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Volumn 50, Issue 23, 2011, Pages 5172-5181

Synergistic interactions between repeats in tau protein and Aβ amyloids may be responsible for accelerated aggregation via polymorphic States

Author keywords

[No Author keywords available]

Indexed keywords

AFM IMAGE; ALZHEIMER'S DISEASE; AMYLOID PLAQUES; NEUROFIBRILLARY TANGLES; OLIGOMERIC COMPLEXES; POLYMORPHIC STATE; STABLE COMPLEXES; STRUCTURE DOMAINS; SYNERGISTIC INTERACTION; TAU PROTEINS;

EID: 79958821061     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200400u     Document Type: Article
Times cited : (96)

References (78)
  • 1
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics
    • DOI 10.1146/annurev.pharmtox.43.100901.140248
    • Selkoe, D. J. and Schenk, D. (2003) Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics Annu. Rev. Pharmacol. Toxicol. 43, 545-584 (Pubitemid 37372653)
    • (2003) Annual Review of Pharmacology and Toxicology , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 4
    • 33751218015 scopus 로고    scopus 로고
    • Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid
    • DOI 10.1083/jcb.200605187
    • King, M. E., Kan, H. M., Baas, P. W., Erisir, A., Glabe, C. G., and Bloom, G. S. (2006) Tau-dependent microtubule disassembly initiated by prefibrillar beta-amyloid J. Cell Biol. 175, 541-546 (Pubitemid 44790607)
    • (2006) Journal of Cell Biology , vol.175 , Issue.4 , pp. 541-546
    • King, M.E.1    Kan, H.-M.2    Baas, P.W.3    Erisir, A.4    Glabe, C.G.5    Bloom, G.S.6
  • 7
    • 33744974998 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in sporadic and genetic Alzheimer's disease
    • DOI 10.1016/j.exger.2006.03.012, PII S0531556506000787, Proceedings of the 4th Conference on Mitochondrial Physiology - MiP2005, Session 8-11
    • Hauptmann, S., Keil, U., Scherping, I., Bonert, A., Eckert, A., and Muller, W. E. (2006) Mitochondrial dysfunction in sporadic and genetic Alzheimer's disease Exp. Gerontol. 41, 668-673 (Pubitemid 43866354)
    • (2006) Experimental Gerontology , vol.41 , Issue.7 , pp. 668-673
    • Hauptmann, S.1    Keil, U.2    Scherping, I.3    Bonert, A.4    Eckert, A.5    Muller, W.E.6
  • 8
    • 40449090190 scopus 로고    scopus 로고
    • Soluble beta-amyloid leads to mitochondrial defects in amyloid precursor protein and tau transgenic mice
    • DOI 10.1159/000113689
    • Eckert, A., Hauptmann, S., Scherping, I., Rhein, V., Muller-Spahn, F., Gotz, J., and Muller, W. E. (2008) Soluble beta-amyloid leads to mitochondrial defects in amyloid precursor protein and tau transgenic mice Neurodegener. Dis. 5, 157-159 (Pubitemid 351347837)
    • (2008) Neurodegenerative Diseases , vol.5 , Issue.3-4 , pp. 157-159
    • Eckert, A.1    Hauptmann, S.2    Scherping, I.3    Rhein, V.4    Muller-Spahn, F.5    Gotz, J.6    Muller, W.E.7
  • 11
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Aβ42 fibrils
    • DOI 10.1126/science.1062097
    • Gotz, J., Chen, F., van Dorpe, J., and Nitsch, R. M. (2001) Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils Science 293, 1491-1495 (Pubitemid 32807681)
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 12
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's Disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction
    • DOI 10.1016/S0896-6273(03)00434-3
    • Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., and LaFerla, F. M. (2003) Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction Neuron 39, 409-421 (Pubitemid 36937044)
    • (2003) Neuron , vol.39 , Issue.3 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6    Metherate, R.7    Mattson, M.P.8    Akbari, Y.9    LaFerla, F.M.10
  • 13
    • 33846047004 scopus 로고    scopus 로고
    • Pathways by which Aβ facilitates tau pathology
