메뉴 건너뛰기




Volumn 4, Issue 1, 2009, Pages 39-53

Conformational changes and cleavage; are these responsible for the tau aggregation in Alzheimer's disease?

Author keywords

Aggregation; Alzheimer's disease; Cleavage; Conformational changes; Neurofibrillary tangles; Neuronal toxicity; Phosphorylated tau

Indexed keywords

TAU PROTEIN;

EID: 67149128179     PISSN: 14796708     EISSN: None     Source Type: Journal    
DOI: 10.2217/14796708.4.1.39     Document Type: Review
Times cited : (17)

References (125)
  • 1
    • 0031796883 scopus 로고    scopus 로고
    • Neurofibrillary pathology of Alzheimer's disease and other tauopathies
    • Goedert M: Neurofibrillary pathology of Alzheimer's disease and other tauopathies. Prog. Brain Res. 117, 287-306 (1998).
    • (1998) Prog. Brain Res , vol.117 , pp. 287-306
    • Goedert, M.1
  • 2
  • 3
    • 0031596261 scopus 로고    scopus 로고
    • The neuropathological diagnosis of Alzheimer disease
    • Jellinger KA: The neuropathological diagnosis of Alzheimer disease. J. Neural Transm. Suppl. 53, 97-118 (1998).
    • (1998) J. Neural Transm. Suppl , vol.53 , pp. 97-118
    • Jellinger, K.A.1
  • 5
    • 0030668423 scopus 로고    scopus 로고
    • Diagnostic criteria for neuropathologic assessment of Alzheimer's disease
    • Braak H, Braak E: Diagnostic criteria for neuropathologic assessment of Alzheimer's disease. Neurobiol. Aging 18, S85-S88 (1997).
    • (1997) Neurobiol. Aging , vol.18
    • Braak, H.1    Braak, E.2
  • 6
    • 0030680922 scopus 로고    scopus 로고
    • Diagnosis and staging of Alzheimer disease
    • Duyckaerts C, Hauw JJ: Diagnosis and staging of Alzheimer disease. Neurobiol. Aging 18, S33-S42 (1997).
    • (1997) Neurobiol. Aging , vol.18
    • Duyckaerts, C.1    Hauw, J.J.2
  • 7
    • 21844431659 scopus 로고    scopus 로고
    • Etiology of sporadic Alzheimer's disease: Somatostatin, neprilysin, and amyloid β peptide
    • Hama E, Saido TC: Etiology of sporadic Alzheimer's disease: somatostatin, neprilysin, and amyloid β peptide. Med. Hypotheses 65, 498-500 (2005).
    • (2005) Med. Hypotheses , vol.65 , pp. 498-500
    • Hama, E.1    Saido, T.C.2
  • 8
    • 24344506180 scopus 로고    scopus 로고
    • Unravelling the mechanism of amyloid-β toxicity in AD
    • Frankish H: Unravelling the mechanism of amyloid-β toxicity in AD. Lancet Neurol. 4, 526 (2005).
    • (2005) Lancet Neurol , vol.4 , pp. 526
    • Frankish, H.1
  • 9
    • 19544362550 scopus 로고    scopus 로고
    • Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease
    • Tanimukai H, Grundke-Iqbal I, Iqbal K: Up-regulation of inhibitors of protein phosphatase-2A in Alzheimer's disease. Am. J. Pathol. 166, 1761-1771 (2005).
    • (2005) Am. J. Pathol , vol.166 , pp. 1761-1771
    • Tanimukai, H.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 10
    • 19944375450 scopus 로고    scopus 로고
    • Tau pathology in Alzheimer disease and other tauopathies
    • Iqbal K, Alonso Adel C, Chen S et al.: Tau pathology in Alzheimer disease and other tauopathies. Biochim. Biophys. Acta 1739, 198-210 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 198-210
    • Iqbal, K.1    Alonso Adel, C.2    Chen, S.3
  • 11
    • 0032704744 scopus 로고    scopus 로고
    • Tau protein and the paired helical filament of Alzheimer's disease
    • Goedert M, Klug A: Tau protein and the paired helical filament of Alzheimer's disease. Brain Res. Bull. 50, 469-470 (1999).
    • (1999) Brain Res. Bull , vol.50 , pp. 469-470
    • Goedert, M.1    Klug, A.2
  • 13
    • 0030005625 scopus 로고    scopus 로고
    • Tau protein and the neurofibrillary pathology of Alzheimer's disease
    • Goedert M: Tau protein and the neurofibrillary pathology of Alzheimer's disease. Ann. NY Acad. Sci. 777, 121-131 (1996).
    • (1996) Ann. NY Acad. Sci , vol.777 , pp. 121-131
    • Goedert, M.1
  • 14
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • Carmel G, Mager EM, Binder LI, Kuret J: The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J. Biol. Chem. 271, 32789-32795 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 15
    • 0035011587 scopus 로고    scopus 로고
    • Tau-66: Evidence for a novel tau conformation in Alzheimer's disease
    • Ghoshal N, Garcia-Sierra F, Fu Y et al.: Tau-66: evidence for a novel tau conformation in Alzheimer's disease. J. Neurochem. 77, 1372-1385 (2001).
    • (2001) J. Neurochem , vol.77 , pp. 1372-1385
    • Ghoshal, N.1    Garcia-Sierra, F.2    Fu, Y.3
  • 16
    • 0034282067 scopus 로고    scopus 로고
    • Conformational change as one of the earliest alterations of tau in Alzheimer's disease
    • Weaver CL, Espinoza M, Kress Y, Davies P: Conformational change as one of the earliest alterations of tau in Alzheimer's disease. Neurobiol. Aging 21, 719-727 (2000).
    • (2000) Neurobiol. Aging , vol.21 , pp. 719-727
    • Weaver, C.L.1    Espinoza, M.2    Kress, Y.3    Davies, P.4
  • 17
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • Gamblin TC, Chen F, Zambrano A et al.: Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc. Natl Acad. Sci. USA 100, 10032-10037 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10032-10037
    • Gamblin, T.C.1    Chen, F.2    Zambrano, A.3
  • 18
    • 0003986552 scopus 로고
    • Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease
    • Wischik CM, Novak M, Thogersen HC et al.: Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease. Proc. Natl Acad. Sci. USA 85, 4506-4510 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4506-4510
    • Wischik, C.M.1    Novak, M.2    Thogersen, H.C.3
  • 20
    • 0026053022 scopus 로고
    • Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51
    • Novak M, Jakes R, Edwards PC, Milstein C, Wischik CM: Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51. Proc. Natl Acad. Sci. USA 88, 5837-5841 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5837-5841
    • Novak, M.1    Jakes, R.2    Edwards, P.C.3    Milstein, C.4    Wischik, C.M.5
  • 21
    • 3242749074 scopus 로고    scopus 로고
    • Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
    • Rissman RA, Poon WW, Blurton-Jones M et al.: Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology. J. Clin. Invest. 114, 121-130 (2004).
