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Volumn 6, Issue 2, 2016, Pages

Molecular mechanisms in the pathogenesis of alzheimer’s disease and Tauopathies-Prion-Like seeded aggregation and phosphorylation

Author keywords

Amyloid 3; APP 5; Fibril 4; MAPT; Prion 2; Synuclein; TDP 43

Indexed keywords

ALKALINE PHOSPHATASE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; PRION PROTEIN; TAU PROTEIN; AMYLOID; PRION;

EID: 85012066425     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom6020024     Document Type: Review
Times cited : (49)

References (95)
  • 1
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • [CrossRef] [PubMed]
    • Braak, H, Braak, E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 1991, 82, 239-259. [CrossRef] [PubMed]
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 3
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
    • [CrossRef]
    • Hardy, J, Allsop, D. Amyloid deposition as the central event in the aetiology of Alzheimer’s disease. Trends Pharmacol. Sci. 1991, 12, 383-388. [CrossRef]
    • (1991) Trends Pharmacol. Sci , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 4
    • 0026597063 scopus 로고
    • Alzheimer’s disease: The amyloid cascade hypothesis
    • [CrossRef] [PubMed]
    • Hardy, J.A, Higgins, G.A. Alzheimer’s disease: The amyloid cascade hypothesis. Science 1992, 256, 184-185. [CrossRef] [PubMed]
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 5
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer’s disease: Progress and problems on the road to therapeutics
    • [CrossRef] [PubMed]
    • Hardy, J, Selkoe, D.J. The amyloid hypothesis of Alzheimer’s disease: Progress and problems on the road to therapeutics. Science 2002, 297, 353-356. [CrossRef] [PubMed]
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 8
    • 0029101491 scopus 로고
    • Familial Alzheimer’s disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer’s disease type 3 gene
    • [CrossRef] [PubMed]
    • Rogaev, E.I, Sherrington, R, Rogaeva, E.A, Levesque, G, Ikeda, M, Liang, Y, Chi, H, Lin, C, Holman, K, Tsuda, T, et al. Familial Alzheimer’s disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer’s disease type 3 gene. Nature 1995, 376, 775-778. [CrossRef] [PubMed]
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3    Levesque, G.4    Ikeda, M.5    Liang, Y.6    Chi, H.7    Lin, C.8    Holman, K.9    Tsuda, T.10
  • 11
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and β-secretase activity
    • [CrossRef] [PubMed]
    • Wolfe, M.S, Xia, W, Ostaszewski, B.L, Diehl, T.S, Kimberly, W.T, Selkoe, D.J. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and β-secretase activity. Nature 1999, 398, 513-517. [CrossRef] [PubMed]
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 12
    • 84874948210 scopus 로고    scopus 로고
    • Alzheimer disease: Aβ-independent processes-rethinking preclinical AD
    • [CrossRef] [PubMed]
    • Chetelat, G. Alzheimer disease: Aβ-independent processes-rethinking preclinical AD. Nat. Rev. Neurol. 2013, 9, 123-124. [CrossRef] [PubMed]
    • (2013) Nat. Rev. Neurol , vol.9 , pp. 123-124
    • Chetelat, G.1
  • 13
    • 84890125171 scopus 로고    scopus 로고
    • Alzheimer disease therapy—moving from amyloid-β to tau
    • [CrossRef] [PubMed]
    • Giacobini, E, Gold, G. Alzheimer disease therapy—moving from amyloid-β to tau. Nat. Rev. Neurol. 2013, 9, 677-686. [CrossRef] [PubMed]
    • (2013) Nat. Rev. Neurol , vol.9 , pp. 677-686
    • Giacobini, E.1    Gold, G.2
  • 14
    • 84929890412 scopus 로고    scopus 로고
    • The case for rejecting the amyloid cascade hypothesis
    • [CrossRef] [PubMed]
    • Herrup, K. The case for rejecting the amyloid cascade hypothesis. Nat. Neurosci. 2015, 18, 794-799. [CrossRef] [PubMed]
    • (2015) Nat. Neurosci , vol.18 , pp. 794-799
    • Herrup, K.1
  • 15
