메뉴 건너뛰기




Volumn 159, Issue 1, 2007, Pages 71-81

Time resolved structure analysis of growing β-amyloid fibers

Author keywords

Amyloid; Aggregation; Time resolved static light scattering

Indexed keywords

AMINO ACID; AMYLOID BETA PROTEIN; BUFFER; SODIUM CHLORIDE;

EID: 34249939503     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2007.02.006     Document Type: Article
Times cited : (13)

References (53)
  • 1
    • 84986760704 scopus 로고
    • Time-resolved, static light scattering: new possibilities in polymer characterisation
    • Becker A., and Schmidt M. Time-resolved, static light scattering: new possibilities in polymer characterisation. Macromol. Chem., Macromol. Symp. 50 (1991) 249-260
    • (1991) Macromol. Chem., Macromol. Symp. , vol.50 , pp. 249-260
    • Becker, A.1    Schmidt, M.2
  • 2
    • 0000457975 scopus 로고
    • Force field parameterization by weak coupling: re-engineering SPC water
    • Berweger C.D., van Gunsteren W.F., and Müller-Plathe F. Force field parameterization by weak coupling: re-engineering SPC water. Chem. Phys. Lett. 232 (1995) 429-436
    • (1995) Chem. Phys. Lett. , vol.232 , pp. 429-436
    • Berweger, C.D.1    van Gunsteren, W.F.2    Müller-Plathe, F.3
  • 3
    • 0008738121 scopus 로고
    • A time-resolved light-scattering photometer
    • Chu B., Zhou Z., and Moser H.O. A time-resolved light-scattering photometer. Rev. Sci. Instrum. 63 (1992) 2954-2957
    • (1992) Rev. Sci. Instrum. , vol.63 , pp. 2954-2957
    • Chu, B.1    Zhou, Z.2    Moser, H.O.3
  • 4
    • 33846823909 scopus 로고
    • Particle mesh Ewald-an N log(N) method for Ewald sums in large systems
    • Darden T., York D., and Pedersen L. Particle mesh Ewald-an N log(N) method for Ewald sums in large systems. J. Chem. Phys. 98 (1993) 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 5
    • 33644606089 scopus 로고
    • Molecular weight determination by light scattering
    • Debye P. Molecular weight determination by light scattering. J. Phys. Colloid Chem. 51 (1947) 18-32
    • (1947) J. Phys. Colloid Chem. , vol.51 , pp. 18-32
    • Debye, P.1
  • 6
    • 0026138283 scopus 로고
    • Determination of chain stiffness and polydispersity from static light scattering
    • Denkinger P., and Burchard W. Determination of chain stiffness and polydispersity from static light scattering. J. Polym. Sci.: B 29 (1991) 589-600
    • (1991) J. Polym. Sci.: B , vol.29 , pp. 589-600
    • Denkinger, P.1    Burchard, W.2
  • 7
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 8
    • 0030087416 scopus 로고    scopus 로고
    • A fiber-optics-based light scattering instrument for time-resolved simultaneous static and dynamic measurements
    • Egelhaaf S.U., and Schurtenberger P. A fiber-optics-based light scattering instrument for time-resolved simultaneous static and dynamic measurements. Rev. Sci. Instrum. 67 (1996) 540-545
    • (1996) Rev. Sci. Instrum. , vol.67 , pp. 540-545
    • Egelhaaf, S.U.1    Schurtenberger, P.2
  • 9
    • 0011750898 scopus 로고    scopus 로고
    • Time-resolved recording of ionic dyestuff aggregation by static light scattering
    • Escudero Inglés S., Katzenstein A., Schlenker W., and Huber K. Time-resolved recording of ionic dyestuff aggregation by static light scattering. Langmuir 16 (2000) 3010-3018
    • (2000) Langmuir , vol.16 , pp. 3010-3018
    • Escudero Inglés, S.1    Katzenstein, A.2    Schlenker, W.3    Huber, K.4
  • 10
    • 33947087594 scopus 로고
    • Application of the cascade theory to calculation of particle scattering factors of polydisperse systems of stiff chains
    • Franken I., and Burchard W. Application of the cascade theory to calculation of particle scattering factors of polydisperse systems of stiff chains. Macromolecules 6 (1973) 848-855