    • (2004) J. Clin. Invest , vol.114 , pp. 121-130
    • Rissman, R.A.1    Poon, W.W.2    Blurton-Jones, M.3
  • 22
    • 0028598882 scopus 로고
    • Tyrosine- versus serine-phosphorylation leads to conformational changes in a synthetic tau peptide
    • Fabian H, Otvos L Jr, Szendrei GI, Lang E, Mantsch HH: Tyrosine- versus serine-phosphorylation leads to conformational changes in a synthetic tau peptide. J. Biomol. Struct. Dyn. 12, 573-579 (1994).
    • (1994) J. Biomol. Struct. Dyn , vol.12 , pp. 573-579
    • Fabian, H.1    Otvos Jr, L.2    Szendrei, G.I.3    Lang, E.4    Mantsch, H.H.5
  • 23
    • 0038291981 scopus 로고    scopus 로고
    • Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease
    • Garcia-Sierra F, Ghoshal N, Quinn B, Berry RW, Binder LI: Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease. J. Alzheimers Dis. 5, 65-77 (2003).
    • (2003) J. Alzheimers Dis , vol.5 , pp. 65-77
    • Garcia-Sierra, F.1    Ghoshal, N.2    Quinn, B.3    Berry, R.W.4    Binder, L.I.5
  • 24
    • 38049030324 scopus 로고    scopus 로고
    • Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease
    • Luna-Munoz J, Chavez-Macias L, Garcia-Sierra F, Mena R: Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease. J. Alzheimers Dis. 12, 365-375 (2007).
    • (2007) J. Alzheimers Dis , vol.12 , pp. 365-375
    • Luna-Munoz, J.1    Chavez-Macias, L.2    Garcia-Sierra, F.3    Mena, R.4
  • 25
    • 40549124991 scopus 로고    scopus 로고
    • Cleavage and conformational changes of tau protein follow phosphorylation during Alzheimer's disease
    • Mondragon-Rodriguez S, Basurto-Islas G, Santa-Maria I et al.: Cleavage and conformational changes of tau protein follow phosphorylation during Alzheimer's disease. Int. J. Exp. Path. 89(2), 81-90 (2008).
    • (2008) Int. J. Exp. Path , vol.89 , Issue.2 , pp. 81-90
    • Mondragon-Rodriguez, S.1    Basurto-Islas, G.2    Santa-Maria, I.3
  • 26
    • 67149127244 scopus 로고    scopus 로고
    • Garcia-Sierra F, Basurto-Islas G, Santa-Maria I, Mena R, Luna-Muñoz J, Binder LI: Tau protein expressed in COS-7 cells displays similar phosphorylation and conformational changes as it occurs in Alzheimer's disease brains. FENS Forum Abstracts 217.7, 4 (2008).
    • Garcia-Sierra F, Basurto-Islas G, Santa-Maria I, Mena R, Luna-Muñoz J, Binder LI: Tau protein expressed in COS-7 cells displays similar phosphorylation and conformational changes as it occurs in Alzheimer's disease brains. FENS Forum Abstracts 217.7, Vol 4 (2008).
  • 27
    • 20044381844 scopus 로고    scopus 로고
    • Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease
    • Guillozet-Bongaarts AL, Garcia-Sierra F, Reynolds MR et al.: Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease. Neurobiol. Aging 26, 1015-1022 (2005).
    • (2005) Neurobiol. Aging , vol.26 , pp. 1015-1022
    • Guillozet-Bongaarts, A.L.1    Garcia-Sierra, F.2    Reynolds, M.R.3
  • 29
    • 1042288284 scopus 로고    scopus 로고
    • Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on β-structure in the core domain
    • Barghorn S, Davies P, Mandelkow E: Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on β-structure in the core domain. Biochemistry 43, 1694-1703 (2004).
    • (2004) Biochemistry , vol.43 , pp. 1694-1703
    • Barghorn, S.1    Davies, P.2    Mandelkow, E.3
  • 30
    • 0037018932 scopus 로고    scopus 로고
    • α-helix structure in Alzheimer's disease aggregates of tau-protein
    • Sadqi M, Hernandez F, Pan U et al.: α-helix structure in Alzheimer's disease aggregates of tau-protein. Biochemistry 41, 7150-7155 (2002).
    • (2002) Biochemistry , vol.41 , pp. 7150-7155
    • Sadqi, M.1    Hernandez, F.2    Pan, U.3
  • 31
    • 0033558929 scopus 로고    scopus 로고
    • Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease
    • Jicha GA, Berenfeld B, Davies P: Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease. J. Neurosci. Res. 55, 713-723 (1999).
    • (1999) J. Neurosci. Res , vol.55 , pp. 713-723
    • Jicha, G.A.1    Berenfeld, B.2    Davies, P.3
  • 32
    • 0030783142 scopus 로고    scopus 로고
    • A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease
    • Jicha GA, Lane E, Vincent I, Otvos L Jr, Hoffmann R, Davies P: A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease. J. Neurochem. 69, 2087-2095 (1997).
    • (1997) J. Neurochem , vol.69 , pp. 2087-2095
    • Jicha, G.A.1    Lane, E.2    Vincent, I.3    Otvos Jr, L.4    Hoffmann, R.5    Davies, P.6
  • 33
    • 24644433910 scopus 로고    scopus 로고
    • Regional conformational change involving phosphorylation of tau protein at the Thr231, precedes the structural change detected by Alz-50 antibody in Alzheimer's disease
    • Luna-Munoz J, Garcia-Sierra F, Falcon V, Menendez I, Chavez-Macias L, Mena R: Regional conformational change involving phosphorylation of tau protein at the Thr231, precedes the structural change detected by Alz-50 antibody in Alzheimer's disease. J. Alzheimers Dis. 8, 29-41 (2005).
