress and the pathogenesis of Alzheimer's disease
    • Agostinho P., Cunha R. A., Oliveira C., Neuroinflammation, oxidative stress and the pathogenesis of Alzheimer's disease Current Pharmaceutical Design 2010 16 25 2766 2778
    • (2010) Current Pharmaceutical Design , vol.16 , Issue.25 , pp. 2766-2778
    • Agostinho, P.1    Cunha, R.A.2    Oliveira, C.3
  • 92
    • 77649184973 scopus 로고    scopus 로고
    • Microglia: Biology and pathology
    • Graeber M. B., Streit W. J., Microglia: biology and pathology Acta Neuropathologica 2010 119 1 89 105
    • (2010) Acta Neuropathologica , vol.119 , Issue.1 , pp. 89-105
    • Graeber, M.B.1    Streit, W.J.2
  • 93
    • 53949085542 scopus 로고    scopus 로고
    • Amyloid-beta peptide decreases glutamate uptake in cultured astrocytes: Involvement of oxidative stress and mitogen-activated protein kinase cascades
    • Matos M., Augusto E., Oliveira C. R., Agostinho P., Amyloid-beta peptide decreases glutamate uptake in cultured astrocytes: involvement of oxidative stress and mitogen-activated protein kinase cascades Neuroscience 2008 156 4 898 910
    • (2008) Neuroscience , vol.156 , Issue.4 , pp. 898-910
    • Matos, M.1    Augusto, E.2    Oliveira, C.R.3    Agostinho, P.4
  • 94
    • 33845954777 scopus 로고    scopus 로고
    • It may take inflammation, phosphorylation and ubiquitination to 'tangle' in Alzheimer's disease
    • DOI 10.1159/000095638
    • Arnaud L., Robakis N. K., Figueiredo-Pereira M. E., It may take inflammation, phosphorylation and ubiquitination to tangle in Alzheimer's disease Neurodegenerative Diseases 2007 3 6 313 319 (Pubitemid 46034207)
    • (2006) Neurodegenerative Diseases , vol.3 , Issue.6 , pp. 313-319
    • Arnaud, L.1    Robakis, N.K.2    Figueiredo-Pereira, M.E.3
  • 96
    • 79960826207 scopus 로고    scopus 로고
    • The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons
    • Yu W., Sun Y., Guo S., Lu B., The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons Human Molecular Genetics 2011 20 16 3227 3240
    • (2011) Human Molecular Genetics , vol.20 , Issue.16 , pp. 3227-3240
    • Yu, W.1    Sun, Y.2    Guo, S.3    Lu, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.