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Volumn 88, Issue 4, 2014, Pages 508-516

Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease

Author keywords

Alzheimer's disease; Lewy body disease; Synapse; Synuclein; Tau

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; GLUTAMATE RECEPTOR; OLIGOMER; TAU PROTEIN;

EID: 84897437047     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2014.01.015     Document Type: Review
Times cited : (187)

References (184)
  • 1
    • 79956076567 scopus 로고    scopus 로고
    • Introduction to the recommendations from the National Institute on Aging-Alzheimer's Association workgroups on diagnostic guidelines for Alzheimer's disease
    • C.R. Jack Jr., M.S. Albert, D.S. Knopman, G.M. McKhann, R.A. Sperling, and M.C. Carrillo et al. Introduction to the recommendations from the National Institute on Aging-Alzheimer's Association workgroups on diagnostic guidelines for Alzheimer's disease Alzheimers Dement 7 2011 257 262
    • (2011) Alzheimers Dement , vol.7 , pp. 257-262
    • Jack, Jr.C.R.1    Albert, M.S.2    Knopman, D.S.3    McKhann, G.M.4    Sperling, R.A.5    Carrillo, M.C.6
  • 2
    • 84856002055 scopus 로고    scopus 로고
    • National Institute on Aging-Alzheimer's Association guidelines for the neuropathologic assessment of Alzheimer's disease
    • B.T. Hyman, C.H. Phelps, T.G. Beach, E.H. Bigio, N.J. Cairns, and M.C. Carrillo et al. National Institute on Aging-Alzheimer's Association guidelines for the neuropathologic assessment of Alzheimer's disease Alzheimers Dement 8 2012 1 13
    • (2012) Alzheimers Dement , vol.8 , pp. 1-13
    • Hyman, B.T.1    Phelps, C.H.2    Beach, T.G.3    Bigio, E.H.4    Cairns, N.J.5    Carrillo, M.C.6
  • 3
    • 84873975872 scopus 로고    scopus 로고
    • Biomarkers for Alzheimer's disease in plasma, serum and blood - Conceptual and practical problems
    • D. Galasko, and T.E. Golde Biomarkers for Alzheimer's disease in plasma, serum and blood - conceptual and practical problems Alzheimers Res Ther 5 2013 10
    • (2013) Alzheimers Res Ther , vol.5 , pp. 10
    • Galasko, D.1    Golde, T.E.2
  • 4
    • 85027933989 scopus 로고    scopus 로고
    • Appropriate use criteria for amyloid PET: A report of the Amyloid Imaging Task Force, the Society of Nuclear Medicine and Molecular Imaging, and the Alzheimer's Association
    • K.A. Johnson, S. Minoshima, N.I. Bohnen, K.J. Donohoe, N.L. Foster, and P. Herscovitch et al. Appropriate use criteria for amyloid PET: a report of the Amyloid Imaging Task Force, the Society of Nuclear Medicine and Molecular Imaging, and the Alzheimer's Association Alzheimers Dement 9 2013 e1 e16
    • (2013) Alzheimers Dement , vol.9
    • Johnson, K.A.1    Minoshima, S.2    Bohnen, N.I.3    Donohoe, K.J.4    Foster, N.L.5    Herscovitch, P.6
  • 5
    • 84878439275 scopus 로고    scopus 로고
    • Analytical challenges in measurement of cerebrospinal fluid amyloid-beta1-42 and tau proteins as Alzheimer disease biomarkers
    • J.H. Kang, M. Korecka, J.B. Toledo, J.Q. Trojanowski, L.M. Shaw, and Clinical Utility Analytical challenges in measurement of cerebrospinal fluid amyloid-beta1-42 and tau proteins as Alzheimer disease biomarkers Clin Chem 2013 903 916
    • (2013) Clin Chem , pp. 903-916
    • Kang, J.H.1    Korecka, M.2    Toledo, J.B.3    Trojanowski, J.Q.4    Shaw, L.M.5    Utility, C.6
  • 7
  • 8
    • 84879829589 scopus 로고    scopus 로고
    • Biochemistry of amyloid beta-protein and amyloid deposits in Alzheimer disease
    • C.L. Masters, and D.J. Selkoe Biochemistry of amyloid beta-protein and amyloid deposits in Alzheimer disease Cold Spring Harb Perspect Med 2 2012 a006262
    • (2012) Cold Spring Harb Perspect Med , vol.2 , pp. 006262
    • Masters, C.L.1    Selkoe, D.J.2
  • 9
    • 84869887960 scopus 로고    scopus 로고
    • Structural features and cytotoxicity of amyloid oligomers: Implications in Alzheimer's disease and other diseases with amyloid deposits
    • M. Stefani Structural features and cytotoxicity of amyloid oligomers: implications in Alzheimer's disease and other diseases with amyloid deposits Prog Neurobiol 99 2012 226 245
    • (2012) Prog Neurobiol , vol.99 , pp. 226-245
    • Stefani, M.1
  • 10
    • 84887899951 scopus 로고    scopus 로고
    • Assessing the causes and consequences of co-polymerization in amyloid formation
    • C.J. Sarell, P.G. Stockley, and S.E. Radford Assessing the causes and consequences of co-polymerization in amyloid formation Prion 7 2013 359 368
    • (2013) Prion , vol.7 , pp. 359-368
    • Sarell, C.J.1    Stockley, P.G.2    Radford, S.E.3
  • 11
    • 84885352675 scopus 로고    scopus 로고
    • Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease
    • A.S. Chesser, S.M. Pritchard, and G.V. Johnson Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease Front Neurol 4 2013 122
    • (2013) Front Neurol , vol.4 , pp. 122
    • Chesser, A.S.1    Pritchard, S.M.2    Johnson, G.V.3
  • 12
    • 84871662000 scopus 로고    scopus 로고
    • Role of tau protein in neuronal damage in Alzheimer's disease and Down syndrome
    • A.M. Cardenas, A.O. Ardiles, N. Barraza, X. Baez-Matus, and P. Caviedes Role of tau protein in neuronal damage in Alzheimer's disease and Down syndrome Arch Med Res 43 2012 645 654
    • (2012) Arch Med Res , vol.43 , pp. 645-654
    • Cardenas, A.M.1    Ardiles, A.O.2    Barraza, N.3    Baez-Matus, X.4    Caviedes, P.5
  • 13
    • 84880188930 scopus 로고    scopus 로고
    • Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): Report of the Consortium on DLB International Workshop
    • I.G. McKeith Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the Consortium on DLB International Workshop J Alzheimers Dis 9 2006 417 423 (Pubitemid 44253336)
    • (2006) Journal of Alzheimer's Disease , vol.9 , Issue.SUPPL. 3 , pp. 417-423
    • McKeith, I.G.1
  • 14
    • 33645116252 scopus 로고    scopus 로고
    • Genetics of Parkinson disease: Paradigm shifts and future prospects
    • M.J. Farrer Genetics of Parkinson disease: paradigm shifts and future prospects Nat Rev Genet 7 2006 306 318
    • (2006) Nat Rev Genet , vol.7 , pp. 306-318
    • Farrer, M.J.1
  • 15
    • 77951185469 scopus 로고    scopus 로고
    • Genome-wide association study confirms SNPs in SNCA and the MAPT region as common risk factors for Parkinson disease
    • T.L. Edwards, W.K. Scott, C. Almonte, A. Burt, E.H. Powell, and G.W. Beecham et al. Genome-wide association study confirms SNPs in SNCA and the MAPT region as common risk factors for Parkinson disease Ann Hum Genet 74 2010 97 109
    • (2010) Ann Hum Genet , vol.74 , pp. 97-109
    • Edwards, T.L.1    Scott, W.K.2    Almonte, C.3    Burt, A.4    Powell, E.H.5    Beecham, G.W.6
  • 16
    • 84877589412 scopus 로고    scopus 로고
    • The central theme of Parkinson's disease: Alpha-synuclein
    • M. Ozansoy, and A.N. Basak The central theme of Parkinson's disease: alpha-synuclein Mol Neurobiol 47 2013 460 465
    • (2013) Mol Neurobiol , vol.47 , pp. 460-465
    • Ozansoy, M.1    Basak, A.N.2
  • 17
    • 77957905690 scopus 로고    scopus 로고
    • Genetic analysis of pathways to Parkinson disease
    • J. Hardy Genetic analysis of pathways to Parkinson disease Neuron 68 2010 201 206
    • (2010) Neuron , vol.68 , pp. 201-206
    • Hardy, J.1
  • 18
    • 84886043880 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • Alzheimer's Association Alzheimer's disease facts and figures Alzheimer's Dement 9 2013 1 71
    • (2013) Alzheimer's Dement , vol.9 , pp. 1-71
    • Association, A.1
  • 19
    • 84888228877 scopus 로고    scopus 로고
    • Amyloid-first and neurodegeneration-first profiles characterize incident amyloid PET positivity
    • C.R. Jack Jr., H.J. Wiste, S.D. Weigand, D.S. Knopman, V. Lowe, and P. Vemuri et al. Amyloid-first and neurodegeneration-first profiles characterize incident amyloid PET positivity Neurology 81 2013 1732 1740
    • (2013) Neurology , vol.81 , pp. 1732-1740
    • Jack, Jr.C.R.1    Wiste, H.J.2    Weigand, S.D.3    Knopman, D.S.4    Lowe, V.5    Vemuri, P.6
  • 20
    • 0031255112 scopus 로고    scopus 로고
    • Consensus recommendations for the postmortem diagnosis of Alzheimer disease from the National Institute on Aging and the Reagan Institute Working Group on diagnostic criteria for the neuropathological assessment of Alzheimer disease
    • B.T. Hyman, and J.Q. Trojanowski Consensus recommendations for the postmortem diagnosis of Alzheimer disease from the National Institute on Aging and the Reagan Institute Working Group on diagnostic criteria for the neuropathological assessment of Alzheimer disease J Neuropathol Exp Neurol 56 1997 1095 1097
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 1095-1097
    • Hyman, B.T.1    Trojanowski, J.Q.2
  • 21