    • (2005) J. Alzheimers Dis , vol.8 , pp. 29-41
    • Luna-Munoz, J.1    Garcia-Sierra, F.2    Falcon, V.3    Menendez, I.4    Chavez-Macias, L.5    Mena, R.6
  • 34
    • 57649129018 scopus 로고    scopus 로고
    • Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of tau and generates a pathological (MC-1) conformation
    • Jeganathan S, Hascher A, Chinnathambi S, Biernat J, Mandelkow EM, Mandelkow E: Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of tau and generates a pathological (MC-1) conformation. J. Biol. Chem. 283(46), 32066-32076 (2008).
    • (2008) J. Biol. Chem , vol.283 , Issue.46 , pp. 32066-32076
    • Jeganathan, S.1    Hascher, A.2    Chinnathambi, S.3    Biernat, J.4    Mandelkow, E.M.5    Mandelkow, E.6
  • 35
    • 49149098756 scopus 로고    scopus 로고
    • Truncation of tau protein and its pathological significance in Alzheimer's disease
    • Garcia-Sierra F, Mondragon-Rodriguez S, Basurto-Islas G: Truncation of tau protein and its pathological significance in Alzheimer's disease. J. Alzheimers Dis. 14, 401-409 (2008).
    • (2008) J. Alzheimers Dis , vol.14 , pp. 401-409
    • Garcia-Sierra, F.1    Mondragon-Rodriguez, S.2    Basurto-Islas, G.3
  • 36
    • 0348047709 scopus 로고
    • Alzheimer disease tangles share immunological similarities with multiphosphorylation repeats in the two large neurofilament proteins
    • Lee VM, Otvos L Jr, Schmidt ML, Trojanowski JQ: Alzheimer disease tangles share immunological similarities with multiphosphorylation repeats in the two large neurofilament proteins. Proc. Natl Acad. Sci. USA 85, 7384-7388 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7384-7388
    • Lee, V.M.1    Otvos Jr, L.2    Schmidt, M.L.3    Trojanowski, J.Q.4
  • 37
    • 40749131329 scopus 로고    scopus 로고
    • Linkage-dependent contribution of repeat peptides to self-aggregation of three- or four-repeat microtubule-binding domains in tau protein
    • Okuyama K, Nishiura C, Mizushima F et al.: Linkage-dependent contribution of repeat peptides to self-aggregation of three- or four-repeat microtubule-binding domains in tau protein. FEBS J. 275, 1529-1539 (2008).
    • (2008) FEBS J , vol.275 , pp. 1529-1539
    • Okuyama, K.1    Nishiura, C.2    Mizushima, F.3
  • 39
    • 34748824095 scopus 로고    scopus 로고
    • Phosphorylation modulates the local conformation and self-aggregation ability of a peptide from the fourth tau microtubule-binding repeat
    • Du JT, Yu CH, Zhou LX et al.: Phosphorylation modulates the local conformation and self-aggregation ability of a peptide from the fourth tau microtubule-binding repeat. FEBS J. 274, 5012-5020 (2007).
    • (2007) FEBS J , vol.274 , pp. 5012-5020
    • Du, J.T.1    Yu, C.H.2    Zhou, L.X.3
  • 40
    • 0036434880 scopus 로고    scopus 로고
    • Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease
    • Ghoshal N, Garcia-Sierra F, Wuu J et al.: Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease. Exp. Neurol. 177, 475-493 (2002).
    • (2002) Exp. Neurol , vol.177 , pp. 475-493
    • Ghoshal, N.1    Garcia-Sierra, F.2    Wuu, J.3
  • 41
    • 14744300176 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: An implication to Alzheimer's disease
    • Kang HJ, Yoon WJ, Moon GJ et al.: Caspase-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: an implication to Alzheimer's disease. Neurobiol. Dis. 18, 450-458 (2005).
    • (2005) Neurobiol. Dis , vol.18 , pp. 450-458
    • Kang, H.J.1    Yoon, W.J.2    Moon, G.J.3
  • 42
  • 43
    • 0027398169 scopus 로고
    • Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • Novak M, Kabat J, Wischik CM: Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO J. 12, 365-370 (1993).
    • (1993) EMBO J , vol.12 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 44
    • 0028458037 scopus 로고
    • Truncated tau protein as a new marker for Alzheimer's disease
    • Novak M: Truncated tau protein as a new marker for Alzheimer's disease. Acta Virol. 38, 173-189 (1994).
    • (1994) Acta Virol , vol.38 , pp. 173-189
    • Novak, M.1
  • 46
    • 0035141757 scopus 로고    scopus 로고
    • Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease
    • Rohn TT, Head E, Su JH et al.: Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease. Am. J. Pathol. 158, 189-198 (2001).
    • (2001) Am. J. Pathol , vol.158 , pp. 189-198
    • Rohn, T.T.1    Head, E.2    Su, J.H.3
  • 47
    • 33746269428 scopus 로고    scopus 로고
    • Coordinated expression of caspase 8, 3 and 7 mRNA in temporal cortex of Alzheimer disease: Relationship to formic acid extractable αβ42 levels
    • Matsui T, Ramasamy K, Ingelsson M et al.: Coordinated expression of caspase 8, 3 and 7 mRNA in temporal cortex of Alzheimer disease: relationship to formic acid extractable αβ42 levels. J. Neuropathol. Exp. Neurol. 65, 508-515 (2006).
    • (2006) J. Neuropathol. Exp. Neurol , vol.65 , pp. 508-515
    • Matsui, T.1    Ramasamy, K.2    Ingelsson, M.3
  • 48
    • 33748466130 scopus 로고    scopus 로고
    • Apoptosis in Alzheimer disease: A mathematical improbability
    • Zhu X, Raina AK, Perry G, Smith MA: Apoptosis in Alzheimer disease: a mathematical improbability. Curr. Alzheimer Res. 3, 393-396 (2006).
    • (2006) Curr. Alzheimer Res , vol.3 , pp. 393-396
    • Zhu, X.1    Raina, A.K.2    Perry, G.3    Smith, M.A.4
  • 50
    • 0033928035 scopus 로고    scopus 로고
    • The neuronal microtubule-associated protein tau is a substrate for caspase-3 and an effector of apoptosis
    • Fasulo L, Ugolini G, Visintin M et al.: The neuronal microtubule-associated protein tau is a substrate for caspase-3 and an effector of apoptosis. J. Neurochem. 75, 624-633 (2000).
