메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

A mechanistic model of tau amyloid aggregation based on direct observation of oligomers

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; OLIGOMER; TAU PROTEIN;

EID: 84928792132     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8025     Document Type: Article
Times cited : (166)

References (44)
  • 1
    • 84883174947 scopus 로고    scopus 로고
    • Parkinson's disease dementia: Convergence of alpha-synuclein, tau and amyloid-beta pathologies
    • Irwin, D. J., Lee, V. M. Y. & Trojanowski, J. Q. Parkinson's disease dementia: convergence of alpha-synuclein, tau and amyloid-beta pathologies. Nat. Rev. Neurosci. 14, 626-636 (2013).
    • (2013) Nat. Rev. Neurosci , vol.14 , pp. 626-636
    • Irwin, D.J.1    Lee, V.M.Y.2    Trojanowski, J.Q.3
  • 3
    • 1042288284 scopus 로고    scopus 로고
    • Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-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 beta-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
  • 4
    • 19744382953 scopus 로고    scopus 로고
    • The MAP2/Tau family of microtubule-associated proteins
    • Dehmelt, L. & Halpain, S. The MAP2/Tau family of microtubule-associated proteins. Genome Biol. 6, 204 (2005).
    • (2005) Genome Biol. , vol.6 , pp. 204
    • Dehmelt, L.1    Halpain, S.2
  • 5
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • Avila, J., Lucas, J. J., Perez, M. & Hernandez, F. Role of tau protein in both physiological and pathological conditions. Physiol. Rev. 84, 361-384 (2004).
    • (2004) Physiol. Rev. , vol.84 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Perez, M.3    Hernandez, F.4
  • 6
    • 53349144370 scopus 로고    scopus 로고
    • The natively unfolded character of Tau and its aggregation to Alzheimer-like paired helical filaments
    • Jeganathan, S., von Bergen, M., Mandelkow, E. M. & Mandelkow, E. The natively unfolded character of Tau and its aggregation to Alzheimer-like paired helical filaments. Biochemistry 47, 10526-10539 (2008).
    • (2008) Biochemistry , vol.47 , pp. 10526-10539
    • Jeganathan, S.1    Von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 7
    • 2442590898 scopus 로고    scopus 로고
    • Surface-decoration of microtubules by human Tau
    • Santarella, R. A. et al. Surface-decoration of microtubules by human Tau. J. Mol. Biol. 339, 539-553 (2004).
    • (2004) J. Mol. Biol. , vol.339 , pp. 539-553
    • Santarella, R.A.1
  • 9
    • 84865663663 scopus 로고    scopus 로고
    • Beta-sheet core of tau paired helical filaments revealed by solidstate NMR
    • Daebel, V. et al. beta-sheet core of tau paired helical filaments revealed by solidstate NMR. J. Am. Chem. Soc. 134, 13982-13989 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 13982-13989
    • Daebel, V.1
  • 10
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • Barghorn, S. & Mandelkow, E. Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. Biochemistry 41, 14885-14896 (2002).
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 12
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert, M. et al. Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383, 550-553 (1996).
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1
  • 13
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • Kampers, T., Friedhoff, P., Biernat, J. & Mandelkow, E. M. RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett. 399, 344-349 (1996).
    • (1996) FEBS Lett. , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4
  • 14
    • 80655128134 scopus 로고    scopus 로고
    • Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by tau protein
    • Ramachandran, G. & Udgaonkar, J. B. Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by tau protein. J. Biol. Chem. 286, 38948-38959 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 38948-38959
    • Ramachandran, G.1    Udgaonkar, J.B.2
  • 15
    • 84858978818 scopus 로고    scopus 로고
    • Protein misfolded oligomers: Experimental approaches, mechanism of formation, and structure-toxicity relationships
    • Bemporad, F. & Chiti, F. Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships. Chem. Biol. 19, 315-327 (2012).
    • (2012) Chem. Biol. , vol.19 , pp. 315-327
    • Bemporad, F.1    Chiti, F.2
  • 16
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • Knowles, T. P. J. et al. An analytical solution to the kinetics of breakable filament assembly. Science 326, 1533-1537 (2009).
    • (2009) Science , vol.326 , pp. 1533-1537
    • Knowles, T.P.J.1
  • 17
    • 80051866825 scopus 로고    scopus 로고
    • Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments
    • Cohen, S. I. A. et al. Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments. J. Chem. Phys. 135, 065105 (2011).