    • 47149112621 scopus 로고    scopus 로고
    • Long-term effects of Aβ42 immunisation in Alzheimer’s disease: Follow-up of a randomised, placebo-controlled phase I trial
    • [CrossRef]
    • Holmes, C, Boche, D, Wilkinson, D, Yadegarfar, G, Hopkins, V, Bayer, A, Jones, R.W, Bullock, R, Love, S, Neal, J.W, et al. Long-term effects of Aβ42 immunisation in Alzheimer’s disease: Follow-up of a randomised, placebo-controlled phase I trial. Lancet 2008, 372, 216-223. [CrossRef]
    • (2008) Lancet , vol.372 , pp. 216-223
    • Holmes, C.1    Boche, D.2    Wilkinson, D.3    Yadegarfar, G.4    Hopkins, V.5    Bayer, A.6    Jones, R.W.7    Bullock, R.8    Love, S.9    Neal, J.W.10
  • 20
    • 84939506533 scopus 로고    scopus 로고
    • Neurodegeneration. Alzheimer’s and Parkinson’s diseases: The prion concept in relation to assembled Aβ, tau, and β-synuclein
    • [CrossRef] [PubMed]
    • Goedert, M. Neurodegeneration. Alzheimer’s and Parkinson’s diseases: The prion concept in relation to assembled Aβ, tau, and β-synuclein. Science 2015. [CrossRef] [PubMed]
    • (2015) Science
    • Goedert, M.1
  • 21
    • 84904488776 scopus 로고    scopus 로고
    • Prion-like properties of tau protein: The importance of extracellular tau as a therapeutic target
    • [CrossRef] [PubMed]
    • Holmes, B.B, Diamond, M.I. Prion-like properties of tau protein: The importance of extracellular tau as a therapeutic target. J. Biol. Chem. 2014, 289, 19855-19861. [CrossRef] [PubMed]
    • (2014) J. Biol. Chem , vol.289 , pp. 19855-19861
    • Holmes, B.B.1    Diamond, M.I.2
  • 22
    • 84883688262 scopus 로고    scopus 로고
    • Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
    • [CrossRef] [PubMed]
    • Jucker, M, Walker, L.C. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 2013, 501, 45-51. [CrossRef] [PubMed]
    • (2013) Nature , vol.501 , pp. 45-51
    • Jucker, M.1    Walker, L.C.2
  • 23
    • 84888594143 scopus 로고    scopus 로고
    • Biology and genetics of prions causing neurodegeneration
    • [CrossRef] [PubMed]
    • Prusiner, S.B. Biology and genetics of prions causing neurodegeneration. Annu. Rev. Genet. 2013, 47, 601-623. [CrossRef] [PubMed]
    • (2013) Annu. Rev. Genet , vol.47 , pp. 601-623
    • Prusiner, S.B.1
  • 24
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • [CrossRef] [PubMed]
    • Frost, B, Diamond, M.I. Prion-like mechanisms in neurodegenerative diseases. Nat. Rev. Neurosci. 2010, 11, 155-159. [CrossRef] [PubMed]
    • (2010) Nat. Rev. Neurosci , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 25
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer’s disease
    • [CrossRef]
    • Goedert, M, Spillantini, M.G, Jakes, R, Rutherford, D, Crowther, R.A. Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer’s disease. Neuron 1989, 3, 519-526. [CrossRef]
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 27
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization
    • [PubMed]
    • Goedert, M, Jakes, R. Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J. 1990, 9, 4225-4230. [PubMed]
    • (1990) EMBO J , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 28
    • 84952718632 scopus 로고    scopus 로고
    • Tau and neurodegenerative disease: The story so far
    • [CrossRef] [PubMed]
    • Iqbal, K, Liu, F, Gong, C.X. Tau and neurodegenerative disease: The story so far. Nat. Rev. Neurol. 2016, 12, 15-27. [CrossRef] [PubMed]
    • (2016) Nat. Rev. Neurol , vol.12 , pp. 15-27
    • Iqbal, K.1    Liu, F.2    Gong, C.X.3
  • 29
    • 0027420369 scopus 로고
    • Tau protein and the neurofibrillary pathology of Alzheimer’s disease
    • [CrossRef]
    • Goedert, M. Tau protein and the neurofibrillary pathology of Alzheimer’s disease. Trends Neurosci. 1993, 16, 460-465. [CrossRef]
    • (1993) Trends Neurosci , vol.16 , pp. 460-465
    • Goedert, M.1
  • 31