    • (2000) J. Neurochem , vol.75 , pp. 624-633
    • Fasulo, L.1    Ugolini, G.2    Visintin, M.3
  • 51
    • 11144228296 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 β induces caspase-cleaved tau aggregation in situ
    • Cho JH, Johnson GV: Glycogen synthase kinase 3 β induces caspase-cleaved tau aggregation in situ. J. Biol. Chem. 279, 54716-54723 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 54716-54723
    • Cho, J.H.1    Johnson, G.V.2
  • 52
    • 0035116325 scopus 로고    scopus 로고
    • Proapoptotic effects of tau cleavage product generated by caspase-3
    • Chung CW, Song YH, Kim IK et al.: Proapoptotic effects of tau cleavage product generated by caspase-3. Neurobiol. Dis. 8, 162-172 (2001).
    • (2001) Neurobiol. Dis , vol.8 , pp. 162-172
    • Chung, C.W.1    Song, Y.H.2    Kim, I.K.3
  • 53
    • 34548162377 scopus 로고    scopus 로고
    • Activation of glycogen synthase kinase 3β promotes the intermolecular association of tau. The use of fluorescence resonance energy transfer microscopy
    • Chun W, Johnson GV: Activation of glycogen synthase kinase 3β promotes the intermolecular association of tau. The use of fluorescence resonance energy transfer microscopy. J. Biol. Chem. 282, 23410-23417 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 23410-23417
    • Chun, W.1    Johnson, G.V.2
  • 54
    • 33845966445 scopus 로고    scopus 로고
    • Neurodegeneration caused by expres- sion of human truncated tau leads to progressive neurobehavioural impairment in transgenic rats
    • Hrnkova M, Zilka N, Minichova Z, Koson P, Novak M: Neurodegeneration caused by expres- sion of human truncated tau leads to progressive neurobehavioural impairment in transgenic rats. Brain Res. 1130, 206-213 (2007).
    • (2007) Brain Res , vol.1130 , pp. 206-213
    • Hrnkova, M.1    Zilka, N.2    Minichova, Z.3    Koson, P.4    Novak, M.5
  • 55
    • 33747606218 scopus 로고    scopus 로고
    • Expression of a truncated tau protein induces oxidative stress in a rodent model of tauopathy
    • Cente M, Filipcik P, Pevalova M, Novak M: Expression of a truncated tau protein induces oxidative stress in a rodent model of tauopathy. Eur. J. Neurosci. 24, 1085-1090 (2006).
    • (2006) Eur. J. Neurosci , vol.24 , pp. 1085-1090
    • Cente, M.1    Filipcik, P.2    Pevalova, M.3    Novak, M.4
  • 56
    • 48249130806 scopus 로고    scopus 로고
    • Truncated tau expression levels determine life span of a rat model of tauopathy without causing neuronal loss or correlating with terminal neurofibrillary tangle load
    • Koson P, Zilka N, Kovac A et al.: Truncated tau expression levels determine life span of a rat model of tauopathy without causing neuronal loss or correlating with terminal neurofibrillary tangle load. Eur. J. Neurosci. 28, 239-246 (2008).
    • (2008) Eur. J. Neurosci , vol.28 , pp. 239-246
    • Koson, P.1    Zilka, N.2    Kovac, A.3
  • 57
    • 0347594304 scopus 로고    scopus 로고
    • Modeling tau polymerization in vitro: A review and synthesis
    • Gamblin TC, Berry RW, Binder LI: Modeling tau polymerization in vitro: a review and synthesis. Biochemistry 42, 15009-15017 (2003).
    • (2003) Biochemistry , vol.42 , pp. 15009-15017
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 58
    • 38749144389 scopus 로고    scopus 로고
    • Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy
    • Delobel P, Lavenir I, Fraser G et al.: Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy. Am. J. Pathol. 172, 123-131 (2008).
    • (2008) Am. J. Pathol , vol.172 , pp. 123-131
    • Delobel, P.1    Lavenir, I.2    Fraser, G.3
  • 59
    • 0023505501 scopus 로고
    • Phosphorylation determines two distinct species of tau in the central nervous system
    • Papasozomenos SC, Binder LI: Phosphorylation determines two distinct species of tau in the central nervous system. Cell Motil. Cytoskeleton 8, 210-226 (1987).
    • (1987) Cell Motil. Cytoskeleton , vol.8 , pp. 210-226
    • Papasozomenos, S.C.1    Binder, L.I.2
  • 60
    • 0026611728 scopus 로고
    • Immunological and conformation characterization of a phosphorylated immunodominant epitope on the paired helical filaments found in Alzheimer's disease
    • Lang E, Szendrei GI, Lee VM, Otvos L Jr: Immunological and conformation characterization of a phosphorylated immunodominant epitope on the paired helical filaments found in Alzheimer's disease. Biochem. Biophys. Res. Commun. 187, 783-790 (1992).
    • (1992) Biochem. Biophys. Res. Commun , vol.187 , pp. 783-790
    • Lang, E.1    Szendrei, G.I.2    Lee, V.M.3    Otvos Jr, L.4
  • 61
    • 0033548661 scopus 로고    scopus 로고
    • Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau
    • Watanabe A, Takio K, Ihara Y: Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau. J. Biol. Chem. 274, 7368-7378 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 7368-7378
    • Watanabe, A.1    Takio, K.2    Ihara, Y.3
  • 62
    • 0022457104 scopus 로고
    • A neuronal antigen in the brains of Alzheimer patients
    • Wolozin BL, Pruchnicki A, Dickson DW, Davies P: A neuronal antigen in the brains of Alzheimer patients. Science 232, 648-650 (1986).
    • (1986) Science , vol.232 , pp. 648-650
    • Wolozin, B.L.1    Pruchnicki, A.2    Dickson, D.W.3    Davies, P.4
  • 64
    • 0028902487 scopus 로고
    • Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B
    • Wang JZ, Gong CX, Zaidi T, Grundke-Iqbal I, Iqbal K: Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B. J. Biol. Chem. 270, 4854-4860 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 4854-4860
    • Wang, J.Z.1    Gong, C.X.2    Zaidi, T.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 65
    • 0029995590 scopus 로고    scopus 로고
    • Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-2A, -2B and -1
    • Wang JZ, Grundke-Iqbal I, Iqbal K: Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-2A, -2B and -1. Brain Res. Mol. Brain Res. 38, 200-208 (1996).