    • 0037172826 scopus 로고    scopus 로고
    • Phases of Aβ-deposition in the human brain and its relevance for the development of AD
    • D.R. Thal, U. Rub, M. Orantes, and H. Braak Phases of A beta-deposition in the human brain and its relevance for the development of AD Neurology 58 2002 1791 1800 (Pubitemid 34663580)
    • (2002) Neurology , vol.58 , Issue.12 , pp. 1791-1800
    • Thal, D.R.1    Rub, U.2    Orantes, M.3    Braak, H.4
  • 22
    • 0025863618 scopus 로고
    • Neuropathological staging of Alzheimer-related changes
    • H. Braak, and E. Braak Neuropathological staging of Alzheimer-related changes Acta Neuropathol 82 1991 239 259
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 23
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • S.S. Mirra, A. Heyman, D. McKeel, S.M. Sumi, B.J. Crain, and L.M. Brownlee et al. The Consortium to Establish a Registry for Alzheimer's Disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease Neurology 41 1991 479 486
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6
  • 24
    • 0033919992 scopus 로고    scopus 로고
    • Lewy bodies in Alzheimer's Disease: A neuropathological review of 145 cases using α-synuclein immunohistochemistry
    • R.L. Hamilton Lewy bodies in Alzheimer's disease: a neuropathological review of 145 cases using alpha-synuclein immunohistochemistry Brain Pathol 10 2000 378 384 (Pubitemid 30431290)
    • (2000) Brain Pathology , vol.10 , Issue.3 , pp. 378-384
    • Hamilton, R.L.1
  • 25
    • 79960842310 scopus 로고    scopus 로고
    • Neuropathology underlying clinical variability in patients with synucleinopathies
    • G.M. Halliday, J.L. Holton, T. Revesz, and D.W. Dickson Neuropathology underlying clinical variability in patients with synucleinopathies Acta Neuropathol 122 2011 187 204
    • (2011) Acta Neuropathol , vol.122 , pp. 187-204
    • Halliday, G.M.1    Holton, J.L.2    Revesz, T.3    Dickson, D.W.4
  • 26
    • 0024406472 scopus 로고
    • A neuropathological subset of Alzheimer's disease with concomitant Lewy body disease and spongiform change
    • DOI 10.1007/BF00688209
    • L. Hansen, E. Masliah, and R. Terry A neuropathologic subset of Alzheimer's disease with concomitant Lewy body disease and spongiform change Acta Neuropathol 78 1989 194 201 (Pubitemid 19160924)
    • (1989) Acta Neuropathologica , vol.78 , Issue.2 , pp. 194-201
    • Hansen, L.A.1    Masliah, E.2    Terry, R.D.3    Mirra, S.S.4
  • 27
  • 28
    • 0028985267 scopus 로고
    • The precursor protein of non-Aβ component of Alzheimer's disease amyloid (NACP) is a presynaptic protein of the central nervous system
    • A. Iwai, E. Masliah, M. Yoshimoto, R. De Silva, N. Ge, and A. Kittel et al. The precursor protein of non-Aβ component of Alzheimer's disease amyloid (NACP) is a presynaptic protein of the central nervous system Neuron 14 1994 467 475
    • (1994) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    De Silva, R.4    Ge, N.5    Kittel, A.6
  • 29
    • 79955484414 scopus 로고    scopus 로고
    • Common variants at ABCA7, MS4A6A/MS4A4E, EPHA1, CD33 and CD2AP are associated with Alzheimer's disease
    • P. Hollingworth, D. Harold, R. Sims, A. Gerrish, J.C. Lambert, and M.M. Carrasquillo et al. Common variants at ABCA7, MS4A6A/MS4A4E, EPHA1, CD33 and CD2AP are associated with Alzheimer's disease Nat Genet 43 2011 429 435
    • (2011) Nat Genet , vol.43 , pp. 429-435
    • Hollingworth, P.1    Harold, D.2    Sims, R.3    Gerrish, A.4    Lambert, J.C.5    Carrasquillo, M.M.6
  • 30
    • 79955464911 scopus 로고    scopus 로고
    • Common variants at MS4A4/MS4A6E, CD2AP, CD33 and EPHA1 are associated with late-onset Alzheimer's disease
    • A.C. Naj, G. Jun, G.W. Beecham, L.S. Wang, B.N. Vardarajan, and J. Buros et al. Common variants at MS4A4/MS4A6E, CD2AP, CD33 and EPHA1 are associated with late-onset Alzheimer's disease Nat Genet 43 2011 436 441
    • (2011) Nat Genet , vol.43 , pp. 436-441
    • Naj, A.C.1    Jun, G.2    Beecham, G.W.3    Wang, L.S.4    Vardarajan, B.N.5    Buros, J.6
  • 32
    • 84881477292 scopus 로고    scopus 로고
    • Alzheimer's disease: From big data to mechanism
    • V. Swarup, and D.H. Geschwind Alzheimer's disease: from big data to mechanism Nature 500 2013 34 35
    • (2013) Nature , vol.500 , pp. 34-35
    • Swarup, V.1    Geschwind, D.H.2
  • 33
    • 84881474284 scopus 로고    scopus 로고
    • Alzheimer disease: The quest for Alzheimer disease genes - Focus on CSF tau
    • N. Ertekin-Taner Alzheimer disease: the quest for Alzheimer disease genes - focus on CSF tau Nat Rev Neurol 9 2013 368 370
    • (2013) Nat Rev Neurol , vol.9 , pp. 368-370
    • Ertekin-Taner, N.1
  • 34
    • 77954358003 scopus 로고    scopus 로고
    • Progressive accumulation of amyloid-beta oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins
    • E. Pham, L. Crews, K. Ubhi, L. Hansen, A. Adame, and A. Cartier et al. Progressive accumulation of amyloid-beta oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins FEBS J 277 2010 3051 3067
    • (2010) FEBS J , vol.277 , pp. 3051-3067
    • Pham, E.1    Crews, L.2    Ubhi, K.3    Hansen, L.4    Adame, A.5    Cartier, A.6
  • 36
    • 84897404115 scopus 로고
    • Confocal laser imaging of synapse-plaque relationships in Alzheimer disease
    • E. Masliah, L. Hansen, R. DeTeresa, and R. Terry Confocal laser imaging of synapse-plaque relationships in Alzheimer disease J Neuropathol Exp Neurol 49 1990 335
    • (1990) J Neuropathol Exp Neurol , vol.49 , pp. 335
    • Masliah, E.1    Hansen, L.2    Deteresa, R.3    Terry, R.4
  • 37
    • 84876689293 scopus 로고    scopus 로고
    • Synaptic changes in the dentate gyrus of APP/PS1 transgenic mice revealed by electron microscopy
    • L. Alonso-Nanclares, P. Merino-Serrais, S. Gonzalez, and J. DeFelipe Synaptic changes in the dentate gyrus of APP/PS1 transgenic mice revealed by electron microscopy J Neuropathol Exp Neurol 72 2013 386 395
    • (2013) J Neuropathol Exp Neurol , vol.72 , pp. 386-395
    • Alonso-Nanclares, L.1    Merino-Serrais, P.2    Gonzalez, S.3    Defelipe, J.4
  • 40
    • 84886592954 scopus 로고    scopus 로고
    • Predominant loss of glutamatergic terminal markers in a beta-amyloid peptide model of Alzheimer's disease
    • P.M. Canas, A.P. Simoes, R.J. Rodrigues, and R.A. Cunha Predominant loss of glutamatergic terminal markers in a beta-amyloid peptide model of Alzheimer's disease Neuropharmacology 76 Pt A 2014 51 56
    • (2014) Neuropharmacology , vol.76 , Issue.PART A , pp. 51-56
    • Canas, P.M.1    Simoes, A.P.2    Rodrigues, R.J.3    Cunha, R.A.4
  • 41
    • 84879879175 scopus 로고    scopus 로고
    • Altered synapses and gliotransmission in Alzheimer's disease and AD model mice
    • S. Mitew, M.T. Kirkcaldie, T.C. Dickson, and J.C. Vickers Altered synapses and gliotransmission in Alzheimer's disease and AD model mice Neurobiol Aging 34 2013 2341 2351
    • (2013) Neurobiol Aging , vol.34 , pp. 2341-2351
    • Mitew, S.1    Kirkcaldie, M.T.2    Dickson, T.C.3    Vickers, J.C.4
  • 43
    • 34247611481 scopus 로고    scopus 로고
    • Synaptic alterations in CA1 in mild Alzheimer disease and mild cognitive impairment
    • DOI 10.1212/01.wnl.0000260698.46517.8f, PII 0000611420070501000011
    • S.W. Scheff, D.A. Price, F.A. Schmitt, S.T. DeKosky, and E.J. Mufson Synaptic alterations in CA1 in mild Alzheimer disease and mild cognitive impairment Neurology 68 2007 1501 1508 (Pubitemid 46685921)
    • (2007) Neurology , vol.68 , Issue.18 , pp. 1501-1508
    • Scheff, S.W.1    Price, D.A.2    Schmitt, F.A.3    Dekosky, S.T.4    Mufson, E.J.5
  • 44
    • 84875262338 scopus 로고    scopus 로고
    • Synaptic genes are extensively downregulated across multiple brain regions in normal human aging and Alzheimer's disease
    • N.C. Berchtold, P.D. Coleman, D.H. Cribbs, J. Rogers, D.L. Gillen, and C.W. Cotman Synaptic genes are extensively downregulated across multiple brain regions in normal human aging and Alzheimer's disease Neurobiol Aging 34 2013 1653 1661
    • (2013) Neurobiol Aging , vol.34 , pp. 1653-1661
    • Berchtold, N.C.1    Coleman, P.D.2    Cribbs, D.H.3    Rogers, J.4    Gillen, D.L.5    Cotman, C.W.6
  • 46
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • R.D. Terry, E. Masliah, D.P. Salmon, N. Butters, R. DeTeresa, and R. Hill et al. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment Ann Neurol 30 1991 572 580
    • (1991) Ann Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    Deteresa, R.5    Hill, R.6
  • 47
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • S. DeKosky, and S. Scheff Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity Ann Neurol 27 1990 457 464 (Pubitemid 20149963)
    • (1990) Annals of Neurology , vol.27 , Issue.5 , pp. 457-464
    • DeKosky, S.T.1    Scheff, S.W.2