    • 0022435132 scopus 로고
    • Image reconstruction of the Alzheimer paired helical filament
    • [PubMed]
    • Crowther, R.A, Wischik, C.M. Image reconstruction of the Alzheimer paired helical filament. EMBO J. 1985, 4, 3661-3665. [PubMed]
    • (1985) EMBO J , vol.4 , pp. 3661-3665
    • Crowther, R.A.1    Wischik, C.M.2
  • 32
    • 0022657213 scopus 로고
    • Subunit structure of the Alzheimer tangle
    • [PubMed]
    • Wischik, C.M, Crowther, R.A. Subunit structure of the Alzheimer tangle. Br. Med. Bull. 1986, 42, 51-56. [PubMed]
    • (1986) Br. Med. Bull , vol.42 , pp. 51-56
    • Wischik, C.M.1    Crowther, R.A.2
  • 33
    • 0024044195 scopus 로고
    • Structural characterization of the core of the paired helical filament of Alzheimer disease
    • [CrossRef] [PubMed]
    • Wischik, C.M, Novak, M, Edwards, P.C, Klug, A, Tichelaar, W, Crowther, R.A. Structural characterization of the core of the paired helical filament of Alzheimer disease. Proc. Nat. Acad. Sci. USA 1988, 85, 4884-4888. [CrossRef] [PubMed]
    • (1988) Proc. Nat. Acad. Sci. USA , vol.85 , pp. 4884-4888
    • Wischik, C.M.1    Novak, M.2    Edwards, P.C.3    Klug, A.4    Tichelaar, W.5    Crowther, R.A.6
  • 35
    • 0024348594 scopus 로고
    • The repeat region of microtubule-associated protein tau forms part of the core of the paired helical filament of Alzheimer’s disease
    • [CrossRef] [PubMed]
    • Crowther, T, Goedert, M, Wischik, C.M. The repeat region of microtubule-associated protein tau forms part of the core of the paired helical filament of Alzheimer’s disease. Ann. Med. 1989, 21, 127-132. [CrossRef] [PubMed]
    • (1989) Ann. Med , vol.21 , pp. 127-132
    • Crowther, T.1    Goedert, M.2    Wischik, C.M.3
  • 36
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cdna encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mrnas in human brain
    • [PubMed]
    • Goedert, M, Spillantini, M.G, Potier, M.C, Ulrich, J, Crowther, R.A. Cloning and sequencing of the cdna encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mrnas in human brain. EMBO J. 1989, 8, 393-399. [PubMed]
    • (1989) EMBO J , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 37
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis
    • [CrossRef] [PubMed]
    • Greenberg, S.G, Davies, P. A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc. Nat. Acad. Sci. USA 1990, 87, 5827-5831. [CrossRef] [PubMed]
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 38
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal tau
    • [CrossRef] [PubMed]
    • Lee, V.M, Balin, B.J, Otvos, L., Jr, Trojanowski, J.Q. A68: A major subunit of paired helical filaments and derivatized forms of normal tau. Science 1991, 251, 675-678. [CrossRef] [PubMed]
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos, L.3    Trojanowski, J.Q.4
  • 39
    • 0026787130 scopus 로고
    • Protein sequence and mass spectrometric analyses of tau in the Alzheimer’s disease brain
    • [PubMed]
    • Hasegawa, M, Morishima-Kawashima, M, Takio, K, Suzuki, M, Titani, K, Ihara, Y. Protein sequence and mass spectrometric analyses of tau in the Alzheimer’s disease brain. J. Biol. Chem. 1992, 267, 17047-17054. [PubMed]
    • (1992) J. Biol. Chem , vol.267 , pp. 17047-17054
    • Hasegawa, M.1    Morishima-Kawashima, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 40
    • 0027155834 scopus 로고
    • Characterization of two distinct monoclonal antibodies to paired helical filaments: Further evidence for fetal-type phosphorylation of the tau in paired helical filaments
    • [CrossRef] [PubMed]
    • Hasegawa, M, Watanabe, A, Takio, K, Suzuki, M, Arai, T, Titani, K, Ihara, Y. Characterization of two distinct monoclonal antibodies to paired helical filaments: Further evidence for fetal-type phosphorylation of the tau in paired helical filaments. J. Neurochem. 1993, 60, 2068-2077. [CrossRef] [PubMed]