    • (1996) Brain Res. Mol. Brain Res , vol.38 , pp. 200-208
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 66
    • 62349108360 scopus 로고    scopus 로고
    • The senescence-accelerated mouse (SAM): A higher oxidative stress and age-dependent degenerative diseases model
    • DOI: 10.1007/s11064-008-9812-8
    • Chiba Y, Shimada A, Kumagai N et al.: The senescence-accelerated mouse (SAM): a higher oxidative stress and age-dependent degenerative diseases model. Neurochem. Res. DOI: 10.1007/s11064-008-9812-8 (2008).
    • (2008) Neurochem. Res
    • Chiba, Y.1    Shimada, A.2    Kumagai, N.3
  • 67
    • 53049093018 scopus 로고    scopus 로고
    • Neurodegeneration in multiple sclerosis: The role of oxidative stress and excitotoxicity
    • Gonsette RE: Neurodegeneration in multiple sclerosis: the role of oxidative stress and excitotoxicity. J. Neurol. Sci. 274, 48-53 (2008).
    • (2008) J. Neurol. Sci , vol.274 , pp. 48-53
    • Gonsette, R.E.1
  • 68
    • 48449092905 scopus 로고    scopus 로고
    • Malondialdehyde, carbonyl proteins and albumin-disulphide as useful oxidative markers in mild cognitive impairment and Alzheimer's disease
    • Greilberger J, Koidl C, Greilberger M et al.: Malondialdehyde, carbonyl proteins and albumin-disulphide as useful oxidative markers in mild cognitive impairment and Alzheimer's disease. Free Radic. Res. 42, 633-638 (2008).
    • (2008) Free Radic. Res , vol.42 , pp. 633-638
    • Greilberger, J.1    Koidl, C.2    Greilberger, M.3
  • 69
    • 41749088686 scopus 로고    scopus 로고
    • Neuronal death and survival under oxidative stress in Alzheimer and Parkinson diseases
    • Nunomura A, Moreira PI, Lee HG et al.: Neuronal death and survival under oxidative stress in Alzheimer and Parkinson diseases. CNS Neurol. Disord. Drug Targets 6, 411-423 (2007).
    • (2007) CNS Neurol. Disord. Drug Targets , vol.6 , pp. 411-423
    • Nunomura, A.1    Moreira, P.I.2    Lee, H.G.3
  • 70
    • 46449083451 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in neurodegeneration; cardiolipin a critical target?
    • Pope S, Land JM, Heales SJ: Oxidative stress and mitochondrial dysfunction in neurodegeneration; cardiolipin a critical target? Biochim. Biophys. Acta 1777, 794-799 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 794-799
    • Pope, S.1    Land, J.M.2    Heales, S.J.3
  • 71
    • 24644443839 scopus 로고    scopus 로고
    • Oxidative stress: The old enemy in Alzheimer's disease pathophysiology
    • Moreira PI, Honda K, Liu Q et al.: Oxidative stress: the old enemy in Alzheimer's disease pathophysiology. Curr. Alzheimer Res. 2, 403-408 (2005).
    • (2005) Curr. Alzheimer Res , vol.2 , pp. 403-408
    • Moreira, P.I.1    Honda, K.2    Liu, Q.3
  • 72
    • 13844267510 scopus 로고    scopus 로고
    • Alzheimer-specific epitopes of tau represent lipid peroxidation-induced conformations
    • Liu Q, Smith MA, Avila J et al.: Alzheimer-specific epitopes of tau represent lipid peroxidation-induced conformations. Free Radic. Biol. Med. 38, 746-754 (2005).
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 746-754
    • Liu, Q.1    Smith, M.A.2    Avila, J.3
  • 73
    • 0041819641 scopus 로고    scopus 로고
    • Aggregation analysis of the microtubule binding domain in tau protein by spectroscopic methods
    • Yao TM, Tomoo K, Ishida T, Hasegawa H, Sasaki M, Taniguchi T: Aggregation analysis of the microtubule binding domain in tau protein by spectroscopic methods. J. Biochem. 134, 91-99 (2003).
    • (2003) J. Biochem , vol.134 , pp. 91-99
    • Yao, T.M.1    Tomoo, K.2    Ishida, T.3    Hasegawa, H.4    Sasaki, M.5    Taniguchi, T.6
  • 74
    • 33646365908 scopus 로고    scopus 로고
    • Hyperphosphorylation of tau induces local polyproline II helix
    • Bielska AA, Zondlo NJ: Hyperphosphorylation of tau induces local polyproline II helix. Biochemistry 45, 5527-5537 (2006).
    • (2006) Biochemistry , vol.45 , pp. 5527-5537
    • Bielska, A.A.1    Zondlo, N.J.2
  • 75
    • 11144283513 scopus 로고    scopus 로고
    • Transcriptional and conformational changes of the tau molecule in Alzheimer's disease
    • Hyman BT, Augustinack JC, Ingelsson M: Transcriptional and conformational changes of the tau molecule in Alzheimer's disease. Biochim. Biophys. Acta 1739, 150-157 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 150-157
    • Hyman, B.T.1    Augustinack, J.C.2    Ingelsson, M.3
  • 76
    • 29344434456 scopus 로고    scopus 로고
    • C-terminal truncation modulates both nucleation and extension phases of tau fibrillization
    • Yin H, Kuret J: C-terminal truncation modulates both nucleation and extension phases of tau fibrillization. FEBS Lett. 580, 211-215 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 211-215
    • Yin, H.1    Kuret, J.2
  • 77
    • 57649233091 scopus 로고    scopus 로고
    • Characterization of truncated forms of abnormal prion protein in Creutzfeldt-Jakob disease
    • Notari S, Strammiello R, Capellari S et al.: Characterization of truncated forms of abnormal prion protein in Creutzfeldt-Jakob disease. J. Biol. Chem. 283(45), 30557-30565 (2008).
    • (2008) J. Biol. Chem , vol.283 , Issue.45 , pp. 30557-30565
    • Notari, S.1    Strammiello, R.2    Capellari, S.3
  • 78
    • 0034929144 scopus 로고    scopus 로고
    • Accumulation of C-terminally truncated tau protein associated with vulnerability of the perforant pathway in early stages of neurofibrillary pathology in Alzheimer's disease
    • Garcia-Sierra F, Wischik CM, Harrington CR, Luna-Munoz J, Mena R: Accumulation of C-terminally truncated tau protein associated with vulnerability of the perforant pathway in early stages of neurofibrillary pathology in Alzheimer's disease. J. Chem. Neuroanat. 22, 65-77 (2001).