    • DOI 10.2174/156720506779025242
    • Blurton-Jones, M. and Laferla, F. M. (2006) Pathways by which Abeta facilitates tau pathology Curr. Alzheimer Res. 3, 437-448 (Pubitemid 46066423)
    • (2006) Current Alzheimer Research , vol.3 , Issue.5 , pp. 437-448
    • Blurton-Jones, M.1    LaFerla, F.M.2
  • 14
    • 77955979357 scopus 로고    scopus 로고
    • Pathways linking Abeta and tau pathologies
    • LaFerla, F. M. (2010) Pathways linking Abeta and tau pathologies Biochem. Soc. Trans. 38, 993-995
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 993-995
    • Laferla, F.M.1
  • 16
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio, J., Lorenzo, A., Yeh, J., and Yankner, B. A. (1995) beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding Neuron 14, 879-888
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 17
    • 0032859938 scopus 로고    scopus 로고
    • Inhibition of tau phosphorylating protein kinase cdk5 prevents β-amyloid-induced neuronal death
    • DOI 10.1016/S0014-5793(99)01279-X, PII S001457939901279X
    • Alvarez, A., Toro, R., Caceres, A., and Maccioni, R. B. (1999) Inhibition of tau phosphorylating protein kinase cdk5 prevents beta-amyloid-induced neuronal death FEBS Lett. 459, 421-426 (Pubitemid 29467380)
    • (1999) FEBS Letters , vol.459 , Issue.3 , pp. 421-426
    • Alvarez, A.1    Toro, R.2    Caceres, A.3    Maccioni, R.B.4
  • 18
    • 0345405447 scopus 로고    scopus 로고
    • Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles
    • DOI 10.1016/S0896-6273(03)00627-5
    • Cruz, J. C., Tseng, H. C., Goldman, J. A., Shih, H., and Tsai, L. H. (2003) Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles Neuron 40, 471-483 (Pubitemid 37494698)
    • (2003) Neuron , vol.40 , Issue.3 , pp. 471-483
    • Cruz, J.C.1    Tseng, H.-C.2    Goldman, J.A.3    Shih, H.4    Tsai, L.-H.5
  • 19
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • DOI 10.1046/j.1471-4159.2000.0750436.x
    • Keller, J. N., Hanni, K. B., and Markesbery, W. R. (2000) Impaired proteasome function in Alzheimer's disease J. Neurochem. 75, 436-439 (Pubitemid 30418211)
    • (2000) Journal of Neurochemistry , vol.75 , Issue.1 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 20
  • 21
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • DOI 10.1016/j.neurobiolaging.2003.08.012
    • Oddo, S., Caccamo, A., Kitazawa, M., Tseng, B. P., and LaFerla, F. M. (2003) Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease Neurobiol. Aging 24, 1063-1070 (Pubitemid 37487883)
    • (2003) Neurobiology of Aging , vol.24 , Issue.8 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 22
    • 0028095224 scopus 로고
    • Levels of normal and abnormally phosphorylated tau in different cellular and regional compartments of Alzheimer disease and control brains
    • Khatoon, S., Grundke-Iqbal, I., and Iqbal, K. (1994) Levels of normal and abnormally phosphorylated tau in different cellular and regional compartments of Alzheimer disease and control brains FEBS Lett. 351, 80-84
    • (1994) FEBS Lett. , vol.351 , pp. 80-84
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 25
    • 21644446496 scopus 로고    scopus 로고
    • Sites of tau important for aggregation populate β-structure and bind to microtubules and polyanions
    • DOI 10.1074/jbc.M501565200
    • Mukrasch, M. D., Biernat, J., von Bergen, M., Griesinger, C., Mandelkow, E., and Zweckstetter, M. (2005) Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions J. Biol. Chem. 280, 24978-24986 (Pubitemid 40934590)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24978-24986
    • Mukrasch, M.D.1    Biernat, J.2    Von Bergen, M.3    Griesinger, C.4    Mandelkow, E.5    Zweckstetter, M.6
  • 27
    • 12344328360 scopus 로고    scopus 로고
