메뉴 건너뛰기




Volumn 9, Issue DEC2016, 2016, Pages

The role of the carboxyl-terminal sequence of tau and MAP2 in the pathogenesis of Dementia

Author keywords

Alzheimer s disease; Inclusion; MAP2; Microtubule associated protein 2; Tau; Tauopathy

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN 2; TAU PROTEIN;

EID: 85010961057     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2016.00158     Document Type: Review
Times cited : (16)

References (53)
  • 1
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer’s disease
    • Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., and Hyman, B. T. (1992). Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer’s disease. Neurology 42, 631–639.
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 2
    • 0030805991 scopus 로고    scopus 로고
    • Frequency of stages of Alzheimer-related lesions in different age categories
    • Braak, H., and Braak, E. (1997). Frequency of stages of Alzheimer-related lesions in different age categories. Neurobiol. Aging 18, 351–357.
    • (1997) Neurobiol. Aging , vol.18 , pp. 351-357
    • Braak, H.1    Braak, E.2
  • 3
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • Braak, E., Braak, H., and Mandelkow, E. M. (1994). A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol. 87, 554–567.
    • (1994) Acta Neuropathol , vol.87 , pp. 554-567
    • Braak, E.1    Braak, H.2    Mandelkow, E.M.3
  • 4
    • 79953087890 scopus 로고    scopus 로고
    • The acetylation of tau inhibits its function and promotes pathological tau aggregation
    • Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., et al. (2011). The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat. Commun. 2:252.
    • (2011) Nat. Commun , vol.2 , pp. 252
    • Cohen, T.J.1    Guo, J.L.2    Hurtado, D.E.3    Kwong, L.K.4    Mills, I.P.5    Trojanowski, J.Q.6
  • 5
    • 84864505483 scopus 로고    scopus 로고
    • Evidence for a role of the rare p.A152T variant in MAPT in increasing the risk for FTD-spectrum and Alzheimer’s diseases
    • Coppola, G., Chinnathambi, S., Lee, J. J., Dombroski, B. A., Baker, M. C., Soto-Ortolaza, A. I., et al. (2012). Evidence for a role of the rare p.A152T variant in MAPT in increasing the risk for FTD-spectrum and Alzheimer’s diseases. Hum. Mol. Genet. 21, 3500–3512.
    • (2012) Hum. Mol. Genet , vol.21 , pp. 3500-3512
    • Coppola, G.1    Chinnathambi, S.2    Lee, J.J.3    Dombroski, B.A.4    Baker, M.C.5    Soto-Ortolaza, A.I.6
  • 6
    • 84883503648 scopus 로고    scopus 로고
    • Are tau aggregates toxic or protective in tauopathies?
    • Cowan, C. M., and Mudher, A. (2013). Are tau aggregates toxic or protective in tauopathies? Front. Neurol. 4:114.
    • (2013) Front. Neurol , vol.4 , pp. 114
    • Cowan, C.M.1    Mudher, A.2
  • 7
    • 85018198790 scopus 로고    scopus 로고
    • Pro-aggregant Tau impairs mossy fiber plasticity due to structural changes and Ca++ dysregulation
    • Decker, J. M., Krüger, L., Sydow, A., Zhao, S., Frotscher, M., Mandelkow, E., et al. (2015). Pro-aggregant Tau impairs mossy fiber plasticity due to structural changes and Ca++ dysregulation. Acta Neuropathol. Commun. 3:23.
    • (2015) Acta Neuropathol. Commun , vol.3 , pp. 23
    • Decker, J.M.1    Krüger, L.2    Sydow, A.3    Zhao, S.4    Frotscher, M.5    Mandelkow, E.6
  • 8
    • 19744382953 scopus 로고    scopus 로고
    • The MAP2/Tau family of microtubule-associated proteins
    • Dehmelt, L., and Halpain, S. (2005). The MAP2/Tau family of microtubule-associated proteins. Genome Biol. 6:204.
    • (2005) Genome Biol , vol.6 , pp. 204
    • Dehmelt, L.1    Halpain, S.2
  • 9
    • 0032894121 scopus 로고    scopus 로고
    • The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer’s disease
    • Delacourte, A., David, J. P., Sergeant, N., Buée, L., Wattez, A., Vermersch, P., et al. (1999). The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer’s disease. Neurology 52, 1158–1165.