    • (1993) J. Neurochem , vol.60 , pp. 2068-2077
    • Hasegawa, M.1    Watanabe, A.2    Takio, K.3    Suzuki, M.4    Arai, T.5    Titani, K.6    Ihara, Y.7
  • 41
    • 0027193036 scopus 로고
    • Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
    • [CrossRef]
    • Morishima-Kawashima, M, Hasegawa, M, Takio, K, Suzuki, M, Titani, K, Ihara, Y. Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments. Neuron 1993, 10, 1151-1160. [CrossRef]
    • (1993) Neuron , vol.10 , pp. 1151-1160
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 44
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • [CrossRef]
    • Goedert, M, Spillantini, M.G, Cairns, N.J, Crowther, R.A. Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms. Neuron 1992, 8, 159-168. [CrossRef]
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 45
    • 0026551711 scopus 로고
    • The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region
    • [PubMed]
    • Biernat, J, Mandelkow, E.M, Schroter, C, Lichtenberg-Kraag, B, Steiner, B, Berling, B, Meyer, H, Mercken, M, Vandermeeren, A, Goedert, M, et al. The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region. EMBO J. 1992, 11, 1593-1597. [PubMed]
    • (1992) EMBO J , vol.11 , pp. 1593-1597
    • Biernat, J.1    Mandelkow, E.M.2    Schroter, C.3    Lichtenberg-Kraag, B.4    Steiner, B.5    Berling, B.6    Meyer, H.7    Mercken, M.8    Vandermeeren, A.9    Goedert, M.10
  • 46
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 in Alzheimer’s disease recapitulates development and contributes to reduced microtubule binding
    • [CrossRef]
    • Bramblett, G.T, Goedert, M, Jakes, R, Merrick, S.E, Trojanowski, J.Q, Lee, V.M. Abnormal tau phosphorylation at Ser396 in Alzheimer’s disease recapitulates development and contributes to reduced microtubule binding. Neuron 1993, 10, 1089-1099. [CrossRef]
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 47
    • 0027217679 scopus 로고
    • The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development
    • [CrossRef] [PubMed]
    • Goedert, M, Jakes, R, Crowther, R.A, Six, J, Lubke, U, Vandermeeren, M, Cras, P, Trojanowski, J.Q, Lee, V.M. The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development. Proc. Nat. Acad. Sci. USA 1993, 90, 5066-5070. [CrossRef] [PubMed]
    • (1993) Proc. Nat. Acad. Sci. USA , vol.90 , pp. 5066-5070
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3    Six, J.4    Lubke, U.5    Vandermeeren, M.6    Cras, P.7    Trojanowski, J.Q.8    Lee, V.M.9
  • 49
    • 0027978991 scopus 로고
    • Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics
    • [CrossRef] [PubMed]
    • Iwatsubo, T, Hasegawa, M, Ihara, Y. Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics. Acta Neuropathol. 1994, 88, 129-136. [CrossRef] [PubMed]
    • (1994) Acta Neuropathol , vol.88 , pp. 129-136
    • Iwatsubo, T.1    Hasegawa, M.2    Ihara, Y.3
  • 50
    • 0039575094 scopus 로고    scopus 로고
    • Comparative biochemistry of tau in progressive supranuclear palsy, corticobasal degeneration, FTDP-17 and Pick’s disease
    • [CrossRef] [PubMed]
    • Buee, L, Delacourte, A. Comparative biochemistry of tau in progressive supranuclear palsy, corticobasal degeneration, FTDP-17 and Pick’s disease. Brain Pathol. 1999, 9, 681-693. [CrossRef] [PubMed]
    • (1999) Brain Pathol , vol.9 , pp. 681-693
    • Buee, L.1    Delacourte, A.2
  • 51
    • 0034940160 scopus 로고    scopus 로고
    • Neurodegenerative tauopathies
    • [CrossRef] [PubMed]
    • Lee, V.M, Goedert, M, Trojanowski, J.Q. Neurodegenerative tauopathies. Annu. Rev. Neurosci. 2001, 24, 1121-1159. [CrossRef] [PubMed]
    • (2001) Annu. Rev. Neurosci , vol.24 , pp. 1121-1159
    • Lee, V.M.1    Goedert, M.2    Trojanowski, J.Q.3
  • 52
    • 0032894227 scopus 로고    scopus 로고