    • Residual structure in the repeat domain of tau: Echoes of microtubule binding and paired helical filament formation
    • DOI 10.1021/bi048953n
    • Eliezer, D., Barre, P., Kobaslija, M., Chan, D., Li, X., and Heend, L. (2005) Residual structure in the repeat domain of tau: echoes of microtubule binding and paired helical filament formation Biochemistry 44, 1026-1036 (Pubitemid 40129662)
    • (2005) Biochemistry , vol.44 , Issue.3 , pp. 1026-1036
    • Eliezer, D.1    Barre, P.2    Kobaslija, M.3    Chan, D.4    Li, X.5    Heend, L.6
  • 30
    • 70349155427 scopus 로고    scopus 로고
    • Tau aggregation followed by atomic force microscopy and surface plasmon resonance, and single molecule tau-tau interaction probed by atomic force spectroscopy
    • Barrantes, A., Sotres, J., Hernando-Perez, M., Benitez, M. J., de Pablo, P. J., Baro, A. M., Avila, J., and Jimenez, J. S. (2009) Tau aggregation followed by atomic force microscopy and surface plasmon resonance, and single molecule tau-tau interaction probed by atomic force spectroscopy J. Alzheimers Dis. 18, 141-151
    • (2009) J. Alzheimers Dis. , vol.18 , pp. 141-151
    • Barrantes, A.1    Sotres, J.2    Hernando-Perez, M.3    Benitez, M.J.4    De Pablo, P.J.5    Baro, A.M.6    Avila, J.7    Jimenez, J.S.8
  • 31
    • 47249159078 scopus 로고    scopus 로고
    • A soluble oligomer of tau associated with fiber formation analyzed by NMR
    • DOI 10.1021/bi702466a
    • Peterson, D. W., Zhou, H., Dahlquist, F. W., and Lew, J. (2008) A soluble oligomer of tau associated with fiber formation analyzed by NMR Biochemistry 47, 7393-7404 (Pubitemid 351991018)
    • (2008) Biochemistry , vol.47 , Issue.28 , pp. 7393-7404
    • Peterson, D.W.1    Zhou, H.2    Dahlquist, F.W.3    Lew, J.4
  • 32
    • 33846002029 scopus 로고    scopus 로고
    • Side chain-dependent stacking modulates tau filament structure
    • DOI 10.1074/jbc.M605336200
    • Margittai, M. and Langen, R. (2006) Side chain-dependent stacking modulates tau filament structure J. Biol. Chem. 281, 37820-37827 (Pubitemid 46042084)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.49 , pp. 37820-37827
    • Margittai, M.1    Langen, R.2
  • 33
    • 58149174069 scopus 로고    scopus 로고
    • Formation and growth of oligomers: A Monte Carlo study of an amyloid tau fragment
    • Li, D. W., Mohanty, S., Irback, A., and Huo, S. (2008) Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragment PLoS Comput. Biol. 4, e1000238
    • (2008) PLoS Comput. Biol. , vol.4 , pp. 1000238
    • Li, D.W.1    Mohanty, S.2    Irback, A.3    Huo, S.4
  • 34
    • 69449099387 scopus 로고    scopus 로고
    • Polymorphism of Alzheimer's Abeta17-42 (p3) oligomers: The importance of the turn location and its conformation
    • Miller, Y., Ma, B., and Nussinov, R. (2009) Polymorphism of Alzheimer's Abeta17-42 (p3) oligomers: the importance of the turn location and its conformation Biophys. J. 97, 1168-1177
    • (2009) Biophys. J. , vol.97 , pp. 1168-1177
    • Miller, Y.1    Ma, B.2    Nussinov, R.3
  • 35
    • 77954892793 scopus 로고    scopus 로고
    • Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape
    • Miller, Y., Ma, B., and Nussinov, R. (2010) Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape Chem. Rev. 110, 4820-4838
    • (2010) Chem. Rev. , vol.110 , pp. 4820-4838
    • Miller, Y.1    Ma, B.2    Nussinov, R.3
  • 39
    • 0000020246 scopus 로고    scopus 로고
    • A five-site J;model for liquid water and the reproduction of the density anomaly by rigid, nonpolarizable potential functions
    • Mahoney, M. W. and Jorgensen, W. L. (2000) A five-site J;model for liquid water and the reproduction of the density anomaly by rigid, nonpolarizable potential functions J. Chem. Phys. 112, 8910-8922