    • (1973) Macromolecules , vol.6 , pp. 848-855
    • Franken, I.1    Burchard, W.2
  • 11
    • 0033849965 scopus 로고    scopus 로고
    • Studies on the in vitro assembly of Abeta 1-40: implications fort the search for Abeta Fibril Formation Inhibitors
    • Goldsbury C.S., Wirtz S.A., Müller S.A., Sunderji S., Wicki P., Aebi U., and Frey P. Studies on the in vitro assembly of Abeta 1-40: implications fort the search for Abeta Fibril Formation Inhibitors. J. Struct. Biol. 130 (2000) 217-231
    • (2000) J. Struct. Biol. , vol.130 , pp. 217-231
    • Goldsbury, C.S.1    Wirtz, S.A.2    Müller, S.A.3    Sunderji, S.4    Wicki, P.5    Aebi, U.6    Frey, P.7
  • 12
    • 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. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002) 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 13
    • 0038819889 scopus 로고    scopus 로고
    • Aggregation of a pseudoisocyanine chloride in aqueous NaCl solution
    • Herzog B., Huber K., and Stegemeyer H. Aggregation of a pseudoisocyanine chloride in aqueous NaCl solution. Langmuir 19 (2003) 5223-5232
    • (2003) Langmuir , vol.19 , pp. 5223-5232
    • Herzog, B.1    Huber, K.2    Stegemeyer, H.3
  • 17
    • 0037015358 scopus 로고    scopus 로고
    • Model of polydisperse wormlike stars and its application to dyestuff aggregates
    • Katzenstein A., and Huber K. Model of polydisperse wormlike stars and its application to dyestuff aggregates. Langmuir 18 (2002) 7049-7056
    • (2002) Langmuir , vol.18 , pp. 7049-7056
    • Katzenstein, A.1    Huber, K.2
  • 18
    • 0027906107 scopus 로고
    • Analytical calculation of the scattering function for polymers of arbitrary flexibility using the dirac propagator
    • Kholodenko L. Analytical calculation of the scattering function for polymers of arbitrary flexibility using the dirac propagator. Macromolecules 26 (1993) 4179-4183
    • (1993) Macromolecules , vol.26 , pp. 4179-4183
    • Kholodenko, L.1
  • 19
    • 0001096593 scopus 로고
    • Light scattering of stiff chain polymers
    • Koyama R. Light scattering of stiff chain polymers. J. Phys. Soc. Jpn. 34 (1973) 1029-1038
    • (1973) J. Phys. Soc. Jpn. , vol.34 , pp. 1029-1038
    • Koyama, R.1
  • 20
    • 84982060514 scopus 로고
    • Röntgenuntersuchung gelöster Fadenmoleküle
    • Kratky O., and Porod P. Röntgenuntersuchung gelöster Fadenmoleküle. Rec. Trav. Chim. Pays-Bas 68 (1949) 1106-1122
    • (1949) Rec. Trav. Chim. Pays-Bas , vol.68 , pp. 1106-1122
    • Kratky, O.1    Porod, P.2
  • 21
    • 34249950591 scopus 로고    scopus 로고
    • Krüger, J. 2006. Struktur und Funktion Acetylcholin bindender Proteine. Dissertationsschrift Universität Paderborn, http://ubdata.upb.de/ediss/13/2006/krueger/.
  • 22
    • 0011066764 scopus 로고
    • Über die Gestalt fadenförmiger Moleküle in Lösungen
    • Kuhn W. Über die Gestalt fadenförmiger Moleküle in Lösungen. Kolloid-Z. 68 (1934) 2-15
    • (1934) Kolloid-Z. , vol.68 , pp. 2-15
    • Kuhn, W.1
  • 23
    • 0019084319 scopus 로고
    • Grenzflächeneigenschaften von Alkylsulfonaten
    • Lange H., and Schwuger M.J. Grenzflächeneigenschaften von Alkylsulfonaten. Colloid & Polymer Sci. 258 (1980) 1263-1270
    • (1980) Colloid & Polymer Sci. , vol.258 , pp. 1263-1270
    • Lange, H.1    Schwuger, M.J.2
  • 24
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants
    • Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., and Teplow D.B. On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. USA 93 (1996) 1125-1129
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 27
    • 0033849811 scopus 로고    scopus 로고
    • Probing the kinetics of beta-amyloid self-association
    • Murphy R.M., and Pallitto M.M. Probing the kinetics of beta-amyloid self-association. J. Struct. Biol. 130 (2000) 109-122