    • (2011) J. Chem. Phys. , vol.135 , pp. 065105
    • Cohen, S.I.A.1
  • 18
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of alpha-synuclein
    • Cremades, N. et al. Direct observation of the interconversion of normal and toxic forms of alpha-synuclein. Cell 149, 1048-1059 (2012).
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1
  • 19
    • 0033070197 scopus 로고    scopus 로고
    • High prevalence of mutations in the microtubule-associated protein tau in a population study of frontotemporal dementia in the Netherlands
    • Rizzu, P. et al. High prevalence of mutations in the microtubule-associated protein tau in a population study of frontotemporal dementia in the Netherlands. Am. J. Hum. Genet. 64, 414-421 (1999).
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 414-421
    • Rizzu, P.1
  • 20
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn, S. et al. Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias. Biochemistry 39, 11714-11721 (2000).
    • (2000) Biochemistry , vol.39 , pp. 11714-11721
    • Barghorn, S.1
  • 21
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis, J. et al. Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat. Genet. 25, 402-405 (2000).
    • (2000) Nat. Genet. , vol.25 , pp. 402-405
    • Lewis, J.1
  • 22
    • 84855391797 scopus 로고    scopus 로고
    • Single molecule fluorescence under conditions of fast flow
    • Horrocks, M. H. et al. Single Molecule Fluorescence under Conditions of Fast Flow. Anal. Chem. 84, 179-185 (2012).
    • (2012) Anal. Chem. , vol.84 , pp. 179-185
    • Horrocks, M.H.1
  • 23
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local betastructure
    • von Bergen, M. et al. Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local betastructure. J. Biol. Chem. 276, 48165-48174 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 48165-48174
    • Von Bergen, M.1
  • 25
    • 79957913270 scopus 로고    scopus 로고
    • Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
    • Lasagna-Reeves, C. A. et al. Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice. Mol. Neurodegener. 6, 39 (2011).
    • (2011) Mol. Neurodegener. , vol.6 , pp. 39
    • Lasagna-Reeves, C.A.1
  • 26
    • 84868269943 scopus 로고    scopus 로고
    • Alzheimer brain-derived tau oligomers propagate pathology from endogenous tau
    • Lasagna-Reeves, C. A. et al. Alzheimer brain-derived tau oligomers propagate pathology from endogenous tau. Sci. Rep. 2, 700 (2012).
    • (2012) Sci. Rep. , vol.2 , pp. 700
    • Lasagna-Reeves, C.A.1
  • 28
    • 33947613349 scopus 로고
    • Theory of linear and helical aggregations of macromolecules
    • Oosawa, F. & Kasai, M. Theory of linear and helical aggregations of macromolecules. J. Mol. Biol. 4, 10-21 (1962).
    • (1962) J. Mol. Biol. , vol.4 , pp. 10-21
    • Oosawa, F.1    Kasai, M.2
  • 29
    • 84904512034 scopus 로고    scopus 로고
    • Stages and conformations of the Tau repeat domain during aggregation and its effect on neuronal toxicity
    • Kumar, S. et al. Stages and conformations of the Tau repeat domain during aggregation and its effect on neuronal toxicity. J. Biol. Chem. 289, 20318-20332 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 20318-20332
    • Kumar, S.1
  • 30
    • 35748954923 scopus 로고    scopus 로고
    • The beta-propensity of Tau determines aggregation and synaptic loss in inducible mouse models of tauopathy
    • Eckermann, K. et al. The beta-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
  • 31
    • 38549129613 scopus 로고    scopus 로고
    • The potential for beta-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. et al. The potential for beta-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).
    • (2008) J. Neurosci. , vol.28 , pp. 737-748
    • Mocanu, M.M.1
  • 32
    • 34547101740 scopus 로고    scopus 로고
    • Fibrillogenic nuclei composed of P301L mutant tau induce elongation of P301L tau but not wild-type tau
    • Aoyagi, H., Hasegawa, M. & Tamaoka, A. Fibrillogenic nuclei composed of P301L mutant tau induce elongation of P301L tau but not wild-type tau. J. Biol. Chem. 282, 20309-20318 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 20309-20318
    • Aoyagi, H.1    Hasegawa, M.2    Tamaoka, A.3
  • 33
    • 37549071037 scopus 로고    scopus 로고
    • Detection and quantification of tau aggregation using a membrane filter assay
    • Chang, E. & Kuret, J. Detection and quantification of tau aggregation using a membrane filter assay. Anal. Biochem. 373, 330-336 (2008).