  • 48
    • 0030513943 scopus 로고    scopus 로고
    • Structural correlates of cognition in dementia: Quantification and assessment of synapse change
    • DOI 10.1006/neur.1996.0056
    • S.T. DeKosky, S.W. Scheff, and S.D. Styren Structural correlates of cognition in dementia: quantification and assessment of synapse change Neurodegeneration 5 1996 417 421 (Pubitemid 27077903)
    • (1996) Neurodegeneration , vol.5 , Issue.4 , pp. 417-421
    • DeKosky, S.T.1    Scheff, S.W.2    Styren, S.D.3
  • 49
    • 0025217385 scopus 로고
    • Quantitative assessment of cortical synaptic density in Alzheimer's disease
    • DOI 10.1016/0197-4580(90)90059-9
    • S.W. Scheff, S.T. DeKosky, and D.A. Price Quantitative assessment of cortical synaptic density in Alzheimer's disease Neurobiol Aging 11 1990 29 37 (Pubitemid 20097857)
    • (1990) Neurobiology of Aging , vol.11 , Issue.1 , pp. 29-37
    • Scheff, S.W.1    DeKosky, S.T.2    Price, D.A.3
  • 50
    • 0027261146 scopus 로고
    • Quantitative assessment of synaptic density in the entorhinal cortex in Alzheimer's disease
    • S. Scheff, D. Sparks, and D. Price Quantitative assessment of synaptic density in the entorhinal cortex in Alzheimer's disease FASEB J 34 1993 356 361 (Pubitemid 23259604)
    • (1993) Annals of Neurology , vol.34 , Issue.3 , pp. 356-361
    • Scheff, S.W.1    Sparks, D.L.2    Price, D.A.3
  • 51
    • 0027140678 scopus 로고
    • The role of synaptic pathology in the mechanisms of dementia in Alzheimer's disease
    • E. Masliah, and R. Terry The role of synaptic pathology in the mechanisms of dementia in Alzheimer's disease Clin Neurosci 1 1994 192 198
    • (1994) Clin Neurosci , vol.1 , pp. 192-198
    • Masliah, E.1    Terry, R.2
  • 53
    • 0025217385 scopus 로고
    • Quantitative assessment of cortical synaptic density in Alzheimer's disease
    • DOI 10.1016/0197-4580(90)90059-9
    • S. Scheff, S. DeKosky, and D. Price Quantitative assessment of cortical synaptic density in Alzheimer's disease Neurobiol Aging 11 1990 29 37 (Pubitemid 20097857)
    • (1990) Neurobiology of Aging , vol.11 , Issue.1 , pp. 29-37
    • Scheff, S.W.1    DeKosky, S.T.2    Price, D.A.3
  • 54
    • 0027400026 scopus 로고
    • Synapse loss in the temporal lobe in Alzheimer's disease
    • DOI 10.1002/ana.410330209
    • S. Scheff, and D. Price Synapse loss in the temporal lobe in Alzheimer's disease Ann Neurol 33 1993 190 199 (Pubitemid 23039928)
    • (1993) Annals of Neurology , vol.33 , Issue.2 , pp. 190-199
    • Scheff, S.W.1    Price, D.A.2
  • 55
    • 84871922036 scopus 로고    scopus 로고
    • Deciphering the mechanism underlying late-onset Alzheimer disease
    • D. Krstic, and I. Knuesel Deciphering the mechanism underlying late-onset Alzheimer disease Nat Rev Neurol 9 2013 25 34
    • (2013) Nat Rev Neurol , vol.9 , pp. 25-34
    • Krstic, D.1    Knuesel, I.2
  • 56
    • 84897467872 scopus 로고    scopus 로고
    • Genetically engineered mouse models of neurodegenerative disorders
    • V.N. Uversky, Kluwer Academic/Plenum New York
    • E. Masliah, and L. Crews Genetically engineered mouse models of neurodegenerative disorders V.N. Uversky, Protein misfolding, aggregation and conformational diseases 2006 Kluwer Academic/Plenum New York
    • (2006) Protein Misfolding, Aggregation and Conformational Diseases
    • Masliah, E.1    Crews, L.2
  • 57
    • 0028985799 scopus 로고
    • Role of the beta-amyloid protein in Alzheimer's disease
    • S.S. Sisodia, and D.L. Price Role of the beta-amyloid protein in Alzheimer's disease FASEB J 9 1995 366 370
    • (1995) FASEB J , vol.9 , pp. 366-370
    • Sisodia, S.S.1    Price, D.L.2
  • 58
    • 0024314702 scopus 로고
    • Amyloid β protein precursor and the pathogenesis of Alzheimer's disease
    • DOI 10.1016/0092-8674(89)90093-7
    • D. Selkoe Amyloid b protein precursor and the pathogenesis of Alzheimer's disease Cell 58 1989 611 612 (Pubitemid 19210954)
    • (1989) Cell , vol.58 , Issue.4 , pp. 611-612
    • Selkoe, D.J.1
  • 59
    • 70349963236 scopus 로고
    • Amyloid β-protein deposition as a seminal pathogenic event in AD: An hypothesis
    • D. Selkoe Amyloid β-protein deposition as a seminal pathogenic event in AD: an hypothesis Neurobiol Aging 11 1990 299
    • (1990) Neurobiol Aging , vol.11 , pp. 299
    • Selkoe, D.1
  • 60
    • 0027367764 scopus 로고
    • Physiological production of the β-amyloid protein and the mechanism of Alzheimer's disease
    • DOI 10.1016/0166-2236(93)90008-A
    • D. Selkoe Physiological production of the β-amyloid protein and the mechanisms of Alzheimer's disease Trends Neurosci 16 1993 403 409 (Pubitemid 23283401)
    • (1993) Trends in Neurosciences , vol.16 , Issue.10 , pp. 403-409
    • Selkoe, D.J.1
  • 61
    • 0034744296 scopus 로고    scopus 로고
    • TGF-β1 promotes microglial amyloid-β clearance and reduces plaque burden in transgenic mice
    • DOI 10.1038/87945
    • T. Wyss-Coray, C. Lin, F. Yan, G.Q. Yu, M. Rohde, and L. McConlogue et al. TGF-beta1 promotes microglial amyloid-beta clearance and reduces plaque burden in transgenic mice Nat Med 7 2001 612 618 (Pubitemid 32448330)
    • (2001) Nature Medicine , vol.7 , Issue.5 , pp. 612-618
    • Wyss-Coray, T.1    Lin, C.2    Yan, F.3    Yu, G.-Q.4    Rohde, M.5    Mcconlogue, L.6    Masliah, E.7    Mucke, L.8
  • 62
    • 38349046973 scopus 로고    scopus 로고
    • Autophagy, amyloidogenesis and Alzheimer disease
    • R.A. Nixon Autophagy, amyloidogenesis and Alzheimer disease J Cell Sci 120 2007 4081 4091
    • (2007) J Cell Sci , vol.120 , pp. 4081-4091
    • Nixon, R.A.1
  • 63
    • 0036173420 scopus 로고    scopus 로고
    • ADDLs and protofibrils - The missing links
    • W.L. Klein ADDLs and protofibrils - the missing links Neurobiol Aging 23 2002 231 235
    • (2002) Neurobiol Aging , vol.23 , pp. 231-235
    • Klein, W.L.1
  • 64
    • 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
    • W.L. Klein, G.A. Krafft, and C.E. Finch Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum Trends Neurosci 24 2001 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
  • 65
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers in the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • DOI 10.2174/0929866043407174
    • D.M. Walsh, and D.J. Selkoe Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration Protein Pept Lett 11 2004 213 228 (Pubitemid 38689025)
    • (2004) Protein and Peptide Letters , vol.11 , Issue.3 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 66
    • 15944426127 scopus 로고    scopus 로고
    • Amyloid accumulation and pathogenesis of Alzheimer's disease: Significance of monomeric, oligomeric and fibrillar Abeta
    • C.C. Glabe Amyloid accumulation and pathogenesis of Alzheimer's disease: significance of monomeric, oligomeric and fibrillar Abeta Subcell Biochem 38 2005 167 177
    • (2005) Subcell Biochem , vol.38 , pp. 167-177
    • Glabe, C.C.1
  • 67
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • C.G. Glabe Structural classification of toxic amyloid oligomers J Biol Chem 283 2008 29639 29643
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 68
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • M.P. Lambert, A.K. Barlow, B.A. Chromy, C. Edwards, R. Freed, and M. Liosatos et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins Proc Natl Acad Sci USA 95 1998 6448 6453
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 69
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior
    • D.J. Selkoe Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior Behav Brain Res 192 2008 106 113
    • (2008) Behav Brain Res , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 70
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • DOI 10.1146/annurev.neuro.26.010302.081142
    • B. Caughey, and P.T. Lansbury Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders Annu Rev Neurosci 26 2003 267 298 (Pubitemid 37064935)
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 71
    • 0032084472 scopus 로고    scopus 로고
    • Structural and kinetic features of amyloid β-protein fibrillogenesis
    • D.B. Teplow Structural and kinetic features of amyloid beta-protein fibrillogenesis Amyloid 5 1998 121 142 (Pubitemid 128691229)
    • (1998) Amyloid , vol.5 , Issue.2 , pp. 121-142
    • Teplow, D.B.1
  • 72
    • 63849197629 scopus 로고    scopus 로고
    • Amyloid beta-protein assembly and Alzheimer disease
    • R. Roychaudhuri, M. Yang, M.M. Hoshi, and D.B. Teplow Amyloid beta-protein assembly and Alzheimer disease J Biol Chem 284 2009 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
  • 73
    • 84872552899 scopus 로고    scopus 로고
    • Synaptotoxic amyloid-beta oligomers: A molecular basis for the cause, diagnosis, and treatment of Alzheimer's disease?
