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Volumn 11, Issue 2, 2016, Pages 252-272

Molecular mechanisms of protein aggregation from global fitting of kinetic models

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; THIOFLAVINE; PROTEIN AGGREGATE;

EID: 84956497412     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2016.010     Document Type: Article
Times cited : (530)

References (33)
  • 1
    • 84924402296 scopus 로고    scopus 로고
    • The physical basis of protein misfolding disorders
    • Knowles, T.P.J., Vendruscolo, M. & Dobson, C.M. The physical basis of protein misfolding disorders. Phys. Today 68, 36 (2015).
    • (2015) Phys. Today , vol.68 , pp. 36
    • Knowles, T.P.J.1    Vendruscolo, M.2    Dobson, C.M.3
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. & Dobson, C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366 (2006).
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C.M. Protein folding and misfolding. Nature 426, 884-890 (2003).
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 4
    • 0242300624 scopus 로고    scopus 로고
    • Games played by rogue proteins in prion disorders and Alzheimer's disease
    • Aguzzi, A. & Haass, C. Games played by rogue proteins in prion disorders and Alzheimer's disease. Science 302, 814-818 (2003).
    • (2003) Science , vol.302 , pp. 814-818
    • Aguzzi, A.1    Haass, C.2
  • 5
    • 77649202326 scopus 로고    scopus 로고
    • Protein aggregation diseases: Pathogenicity and therapeutic perspectives
    • Aguzzi, A. & O'Connor, T. Protein aggregation diseases: pathogenicity and therapeutic perspectives. Nat. Rev. Drug Discov. 9, 237-248 (2010).
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 237-248
    • Aguzzi, A.1    O'Connor, T.2
  • 6
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J. & Selkoe, D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356 (2002).
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 7
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
    • Hu, X. et al. Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proc. Natl. Acad. Sci. USA 106, 20324-20329 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20324-20329
    • Hu, X.1
  • 9
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism
    • Ferrone, F.A., Hofrichter, J. & Eaton, W.A. Kinetics of sickle hemoglobin polymerization. II. 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
  • 11
    • 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
  • 12
    • 84924196173 scopus 로고    scopus 로고
    • The molecular chaperone brichos breaks the catalytic cycle that generates toxic Aβ oligomers
    • Cohen, S.I.A. et al. The molecular chaperone brichos breaks the catalytic cycle that generates toxic Aβ oligomers. Nat. Struct. Mol. Biol. 22, 207-213 (2015).
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , pp. 207-213
    • Cohen, S.I.A.1
  • 13
    • 84896695581 scopus 로고    scopus 로고
    • Chemical kinetics for drug discovery to combat protein aggregation diseases
    • Arosio, P., Vendruscolo, M., Dobson, C.M. & Knowles, T.P.J. Chemical kinetics for drug discovery to combat protein aggregation diseases. Trends Pharmacol. Sci. 35, 127-135 (2014).
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 127-135
    • Arosio, P.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.J.4
  • 15
    • 34547638452 scopus 로고    scopus 로고
    • Fiber-dependent amyloid formation as catalysis of an existing reaction pathway
    • Ruschak, A.M. & Miranker, A.D. Fiber-dependent amyloid formation as catalysis of an existing reaction pathway. Proc. Natl. Acad. Sci. USA 104, 12341-12346 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12341-12346
    • Ruschak, A.M.1    Miranker, A.D.2
  • 16
    • 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
    • Cohen, S.I.A.1
  • 17
    • 80051899060 scopus 로고    scopus 로고
    • Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations
    • Cohen, S.I.A., Vendruscolo, M., Dobson, C.M. & Knowles, T.P.J. Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations. J. Chem. Phys. 135, 065106 (2011).
    • (2011) J. Chem. Phys. , vol.135
    • Cohen, S.I.A.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.J.4
  • 18
    • 84903696629 scopus 로고    scopus 로고
    • Differences in nucleation behavior underlie the contrasting aggregation kinetics of the aβ40 and aβ42 peptides
    • Meisl, G. et al. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the aβ40 and aβ42 peptides. Proc. Natl. Acad. Sci. USA 111, 9384-9389 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 9384-9389
    • Meisl, G.1
  • 19
    • 84928580256 scopus 로고    scopus 로고
    • Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation
    • Abelein, A., Graslund, A. & Danielsson, J. Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation. Proc. Natl. Acad. Sci. USA 112, 5407-5412 (2015).
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 5407-5412