    • (1999) Neurology , vol.52 , pp. 1158-1165
    • Delacourte, A.1    David, J.P.2    Sergeant, N.3    Buée, L.4    Wattez, A.5    Vermersch, P.6
  • 10
    • 84890125171 scopus 로고    scopus 로고
    • Alzheimer disease therapy—moving from amyloid-β to tau
    • Giacobini, E., and Gold, G. (2013). Alzheimer disease therapy—moving from amyloid-β to tau. Nat. Rev. Neurol. 9, 677–686.
    • (2013) Nat. Rev. Neurol , vol.9 , pp. 677-686
    • Giacobini, E.1    Gold, G.2
  • 11
    • 84959462799 scopus 로고    scopus 로고
    • Mislocalization of neuronal tau in the absence of tangle pathology in phosphomutant tauknockin mice
    • Gilley, J., Ando, K., Seereeram, A., Rodríguez-Martín, T., Pooler, A. M., Sturdee, L., et al. (2016). Mislocalization of neuronal tau in the absence of tangle pathology in phosphomutant tauknockin mice. Neurobiol. Aging 39, 1–18.
    • (2016) Neurobiol. Aging , vol.39 , pp. 1-18
    • Gilley, J.1    Ando, K.2    Seereeram, A.3    Rodríguez-Martín, T.4    Pooler, A.M.5    Sturdee, L.6
  • 12
    • 0032214501 scopus 로고    scopus 로고
    • Tau mutations cause frontotemporal dementias
    • Goedert, M., Crowther, R. A., and Spillantini, M. G. (1998). Tau mutations cause frontotemporal dementias. Neuron 21, 955–958.
    • (1998) Neuron , vol.21 , pp. 955-958
    • Goedert, M.1    Crowther, R.A.2    Spillantini, M.G.3
  • 13
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., and Crowther, R. A. (1996). Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383, 550–553.
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 14
    • 0344653664 scopus 로고    scopus 로고
    • Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer’s disease
    • Gomez-Isla, T., Hollister, R., West, H., Mui, S., Growdon, J. H., Petersen, R. C., et al. (1997). Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer’s disease. Ann. Neurol. 41, 17–24.
    • (1997) Ann. Neurol , vol.41 , pp. 17-24
    • Gomez-Isla, T.1    Hollister, R.2    West, H.3    Mui, S.4    Growdon, J.H.5    Petersen, R.C.6
  • 15
    • 84960510155 scopus 로고    scopus 로고
    • Acetylation mimic of lysine 280 exacerbates human Tau neurotoxicity in vivo
    • Gorsky, M. K., Burnouf, S., Dols, J., Mandelkow, E., and Partridge, L. (2016). Acetylation mimic of lysine 280 exacerbates human Tau neurotoxicity in vivo. Sci. Rep. 6:22685.
    • (2016) Sci. Rep , vol.6 , pp. 22685
    • Gorsky, M.K.1    Burnouf, S.2    Dols, J.3    Mandelkow, E.4    Partridge, L.5
  • 16
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer’s disease: Progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002). The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics. Science 297, 353–356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 17
    • 85018215020 scopus 로고    scopus 로고
    • Preventive methylene blue treatment preserves cognition in mice expressing full-length pro-aggregant human Tau
    • Hochgräfe, K., Sydow, A., Matenia, D., Cadinu, D., Könen, S., Petrova, O., et al. (2015). Preventive methylene blue treatment preserves cognition in mice expressing full-length pro-aggregant human Tau. Acta Neuropathol. Commun. 3:25.
    • (2015) Acta Neuropathol. Commun , vol.3 , pp. 25
    • Hochgräfe, K.1    Sydow, A.2    Matenia, D.3    Cadinu, D.4    Könen, S.5    Petrova, O.6
  • 18
    • 0025785076 scopus 로고
    • Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer’s disease
    • Jakes, R., Novak, M., Davison, M., and Wischik, C. M. (1991). Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer’s disease. EMBO J. 10, 2725–2729.
    • (1991) EMBO J , vol.10 , pp. 2725-2729
    • Jakes, R.1    Novak, M.2    Davison, M.3    Wischik, C.M.4
  • 20
    • 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., Pickhardt, M., von Bergen, M., Gazova, Z., et al. (2006). 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) J. Biol. Chem , vol.281 , pp. 1205-1214
    • Khlistunova, I.1    Biernat, J.2    Wang, Y.3    Pickhardt, M.4    von Bergen, M.5    Gazova, Z.6
  • 22
    • 0024109663 scopus 로고
    • The carboxyl third of tau is tightly bound to paired helical filaments
    • Kondo, J., Honda, T., Mori, H., Hamada, Y., Miura, R., Ogawara, M., et al. (1988). The carboxyl third of tau is tightly bound to paired helical filaments. Neuron 1, 827–834.