    • (2000) J. Chem. Phys. , vol.112 , pp. 8910-8922
    • Mahoney, M.W.1    Jorgensen, W.L.2
  • 41
    • 36449003554 scopus 로고
    • Constant-Pressure Molecular-Dynamics Algorithms
    • Martyna, G. J., Tobias, D. J., and Klein, M. L. (1994) Constant-Pressure Molecular-Dynamics Algorithms J. Chem. Phys. 101, 4177-4189
    • (1994) J. Chem. Phys. , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 42
    • 36449007836 scopus 로고
    • Constant-Pressure Molecular-Dynamics Simulation - The Langevin Piston Method
    • Feller, S. E., Zhang, Y. H., Pastor, R. W., and Brooks, B. R. (1995) Constant-Pressure Molecular-Dynamics Simulation-the Langevin Piston Method J. Chem. Phys. 103, 4613-4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.H.2    Pastor, R.W.3    Brooks, B.R.4
  • 43
    • 33846823909 scopus 로고
    • Particle Mesh Ewald - An N.Log(N) Method for Ewald Sums in Large Systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle Mesh Ewald-an N.Log(N) Method for Ewald Sums in Large Systems J. Chem. Phys. 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 45
    • 33646940952 scopus 로고
    • Numerical-Integration of Cartesian Equations of Motion of a System with Constraints - Molecular-Dynamics of N-Alkanes
    • Ryckaert, J. P., Ciccotti, G., and Berendsen, H. J. C. (1977) Numerical-Integration of Cartesian Equations of Motion of a System with Constraints-Molecular-Dynamics of N-Alkanes J. Comput. Phys. 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 46
    • 0038792211 scopus 로고    scopus 로고
    • New analytic approximation to the standard molecular volume definition and its application to generalized born calculations
    • Lee, M. S., Feig, M., Salsbury, F. R., and Brooks, C. L. (2003) New analytic approximation to the standard molecular volume definition and its application to generalized born calculations J. Comput. Chem. 24, 1348-1356
    • (2003) J. Comput. Chem. , vol.24 , pp. 1348-1356
    • Lee, M.S.1    Feig, M.2    Salsbury, F.R.3    Brooks, C.L.4
  • 48
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure
    • von Bergen, M., Barghorn, S., Li, L., Marx, A., Biernat, J., Mandelkow, E. M., and Mandelkow, E. (2001) Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure J. Biol. Chem. 276, 48165-48174
    • (2001) J. Biol. Chem. , vol.276 , pp. 48165-48174
    • Von Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 51
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • DOI 10.1021/bi051952q
    • Petkova, A. T., Yau, W. M., and Tycko, R. (2006) Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils Biochemistry 45, 498-512 (Pubitemid 43100415)
    • (2006) Biochemistry , vol.45 , Issue.2 , pp. 498-512
    • Petkova, A.T.1    Yau, W.-M.2    Tycko, R.3
  • 52
    • 77956242962 scopus 로고    scopus 로고
    • Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability
    • Wegmann, S., Jung, Y. J., Chinnathambi, S., Mandelkow, E. M., Mandelkow, E., and Muller, D. J. (2010) Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability J. Biol. Chem. 285, 27302-27313
    • (2010) J. Biol. Chem. , vol.285 , pp. 27302-27313
    • Wegmann, S.1    Jung, Y.J.2    Chinnathambi, S.3    Mandelkow, E.M.4    Mandelkow, E.5    Muller, D.J.6
  • 54
    • 77952759080 scopus 로고    scopus 로고
    • Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling
    • Ladner, C. L., Chen, M., Smith, D. P., Platt, G. W., Radford, S. E., and Langen, R. (2010) Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling J. Biol. Chem. 285, 17137-17147
    • (2010) J. Biol. Chem. , vol.285 , pp. 17137-17147
    • Ladner, C.L.1    Chen, M.2    Smith, D.P.3    Platt, G.W.4    Radford, S.E.5    Langen, R.6
  • 55
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt, L., Teng, P. K., Riek, R., and Eisenberg, D. (2010) Identifying the amylome, proteins capable of forming amyloid-like fibrils Proc. Natl. Acad. Sci. U.S.A. 107, 3487-3492