    • (2001) J. Chem. Neuroanat , vol.22 , pp. 65-77
    • Garcia-Sierra, F.1    Wischik, C.M.2    Harrington, C.R.3    Luna-Munoz, J.4    Mena, R.5
  • 79
    • 33751557958 scopus 로고    scopus 로고
    • Caspase-3- and calpain-mediated tau cleavage are differentially prevented by estrogen and testosterone in β-amyloid-treated hippocampal neurons
    • Park SY, Tournell C, Sinjoanu RC, Ferreira A: Caspase-3- and calpain-mediated tau cleavage are differentially prevented by estrogen and testosterone in β-amyloid-treated hippocampal neurons. Neuroscience 144, 119-127 (2007).
    • (2007) Neuroscience , vol.144 , pp. 119-127
    • Park, S.Y.1    Tournell, C.2    Sinjoanu, R.C.3    Ferreira, A.4
  • 80
    • 41149176407 scopus 로고    scopus 로고
    • Lack of pathology in a triple transgenic mouse model of Alzheimer's disease after overexpression of the anti-apoptotic protein Bcl-2
    • Rohn TT, Vyas V, Hernandez-Estrada T, Nichol KE, Christie LA, Head E: Lack of pathology in a triple transgenic mouse model of Alzheimer's disease after overexpression of the anti-apoptotic protein Bcl-2. J. Neurosci. 28, 3051-3059 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 3051-3059
    • Rohn, T.T.1    Vyas, V.2    Hernandez-Estrada, T.3    Nichol, K.E.4    Christie, L.A.5    Head, E.6
  • 81
    • 0033677809 scopus 로고    scopus 로고
    • C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease
    • Abraha A, Ghoshal N, Gamblin TC et al.: C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease. J. Cell Sci. 113 (Pt21), 3737-3745 (2000).
    • (2000) J. Cell Sci , vol.113 , Issue.PT21 , pp. 3737-3745
    • Abraha, A.1    Ghoshal, N.2    Gamblin, T.C.3
  • 82
    • 0037826853 scopus 로고    scopus 로고
    • Inhibition of tau polymerization by its carboxy-terminal caspase cleavage fragment
    • Berry RW, Abraha A, Lagalwar S et al.: Inhibition of tau polymerization by its carboxy-terminal caspase cleavage fragment. Biochemistry 42, 8325-8331 (2003).
    • (2003) Biochemistry , vol.42 , pp. 8325-8331
    • Berry, R.W.1    Abraha, A.2    Lagalwar, S.3
  • 83
    • 0037465354 scopus 로고    scopus 로고
    • Tau polymerization: Role of the amino terminus
    • Gamblin TC, Berry RW, Binder LI: Tau polymerization: role of the amino terminus. Biochemistry 42, 2252-2257(2003).
    • (2003) Biochemistry , vol.42 , pp. 2252-2257
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 84
    • 0030463704 scopus 로고    scopus 로고
    • Overexpression of Alzheimer's PHF core tau fragments: Implications for the tau truncation hypothesis
    • Fasulo L, Ovecka M, Kabat J, Bradbury A, Novak M, Cattaneo A: Overexpression of Alzheimer's PHF core tau fragments: implications for the tau truncation hypothesis. Alzheimers Res. 2, 195-200 (1996).
    • (1996) Alzheimers Res , vol.2 , pp. 195-200
    • Fasulo, L.1    Ovecka, M.2    Kabat, J.3    Bradbury, A.4    Novak, M.5    Cattaneo, A.6
  • 85
    • 15244347753 scopus 로고    scopus 로고
    • Apoptotic effect of caspase-3 cleaved tau in hippocampal neurons and its potentiation by tau FTDP-mutation N279K
    • Fasulo L, Ugolini G, Cattaneo A: Apoptotic effect of caspase-3 cleaved tau in hippocampal neurons and its potentiation by tau FTDP-mutation N279K. J. Alzheimers Dis. 7, 3-13 (2005).
    • (2005) J. Alzheimers Dis , vol.7 , pp. 3-13
    • Fasulo, L.1    Ugolini, G.2    Cattaneo, A.3
  • 86
    • 33745152289 scopus 로고    scopus 로고
    • Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo
    • Zilka N, Filipcik P, Koson P et al.: Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo. FEBS Lett. 580, 3582-3588 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 3582-3588
    • Zilka, N.1    Filipcik, P.2    Koson, P.3
  • 87
    • 23744482703 scopus 로고    scopus 로고
    • Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates
    • Vega IE, Cui L, Propst JA, Hutton ML, Lee G, Yen SH: Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates. Brain Res. Mol. Brain Res. 138, 135-144 (2005).
    • (2005) Brain Res. Mol. Brain Res , vol.138 , pp. 135-144
    • Vega, I.E.1    Cui, L.2    Propst, J.A.3    Hutton, M.L.4    Lee, G.5    Yen, S.H.6
  • 90
    • 33847674888 scopus 로고    scopus 로고
    • Phosphorylation of tau antagonizes apoptosis by stabilizing β-catenin, a mechanism involved in Alzheimer's neurodegeneration
    • Li HL, Wang HH, Liu SJ et al.: Phosphorylation of tau antagonizes apoptosis by stabilizing β-catenin, a mechanism involved in Alzheimer's neurodegeneration. Proc. Natl Acad. Sci. USA 104, 3591-3596 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 3591-3596
    • Li, H.L.1    Wang, H.H.2    Liu, S.J.3
  • 91
    • 0035851157 scopus 로고    scopus 로고
    • Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein
    • Alonso AD, Zaidi T, Novak M, Barra HS, Grundke-Iqbal I, Iqbal K: Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein. J. Biol. Chem. 276, 37967-37973 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 37967-37973
    • Alonso, A.D.1    Zaidi, T.2    Novak, M.3    Barra, H.S.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 92
    • 33745024475 scopus 로고    scopus 로고
    • Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity
    • Alonso Adel C, Li B, Grundke-Iqbal I, Iqbal K: Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity. Proc. Natl Acad. Sci. USA 103, 8864-8869 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8864-8869
    • Alonso Adel, C.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 93
    • 33746355958 scopus 로고    scopus 로고
    • Axonal transport and Alzheimer's disease
    • Stokin GB, Goldstein LS: Axonal transport and Alzheimer's disease. Annu. Rev. Biochem. 75, 607-627 (2006).