    • (2000) J. Struct. Biol. , vol.130 , pp. 109-122
    • Murphy, R.M.1    Pallitto, M.M.2
  • 28
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro
    • Naiki H., and Nakakuki K. First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro. Lab. Invest. 74 (1996) 374-383
    • (1996) Lab. Invest. , vol.74 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 29
    • 84981785336 scopus 로고
    • Berechnung der Lichtzerstreuung von Fadenkettenlösungen
    • Neugebauer T. Berechnung der Lichtzerstreuung von Fadenkettenlösungen. Ann. Phys. 434 (1943) 509-533
    • (1943) Ann. Phys. , vol.434 , pp. 509-533
    • Neugebauer, T.1
  • 30
    • 0037076539 scopus 로고    scopus 로고
    • Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association Characterization of distinct products by light scattering and atomic force microscopy
    • Nichols M.R., Moss M.A., Reed D.K., Lin W.-L., Mukhopadhyay R., Hoh J.H., and Rosenberry T.L. Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association Characterization of distinct products by light scattering and atomic force microscopy. Biochemistry 41 19 (2002) 6115-6127
    • (2002) Biochemistry , vol.41 , Issue.19 , pp. 6115-6127
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Lin, W.-L.4    Mukhopadhyay, R.5    Hoh, J.H.6    Rosenberry, T.L.7
  • 31
    • 0020006501 scopus 로고
    • Excluded volume effects in dilute polymer solutions XIII. Effects of chain stiffness
    • Norisuye T., and Fujita H. Excluded volume effects in dilute polymer solutions XIII. Effects of chain stiffness. Polymer J. 14 (1982) 143-147
    • (1982) Polymer J. , vol.14 , pp. 143-147
    • Norisuye, T.1    Fujita, H.2
  • 32
    • 0000625389 scopus 로고
    • Radius of gyration versus molar mass relation from light scattering for polydisperse non-gaussian chain molecules
    • Oberthür R.C. Radius of gyration versus molar mass relation from light scattering for polydisperse non-gaussian chain molecules. Makromol. Chem. 179 (1978) 2693-2706
    • (1978) Makromol. Chem. , vol.179 , pp. 2693-2706
    • Oberthür, R.C.1
  • 33
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state
    • Pallitto M.M., and Murphy R.M. A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state. Biophys. J. 81 3 (2001) 1805-1822
    • (2001) Biophys. J. , vol.81 , Issue.3 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 34
    • 0030569147 scopus 로고    scopus 로고
    • Scattering functions of semiflexible polymers with and without excluded volume
    • Pedersen J.S., and Schurtenberger P. Scattering functions of semiflexible polymers with and without excluded volume. Macromolecules 29 (1996) 7602-7611
    • (1996) Macromolecules , vol.29 , pp. 7602-7611
    • Pedersen, J.S.1    Schurtenberger, P.2
  • 35
    • 0033646742 scopus 로고    scopus 로고
    • Analysis of the conformation of worm-like chains by small-angle scattering: Monte-Carlo Simulations in comparison to analytical theory
    • Pötschke D., Hickl P., Ballauff M., Astrand P.-O., and Pedersen J.S. Analysis of the conformation of worm-like chains by small-angle scattering: Monte-Carlo Simulations in comparison to analytical theory. Macrom. Theory Simul. 9 (2000) 345-353
    • (2000) Macrom. Theory Simul. , vol.9 , pp. 345-353
    • Pötschke, D.1    Hickl, P.2    Ballauff, M.3    Astrand, P.-O.4    Pedersen, J.S.5
  • 36
    • 0000423279 scopus 로고
    • On the diffraction of light by spheres of small relative refraction
    • Rayleigh L. On the diffraction of light by spheres of small relative refraction. Proc. R. Soc. London, Ser. A 90 (1914) 219-225
    • (1914) Proc. R. Soc. London, Ser. A , vol.90 , pp. 219-225
    • Rayleigh, L.1
  • 37
    • 20544466133 scopus 로고    scopus 로고