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 56
    • 77956269194 scopus 로고    scopus 로고
    • Hollow core of Alzheimer's Abeta42 amyloid observed by cryoEM is relevant at physiological pH
    • Miller, Y., Ma, B., Tsai, C. J., and Nussinov, R. (2010) Hollow core of Alzheimer's Abeta42 amyloid observed by cryoEM is relevant at physiological pH Proc. Natl. Acad. Sci. U.S.A. 107, 14128-14133
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 14128-14133
    • Miller, Y.1    Ma, B.2    Tsai, C.J.3    Nussinov, R.4
  • 58
    • 0842265772 scopus 로고    scopus 로고
    • Different associational and conformational behaviors between the second and third repeat fragments in the tau microtubule-binding domain
    • DOI 10.1046/j.1432-1033.2003.03956.x
    • Minoura, K., Yao, T. M., Tomoo, K., Sumida, M., Sasaki, M., Taniguchi, T., and Ishida, T. (2004) Different associational and conformational behaviors between the second and third repeat fragments in the tau microtubule-binding domain Eur. J. Biochem. 271, 545-552 (Pubitemid 38183628)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.3 , pp. 545-552
    • Minoura, K.1    Yao, T.-M.2    Tomoo, K.3    Sumida, M.4    Sasaki, M.5    Taniguchi, T.6    Ishida, T.7
  • 60
    • 0037018932 scopus 로고    scopus 로고
    • α-helix structure in Alzheimer's disease aggregates of tau-protein
    • DOI 10.1021/bi025777e
    • Sadqi, M., Hernandez, F., Pan, U., Perez, M., Schaeberle, M. D., Avila, J., and Munoz, V. (2002) Alpha-helix structure in Alzheimer's disease aggregates of tau-protein Biochemistry 41, 7150-7155 (Pubitemid 34575688)
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 7150-7155
    • Sadqi, M.1    Hernandez, F.2    Pan, U.3    Perez, M.4    Schaeberle, M.D.5    Avila, J.6    Munoz, V.7
  • 62
    • 78149318021 scopus 로고    scopus 로고
    • Age-dependent changes in TDP-43 levels in a mouse model of Alzheimer disease are linked to Abeta oligomers accumulation
    • Caccamo, A., Magri, A., and Oddo, S. (2010) Age-dependent changes in TDP-43 levels in a mouse model of Alzheimer disease are linked to Abeta oligomers accumulation Mol. Neurodegener. 5, 51
    • (2010) Mol. Neurodegener. , vol.5 , pp. 51
    • Caccamo, A.1    Magri, A.2    Oddo, S.3
  • 63
    • 78650644432 scopus 로고    scopus 로고
    • Visualization of polymorphism in apolipoprotein C-II amyloid fibrils
    • Teoh, C. L., Yagi, H., Griffin, M. D., Goto, Y., and Howlett, G. J. (2011) Visualization of polymorphism in apolipoprotein C-II amyloid fibrils J. Biochem. 149, 67-74
    • (2011) J. Biochem. , vol.149 , pp. 67-74
    • Teoh, C.L.1    Yagi, H.2    Griffin, M.D.3    Goto, Y.4    Howlett, G.J.5
  • 64
    • 77953113490 scopus 로고    scopus 로고
    • Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states
    • Miller, Y., Ma, B., and Nussinov, R. (2010) Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states Proc. Natl. Acad. Sci. U.S.A. 107, 9490-9495
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9490-9495
    • Miller, Y.1    Ma, B.2    Nussinov, R.3
  • 65
    • 79952258282 scopus 로고    scopus 로고
    • The unique Alzheimer's β-amyloid triangular fibril has a cavity along the fibril axis under physiological conditions
    • in press.
    • Miller, Y., Ma, B., and Nussinov, R. The unique Alzheimer's β-amyloid triangular fibril has a cavity along the fibril axis under physiological conditions. J. Am. Chem. Soc. 2011, in press.
    • (2011) J. Am. Chem. Soc.
    • Miller, Y.1    Ma, B.2    Nussinov, R.3
  • 66
    • 79952614047 scopus 로고    scopus 로고
    • Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer's β by Solid-State NMR Spectroscopy
    • not supplied.