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 607-627
    • Stokin, G.B.1    Goldstein, L.S.2
  • 94
    • 33645019621 scopus 로고    scopus 로고
    • Linking molecular motors to Alzheimer's disease
    • Stokin GB, Goldstein LS: Linking molecular motors to Alzheimer's disease. J. Physiol. Paris 99, 193-200 (2006).
    • (2006) J. Physiol. Paris , vol.99 , pp. 193-200
    • Stokin, G.B.1    Goldstein, L.S.2
  • 95
    • 20044385920 scopus 로고    scopus 로고
    • Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease
    • Stokin GB, Lillo C, Falzone TL et al.: Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 307, 1282-1288 (2005).
    • (2005) Science , vol.307 , pp. 1282-1288
    • Stokin, G.B.1    Lillo, C.2    Falzone, T.L.3
  • 96
    • 34147161245 scopus 로고    scopus 로고
    • In vivo axonal transport rates decrease in a mouse model of Alzheimer's disease
    • Smith KD, Kallhoff V, Zheng H, Pautler RG: In vivo axonal transport rates decrease in a mouse model of Alzheimer's disease. Neuroimage 35, 1401-1408 (2007).
    • (2007) Neuroimage , vol.35 , pp. 1401-1408
    • Smith, K.D.1    Kallhoff, V.2    Zheng, H.3    Pautler, R.G.4
  • 97
    • 35748954923 scopus 로고    scopus 로고
    • The β-propensity of tau determines aggregation and synaptic loss in inducible mouse models of tauopathy
    • Eckermann K, Mocanu MM, Khlistunova I et al.: The β-propensity of tau determines aggregation and synaptic loss in inducible mouse models of tauopathy. J. Biol. Chem. 282, 31755-31765 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 31755-31765
    • Eckermann, K.1    Mocanu, M.M.2    Khlistunova, I.3
  • 98
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer K, Vogel R, Thies E, Mandelkow E, Mandelkow EM: Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J. Cell Biol. 156, 1051-1063 (2002).
    • (2002) J. Cell Biol , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 99
    • 34250317264 scopus 로고    scopus 로고
    • Tau binding to microtubules does not directly affect microtubule-based vesicle motility
    • Morfini G, Pigino G, Mizuno N, Kikkawa M, Brady ST: Tau binding to microtubules does not directly affect microtubule-based vesicle motility. J. Neurosci. Res. 85, 2620-2630 (2007).
    • (2007) J. Neurosci. Res , vol.85 , pp. 2620-2630
    • Morfini, G.1    Pigino, G.2    Mizuno, N.3    Kikkawa, M.4    Brady, S.T.5
  • 100
    • 21444454231 scopus 로고    scopus 로고
    • Axonal transport hypothesis moves on to implicate presenilin: Alzheimer research forum live discussion
    • Axonal transport hypothesis moves on to implicate presenilin: Alzheimer research forum live discussion. J. Alzheimers Dis. 6, 537-545 (2004).
    • (2004) J. Alzheimers Dis , vol.6 , pp. 537-545
  • 101
    • 0036047004 scopus 로고    scopus 로고
    • Axonal transport, tau protein, and neurodegeneration in Alzheimer's disease
    • Terwel D, Dewachter I, Van Leuven F: Axonal transport, tau protein, and neurodegeneration in Alzheimer's disease. Neuromolecular Med. 2, 151-165 (2002).
    • (2002) Neuromolecular Med , vol.2 , pp. 151-165
    • Terwel, D.1    Dewachter, I.2    Van Leuven, F.3
  • 102
    • 0037032099 scopus 로고    scopus 로고
    • Impaired axonal transport of cortical neurons in Alzheimer's disease is associated with neuropathological changes
    • Dai J, Buijs RM, Kamphorst W, Swaab DF: Impaired axonal transport of cortical neurons in Alzheimer's disease is associated with neuropathological changes. Brain Res. 948, 138-144 (2002).
    • (2002) Brain Res , vol.948 , pp. 138-144
    • Dai, J.1    Buijs, R.M.2    Kamphorst, W.3    Swaab, D.F.4
  • 103
    • 51349143580 scopus 로고    scopus 로고
    • Phosphorylation of tau regulates its axonal transport by controlling its binding to kinesin
    • Cuchillo-Ibanez I, Seereeram A, Byers HL et al.: Phosphorylation of tau regulates its axonal transport by controlling its binding to kinesin. FASEB J. 22, 3186-3195 (2008).
    • (2008) FASEB J , vol.22 , pp. 3186-3195
    • Cuchillo-Ibanez, I.1    Seereeram, A.2    Byers, H.L.3
  • 104
    • 67149133851 scopus 로고    scopus 로고
    • Aggregation mechanism investigation of the GIFQINS cross-β amyloid fibril
    • Chen HF: Aggregation mechanism investigation of the GIFQINS cross-β amyloid fibril. Comput. Biol. Chem. (2008).
    • (2008) Comput. Biol. Chem
    • Chen, H.F.1
  • 105
    • 50649114611 scopus 로고    scopus 로고
    • Amyloid-β dynamics correlate with neurological status in the injured human brain
    • Brody DL, Magnoni S, Schwetye KE et al.: Amyloid-β dynamics correlate with neurological status in the injured human brain. Science 321, 1221-1224 (2008).
    • (2008) Science , vol.321 , pp. 1221-1224
    • Brody, D.L.1    Magnoni, S.2    Schwetye, K.E.3
  • 106
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain
    • Takahashi RH, Almeida CG, Kearney PF et al.: Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain. J. Neurosci. 24, 3592-3599 (2004).
    • (2004) J. Neurosci , vol.24 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3
  • 107
    • 51849126363 scopus 로고    scopus 로고
    • Phosphorylated tau in neuritic plaques of APP(sw)/Tau (vlw) transgenic mice and Alzheimer disease
    • Perez M, Moran MA, Ferrer I, Avila J, Gomez-Ramos P: Phosphorylated tau in neuritic plaques of APP(sw)/Tau (vlw) transgenic mice and Alzheimer disease. Acta Neuropathol. 116, 409-418 (2008).