    • The tauopathies: Toward an experimental animal model
    • [CrossRef]
    • Goedert, M, Hasegawa, M. The tauopathies: Toward an experimental animal model. Am. J. Pathol. 1999, 154, 1-6. [CrossRef]
    • (1999) Am. J. Pathol , vol.154 , pp. 1-6
    • Goedert, M.1    Hasegawa, M.2
  • 53
    • 84923006997 scopus 로고    scopus 로고
    • Invited review: Neuropathology of tauopathies: Principles and practice
    • [CrossRef] [PubMed]
    • Kovacs, G.G. Invited review: Neuropathology of tauopathies: Principles and practice. Neuropathol. Appl. Neurobiol. 2015, 41, 3-23. [CrossRef] [PubMed]
    • (2015) Neuropathol. Appl. Neurobiol , vol.41 , pp. 3-23
    • Kovacs, G.G.1
  • 54
    • 1842451983 scopus 로고    scopus 로고
    • Alterations in human tau transcripts correlate with those of neurofilament in sporadic tauopathies
    • [CrossRef] [PubMed]
    • Umeda, Y, Taniguchi, S, Arima, K, Piao, Y.S, Takahashi, H, Iwatsubo, T, Mann, D, Hasegawa, M. Alterations in human tau transcripts correlate with those of neurofilament in sporadic tauopathies. Neurosci. Lett. 2004, 359, 151-154. [CrossRef] [PubMed]
    • (2004) Neurosci. Lett , vol.359 , pp. 151-154
    • Umeda, Y.1    Taniguchi, S.2    Arima, K.3    Piao, Y.S.4    Takahashi, H.5    Iwatsubo, T.6    Mann, D.7    Hasegawa, M.8
  • 56
    • 0030887854 scopus 로고    scopus 로고
    • Familial multiple system tauopathy with presenile dementia: A disease with abundant neuronal and glial tau filaments
    • [CrossRef] [PubMed]
    • Spillantini, M.G, Goedert, M, Crowther, R.A, Murrell, J.R, Farlow, M.R, Ghetti, B. Familial multiple system tauopathy with presenile dementia: A disease with abundant neuronal and glial tau filaments. Proc. Nat. Acad. Sci. USA 1997, 94, 4113-4118. [CrossRef] [PubMed]
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 4113-4118
    • Spillantini, M.G.1    Goedert, M.2    Crowther, R.A.3    Murrell, J.R.4    Farlow, M.R.5    Ghetti, B.6
  • 58
    • 0032560487 scopus 로고    scopus 로고
    • Mutation in the tau gene in familial multiple system tauopathy with presenile dementia
    • [CrossRef] [PubMed]
    • Spillantini, M.G, Murrell, J.R, Goedert, M, Farlow, M.R, Klug, A, Ghetti, B. Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc. Nat. Acad. Sci. USA 1998, 95, 7737-7741. [CrossRef] [PubMed]
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 7737-7741
    • Spillantini, M.G.1    Murrell, J.R.2    Goedert, M.3    Farlow, M.R.4    Klug, A.5    Ghetti, B.6
  • 59
    • 0032214501 scopus 로고    scopus 로고
    • Tau mutations cause frontotemporal dementias
    • [CrossRef]
    • Goedert, M, Crowther, R.A, Spillantini, M.G. Tau mutations cause frontotemporal dementias. Neuron 1998, 21, 955-958. [CrossRef]
    • (1998) Neuron , vol.21 , pp. 955-958
    • Goedert, M.1    Crowther, R.A.2    Spillantini, M.G.3
  • 60
    • 84864383087 scopus 로고    scopus 로고
    • Frontotemporal dementia: Implications for understanding Alzheimer disease
    • [CrossRef] [PubMed]
    • Goedert, M, Ghetti, B, Spillantini, M.G. Frontotemporal dementia: Implications for understanding Alzheimer disease. Cold Spring Harb. Perspect. Med. 2012. [CrossRef] [PubMed]
    • (2012) Cold Spring Harb. Perspect. Med
    • Goedert, M.1    Ghetti, B.2    Spillantini, M.G.3
  • 61
    • 84954385047 scopus 로고    scopus 로고
    • Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometric analyses of sarkosyl-insoluble and trypsin-resistant tau
    • [CrossRef] [PubMed]
    • Taniguchi-Watanabe, S, Arai, T, Kametani, F, Nonaka, T, Masuda-Suzukake, M, Tarutani, A, Murayama, S, Saito, Y, Arima, K, Yoshida, M, et al. Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometric analyses of sarkosyl-insoluble and trypsin-resistant tau. Acta Neuropathol. 2016, 131, 267-280. [CrossRef] [PubMed]
    • (2016) Acta Neuropathol , vol.131 , pp. 267-280