    • W.L. Klein Synaptotoxic amyloid-beta oligomers: a molecular basis for the cause, diagnosis, and treatment of Alzheimer's disease? J Alzheimers Dis 33 Suppl. 1 2013 S49 S65
    • (2013) J Alzheimers Dis , vol.33 , Issue.SUPPL. 1
    • Klein, W.L.1
  • 74
    • 84880759156 scopus 로고    scopus 로고
    • Neurotoxicity of amyloid beta-protein: Synaptic and network dysfunction
    • L. Mucke, and D.J. Selkoe Neurotoxicity of amyloid beta-protein: synaptic and network dysfunction Cold Spring Harb Perspect Med 2 2012 a006338
    • (2012) Cold Spring Harb Perspect Med , vol.2 , pp. 006338
    • Mucke, L.1    Selkoe, D.J.2
  • 75
    • 84894039447 scopus 로고    scopus 로고
    • Structural diversity of Alzheimer's disease amyloid-beta dimers and their role in oligomerization and fibril formation
    • 10.3233/JAD-131589
    • I.F. Tsigelny, Y. Sharikov, V.L. Kouznetsova, J.P. Greenberg, W. Wrasidlo, and T. Gonzalez et al. Structural diversity of Alzheimer's disease amyloid-beta dimers and their role in oligomerization and fibril formation J Alzheimers Dis 2013 10.3233/JAD-131589
    • (2013) J Alzheimers Dis
    • Tsigelny, I.F.1    Sharikov, Y.2    Kouznetsova, V.L.3    Greenberg, J.P.4    Wrasidlo, W.5    Gonzalez, T.6
  • 76
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Abeta oligomer and Alzheimer's disease: An emperor in need of clothes
    • I. Benilova, E. Karran, and B. De Strooper The toxic Abeta oligomer and Alzheimer's disease: an emperor in need of clothes Nat Neurosci 15 2012 349 357
    • (2012) Nat Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 77
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • S. Lesne, M.T. Koh, L. Kotilinek, R. Kayed, C.G. Glabe, and A. Yang et al. A specific amyloid-beta protein assembly in the brain impairs memory Nature 440 2006 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
  • 78
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid beta-protein on hippocampal synaptic plasticity: A potent role for trimers
    • M. Townsend, G.M. Shankar, T. Mehta, D.M. Walsh, and D.J. Selkoe Effects of secreted oligomers of amyloid beta-protein on hippocampal synaptic plasticity: a potent role for trimers J Physiol 572 2006 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
  • 79
    • 84878799974 scopus 로고    scopus 로고
    • A new player in the synaptopathy of Alzheimer's disease - Arc/arg 3.1
    • T.L. Kerrigan, and A.D. Randall A new player in the synaptopathy of Alzheimer's disease - arc/arg 3.1 Front Neurol 4 2013 9
    • (2013) Front Neurol , vol.4 , pp. 9
    • Kerrigan, T.L.1    Randall, A.D.2
  • 80
    • 42949155299 scopus 로고    scopus 로고
    • Amyloid beta protein dimer-containing human CSF disrupts synaptic plasticity: Prevention by systemic passive immunization
    • I. Klyubin, V. Betts, A.T. Welzel, K. Blennow, H. Zetterberg, and A. Wallin et al. Amyloid beta protein dimer-containing human CSF disrupts synaptic plasticity: prevention by systemic passive immunization J Neurosci 28 2008 4231 4237
    • (2008) J Neurosci , vol.28 , pp. 4231-4237
    • Klyubin, I.1    Betts, V.2    Welzel, A.T.3    Blennow, K.4    Zetterberg, H.5    Wallin, A.6
  • 81
    • 33846633336 scopus 로고    scopus 로고
    • Aβ oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • DOI 10.1523/JNEUROSCI.3501-06.2007
    • P.N. Lacor, M.C. Buniel, P.W. Furlow, A.S. Clemente, P.T. Velasco, and M. Wood et al. Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease J Neurosci 27 2007 796 807 (Pubitemid 46174498)
    • (2007) Journal of Neuroscience , vol.27 , Issue.4 , pp. 796-807
    • Lacor, P.N.1    Buniel, M.C.2    Furlow, P.W.3    Clemente, A.S.4    Velasco, P.T.5    Wood, M.6    Viola, K.L.7    Klein, W.L.8
  • 82
    • 7244223228 scopus 로고    scopus 로고
    • Snaptic changes in alzheimer's disease: Increased amyloid-β and gliosis in surviving terminals is accompanied by decreased PSD-95 fluorescence
    • K.H. Gylys, J.A. Fein, F. Yang, D.J. Wiley, C.A. Miller, and G.M. Cole Synaptic changes in Alzheimer's disease: increased amyloid-beta and gliosis in surviving terminals is accompanied by decreased PSD-95 fluorescence Am J Pathol 165 2004 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
  • 84
    • 62649174753 scopus 로고    scopus 로고
    • Oligomeric amyloid beta associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques
    • R.M. Koffie, M. Meyer-Luehmann, T. Hashimoto, K.W. Adams, M.L. Mielke, and M. Garcia-Alloza et al. Oligomeric amyloid beta associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques Proc Natl Acad Sci USA 106 2009 4012 4017
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4012-4017
    • Koffie, R.M.1    Meyer-Luehmann, M.2    Hashimoto, T.3    Adams, K.W.4    Mielke, M.L.5    Garcia-Alloza, M.6
  • 85
    • 73949103706 scopus 로고    scopus 로고
    • Decreased levels of PSD95 and two associated proteins and increased levels of BCl2 and caspase 3 in hippocampus from subjects with amnestic mild cognitive impairment: Insights into their potential roles for loss of synapses and memory, accumulation of Abeta, and neurodegeneration in a prodromal stage of Alzheimer's disease
    • R. Sultana, W.A. Banks, and D.A. Butterfield Decreased levels of PSD95 and two associated proteins and increased levels of BCl2 and caspase 3 in hippocampus from subjects with amnestic mild cognitive impairment: insights into their potential roles for loss of synapses and memory, accumulation of Abeta, and neurodegeneration in a prodromal stage of Alzheimer's disease J Neurosci Res 88 2010 469 477
    • (2010) J Neurosci Res , vol.88 , pp. 469-477
    • Sultana, R.1    Banks, W.A.2    Butterfield, D.A.3
  • 87
    • 84887973227 scopus 로고    scopus 로고
    • Treating Alzheimer's disease with monoclonal antibodies: Current status and outlook for the future
    • N.D. Prins, and P. Scheltens Treating Alzheimer's disease with monoclonal antibodies: current status and outlook for the future Alzheimers Res Ther 5 2013 56
    • (2013) Alzheimers Res Ther , vol.5 , pp. 56
    • Prins, N.D.1    Scheltens, P.2
  • 88
    • 76849091134 scopus 로고    scopus 로고
    • Can Alzheimer disease be prevented by amyloid-beta immunotherapy
    • C.A. Lemere, and E. Masliah Can Alzheimer disease be prevented by amyloid-beta immunotherapy Nat Rev Neurol 6 2010 108 119
    • (2010) Nat Rev Neurol , vol.6 , pp. 108-119
    • Lemere, C.A.1    Masliah, E.2
  • 89
    • 84886641553 scopus 로고    scopus 로고
    • Dysfunctional synapse in Alzheimer's disease - A focus on NMDA receptors
    • S.I. Mota, I.L. Ferreira, and A.C. Rego Dysfunctional synapse in Alzheimer's disease - a focus on NMDA receptors Neuropharmacology 76 Pt A 2014 16 26
    • (2014) Neuropharmacology , vol.76 , Issue.PART A , pp. 16-26
    • Mota, S.I.1    Ferreira, I.L.2    Rego, A.C.3
  • 90
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss
    • DOI 10.1016/j.neuron.2006.10.035, PII S0896627306008725
    • H. Hsieh, J. Boehm, C. Sato, T. Iwatsubo, T. Tomita, and S. Sisodia et al. AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss Neuron 52 2006 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
  • 91
    • 33750339228 scopus 로고    scopus 로고
    • A network dysfunction perspective on neurodegenerative diseases
    • DOI 10.1038/nature05289, PII NATURE05289
    • J.J. Palop, J. Chin, and L. Mucke A network dysfunction perspective on neurodegenerative diseases Nature 443 2006 768 773 (Pubitemid 44622680)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 768-773
    • Palop, J.J.1    Chin, J.2    Mucke, L.3
  • 92
    • 84934441665 scopus 로고    scopus 로고
    • Quantifying biomarkers of cognitive dysfunction and neuronal network hyperexcitability in mouse models of Alzheimer's disease: Depletion of calcium-dependent proteins and inhibitory hippocampal remodeling