    • (2008) Acta Neuropathol , vol.116 , pp. 409-418
    • Perez, M.1    Moran, M.A.2    Ferrer, I.3    Avila, J.4    Gomez-Ramos, P.5
  • 109
    • 33644851265 scopus 로고    scopus 로고
    • Inducible expression of tau repeat domain in cell models of tauopathy: Aggregation is toxic to cells but can be reversed by inhibitor drugs
    • Khlistunova I, Biernat J, Wang Y et al.: Inducible expression of tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs. J. Biol. Chem. 281, 1205-1214 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 1205-1214
    • Khlistunova, I.1    Biernat, J.2    Wang, Y.3
  • 110
    • 0035958642 scopus 로고    scopus 로고
    • Tauopathy in Drosophila: Neurodegeneration without neurofibrillary tangles
    • Wittmann CW, Wszolek MF, Shulman JM et al.: Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles. Science 293, 711-714 (2001).
    • (2001) Science , vol.293 , pp. 711-714
    • Wittmann, C.W.1    Wszolek, M.F.2    Shulman, J.M.3
  • 111
    • 51349125291 scopus 로고    scopus 로고
    • Neuronal apoptosis and autophagy cross talk in aging PS/APP mice, a model of Alzheimer's disease
    • Yang DS, Kumar A, Stavrides P et al.: Neuronal apoptosis and autophagy cross talk in aging PS/APP mice, a model of Alzheimer's disease. Am. J. Pathol. 173, 665-681 (2008).
    • (2008) Am. J. Pathol , vol.173 , pp. 665-681
    • Yang, D.S.1    Kumar, A.2    Stavrides, P.3
  • 113
    • 33244456786 scopus 로고    scopus 로고
    • Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease
    • Maeda S, Sahara N, Saito Y, Murayama S, Ikai A, Takashima A: Increased levels of granular tau oligomers: an early sign of brain aging and Alzheimer's disease. Neurosci. Res. 54, 197-201 (2006).
    • (2006) Neurosci. Res , vol.54 , pp. 197-201
    • Maeda, S.1    Sahara, N.2    Saito, Y.3    Murayama, S.4    Ikai, A.5    Takashima, A.6
  • 114
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments
    • Alonso A, Zaidi T, Novak M, Grundke-Iqbal I, Iqbal K: Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc. Natl Acad. Sci. USA 98, 6923-6928 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 6923-6928
    • Alonso, A.1    Zaidi, T.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 115
    • 55249086251 scopus 로고    scopus 로고
    • Hyperphosphorylation of microtubule-associated protein tau: A promising therapeutic target for Alzheimer disease
    • Gong CX, Iqbal K: Hyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer disease. Curr. Med. Chem. 15, 2321-2328 (2008).
    • (2008) Curr. Med. Chem , vol.15 , pp. 2321-2328
    • Gong, C.X.1    Iqbal, K.2
  • 116
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease
    • Alonso AC, Zaidi T, Grundke-Iqbal I, Iqbal K: Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc. Natl Acad. Sci. USA 91, 5562-5566 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5562-5566
    • Alonso, A.C.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 117
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • Alonso AC, Grundke-Iqbal I, Iqbal K: Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat. Med. 2, 783-787 (1996).
    • (1996) Nat. Med , vol.2 , pp. 783-787
    • Alonso, A.C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 118
    • 49149105134 scopus 로고    scopus 로고
    • Cytosolic abnormally hyperphosphorylated tau but not paired helical filaments sequester normal MAPs and inhibit microtubule assembly
    • Iqbal K, Alonso Adel C, Grundke-Iqbal I: Cytosolic abnormally hyperphosphorylated tau but not paired helical filaments sequester normal MAPs and inhibit microtubule assembly. J. Alzheimers Dis. 14, 365-370 (2008).
    • (2008) J. Alzheimers Dis , vol.14 , pp. 365-370
    • Iqbal, K.1    Alonso Adel, C.2    Grundke-Iqbal, I.3
  • 120
    • 33646080573 scopus 로고    scopus 로고
    • Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: In vitro evidence and implications for tangle formation in vivo
    • Guillozet-Bongaarts AL, Cahill ME, Cryns VL, Reynolds MR, Berry RW, Binder LI: Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo. J. Neurochem. 97, 1005-1014 (2006).
    • (2006) J. Neurochem , vol.97 , pp. 1005-1014
    • Guillozet-Bongaarts, A.L.1    Cahill, M.E.2    Cryns, V.L.3    Reynolds, M.R.4    Berry, R.W.5    Binder, L.I.6
  • 121
    • 17044435830 scopus 로고    scopus 로고
    • Tau phosphorylation in Alzheimer's disease: Pathogen or protector?
    • Lee HG, Perry G, Moreira PI et al.: Tau phosphorylation in Alzheimer's disease: pathogen or protector? Trends Mol. Med. 11, 164-169 (2005).
    • (2005) Trends Mol. Med , vol.11 , pp. 164-169
    • Lee, H.G.1    Perry, G.2    Moreira, P.I.3
  • 122
    • 34548689646 scopus 로고    scopus 로고
    • Alzhemed: A potential treatment for Alzheimer's disease
    • Aisen PS, Gauthier S, Vellas B et al.: Alzhemed: a potential treatment for Alzheimer's disease. Curr. Alzheimer Res. 4, 473-478 (2007).
    • (2007) Curr. Alzheimer Res , vol.4 , pp. 473-478
    • Aisen, P.S.1    Gauthier, S.2    Vellas, B.3
  • 123
    • 35748977086 scopus 로고    scopus 로고
    • Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau
    • Santa-Maria I, Hernandez F, Del Rio J, Moreno FJ, Avila J: Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau. Mol. Neurodegener. 2, 17 (2007).
    • (2007) Mol. Neurodegener , vol.2 , pp. 17
    • Santa-Maria, I.1    Hernandez, F.2    Del Rio, J.3    Moreno, F.J.4    Avila, J.5
  • 125
    • 41649089737 scopus 로고    scopus 로고
    • Neural network dysfunction in Alzheimer's disease: A drug development perspective
    • Small DH: Neural network dysfunction in Alzheimer's disease: a drug development perspective. Drug News Perspect. 20, 557-563 (2007).
    • (2007) Drug News Perspect , vol.20 , pp. 557-563
    • Small, D.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.