    • Taniguchi-Watanabe, S.1    Arai, T.2    Kametani, F.3    Nonaka, T.4    Masuda-Suzukake, M.5    Tarutani, A.6    Murayama, S.7    Saito, Y.8    Arima, K.9    Yoshida, M.10
  • 63
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer’s disease paired helical filament tau
    • [CrossRef]
    • Matsuo, E.S, Shin, R.W, Billingsley, M.L, van deVoorde, A, O’Connor, M, Trojanowski, J.Q, Lee, V.M. Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer’s disease paired helical filament tau. Neuron 1994, 13, 989-1002. [CrossRef]
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.W.2    Billingsley, M.L.3    Van Devoorde, A.4    O’Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 64
    • 0029416987 scopus 로고
    • Dephosphorylation of fetal-tau and paired helical filaments-tau by protein phosphatases 1 and 2A and calcineurin
    • [PubMed]
    • Yamamoto, H, Hasegawa, M, Ono, T, Tashima, K, Ihara, Y, Miyamoto, E. Dephosphorylation of fetal-tau and paired helical filaments-tau by protein phosphatases 1 and 2A and calcineurin. J. Biochem. 1995, 118, 1224-1231. [PubMed]
    • (1995) J. Biochem , vol.118 , pp. 1224-1231
    • Yamamoto, H.1    Hasegawa, M.2    Ono, T.3    Tashima, K.4    Ihara, Y.5    Miyamoto, E.6
  • 65
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif 306VQIVYK311 forming β structure
    • [CrossRef] [PubMed]
    • Von Bergen, M, Friedhoff, P, Biernat, J, Heberle, J, Mandelkow, E.M, Mandelkow, E. Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif 306VQIVYK311 forming β structure. Proc. Nat. Acad. Sci. USA 2000, 97, 5129-5134. [CrossRef] [PubMed]
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , pp. 5129-5134
    • Von Bergen, M.1    Friedhoff, P.2    Biernat, J.3    Heberle, J.4    Mandelkow, E.M.5    Mandelkow, E.6
  • 66
    • 9144224301 scopus 로고    scopus 로고
    • Identification of amino-terminally cleaved tau fragments that distinguish progressive supranuclear palsy from corticobasal degeneration
    • [CrossRef] [PubMed]
    • Arai, T, Ikeda, K, Akiyama, H, Nonaka, T, Hasegawa, M, Ishiguro, K, Iritani, S, Tsuchiya, K, Iseki, E, Yagishita, S, et al. Identification of amino-terminally cleaved tau fragments that distinguish progressive supranuclear palsy from corticobasal degeneration. Ann. Neurol. 2004, 55, 72-79. [CrossRef] [PubMed]
    • (2004) Ann. Neurol , vol.55 , pp. 72-79
    • Arai, T.1    Ikeda, K.2    Akiyama, H.3    Nonaka, T.4    Hasegawa, M.5    Ishiguro, K.6    Iritani, S.7    Tsuchiya, K.8    Iseki, E.9    Yagishita, S.10
  • 67
    • 0025852163 scopus 로고
    • Structural stability of paired helical filaments requires microtubule-binding domains of tau: A model for self-association
    • [CrossRef]
    • Ksiezak-Reding, H, Yen, S.H. Structural stability of paired helical filaments requires microtubule-binding domains of tau: A model for self-association. Neuron 1991, 6, 717-728. [CrossRef]
    • (1991) Neuron , vol.6 , pp. 717-728
    • Ksiezak-Reding, H.1    Yen, S.H.2
  • 68
  • 69
    • 0029850476 scopus 로고    scopus 로고
    • Pick’s disease: Hyperphosphorylated tau protein segregates to the somatoaxonal compartment
    • [CrossRef] [PubMed]
    • Probst, A, Tolnay, M, Langui, D, Goedert, M, Spillantini, M.G. Pick’s disease: Hyperphosphorylated tau protein segregates to the somatoaxonal compartment. Acta Neuropathol. 1996, 92, 588-596. [CrossRef] [PubMed]
    • (1996) Acta Neuropathol , vol.92 , pp. 588-596
    • Probst, A.1    Tolnay, M.2    Langui, D.3    Goedert, M.4    Spillantini, M.G.5
  • 70
    • 0038050650 scopus 로고    scopus 로고
    • Different immunoreactivities of the microtubule-binding region of tau and its molecular basis in brains from patients with Alzheimer’s disease, Pick’s disease, progressive supranuclear palsy and corticobasal degeneration
    • [PubMed]