    • (1988) Neuron , vol.1 , pp. 827-834
    • Kondo, J.1    Honda, T.2    Mori, H.3    Hamada, Y.4    Miura, R.5    Ogawara, M.6
  • 23
    • 0021739339 scopus 로고
    • Microtubule-associated protein 2: Monoclonal antibodies demonstrate the selective incorporation of certain epitopes into Alzheimer neurofibrillary tangles
    • Kosik, K. S., Duffy, L. K., Dowling, M. M., Abraham, C., McCluskey, A., and Selkoe, D. J. (1984). Microtubule-associated protein 2: monoclonal antibodies demonstrate the selective incorporation of certain epitopes into Alzheimer neurofibrillary tangles. Proc. Natl. Acad. Sci. U S A 81, 7941–7945.
    • (1984) Proc. Natl. Acad. Sci. U S A , vol.81 , pp. 7941-7945
    • Kosik, K.S.1    Duffy, L.K.2    Dowling, M.M.3    Abraham, C.4    McCluskey, A.5    Selkoe, D.J.6
  • 27
    • 84885763064 scopus 로고    scopus 로고
    • Modeling neurodegenerative diseases in Caenorhabditis elegans
    • Li, J., and Le, W. (2013). Modeling neurodegenerative diseases in Caenorhabditis elegans. Exp. Neurol. 250, 94–103.
    • (2013) Exp. Neurol , vol.250 , pp. 94-103
    • Li, J.1    Le, W.2
  • 28
    • 84959518689 scopus 로고    scopus 로고
    • Expression of A152T human tau causes age-dependent neuronal dysfunction and loss in transgenic mice
    • Maeda, S., Djukic, B., Taneja, P., Yu, G. Q., Lo, I., Davis, A., et al. (2016). Expression of A152T human tau causes age-dependent neuronal dysfunction and loss in transgenic mice. EMBO Rep. 17, 530–551.
    • (2016) EMBO Rep , vol.17 , pp. 530-551
    • Maeda, S.1    Djukic, B.2    Taneja, P.3    Yu, G.Q.4    Lo, I.5    Davis, A.6
  • 29
    • 84863882357 scopus 로고    scopus 로고
    • Biochemistry and cell biology of tau protein in neurofibrillary degeneration
    • Mandelkow, E. M., and Mandelkow, E. (2012). Biochemistry and cell biology of tau protein in neurofibrillary degeneration. Cold Spring Harb. Perspect. Med. 2:a006247.
    • (2012) Cold Spring Harb. Perspect. Med , vol.2
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 30
    • 78650117774 scopus 로고    scopus 로고
    • Modeling human diseases in Caenorhabditis elegans
    • Markaki, M., and Tavernarakis, N. (2010). Modeling human diseases in Caenorhabditis elegans. Biotechnol. J. 5, 1261–1276.
    • (2010) Biotechnol. J , vol.5 , pp. 1261-1276
    • Markaki, M.1    Tavernarakis, N.2
  • 33
    • 38549129613 scopus 로고    scopus 로고
    • The potential for β-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss and coassembly with endogenous Tau in inducible mouse models of tauopathy
    • Mocanu, M. M., Nissen, A., Eckermann, K., Khlistunova, I., Biernat, J., Drexler, D., et al. (2008). The potential for β-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss and coassembly with endogenous Tau in inducible mouse models of tauopathy. J. Neurosci. 28, 737–748.
    • (2008) J. Neurosci , vol.28 , pp. 737-748
    • Mocanu, M.M.1    Nissen, A.2    Eckermann, K.3    Khlistunova, I.4    Biernat, J.5    Drexler, D.6
  • 34
    • 58849137188 scopus 로고    scopus 로고
    • Clinical and pathological features of an Alzheimer’s disease patient with the MAPT ∆K280 mutation
    • Momeni, P., Pittman, A., Lashley, T., Vandrovcova, J., Malzer, E., Luk, C., et al. (2009). Clinical and pathological features of an Alzheimer’s disease patient with the MAPT ∆K280 mutation. Neurobiol. Aging 30, 388–393.