    • J.J. Palop, L. Mucke, and E.D. Roberson Quantifying biomarkers of cognitive dysfunction and neuronal network hyperexcitability in mouse models of Alzheimer's disease: depletion of calcium-dependent proteins and inhibitory hippocampal remodeling Methods Mol Biol 670 2011 245 262
    • (2011) Methods Mol Biol , vol.670 , pp. 245-262
    • Palop, J.J.1    Mucke, L.2    Roberson, E.D.3
  • 93
    • 77953658771 scopus 로고    scopus 로고
    • Deleterious effects of amyloid beta oligomers acting as an extracellular scaffold for mGluR5
    • M. Renner, P.N. Lacor, P.T. Velasco, J. Xu, A. Contractor, and W.L. Klein et al. Deleterious effects of amyloid beta oligomers acting as an extracellular scaffold for mGluR5 Neuron 66 2010 739 754
    • (2010) Neuron , vol.66 , pp. 739-754
    • Renner, M.1    Lacor, P.N.2    Velasco, P.T.3    Xu, J.4    Contractor, A.5    Klein, W.L.6
  • 94
    • 78650970378 scopus 로고    scopus 로고
    • Reversing EphB2 depletion rescues cognitive functions in Alzheimer model
    • M. Cisse, B. Halabisky, J. Harris, N. Devidze, D.B. Dubal, and B. Sun et al. Reversing EphB2 depletion rescues cognitive functions in Alzheimer model Nature 469 2011 47 52
    • (2011) Nature , vol.469 , pp. 47-52
    • Cisse, M.1    Halabisky, B.2    Harris, J.3    Devidze, N.4    Dubal, D.B.5    Sun, B.6
  • 95
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • J. Lauren, D.A. Gimbel, H.B. Nygaard, J.W. Gilbert, and S.M. Strittmatter Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers Nature 457 2009 1128 1132
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 97
    • 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
    • J. Chin, J.J. Palop, G.Q. Yu, N. Kojima, E. Masliah, and L. Mucke Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice J Neurosci 24 2004 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
  • 98
    • 84874585213 scopus 로고    scopus 로고
    • Amyloid-beta induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease
    • J.W. Um, and S.M. Strittmatter Amyloid-beta induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease Prion 7 2013 37 41
    • (2013) Prion , vol.7 , pp. 37-41
    • Um, J.W.1    Strittmatter, S.M.2
  • 99
    • 84884200967 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a co-receptor for Alzheimer abeta oligomer bound to cellular prion protein
    • J.W. Um, A.C. Kaufman, M. Kostylev, J.K. Heiss, M. Stagi, and H. Takahashi et al. Metabotropic glutamate receptor 5 is a co-receptor for Alzheimer abeta oligomer bound to cellular prion protein Neuron 79 2013 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    Takahashi, H.6
  • 100
    • 84879979361 scopus 로고    scopus 로고
    • Deregulation of excitatory neurotransmission underlying synapse failure in Alzheimer's disease
    • A.C. Paula-Lima, J. Brito-Moreira, and S.T. Ferreira Deregulation of excitatory neurotransmission underlying synapse failure in Alzheimer's disease J Neurochem 126 2013 191 202
    • (2013) J Neurochem , vol.126 , pp. 191-202
    • Paula-Lima, A.C.1    Brito-Moreira, J.2    Ferreira, S.T.3
  • 101
    • 84876850027 scopus 로고    scopus 로고
    • Pathogenesis of Abeta oligomers in synaptic failure
    • S. Sivanesan, A. Tan, and J. Rajadas Pathogenesis of Abeta oligomers in synaptic failure Curr Alzheimer Res 10 2013 316 323
    • (2013) Curr Alzheimer Res , vol.10 , pp. 316-323
    • Sivanesan, S.1    Tan, A.2    Rajadas, J.3
  • 102
    • 84879732252 scopus 로고    scopus 로고
    • Abeta induces astrocytic glutamate release, extrasynaptic NMDA receptor activation, and synaptic loss
    • M. Talantova, S. Sanz-Blasco, X. Zhang, P. Xia, M.W. Akhtar, and S. Okamoto et al. Abeta induces astrocytic glutamate release, extrasynaptic NMDA receptor activation, and synaptic loss Proc Natl Acad Sci USA 110 2013 E2518 E2527
    • (2013) Proc Natl Acad Sci USA , vol.110
    • Talantova, M.1    Sanz-Blasco, S.2    Zhang, X.3    Xia, P.4    Akhtar, M.W.5    Okamoto, S.6
  • 103
    • 84884630099 scopus 로고    scopus 로고
    • Human LilrB2 is a beta-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer's model
    • T. Kim, G.S. Vidal, M. Djurisic, C.M. William, M.E. Birnbaum, and K.C. Garcia et al. Human LilrB2 is a beta-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer's model Science 341 2013 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    Garcia, K.C.6
  • 104
    • 84886509822 scopus 로고    scopus 로고
    • A role for tau at the synapse in Alzheimer's disease pathogenesis
    • A.M. Pooler, W. Noble, and D.P. Hanger A role for tau at the synapse in Alzheimer's disease pathogenesis Neuropharmacology 76 Pt A 2014 1 8
    • (2014) Neuropharmacology , vol.76 , Issue.PART A , pp. 1-8
    • Pooler, A.M.1    Noble, W.2    Hanger, D.P.3
  • 105
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models
    • L.M. Ittner, Y.D. Ke, F. Delerue, M. Bi, A. Gladbach, and J. van Eersel et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models Cell 142 2010 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    Van Eersel, J.6
  • 107
    • 84857073309 scopus 로고    scopus 로고
    • Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease
    • K. Shahpasand, I. Uemura, T. Saito, T. Asano, K. Hata, and K. Shibata et al. Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease J Neurosci 32 2012 2430 2441
    • (2012) J Neurosci , vol.32 , pp. 2430-2441
    • Shahpasand, K.1    Uemura, I.2    Saito, T.3    Asano, T.4    Hata, K.5    Shibata, K.6
  • 108
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • DOI 10.1523/JNEUROSCI.2361-07.2007
    • A.A. Asuni, A. Boutajangout, D. Quartermain, and E.M. Sigurdsson Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements J Neurosci 27 2007 9115 9129 (Pubitemid 47312068)
    • (2007) Journal of Neuroscience , vol.27 , Issue.34 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 109
    • 77956587739 scopus 로고    scopus 로고
    • Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines
    • H. Zempel, E. Thies, E. Mandelkow, and E.M. Mandelkow Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines J Neurosci 30 2010 11938 11950
    • (2010) J Neurosci , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 110
    • 84887828122 scopus 로고    scopus 로고
    • Amyloid-beta oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin
    • H. Zempel, J. Luedtke, Y. Kumar, J. Biernat, H. Dawson, and E. Mandelkow et al. Amyloid-beta oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin EMBO J 32 2013 2920 2937
    • (2013) EMBO J , vol.32 , pp. 2920-2937
    • Zempel, H.1    Luedtke, J.2    Kumar, Y.3    Biernat, J.4    Dawson, H.5    Mandelkow, E.6
  • 111
    • 84882940367 scopus 로고    scopus 로고
    • Synaptic protein alpha1-takusan mitigates amyloid-beta-induced synaptic loss via interaction with tau and postsynaptic density-95 at postsynaptic sites
    • N. Nakanishi, S.D. Ryan, X. Zhang, A. Khan, T. Holland, and E.G. Cho et al. Synaptic protein alpha1-takusan mitigates amyloid-beta-induced synaptic loss via interaction with tau and postsynaptic density-95 at postsynaptic sites J Neurosci 33 2013 14170 14183
    • (2013) J Neurosci , vol.33 , pp. 14170-14183
    • Nakanishi, N.1    Ryan, S.D.2    Zhang, X.3    Khan, A.4    Holland, T.5    Cho, E.G.6
  • 112
    • 84879656519 scopus 로고    scopus 로고
    • Abnormal interaction of oligomeric amyloid-beta with phosphorylated tau: Implications to synaptic dysfunction and neuronal damage
    • M. Manczak, and P.H. Reddy Abnormal interaction of oligomeric amyloid-beta with phosphorylated tau: implications to synaptic dysfunction and neuronal damage J Alzheimers Dis 36 2013 285 295
    • (2013) J Alzheimers Dis , vol.36 , pp. 285-295
    • Manczak, M.1    Reddy, P.H.2
  • 113
    • 77951776829 scopus 로고    scopus 로고
    • Alzheimer's disease: Strategies for disease modification