    • Arai, T, Ikeda, K, Akiyama, H, Tsuchiya, K, Iritani, S, Ishiguro, K, Yagishita, S, Oda, T, Odawara, T, Iseki, E. Different immunoreactivities of the microtubule-binding region of tau and its molecular basis in brains from patients with Alzheimer’s disease, Pick’s disease, progressive supranuclear palsy and corticobasal degeneration. Acta Neuropathol. 2003, 105, 489-498. [PubMed]
    • (2003) Acta Neuropathol , vol.105 , pp. 489-498
    • Arai, T.1    Ikeda, K.2    Akiyama, H.3    Tsuchiya, K.4    Iritani, S.5    Ishiguro, K.6    Yagishita, S.7    Oda, T.8    Odawara, T.9    Iseki, E.10
  • 71
    • 34547101740 scopus 로고    scopus 로고
    • Fibrillogenic nuclei composed of P301L mutant tau induce elongation of P301L tau but not wild-type tau
    • [CrossRef] [PubMed]
    • Aoyagi, H, Hasegawa, M, Tamaoka, A. Fibrillogenic nuclei composed of P301L mutant tau induce elongation of P301L tau but not wild-type tau. J. Biol. Chem. 2007, 282, 20309-20318. [CrossRef] [PubMed]
    • (2007) J. Biol. Chem , vol.282 , pp. 20309-20318
    • Aoyagi, H.1    Hasegawa, M.2    Tamaoka, A.3
  • 72
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • [CrossRef] [PubMed]
    • Frost, B, Jacks, R.L, Diamond, M.I. Propagation of tau misfolding from the outside to the inside of a cell. J. Biol. Chem. 2009, 284, 12845-12852. [CrossRef] [PubMed]
    • (2009) J. Biol. Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 73
    • 78049376559 scopus 로고    scopus 로고
    • Seeded aggregation and toxicity of β-synuclein and tau: Cellular models of neurodegenerative diseases
    • [CrossRef] [PubMed]
    • Nonaka, T, Watanabe, S.T, Iwatsubo, T, Hasegawa, M. Seeded aggregation and toxicity of β-synuclein and tau: Cellular models of neurodegenerative diseases. J. Biol. Chem. 2010, 285, 34885-34898. [CrossRef] [PubMed]
    • (2010) J. Biol. Chem , vol.285 , pp. 34885-34898
    • Nonaka, T.1    Watanabe, S.T.2    Iwatsubo, T.3    Hasegawa, M.4
  • 77
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • [CrossRef] [PubMed]
    • Goedert, M, Clavaguera, F, Tolnay, M. The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci. 2010, 33, 317-325. [CrossRef] [PubMed]
    • (2010) Trends Neurosci , vol.33 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 78
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • [CrossRef] [PubMed]
    • Aguzzi, A, Rajendran, L. The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 2009, 64, 783-790. [CrossRef] [PubMed]
    • (2009) Neuron , vol.64 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 79
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • [CrossRef] [PubMed]
    • Brundin, P, Melki, R, Kopito, R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat. Rev. Mol. Cell Biol. 2010, 11, 301-307. [CrossRef] [PubMed]
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 80
    • 84929991867 scopus 로고    scopus 로고
    • Extracellular association of app and tau fibrils induces intracellular aggregate formation of tau
    • [CrossRef] [PubMed]
    • Takahashi, M, Miyata, H, Kametani, F, Nonaka, T, Akiyama, H, Hisanaga, S, Hasegawa, M. Extracellular association of app and tau fibrils induces intracellular aggregate formation of tau. Acta Neuropathol. 2015, 129, 895-907. [CrossRef] [PubMed]
    • (2015) Acta Neuropathol , vol.129 , pp. 895-907
    • Takahashi, M.1    Miyata, H.2    Kametani, F.3    Nonaka, T.4    Akiyama, H.5    Hisanaga, S.6    Hasegawa, M.7
  • 81
    • 79451471618 scopus 로고    scopus 로고
    • The pathological process underlying Alzheimer’s disease in individuals under thirty
    • [CrossRef] [PubMed]
    • Braak, H, Del Tredici, K. The pathological process underlying Alzheimer’s disease in individuals under thirty. Acta Neuropathol. 2011, 121, 171-181. [CrossRef] [PubMed]
    • (2011) Acta Neuropathol , vol.121 , pp. 171-181
    • Braak, H.1    Del Tredici, K.2
  • 82
    • 84885476621 scopus 로고    scopus 로고
    • Amyloid or tau: The chicken or the egg?