    • (2009) Neurobiol. Aging , vol.30 , pp. 388-393
    • Momeni, P.1    Pittman, A.2    Lashley, T.3    Vandrovcova, J.4    Malzer, E.5    Luk, C.6
  • 35
    • 0348047708 scopus 로고
    • Recognition of Alzheimer paired helical filaments by monoclonal neurofilament antibodies is due to crossreaction with tau protein
    • Nukina, N., Kosik, K. S., and Selkoe, D. J. (1987). Recognition of Alzheimer paired helical filaments by monoclonal neurofilament antibodies is due to crossreaction with tau protein. Proc. Natl. Acad. Sci. U S A 84, 3415–3419.
    • (1987) Proc. Natl. Acad. Sci. U S A , vol.84 , pp. 3415-3419
    • Nukina, N.1    Kosik, K.S.2    Selkoe, D.J.3
  • 36
    • 79959571777 scopus 로고    scopus 로고
    • Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease
    • Patterson, K. R., Remmers, C., Fu, Y., Brooker, S., Kanaan, N. M., Vana, L., et al. (2011). Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease. J. Biol. Chem. 286, 23063–23076.
    • (2011) J. Biol. Chem , vol.286 , pp. 23063-23076
    • Patterson, K.R.1    Remmers, C.2    Fu, Y.3    Brooker, S.4    Kanaan, N.M.5    Vana, L.6
  • 38
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer’s disease mouse model
    • Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., et al. (2007). Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer’s disease mouse model. Science 316, 750–754.
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6
  • 39
    • 0024335002 scopus 로고
    • Alzheimer’s disease: Microtubule-associated proteins 2 (MAP2) are not components of paired helical filaments
    • Rosemblatt, M., Fellous, A., Mazie, J. C., Delacourte, A., and Defossez, A. (1989). Alzheimer’s disease: microtubule-associated proteins 2 (MAP2) are not components of paired helical filaments. FEBS Lett. 252, 91–94.
    • (1989) FEBS Lett , vol.252 , pp. 91-94
    • Rosemblatt, M.1    Fellous, A.2    Mazie, J.C.3    Delacourte, A.4    Defossez, A.5
  • 40
    • 84902486430 scopus 로고    scopus 로고
    • Distinct tau prion strains propagate in cells and mice and define different tauopathies
    • Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., et al. (2014). Distinct tau prion strains propagate in cells and mice and define different tauopathies. Neuron 82, 1271–1288.
    • (2014) Neuron , vol.82 , pp. 1271-1288
    • Sanders, D.W.1    Kaufman, S.K.2    Devos, S.L.3    Sharma, A.M.4    Mirbaha, H.5    Li, A.6
  • 41
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., et al. (2005). Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476–481.
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3    Paulson, J.4    Kotilinek, L.5    Ingelsson, M.6
  • 42
    • 0034051721 scopus 로고    scopus 로고
    • Tau mutations in familial frontotemporal dementia
    • Spillantini, M. G., and Goedert, M. (2000). Tau mutations in familial frontotemporal dementia. Brain 123, 857–859.
    • (2000) Brain , vol.123 , pp. 857-859
    • Spillantini, M.G.1    Goedert, M.2
  • 43
    • 84877906835 scopus 로고    scopus 로고
    • Tau pathology and neurodegeneration
    • Spillantini, M. G., and Goedert, M. (2013). Tau pathology and neurodegeneration. Lancet Neurol. 12, 609–622.
    • (2013) Lancet Neurol , vol.12 , pp. 609-622
    • Spillantini, M.G.1    Goedert, M.2
  • 44
    • 0032786370 scopus 로고    scopus 로고
    • Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein
    • Spittaels, K., Van den Haute, C., Van Dorpe, J., Bruynseels, K., Vandezande, K., Laenen, I., et al. (1999). Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein. Am. J. Pathol. 155, 2153–2165.
    • (1999) Am. J. Pathol , vol.155 , pp. 2153-2165
    • Spittaels, K.1    Van den Haute, C.2    Van Dorpe, J.3    Bruynseels, K.4    Vandezande, K.5    Laenen, I.6
  • 45
    • 84954385047 scopus 로고    scopus 로고
    • Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometricanalyses of sarkosyl-insoluble and trypsin-resistant tau
    • Taniguchi-Watanabe, S., Arai, T., Kametani, F., Nonaka, T., Masuda-Suzukake, M., Tarutani, A., et al. (2016). Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometricanalyses of sarkosyl-insoluble and trypsin-resistant tau. Acta Neuropathol. 131, 267–280.
    • (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
  • 46
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming β structure
    • von Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., Mandelkow, E. M., and Mandelkow, E. (2000). Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming β structure. Proc. Natl. Acad. Sci. U S A 97, 5129–5134.