    • M. Citron Alzheimer's disease: strategies for disease modification Nat Rev Drug Discov 9 2010 387 398
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 387-398
    • Citron, M.1
  • 115
    • 84858195896 scopus 로고    scopus 로고
    • New pharmacological strategies for treatment of Alzheimer's disease: Focus on disease modifying drugs
    • S. Salomone, F. Caraci, G.M. Leggio, J. Fedotova, and F. Drago New pharmacological strategies for treatment of Alzheimer's disease: focus on disease modifying drugs Br J Clin Pharmacol 73 2012 504 517
    • (2012) Br J Clin Pharmacol , vol.73 , pp. 504-517
    • Salomone, S.1    Caraci, F.2    Leggio, G.M.3    Fedotova, J.4    Drago, F.5
  • 117
    • 0028985267 scopus 로고
    • The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • A. Iwai, E. Masliah, M. Yoshimoto, N. Ge, L. Flanagan, and H.A. de Silva et al. The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system Neuron 14 1995 467 475
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    Ge, N.4    Flanagan, L.5    De Silva, H.A.6
  • 118
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • DOI 10.1016/0014-5793(94)00395-5
    • R. Jakes, M.G. Spillantini, and M. Goedert Identification of two distinct synucleins from human brain FEBS Lett 345 1994 27 32 (Pubitemid 24154659)
    • (1994) FEBS Letters , vol.345 , Issue.1 , pp. 27-32
    • Jakes, R.1    Spillantini, M.G.2    Goedert, M.3
  • 119
    • 0031051539 scopus 로고    scopus 로고
    • Delayed localization of synelfin (synuclein, NACP) to presynaptic terminals in cultured rat hippocampal neurons
    • DOI 10.1016/S0165-3806(96)00210-6, PII S0165380696002106
    • G.S. Withers, J.M. George, G.A. Banker, and D.F. Clayton Delayed localization of synelfin (synuclein, NACP) to presynaptic terminals in cultured rat hippocampal neurons Brain Res Dev Brain Res 99 1997 87 94 (Pubitemid 27112848)
    • (1997) Developmental Brain Research , vol.99 , Issue.1 , pp. 87-94
    • Withers, G.S.1    George, J.M.2    Banker, G.A.3    Clayton, D.F.4
  • 120
    • 0034280435 scopus 로고    scopus 로고
    • Subcellular localization of wild-type and Parkinson's disease-associated mutant alpha-synuclein in human and transgenic mouse brain
    • P.J. Kahle, M. Neumann, L. Ozmen, V. Muller, H. Jacobsen, and A. Schindzielorz et al. Subcellular localization of wild-type and Parkinson's disease-associated mutant alpha-synuclein in human and transgenic mouse brain J Neurosci 20 2000 6365 6373
    • (2000) J Neurosci , vol.20 , pp. 6365-6373
    • Kahle, P.J.1    Neumann, M.2    Ozmen, L.3    Muller, V.4    Jacobsen, H.5    Schindzielorz, A.6
  • 121
    • 61949430447 scopus 로고    scopus 로고
    • Alpha-synuclein is localized in a subpopulation of rat brain synaptic vesicles
    • S.J. Lee, H. Jeon, and K.V. Kandror Alpha-synuclein is localized in a subpopulation of rat brain synaptic vesicles Acta Neurobiol Exp 68 2008 509 515
    • (2008) Acta Neurobiol Exp , vol.68 , pp. 509-515
    • Lee, S.J.1    Jeon, H.2    Kandror, K.V.3
  • 122
    • 56049093847 scopus 로고    scopus 로고
    • Semi-quantitative analysis of alpha-synuclein in subcellular pools of rat brain neurons: An immunogold electron microscopic study using a C-terminal specific monoclonal antibody
    • L. Zhang, C. Zhang, Y. Zhu, Q. Cai, P. Chan, and K. Ueda et al. Semi-quantitative analysis of alpha-synuclein in subcellular pools of rat brain neurons: an immunogold electron microscopic study using a C-terminal specific monoclonal antibody Brain Res 1244 2008 40 52
    • (2008) Brain Res , vol.1244 , pp. 40-52
    • Zhang, L.1    Zhang, C.2    Zhu, Y.3    Cai, Q.4    Chan, P.5    Ueda, K.6
  • 123
    • 77953796839 scopus 로고    scopus 로고
    • A pathologic cascade leading to synaptic dysfunction in alpha-synuclein-induced neurodegeneration
    • D.A. Scott, I. Tabarean, Y. Tang, A. Cartier, E. Masliah, and S. Roy A pathologic cascade leading to synaptic dysfunction in alpha-synuclein-induced neurodegeneration J Neurosci 30 2010 8083 8095
    • (2010) J Neurosci , vol.30 , pp. 8083-8095
    • Scott, D.A.1    Tabarean, I.2    Tang, Y.3    Cartier, A.4    Masliah, E.5    Roy, S.6
  • 125
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • R. Kruger, W. Kuhn, T. Muller, D. Woitalla, M. Graeber, and S. Kosel et al. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease Nat Genet 18 1998 106 108
    • (1998) Nat Genet , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5    Kosel, S.6
  • 129
    • 70549088602 scopus 로고    scopus 로고
    • Genome-wide association study reveals genetic risk underlying Parkinson's disease
    • J. Simon-Sanchez, C. Schulte, J.M. Bras, M. Sharma, J.R. Gibbs, and D. Berg et al. Genome-wide association study reveals genetic risk underlying Parkinson's disease Nat Genet 41 2009 1308 1312
    • (2009) Nat Genet , vol.41 , pp. 1308-1312
    • Simon-Sanchez, J.1    Schulte, C.2    Bras, J.M.3    Sharma, M.4    Gibbs, J.R.5    Berg, D.6
  • 130
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease
    • DOI 10.1038/3311
    • K.A. Conway, J.D. Harper, and P.T. Lansbury Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease Nat Med 4 1998 1318 1320 (Pubitemid 28512115)
    • (1998) Nature Medicine , vol.4 , Issue.11 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 131
    • 55949104903 scopus 로고    scopus 로고
    • Mechanism of alpha-synuclein oligomerization and membrane interaction: Theoretical approach to unstructured proteins studies
    • I.F. Tsigelny, Y. Sharikov, M.A. Miller, and E. Masliah Mechanism of alpha-synuclein oligomerization and membrane interaction: theoretical approach to unstructured proteins studies Nanomedicine 4 2008 350 357
    • (2008) Nanomedicine , vol.4 , pp. 350-357
    • Tsigelny, I.F.1    Sharikov, Y.2    Miller, M.A.3    Masliah, E.4
  • 132
    • 77955366745 scopus 로고    scopus 로고
    • Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: Implications for Parkinson's disease pathogenesis and therapies
    • A. Oueslati, M. Fournier, and H.A. Lashuel Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies Prog Brain Res 183 2010 115 145
    • (2010) Prog Brain Res , vol.183 , pp. 115-145
    • Oueslati, A.1    Fournier, M.2    Lashuel, H.A.3
  • 133
    • 84862672217 scopus 로고    scopus 로고
    • Aggregation of alpha-synuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons
    • G. Taschenberger, M. Garrido, Y. Tereshchenko, M. Bahr, M. Zweckstetter, and S. Kugler Aggregation of alpha-synuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons Acta Neuropathol 123 2012 671 683
    • (2012) Acta Neuropathol , vol.123 , pp. 671-683
    • Taschenberger, G.1    Garrido, M.2    Tereshchenko, Y.3    Bahr, M.4    Zweckstetter, M.5    Kugler, S.6
  • 135
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of alpha-synuclein: From structure and toxicity to therapeutic target
    • H.A. Lashuel, C.R. Overk, A. Oueslati, and E. Masliah The many faces of alpha-synuclein: from structure and toxicity to therapeutic target Nat Rev Neurosci 14 2013 38 48
    • (2013) Nat Rev Neurosci , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 136
    • 33749240943 scopus 로고    scopus 로고
    • Mechanisms of Parkinson's Disease Linked to Pathological α-Synuclein: New Targets for Drug Discovery
    • DOI 10.1016/j.neuron.2006.09.026, PII S0896627306007331
    • V.M. Lee, and J.Q. Trojanowski Mechanisms of Parkinson's disease linked to pathological alpha-synuclein: new targets for drug discovery Neuron 52 2006 33 38 (Pubitemid 44479831)
    • (2006) Neuron , vol.52 , Issue.1 , pp. 33-38
    • Lee, V.M.-Y.1    Trojanowski, J.Q.2
  • 137
    • 0025310897 scopus 로고
    • Diffuse Lewy body disease in Japan
    • DOI 10.1007/BF00314594
    • K. Kosaka Diffuse Lewy body disease in Japan J Neurol 237 1990 197 204 (Pubitemid 20209309)
