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Volumn 1834, Issue 12, 2013, Pages 2480-2485

Acceleration of the depolymerization of amyloid β fibrils by ultrasonication

Author keywords

Amyloid ; Amyloid fibril; Solubility; Supersaturation; Ultrasonication

Indexed keywords

AMYLOID BETA PROTEIN; MONOMER;

EID: 84884685634     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.08.013     Document Type: Article
Times cited : (43)

References (41)
  • 1
    • 0031825554 scopus 로고    scopus 로고
    • From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation
    • DOI 10.1017/S0033583598003400
    • M. Sunde, and C.C. Blake From the globular to the fibrous state: protein structure and structural conversion in amyloid formation Q. Rev. Biophys. 31 1998 1 39 (Pubitemid 28379176)
    • (1998) Quarterly Reviews of Biophysics , vol.31 , Issue.1 , pp. 1-39
    • Sunde, M.1    Blake, C.C.F.2
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890 (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 3
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • DOI 10.1038/nature02265
    • F.E. Cohen, and J.W. Kelly Therapeutic approaches to protein-misfolding diseases Nature 426 2003 905 909 (Pubitemid 38056884)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 4
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 84868374880 scopus 로고    scopus 로고
    • Amyloid fibril protein nomenclature: 2012 recommendations from the Nomenclature Committee of the International Society of Amyloidosis
    • J.D. Sipe, M.D. Benson, J.N. Buxbaum, S. Ikeda, G. Merlini, M.J. Saraiva, and P. Westermark Amyloid fibril protein nomenclature: 2012 recommendations from the Nomenclature Committee of the International Society of Amyloidosis Amyloid 19 2012 167 170
    • (2012) Amyloid , vol.19 , pp. 167-170
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.4    Merlini, G.5    Saraiva, M.J.6    Westermark, P.7
  • 8
    • 34247899121 scopus 로고    scopus 로고
    • Functional amyloid - from bacteria to humans
    • DOI 10.1016/j.tibs.2007.03.003, PII S096800040700059X
    • D.M. Fowler, A.V. Koulov, W.E. Balch, and J.W. Kelly Functional amyloid - from bacteria to humans Trends Biochem. Sci. 32 2007 217 224 (Pubitemid 46694328)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.5 , pp. 217-224
    • Fowler, D.M.1    Koulov, A.V.2    Balch, W.E.3    Kelly, J.W.4
  • 11
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • J.T. Jarrett, and P.T. Lansbury Jr. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73 1993 1055 1058 (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 12
    • 14044250915 scopus 로고    scopus 로고
    • In vitro conversion of mammalian prion protein into amyloid fibrils displays unusual features
    • DOI 10.1021/bi048322t
    • I.V. Baskakov, and O.V. Bocharova In vitro conversion of mammalian prion protein into amyloid fibrils displays unusual features Biochemistry 44 2005 2339 2348 (Pubitemid 40279538)
    • (2005) Biochemistry , vol.44 , Issue.7 , pp. 2339-2348
    • Baskakov, I.V.1    Bocharova, O.V.2
  • 13
    • 34447639279 scopus 로고    scopus 로고
    • Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils
    • DOI 10.1111/j.1742-4658.2007.05916.x
    • I.V. Baskakov Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils FEBS J. 274 2007 3756 3765 (Pubitemid 47087672)
    • (2007) FEBS Journal , vol.274 , Issue.15 , pp. 3756-3765
    • Baskakov, I.V.1
  • 15
    • 37349062389 scopus 로고    scopus 로고
    • Visualization and classification of amyloid β supramolecular assemblies
    • DOI 10.1021/bi701842n
    • H. Yagi, T. Ban, K. Morigaki, H. Naiki, and Y. Goto Visualization and classification of amyloid β supramolecular assemblies Biochemistry 46 2007 15009 15017 (Pubitemid 350308892)
    • (2007) Biochemistry , vol.46 , Issue.51 , pp. 15009-15017
    • Yagi, H.1    Ban, T.2    Morigaki, K.3    Naiki, H.4    Goto, Y.5
  • 17
    • 0000079910 scopus 로고    scopus 로고
    • Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro
    • H. Naiki, S. Hashimoto, H. Suzuki, K. Kimura, K. Nakakuki, and F. Gejyo Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro Amyloid 4 1997 223 232 (Pubitemid 127716139)
    • (1997) Amyloid , vol.4 , Issue.4 , pp. 223-232
    • Naiki, H.1    Hashimoto, N.2    Suzuki, S.3    Kimura, H.4    Nakakuki, K.5    Gejyo, F.6
  • 21
    • 0242462517 scopus 로고
    • Sonic degradation of high polymers in solution
    • J.R. Thomas Sonic degradation of high polymers in solution J. Phys. Chem. 63 1959 1725 1729
    • (1959) J. Phys. Chem. , vol.63 , pp. 1725-1729
    • Thomas, J.R.1
  • 22
    • 0346426794 scopus 로고
    • Cavitation
    • E. Webster Cavitation Ultrasonics 1 1963 39 48
    • (1963) Ultrasonics , vol.1 , pp. 39-48
    • Webster, E.1
  • 23
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • DOI 10.1146/annurev.biochem.66.1.385