    • (2000) Proc. Natl. Acad. Sci. U S A , 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
  • 47
    • 84937513802 scopus 로고    scopus 로고
    • Emerging drug targets for Aβ and tau in Alzheimer’s disease: A systematic review
    • West, S., and Bhugra, P. (2015). Emerging drug targets for Aβ and tau in Alzheimer’s disease: a systematic review. Br. J. Clin. Pharmacol. 80, 221–234.
    • (2015) Br. J. Clin. Pharmacol , vol.80 , pp. 221-234
    • West, S.1    Bhugra, P.2
  • 48
    • 85018237568 scopus 로고    scopus 로고
    • High copy wildtype human 1N4R tau expression promotes early pathological tauopathy accompanied by cognitive deficits without progressive neurofibrillary degeneration
    • Wheeler, J. M., McMillan, P. J., Hawk, M., Iba, M., Robinson, L., Xu, G. J., et al. (2015). High copy wildtype human 1N4R tau expression promotes early pathological tauopathy accompanied by cognitive deficits without progressive neurofibrillary degeneration. Acta Neuropathol. Commun. 3:33.
    • (2015) Acta Neuropathol. Commun , vol.3 , pp. 33
    • Wheeler, J.M.1    McMillan, P.J.2    Hawk, M.3    Iba, M.4    Robinson, L.5    Xu, G.J.6
  • 49
    • 0003986552 scopus 로고
    • Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease
    • Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., et al. (1988). Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease. Proc. Natl. Acad. Sci. U S A 85, 4506–4510.
    • (1988) Proc. Natl. Acad. Sci. U S A , vol.85 , pp. 4506-4510
    • Wischik, C.M.1    Novak, M.2    Thøgersen, H.C.3    Edwards, P.C.4    Runswick, M.J.5    Jakes, R.6
  • 50
    • 84896130231 scopus 로고    scopus 로고
    • The homologous carboxyl-terminal domains of microtubule-associated protein 2 and Tau induce neuronal dysfunction and have differential fates in the evolution of neurofibrillary tangles
    • Xie, C., Miyasaka, T., Yoshimura, S., Hatsuta, H., Yoshina, S., Kage-Nakadai, E., et al. (2014). The homologous carboxyl-terminal domains of microtubule-associated protein 2 and Tau induce neuronal dysfunction and have differential fates in the evolution of neurofibrillary tangles. PLoS One 9:e89796.
    • (2014) Plos One , vol.9
    • Xie, C.1    Miyasaka, T.2    Yoshimura, S.3    Hatsuta, H.4    Yoshina, S.5    Kage-Nakadai, E.6
  • 51
    • 84942502608 scopus 로고    scopus 로고
    • Identification of key amino acids responsible for the distinct aggregation properties of microtubule-associated protein 2 and tau
    • Xie, C., Soeda, Y., Shinzaki, Y., In, Y., Tomoo, K., Ihara, Y., et al. (2015). Identification of key amino acids responsible for the distinct aggregation properties of microtubule-associated protein 2 and tau. J. Neurochem. 135, 19–26.
    • (2015) J. Neurochem , vol.135 , pp. 19-26
    • Xie, C.1    Soeda, Y.2    Shinzaki, Y.3    In, Y.4    Tomoo, K.5    Ihara, Y.6
  • 52
    • 84969801994 scopus 로고    scopus 로고
    • How does Hyperphosphorylation promote tau aggregation and filament structure and stability?
    • Xu, L., Zheng, J., Margittai, M., Nussinov, R., and Ma, B. (2016). How does Hyperphosphorylation promote tau aggregation and filament structure and stability? ACS Chem Neurosci. 7, 565–575.
    • (2016) ACS Chem Neurosci , vol.7 , pp. 565-575
    • Xu, L.1    Zheng, J.2    Margittai, M.3    Nussinov, R.4    Ma, B.5
  • 53
    • 84858664547 scopus 로고    scopus 로고
    • Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation. Nat
    • Yuzwa, S. A., Shan, X., Macauley, M. S., Clark, T., Skorobogatko, Y., Vosseller, K., et al. (2012). Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation. Nat. Chem. Biol. 8, 393–399.
    • (2012) Chem. Biol , vol.8 , pp. 393-399
    • Yuzwa, S.A.1    Shan, X.2    Macauley, M.S.3    Clark, T.4    Skorobogatko, Y.5    Vosseller, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.