    • (1990) Journal of Neurology , vol.237 , Issue.3 , pp. 197-204
    • Kosaka, K.1
  • 142
    • 84857438892 scopus 로고    scopus 로고
    • Mechanisms of protein oligomerization: Inhibitor of functional amyloids templates alpha-synuclein fibrillation
    • I. Horvath, C.F. Weise, E.K. Andersson, E. Chorell, M. Sellstedt, and C. Bengtsson et al. Mechanisms of protein oligomerization: inhibitor of functional amyloids templates alpha-synuclein fibrillation J Am Chem Soc 134 2012 3439 3444
    • (2012) J Am Chem Soc , vol.134 , pp. 3439-3444
    • Horvath, I.1    Weise, C.F.2    Andersson, E.K.3    Chorell, E.4    Sellstedt, M.5    Bengtsson, C.6
  • 143
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of alpha-synuclein
    • N. Cremades, S.I. Cohen, E. Deas, A.Y. Abramov, A.Y. Chen, and A. Orte et al. Direct observation of the interconversion of normal and toxic forms of alpha-synuclein Cell 149 2012 1048 1059
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1    Cohen, S.I.2    Deas, E.3    Abramov, A.Y.4    Chen, A.Y.5    Orte, A.6
  • 146
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • T. Bartels, J.G. Choi, and D.J. Selkoe alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation Nature 477 2011 107 110
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 147
    • 84859577559 scopus 로고    scopus 로고
    • Alpha-synuclein in the central nervous system and from erythrocytes, mammalian cells and E. Coli exists predominantly as a disordered monomer
    • B. Fauvet, M.K. Mbefo, M.B. Fares, C. Desobry, S. Michael, and M.T. Ardah et al. Alpha-synuclein in the central nervous system and from erythrocytes, mammalian cells and E. coli exists predominantly as a disordered monomer J Biol Chem 287 2012 15345 15364
    • (2012) J Biol Chem , vol.287 , pp. 15345-15364
    • Fauvet, B.1    Mbefo, M.K.2    Fares, M.B.3    Desobry, C.4    Michael, S.5    Ardah, M.T.6
  • 151
    • 0142154275 scopus 로고    scopus 로고
    • Alpha-synuclein degradation by serine protease neurosin: Implication for pathogenesis of synucleinopathies
    • DOI 10.1093/hmg/ddg283
    • A. Iwata, M. Maruyama, T. Akagi, T. Hashikawa, I. Kanazawa, and S. Tsuji et al. Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies Hum Mol Genet 12 2003 2625 2635 (Pubitemid 37304685)
    • (2003) Human Molecular Genetics , vol.12 , Issue.20 , pp. 2625-2635
    • Iwata, A.1    Maruyama, M.2    Akagi, T.3    Hashikawa, T.4    Kanazawa, I.5    Tsuji, S.6    Nukina, N.7
  • 152
    • 2942620074 scopus 로고    scopus 로고
    • Reduces alpha-synuclein aggregation and toxicity
    • J. Klucken, Y. Shin, E. Masliah, B.T. Hyman, and McLean P.J. Hsp70 Reduces alpha-synuclein aggregation and toxicity J Biol Chem 279 2004 25497 25502
    • (2004) J Biol Chem , vol.279 , pp. 25497-25502
    • Klucken, J.1    Shin, Y.2    Masliah, E.3    Hyman, B.T.4
  • 153
    • 0036316947 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures
    • DOI 10.1046/j.1471-4159.2002.00821.x
    • K.S. McNaught, C. Mytilineou, R. Jnobaptiste, J. Yabut, P. Shashidharan, and P. Jennert et al. Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures J Neurochem 81 2002 301 306 (Pubitemid 34809355)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.2 , pp. 301-306
    • McNaught, K.St.P.1    Mytilin, C.2    JnoBaptiste, R.3    Yabut, J.4    Shashidharan, P.5    Jenner, P.6    Olanow, C.W.7
  • 156
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy
    • DOI 10.1126/science.1101738
    • A.M. Cuervo, L. Stefanis, R. Fredenburg, P.T. Lansbury, and D. Sulzer Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy Science 305 2004 1292 1295 (Pubitemid 39129234)
    • (2004) Science , vol.305 , Issue.5688 , pp. 1292-1295
    • Cuervo, A.M.1    Stafanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 157
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein
    • P. Desplats, H.J. Lee, E.J. Bae, C. Patrick, E. Rockenstein, and L. Crews et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein Proc Natl Acad Sci USA 106 2009 13010 13015
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13010-13015
    • Desplats, P.1    Lee, H.J.2    Bae, E.J.3    Patrick, C.4    Rockenstein, E.5    Crews, L.6
  • 158
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases
    • B. Spencer, R. Potkar, M. Trejo, E. Rockenstein, C. Patrick, and R. Gindi et al. Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases J Neurosci 29 2009 13578 13588
    • (2009) J Neurosci , vol.29 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5    Gindi, R.6
  • 159
    • 77949504405 scopus 로고    scopus 로고
    • Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy
    • L. Crews, B. Spencer, P. Desplats, C. Patrick, A. Paulino, and E. Rockenstein et al. Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy PLoS ONE 5 2010 e9313
    • (2010) PLoS ONE , vol.5 , pp. 9313
    • Crews, L.1    Spencer, B.2    Desplats, P.3    Patrick, C.4    Paulino, A.5    Rockenstein, E.6
  • 160
    • 77957264418 scopus 로고    scopus 로고
    • The synaptic pathology of alpha-synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementia
    • W.J. Schulz-Schaeffer The synaptic pathology of alpha-synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementia Acta Neuropathol 120 2010 131 143
    • (2010) Acta Neuropathol , vol.120 , pp. 131-143
    • Schulz-Schaeffer, W.J.1
  • 161
    • 33846997878 scopus 로고    scopus 로고
    • Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies
    • M.L. Kramer, and W.J. Schulz-Schaeffer Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies J Neurosci 27 2007 1405 1410
    • (2007) J Neurosci , vol.27 , pp. 1405-1410
    • Kramer, M.L.1    Schulz-Schaeffer, W.J.2
  • 162
    • 0027292769 scopus 로고
    • Differing patterns of aberrant neuronal sprouting in Alzheimer's disease with and without Lewy bodies
    • DOI 10.1016/0006-8993(93)91093-8
    • E. Masliah, M. Mallory, R. DeTeresa, M. Alford, and L. Hansen Differing patterns of aberrant neuronal sprouting in Alzheimer's disease with and without Lewy bodies Brain Res 617 1993 258 266 (Pubitemid 23209792)
    • (1993) Brain Research , vol.617 , Issue.2 , pp. 258-266
    • Masliah, E.1    Mallory, M.2    De Teresa, R.3    Alford, M.4    Hansen, L.5
  • 164
    • 84883420073 scopus 로고    scopus 로고
    • Dysfunction of the autophagy/lysosomal degradation pathway is a shared feature of the genetic synucleinopathies
    • C. Manzoni, and P.A. Lewis Dysfunction of the autophagy/lysosomal degradation pathway is a shared feature of the genetic synucleinopathies FASEB J 27 2013 3424 3429
    • (2013) FASEB J , vol.27 , pp. 3424-3429
    • Manzoni, C.1    Lewis, P.A.2
  • 166
    • 78649516910 scopus 로고    scopus 로고
    • Alterations in mGluR5 expression and signaling in Lewy body disease and in transgenic models of alpha-synucleinopathy - Implications for excitotoxicity
    • D.L. Price, E. Rockenstein, K. Ubhi, V. Phung, N. MacLean-Lewis, and D. Askay et al. Alterations in mGluR5 expression and signaling in Lewy body disease and in transgenic models of alpha-synucleinopathy - implications for excitotoxicity PLoS ONE 5 2010 e14020
    • (2010) PLoS ONE , vol.5 , pp. 14020
    • Price, D.L.1    Rockenstein, E.2    Ubhi, K.3    Phung, V.4    Maclean-Lewis, N.5    Askay, D.6
  • 167
    • 79960984489 scopus 로고    scopus 로고
    • Region-specific tauopathy and synucleinopathy in brain of the alpha-synuclein overexpressing mouse model of Parkinson's disease
    • T. Kaul, J. Credle, T. Haggerty, A.W. Oaks, E. Masliah, and A. Sidhu Region-specific tauopathy and synucleinopathy in brain of the alpha-synuclein overexpressing mouse model of Parkinson's disease BMC Neurosci 12 2011 79
    • (2011) BMC Neurosci , vol.12 , pp. 79
    • Kaul, T.1    Credle, J.2    Haggerty, T.3    Oaks, A.W.4    Masliah, E.5    Sidhu, A.6