    • [CrossRef] [PubMed]
    • Mann, D.M, Hardy, J. Amyloid or tau: The chicken or the egg? Acta Neuropathol. 2013, 126, 609-613. [CrossRef] [PubMed]
    • (2013) Acta Neuropathol , vol.126 , pp. 609-613
    • Mann, D.M.1    Hardy, J.2
  • 83
    • 84885474583 scopus 로고    scopus 로고
    • Reply: The early pathological process in sporadic Alzheimer’s disease
    • [CrossRef] [PubMed]
    • Braak, H, Del Tredici, K. Reply: The early pathological process in sporadic Alzheimer’s disease. Acta Neuropathol. 2013, 126, 615-618. [CrossRef] [PubMed]
    • (2013) Acta Neuropathol , vol.126 , pp. 615-618
    • Braak, H.1    Del Tredici, K.2
  • 84
    • 84888205849 scopus 로고    scopus 로고
    • Intraneuronal tau aggregation precedes diffuse plaque deposition, but amyloid-β changes occur before increases of tau in cerebrospinal fluid
    • [CrossRef] [PubMed]
    • Braak, H, Zetterberg, H, Del Tredici, K, Blennow, K. Intraneuronal tau aggregation precedes diffuse plaque deposition, but amyloid-β changes occur before increases of tau in cerebrospinal fluid. Acta Neuropathol. 2013, 126, 631-641. [CrossRef] [PubMed]
    • (2013) Acta Neuropathol , vol.126 , pp. 631-641
    • Braak, H.1    Zetterberg, H.2    Del Tredici, K.3    Blennow, K.4
  • 87
    • 84881085093 scopus 로고    scopus 로고
    • Amyloid-β may be released from non-junctional varicosities of axons generated from abnormal tau-containing brainstem nuclei in sporadic Alzheimer’s disease
    • [CrossRef] [PubMed]
    • Braak, H, Del Tredici, K. Amyloid-β may be released from non-junctional varicosities of axons generated from abnormal tau-containing brainstem nuclei in sporadic Alzheimer’s disease: A hypothesis. Acta Neuropathol. 2013, 126, 303-306. [CrossRef] [PubMed]
    • (2013) A Hypothesis. Acta Neuropathol. , vol.126 , pp. 303-306
    • Braak, H.1    Del Tredici, K.2
  • 88
    • 14844303721 scopus 로고    scopus 로고
    • Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins
    • [CrossRef] [PubMed]
    • Taniguchi, S, Suzuki, N, Masuda, M, Hisanaga, S, Iwatsubo, T, Goedert, M, Hasegawa, M. Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins. J. Biol. Chem. 2005, 280, 7614-7623. [CrossRef] [PubMed]
    • (2005) J. Biol. Chem. , vol.280 , pp. 7614-7623
    • Taniguchi, S.1    Suzuki, N.2    Masuda, M.3    Hisanaga, S.4    Iwatsubo, T.5    Goedert, M.6    Hasegawa, M.7
  • 90
    • 84928401341 scopus 로고    scopus 로고
    • Cellular models of aggregation-dependent template-directed proteolysis to characterize tau aggregation inhibitors for treatment of Alzheimer disease
    • [CrossRef] [PubMed]
    • Harrington, C.R, Storey, J.M, Clunas, S, Harrington, K.A, Horsley, D, Ishaq, A, Kemp, S.J, Larch, C.P, Marshall, C, Nicoll, S.L, et al. Cellular models of aggregation-dependent template-directed proteolysis to characterize tau aggregation inhibitors for treatment of Alzheimer disease. J. Biol. Chem. 2015, 290, 10862-10875. [CrossRef] [PubMed]
    • (2015) J. Biol. Chem , vol.290 , pp. 10862-10875
    • Harrington, C.R.1    Storey, J.M.2    Clunas, S.3    Harrington, K.A.4    Horsley, D.5    Ishaq, A.6    Kemp, S.J.7    Larch, C.P.8    Marshall, C.9    Nicoll, S.L.10
  • 91
    • 84898059466 scopus 로고    scopus 로고
    • Tau-aggregation inhibitor therapy for Alzheimer’s disease
    • [CrossRef] [PubMed]
    • Wischik, C.M, Harrington, C.R, Storey, J.M. Tau-aggregation inhibitor therapy for Alzheimer’s disease. Biochem. Pharmacol. 2014, 88, 529-539. [CrossRef] [PubMed]
    • (2014) Biochem. Pharmacol , vol.88 , pp. 529-539
    • Wischik, C.M.1    Harrington, C.R.2    Storey, J.M.3
  • 92
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • [CrossRef] [PubMed]
    • Asuni, A.A, Boutajangout, A, Quartermain, D, Sigurdsson, E.M. Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J. Neurosci. 2007, 27, 9115-9129. [CrossRef] [PubMed]
    • (2007) J. Neurosci , vol.27 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 94
    • 84892989659 scopus 로고    scopus 로고
    • Neurodegenerative disease: Tau immunotherapy targets transcellular propagation
    • [CrossRef] [PubMed]
    • Flight, M.H. Neurodegenerative disease: Tau immunotherapy targets transcellular propagation. Nat. Rev. Drug Discov. 2013. [CrossRef] [PubMed]
    • (2013) Nat. Rev. Drug Discov
    • Flight, M.H.1


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