    • (2008) Anal. Biochem. , vol.373 , pp. 330-336
    • Chang, E.1    Kuret, J.2
  • 34
    • 84868104221 scopus 로고    scopus 로고
    • FTDP-17 tau mutations induce distinct effects on aggregation and microtubule interactions
    • Combs, B. & Gamblin, T. C. FTDP-17 tau mutations induce distinct effects on aggregation and microtubule interactions. Biochemistry 51, 8597-8607 (2012).
    • (2012) Biochemistry , vol.51 , pp. 8597-8607
    • Combs, B.1    Gamblin, T.C.2
  • 35
    • 79956223051 scopus 로고    scopus 로고
    • Variations in filament conformation dictate seeding barrier between three-and four-repeat tau
    • Dinkel, P. D., Siddiqua, A., Huynh, H., Shah, M. & Margittai, M. Variations in filament conformation dictate seeding barrier between three-and four-repeat tau. Biochemistry 50, 4330-4336 (2011).
    • (2011) Biochemistry , vol.50 , pp. 4330-4336
    • Dinkel, P.D.1    Siddiqua, A.2    Huynh, H.3    Shah, M.4    Margittai, M.5
  • 36
    • 63649160214 scopus 로고    scopus 로고
    • Conformational diversity of wild-type tau fibrils specified by templated conformation change
    • Frost, B., Ollesch, J., Wille, H. & Diamond, M. I. Conformational diversity of wild-type tau fibrils specified by templated conformation change. J. Biol. Chem. 284, 3546-3551 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 3546-3551
    • Frost, B.1    Ollesch, J.2    Wille, H.3    Diamond, M.I.4
  • 37
    • 84879232559 scopus 로고    scopus 로고
    • Spreading of tau pathology in Alzheimer's disease by cell-to-cell transmission
    • Mohamed, N. V., Herrou, T., Plouffe, V., Piperno, N. & Leclerc, N. Spreading of tau pathology in Alzheimer's disease by cell-to-cell transmission. Eur. J. Neurosci. 37, 1939-1948 (2013).
    • (2013) Eur. J. Neurosci. , vol.37 , pp. 1939-1948
    • Mohamed, N.V.1    Herrou, T.2    Plouffe, V.3    Piperno, N.4    Leclerc, N.5
  • 38
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • Frost, B. & Diamond, M. I. Prion-like mechanisms in neurodegenerative diseases. Nat. Rev. Neurosci. 11, 155-159 (2010).
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 39
    • 33751204491 scopus 로고    scopus 로고
    • Determination of the fraction and stoichiometry of femtomolar levels of biomolecular complexes in an excess of monomer using single-molecule, two-color coincidence detection
    • Orte, A., Clarke, R., Balasubramanian, S. & Klenerman, D. Determination of the fraction and stoichiometry of femtomolar levels of biomolecular complexes in an excess of monomer using single-molecule, two-color coincidence detection. Anal. Chem. 78, 7707-7715 (2006).
    • (2006) Anal. Chem. , vol.78 , pp. 7707-7715
    • Orte, A.1    Clarke, R.2    Balasubramanian, S.3    Klenerman, D.4
  • 40
    • 84873809834 scopus 로고    scopus 로고
    • Single molecule characterization of the interactions between amyloid-beta peptides and the membranes of hippocampal cells
    • Narayan, P. et al. Single molecule characterization of the interactions between amyloid-beta peptides and the membranes of hippocampal cells. J. Am. Chem. Soc. 135, 1491-1498 (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 1491-1498
    • Narayan, P.1
  • 41
    • 84878994873 scopus 로고    scopus 로고
    • Proliferation of amyloid-beta 42 aggregates occurs through a secondary nucleation mechanism
    • Cohen, S. I. A. et al. Proliferation of amyloid-beta 42 aggregates occurs through a secondary nucleation mechanism. Proc. Natl Acad. Sci. USA 110, 9758-9763 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9758-9763
    • Cohen, S.I.A.1
  • 42
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. 2. A double nucleation mechanism
    • Ferrone, F. A., Hofrichter, J. & Eaton, W. A. Kinetics of sickle hemoglobin polymerization. 2. A double nucleation mechanism. J. Mol Biol. 183, 611-631 (1985).
    • (1985) J. Mol Biol. , vol.183 , pp. 611-631
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 43
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure
    • von Bergen, M. et al. Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. Proc. Natl Acad. Sci. USA 97, 5129-5134 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5129-5134
    • Von Bergen, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.