    • Abelein, A.1    Graslund, A.2    Danielsson, J.3
  • 20
    • 84863981137 scopus 로고    scopus 로고
    • From macroscopic measurements to microscopic mechanisms of protein aggregation
    • Cohen, S.I.A., Vendruscolo, M., Dobson, C.M. & Knowles, T.P.J. From macroscopic measurements to microscopic mechanisms of protein aggregation. J. Mol. Biol. 421, 160-171 (2012).
    • (2012) J. Mol. Biol. , vol.421 , pp. 160-171
    • Cohen, S.I.A.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.J.4
  • 22
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of α-synuclein
    • Cremades, N. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 149, 1048-1059 (2012).
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1
  • 23
    • 84902440293 scopus 로고    scopus 로고
    • Role of filament annealing in the kinetics and thermodynamics of nucleated polymerization
    • Michaels, T.C.T. & Knowles, T.P.J. Role of filament annealing in the kinetics and thermodynamics of nucleated polymerization. J. Chem. Phys. 140, 214904 (2014).
    • (2014) J. Chem. Phys. , vol.140
    • Michaels, T.C.T.1    Knowles, T.P.J.2
  • 24
    • 1442330505 scopus 로고    scopus 로고
    • The elongation of yeast prion fibers involves separable steps of association and conversion
    • Scheibel, T., Bloom, J. & Lindquist, S.L. The elongation of yeast prion fibers involves separable steps of association and conversion. Proc. Natl. Acad. Sci. USA 101, 2287-2292 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2287-2292
    • Scheibel, T.1    Bloom, J.2    Lindquist, S.L.3
  • 25
    • 0034733023 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism
    • Esler, W.P. et al. Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism. Biochemistry 39, 6288-6295 (2000).
    • (2000) Biochemistry , vol.39 , pp. 6288-6295
    • Esler, W.P.1
  • 26
    • 33947613349 scopus 로고
    • A theory of linear and helical aggregations of macromolecules
    • Oosawa, F. & Kasai, M. A 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
  • 27
    • 0000560869 scopus 로고    scopus 로고
    • Global optimization by basin-hopping and the lowest energy structures of Lennard-Jones clusters containing up to 110 atoms
    • Wales, D.J. & Doye, J.P.K. Global optimization by basin-hopping and the lowest energy structures of Lennard-Jones clusters containing up to 110 atoms. J. Phys. Chem. A 101, 5111-5116 (1997).
    • (1997) J. Phys. Chem. A , vol.101 , pp. 5111-5116
    • Wales, D.J.1    Doye, J.P.K.2
  • 28
    • 84878994873 scopus 로고    scopus 로고
    • Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
    • Cohen, S.I.A. et al. Proliferation of amyloid-β42 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
  • 29
    • 84892178364 scopus 로고    scopus 로고
    • Quantification of the concentration of aβ42 propagons during the lag phase by an amyloid chain reaction assay
    • Paolo Arosio, P., Cukalevski, R., Frohm, B., Knowles, T.P.J. & Linse, S. Quantification of the concentration of aβ42 propagons during the lag phase by an amyloid chain reaction assay. J. Am. Chem. Soc. 136, 219-225 (2014).
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 219-225
    • Paolo Arosio, P.1    Cukalevski, R.2    Frohm, B.3    Knowles, T.P.J.4    Linse, S.5
  • 30
    • 60349100306 scopus 로고    scopus 로고
    • A facile method for expression and purification of the Alzheimer's disease-associated amyloid β-peptide
    • Walsh, D.M. et al. A facile method for expression and purification of the Alzheimer's disease-associated amyloid β-peptide. FEBS J. 276, 1266-1281 (2009).
    • (2009) FEBS J , vol.276 , pp. 1266-1281
    • Walsh, D.M.1
  • 31
    • 74649086711 scopus 로고    scopus 로고
    • The recombinant amyloid-beta peptide Aβ1-42 aggregates faster and is more neurotoxic than synthetic Aβ1-42
    • Finder, V.H., Vodopivec, I., Nitsch, R.M. & Glockshuber, R. The recombinant amyloid-beta peptide Aβ1-42 aggregates faster and is more neurotoxic than synthetic Aβ1-42. J. Mol. Biol. 396, 9-18 (2010).
    • (2010) J. Mol. Biol. , vol.396 , pp. 9-18
    • Finder, V.H.1    Vodopivec, I.2    Nitsch, R.M.3    Glockshuber, R.4
  • 32
    • 84871285635 scopus 로고    scopus 로고
    • Role of aromatic side chains in amyloid β-protein aggregation
    • Cukalevski, R. et al. Role of aromatic side chains in amyloid β-protein aggregation. ACS Chem. Neurosci. 3, 1008-1016 (2012).
    • (2012) ACS Chem. Neurosci , vol.3 , pp. 1008-1016
    • Cukalevski, R.1
  • 33
    • 77951676986 scopus 로고    scopus 로고
    • Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process
    • Hellstrand, E., Boland, B., Walsh, D.M. & Linse, S. Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process. ACS Chem. Neurosci. 1, 13-18 (2010).
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 13-18
    • Hellstrand, E.1    Boland, B.2    Walsh, D.M.3    Linse, S.4


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