    • J.D. Harper, and P.T. Lansbury Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 66 1997 385 407 (Pubitemid 27274662)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 25
    • 80052968365 scopus 로고    scopus 로고
    • Ultrasonication-dependent acceleration of amyloid fibril formation
    • M. So, H. Yagi, K. Sakurai, H. Ogi, H. Naiki, and Y. Goto Ultrasonication-dependent acceleration of amyloid fibril formation J. Mol. Biol. 412 2011 568 577
    • (2011) J. Mol. Biol. , vol.412 , pp. 568-577
    • So, M.1    Yagi, H.2    Sakurai, K.3    Ogi, H.4    Naiki, H.5    Goto, Y.6
  • 27
    • 84455204797 scopus 로고    scopus 로고
    • Proper calibration of ultrasonic power enabled the quantitative analysis of the ultrasonication-induced amyloid formation process
    • K. Yamaguchi, T. Matsumoto, and K. Kuwata Proper calibration of ultrasonic power enabled the quantitative analysis of the ultrasonication- induced amyloid formation process Protein Sci. 21 2012 38 49
    • (2012) Protein Sci. , vol.21 , pp. 38-49
    • Yamaguchi, K.1    Matsumoto, T.2    Kuwata, K.3
  • 28
    • 33947613349 scopus 로고
    • A theory of linear and helical aggregations of macromolecules
    • F. Oosawa, and M. Kasai A theory of linear and helical aggregations of macromolecules J. Mol. Biol. 4 1962 10 21
    • (1962) J. Mol. Biol. , vol.4 , pp. 10-21
    • Oosawa, F.1    Kasai, M.2
  • 29
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
    • A.M. Morris, M.A. Watzky, and R.G. Finke Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature Biochim. Biophys. Acta 1794 2009 375 397
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 30
    • 33749824175 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of amyloid fibril assembly
    • R. Wetzel Kinetics and thermodynamics of amyloid fibril assembly Accounts Chem. Res. 39 2006 671 679
    • (2006) Accounts Chem. Res. , vol.39 , pp. 671-679
    • Wetzel, R.1
  • 31
    • 0018118740 scopus 로고
    • Crystallization of proteins
    • Z. Kam, H.B. Shore, and G. Feher Crystallization of proteins J. Mol. Biol. 123 1978 539 555
    • (1978) J. Mol. Biol. , vol.123 , pp. 539-555
    • Kam, Z.1    Shore, H.B.2    Feher, G.3
  • 33
    • 4344568810 scopus 로고    scopus 로고
    • Protein crystallization and phase diagrams
    • DOI 10.1016/j.ymeth.2004.03.028, PII S1046202304001100
    • N. Asherie Protein crystallization and phase diagrams Methods 34 2004 266 272 (Pubitemid 39119813)
    • (2004) Methods , vol.34 , Issue.3 , pp. 266-272
    • Asherie, N.1
  • 34
    • 4344602994 scopus 로고    scopus 로고
    • Introduction to protein crystallization
    • DOI 10.1016/j.ymeth.2004.03.019, PII S1046202304001094
    • A. McPherson Introduction to protein crystallization Methods 34 2004 254 265 (Pubitemid 39119812)
    • (2004) Methods , vol.34 , Issue.3 , pp. 254-265
    • McPherson, A.1
  • 35
    • 84863958621 scopus 로고    scopus 로고
    • Protein solubility and protein homeostasis: A generic view of protein misfolding disorders
    • M. Vendruscolo, T.P. Knowles, and C.M. Dobson Protein solubility and protein homeostasis: a generic view of protein misfolding disorders Cold Spring Harb. Perspect. Biol. 3 2011
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Vendruscolo, M.1    Knowles, T.P.2    Dobson, C.M.3
  • 38
    • 84880986533 scopus 로고    scopus 로고
    • Ultrasonication: An efficient agitation for accelerating the supersaturation-limited amyloid fibrillation of proteins
    • 07HA01
    • Y. Yoshimura, M. So, H. Yagi, and Y. Goto Ultrasonication: an efficient agitation for accelerating the supersaturation-limited amyloid fibrillation of proteins Jpn. J. Appl. Phys. 52 07HA01 2013 01 08
    • (2013) Jpn. J. Appl. Phys. , vol.52 , pp. 01-08
    • Yoshimura, Y.1    So, M.2    Yagi, H.3    Goto, Y.4
  • 39
    • 0037137225 scopus 로고    scopus 로고
    • Kinetic modeling and determination of reaction constants of Alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance
    • DOI 10.1021/bi020369w
    • K. Hasegawa, K. Ono, M. Yamada, and H. Naiki Kinetic modeling and determination of reaction constants of Alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance Biochemistry 41 2002 13489 13498 (Pubitemid 35332684)
    • (2002) Biochemistry , vol.41 , Issue.46 , pp. 13489-13498
    • Hasegawa, K.1    Ono, K.2    Yamada, M.3    Naiki, H.4
  • 40
  • 41
    • 27644491161 scopus 로고    scopus 로고
    • Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer's β-amyloid variants
    • DOI 10.1110/ps.051585905
    • P. Hortschansky, T. Christopeit, V. Schroeckh, and M. Fandrich Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer's β-amyloid variants Protein Sci. 14 2005 2915 2918 (Pubitemid 41577272)
    • (2005) Protein Science , vol.14 , Issue.11 , pp. 2915-2918
    • Hortschansky, P.1    Christopeit, T.2    Schroeckh, V.3    Fandrich, M.4


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