    • Parthasarathy, S., Long, F., Miller, Y., Xiao, Y., McElheny, D., Thurber, K., Ma, B., Nussinov, R., and Ishii, Y. Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer's β by Solid-State NMR Spectroscopy. J. Am. Chem. Soc 2011, not supplied.
    • (2011) J. Am. Chem. Soc
    • Parthasarathy, S.1    Long, F.2    Miller, Y.3    Xiao, Y.4    McElheny, D.5    Thurber, K.6    Ma, B.7    Nussinov, R.8    Ishii, Y.9
  • 69
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn, S., Zheng-Fischhofer, Q., Ackmann, M., Biernat, J., von Bergen, M., Mandelkow, E. M., and Mandelkow, E. (2000) Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias Biochemistry 39, 11714-11721
    • (2000) Biochemistry , vol.39 , pp. 11714-11721
    • Barghorn, S.1    Zheng-Fischhofer, Q.2    Ackmann, M.3    Biernat, J.4    Von Bergen, M.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 71
    • 0032919462 scopus 로고    scopus 로고
    • Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments
    • DOI 10.1016/S0014-5793(99)00508-6, PII S0014579399005086
    • Goedert, M., Jakes, R., and Crowther, R. A. (1999) Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments FEBS Lett. 450, 306-311 (Pubitemid 29219534)
    • (1999) FEBS Letters , vol.450 , Issue.3 , pp. 306-311
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3
  • 72
    • 0345561533 scopus 로고    scopus 로고
    • Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations
    • DOI 10.1016/S0014-5793(99)00210-0, PII S0014579399002100
    • Arrasate, M., Perez, M., Armas-Portela, R., and Avila, J. (1999) Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations FEBS Lett. 446, 199-202 (Pubitemid 29127276)
    • (1999) FEBS Letters , vol.446 , Issue.1 , pp. 199-202
    • Arrasate, M.1    Perez, M.2    Armas-Portela, R.3    Avila, J.4
  • 73
    • 0033011181 scopus 로고    scopus 로고
    • Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
    • DOI 10.1016/S0014-5793(99)00294-X, PII S001457939900294X
    • Nacharaju, P., Lewis, J., Easson, C., Yen, S., Hackett, J., Hutton, M., and Yen, S. H. (1999) Accelerated filament formation from tau protein with specific FTDP-17 missense mutations FEBS Lett. 447, 195-199 (Pubitemid 29146084)
    • (1999) FEBS Letters , vol.447 , Issue.2-3 , pp. 195-199
    • Nacharaju, P.1    Lewis, J.2    Easson, C.3    Yen, S.4    Hackett, J.5    Hutton, M.6    Yen, S.-H.7
  • 74
    • 0034705192 scopus 로고    scopus 로고
    • In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants
    • DOI 10.1021/bi000201f
    • Gamblin, T. C., King, M. E., Dawson, H., Vitek, M. P., Kuret, J., Berry, R. W., and Binder, L. I. (2000) In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants Biochemistry 39, 6136-6144 (Pubitemid 30327089)
    • (2000) Biochemistry , vol.39 , Issue.20 , pp. 6136-6144
    • Gamblin, T.C.1    King, M.E.2    Dawson, H.3    Vitek, M.P.4    Kuret, J.5    Berry, R.W.6    Binder, L.I.7
  • 77
    • 0033982344 scopus 로고    scopus 로고
    • Missense tau mutations identified in FTDP-17 have a small effect on tau-microtubule interactions
    • DOI 10.1016/S0006-8993(99)02124-1, PII S0006899399021241
    • DeTure, M., Ko, L. W., Yen, S., Nacharaju, P., Easson, C., Lewis, J., van Slegtenhorst, M., Hutton, M., and Yen, S. H. (2000) Missense tau mutations identified in FTDP-17 have a small effect on tau-microtubule interactions Brain Res. 853, 5-14 (Pubitemid 30015993)
    • (2000) Brain Research , vol.853 , Issue.1 , pp. 5-14
    • Deture, M.1    Ko, L.-W.2    Yen, S.3    Nacharaju, P.4    Easson, C.5    Lewis, J.6    Van Slegtenhorst, M.7    Hutton, M.8    Yen, S.-H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.