  • 168
    • 79955535364 scopus 로고    scopus 로고
    • Hyperphosphorylated Tau in an alpha-synuclein-overexpressing transgenic model of Parkinson's disease
    • T. Haggerty, J. Credle, O. Rodriguez, J. Wills, A.W. Oaks, and E. Masliah et al. Hyperphosphorylated Tau in an alpha-synuclein-overexpressing transgenic model of Parkinson's disease Eur J Neurosci 33 2011 1598 1610
    • (2011) Eur J Neurosci , vol.33 , pp. 1598-1610
    • Haggerty, T.1    Credle, J.2    Rodriguez, O.3    Wills, J.4    Oaks, A.W.5    Masliah, E.6
  • 169
    • 77955664249 scopus 로고    scopus 로고
    • Elevated tauopathy and alpha-synuclein pathology in postmortem Parkinson's disease brains with and without dementia
    • J. Wills, J. Jones, T. Haggerty, V. Duka, J.N. Joyce, and A. Sidhu Elevated tauopathy and alpha-synuclein pathology in postmortem Parkinson's disease brains with and without dementia Exp Neurol 225 2010 210 218
    • (2010) Exp Neurol , vol.225 , pp. 210-218
    • Wills, J.1    Jones, J.2    Haggerty, T.3    Duka, V.4    Joyce, J.N.5    Sidhu, A.6
  • 170
    • 84884478145 scopus 로고    scopus 로고
    • Identification of the sites of tau hyperphosphorylation and activation of tau kinases in synucleinopathies and Alzheimer's diseases
    • V. Duka, J.H. Lee, J. Credle, J. Wills, A. Oaks, and C. Smolinsky et al. Identification of the sites of tau hyperphosphorylation and activation of tau kinases in synucleinopathies and Alzheimer's diseases PLoS ONE 8 2013 e75025
    • (2013) PLoS ONE , vol.8 , pp. 75025
    • Duka, V.1    Lee, J.H.2    Credle, J.3    Wills, J.4    Oaks, A.5    Smolinsky, C.6
  • 171
    • 83655181921 scopus 로고    scopus 로고
    • Tau reduction does not prevent motor deficits in two mouse models of Parkinson's disease
    • M. Morris, A. Koyama, E. Masliah, and L. Mucke Tau reduction does not prevent motor deficits in two mouse models of Parkinson's disease PLoS ONE 6 2011 e29257
    • (2011) PLoS ONE , vol.6 , pp. 29257
    • Morris, M.1    Koyama, A.2    Masliah, E.3    Mucke, L.4
  • 172
    • 77951885732 scopus 로고    scopus 로고
    • Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions
    • A. Jang, H.J. Lee, J.E. Suk, J.W. Jung, K.P. Kim, and S.J. Lee Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions J Neurochem 113 2010 1263 1274
    • (2010) J Neurochem , vol.113 , pp. 1263-1274
    • Jang, A.1    Lee, H.J.2    Suk, J.E.3    Jung, J.W.4    Kim, K.P.5    Lee, S.J.6
  • 173
    • 79251565507 scopus 로고    scopus 로고
    • Heat-shock protein 70 modulates toxic extracellular alpha-synuclein oligomers and rescues trans-synaptic toxicity
    • K.M. Danzer, W.P. Ruf, P. Putcha, D. Joyner, T. Hashimoto, and C. Glabe et al. Heat-shock protein 70 modulates toxic extracellular alpha-synuclein oligomers and rescues trans-synaptic toxicity FASEB J 25 2011 326 336
    • (2011) FASEB J , vol.25 , pp. 326-336
    • Danzer, K.M.1    Ruf, W.P.2    Putcha, P.3    Joyner, D.4    Hashimoto, T.5    Glabe, C.6
  • 174
    • 79951948479 scopus 로고    scopus 로고
    • Alpha-synuclein release by neurons activates the inflammatory response in a microglial cell line
    • L. Alvarez-Erviti, Y. Couch, J. Richardson, J.M. Cooper, and M.J. Wood Alpha-synuclein release by neurons activates the inflammatory response in a microglial cell line Neurosci Res 69 2011 337 342
    • (2011) Neurosci Res , vol.69 , pp. 337-342
    • Alvarez-Erviti, L.1    Couch, Y.2    Richardson, J.3    Cooper, J.M.4    Wood, M.J.5
  • 175
    • 84881147729 scopus 로고    scopus 로고
    • Autophagic failure promotes the exocytosis and intercellular transfer of alpha-synuclein
    • H.J. Lee, E.D. Cho, K.W. Lee, J.H. Kim, S.G. Cho, and S.J. Lee Autophagic failure promotes the exocytosis and intercellular transfer of alpha-synuclein Exp Mol Med 45 2013 e22
    • (2013) Exp Mol Med , vol.45 , pp. 22
    • Lee, H.J.1    Cho, E.D.2    Lee, K.W.3    Kim, J.H.4    Cho, S.G.5    Lee, S.J.6
  • 176
    • 77950571596 scopus 로고    scopus 로고
    • Direct transfer of alpha-synuclein from neuron to astroglia causes inflammatory responses in synucleinopathies
    • H.J. Lee, J.E. Suk, C. Patrick, E.J. Bae, J.H. Cho, and S. Rho et al. Direct transfer of alpha-synuclein from neuron to astroglia causes inflammatory responses in synucleinopathies J Biol Chem 285 2010 9262 9272
    • (2010) J Biol Chem , vol.285 , pp. 9262-9272
    • Lee, H.J.1    Suk, J.E.2    Patrick, C.3    Bae, E.J.4    Cho, J.H.5    Rho, S.6
  • 177
    • 80053613574 scopus 로고    scopus 로고
    • Exogenous alpha-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death
    • L.A. Volpicelli-Daley, K.C. Luk, T.P. Patel, S.A. Tanik, D.M. Riddle, and A. Stieber et al. Exogenous alpha-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death Neuron 72 2011 57 71
    • (2011) Neuron , vol.72 , pp. 57-71
    • Volpicelli-Daley, L.A.1    Luk, K.C.2    Patel, T.P.3    Tanik, S.A.4    Riddle, D.M.5    Stieber, A.6
  • 178
    • 84875898265 scopus 로고    scopus 로고
    • Neuron-released oligomeric alpha-synuclein is an endogenous agonist of TLR2 for paracrine activation of microglia
    • C. Kim, D.H. Ho, J.E. Suk, S. You, S. Michael, and J. Kang et al. Neuron-released oligomeric alpha-synuclein is an endogenous agonist of TLR2 for paracrine activation of microglia Nat Commun 4 2013 1562
    • (2013) Nat Commun , vol.4 , pp. 1562
    • Kim, C.1    Ho, D.H.2    Suk, J.E.3    You, S.4    Michael, S.5    Kang, J.6
  • 179
    • 42949133399 scopus 로고    scopus 로고
    • Alpha-synuclein alters Notch-1 expression and neurogenesis in mouse embryonic stem cells and in the hippocampus of transgenic mice
    • L. Crews, H. Mizuno, P. Desplats, E. Rockenstein, A. Adame, and C. Patrick et al. Alpha-synuclein alters Notch-1 expression and neurogenesis in mouse embryonic stem cells and in the hippocampus of transgenic mice J Neurosci 28 2008 4250 4260
    • (2008) J Neurosci , vol.28 , pp. 4250-4260
    • Crews, L.1    Mizuno, H.2    Desplats, P.3    Rockenstein, E.4    Adame, A.5    Patrick, C.6
  • 180
    • 79551519276 scopus 로고    scopus 로고
    • Alpha-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells
    • C. Hansen, E. Angot, A.L. Bergstrom, J.A. Steiner, L. Pieri, and G. Paul et al. alpha-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells J Clin Invest 121 2011 715 725
    • (2011) J Clin Invest , vol.121 , pp. 715-725
    • Hansen, C.1    Angot, E.2    Bergstrom, A.L.3    Steiner, J.A.4    Pieri, L.5    Paul, G.6
  • 181
    • 0031715399 scopus 로고    scopus 로고
    • Accumulation of α-synuclein/NACP is a cytopathological feature common to Lewy body disease and multiple system atrophy
    • DOI 10.1007/s004010050918
    • K. Wakabayashi, S. Hayashi, A. Kakita, M. Yamada, Y. Toyoshima, and M. Yoshimoto et al. Accumulation of α-synuclein/NACP is a cytopathological feature common to Lewy body disease and multiple system atrophy Acta Neuropathol 96 1998 445 452 (Pubitemid 28474751)
    • (1998) Acta Neuropathologica , vol.96 , Issue.5 , pp. 445-452
    • Wakabayashi, K.1    Hayashi, S.2    Kakita, A.3    Yamada, M.4    Toyoshima, Y.5    Yoshimoto, M.6    Takahashi, H.7
  • 182
  • 183
    • 84869109864 scopus 로고    scopus 로고
    • Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • K.C. Luk, V. Kehm, J. Carroll, B. Zhang, P. O'Brien, and J.Q. Trojanowski et al. Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice Science 338 2012 949 953
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6
  • 184
    • 84861671617 scopus 로고    scopus 로고
    • The spread of neurodegenerative disease
    • J. Hardy, and T. Revesz The spread of neurodegenerative disease N Engl J Med 366 2012 2126 2128
    • (2012) N Engl J Med , vol.366 , pp. 2126-2128
    • Hardy, J.1    Revesz, T.2


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