    • Evidence of the existence of micelles in the fibrillogenesis of beta-amyloid peptide
    • Sabaté R., and Estelrich J. Evidence of the existence of micelles in the fibrillogenesis of beta-amyloid peptide. J. Phys. Chem. B 109 (2005) 11027-11032
    • (2005) J. Phys. Chem. B , vol.109 , pp. 11027-11032
    • Sabaté, R.1    Estelrich, J.2
  • 38
    • 0038795608 scopus 로고    scopus 로고
    • An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid
    • Sabaté R., Gallardo M., and Estelrich J. An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid. Biopolymers 71 (2003) 190-195
    • (2003) Biopolymers , vol.71 , pp. 190-195
    • Sabaté, R.1    Gallardo, M.2    Estelrich, J.3
  • 39
    • 0027989805 scopus 로고
    • Effect of acid predissolution on fibril size and fibril flexibility of synthetic beta-amyloid Peptide
    • Shen C.-L., Fitzgerald M.C., and Murphy R.M. Effect of acid predissolution on fibril size and fibril flexibility of synthetic beta-amyloid Peptide. Biophys. J. 67 (1994) 1238-1246
    • (1994) Biophys. J. , vol.67 , pp. 1238-1246
    • Shen, C.-L.1    Fitzgerald, M.C.2    Murphy, R.M.3
  • 41
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis
    • Stine W.B., Dahlgren K.N., Krafft G.A., and LaDu M.J. In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. J. Biol. Chem. 278 (2003) 11612-11622
    • (2003) J. Biol. Chem. , vol.278 , pp. 11612-11622
    • Stine, W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 42
    • 0032084472 scopus 로고    scopus 로고
    • Structural and kinetic features of amyloid beta-protein fibrillogenesis
    • Teplow D.B. Structural and kinetic features of amyloid beta-protein fibrillogenesis. Amyloid: Int. J. Exp. Clin. Invest. 5 (1998) 121-142
    • (1998) Amyloid: Int. J. Exp. Clin. Invest. , vol.5 , pp. 121-142
    • Teplow, D.B.1
  • 43
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • Tycko R. Progress towards a molecular-level structural understanding of amyloid fibrils. Cur. Opin. Struct. Biol. 14 (2004) 96-103
    • (2004) Cur. Opin. Struct. Biol. , vol.14 , pp. 96-103
    • Tycko, R.1
  • 44
    • 0008168839 scopus 로고
    • Rayleigh scattering by linear flexible macromolecules
    • Utiyama H., Tsunashima Y., and Kurata M. Rayleigh scattering by linear flexible macromolecules. J. Chem. Phys. 55 (1971) 3133-3145
    • (1971) J. Chem. Phys. , vol.55 , pp. 3133-3145
    • Utiyama, H.1    Tsunashima, Y.2    Kurata, M.3
  • 48
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis: detection of a protofibrillar intermediate
    • Walsh D.M., Lomakin A., Benedek G.B., Condron M., and Teplow D.B. Amyloid beta-protein fibrillogenesis: detection of a protofibrillar intermediate. J. Biol. Chem. 272 (1997) 22364-22372
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.4    Teplow, D.B.5
  • 50
    • 3342976023 scopus 로고    scopus 로고
    • Formation of branched calixarene aggregates - a time-resolved static light scattering study
    • Witte T., Decker B., Mattay J., and Huber K. Formation of branched calixarene aggregates - a time-resolved static light scattering study. J. Am. Chem. Soc. 126 (2004) 9276-9282
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9276-9282
    • Witte, T.1    Decker, B.2    Mattay, J.3    Huber, K.4
  • 51
    • 0027649592 scopus 로고
    • An evaluation of the DAWN-B light scattering unit from Wyatt technology: suggested calibration, normalization and clarification procedures
    • Yunan W., Zhongde X., Li J., Rosenblum W.M., and Mays J.W. An evaluation of the DAWN-B light scattering unit from Wyatt technology: suggested calibration, normalization and clarification procedures. J. Apl. Polym. Sci. 49 (1993) 967-973
    • (1993) J. Apl. Polym. Sci. , vol.49 , pp. 967-973
    • Yunan, W.1    Zhongde, X.2    Li, J.3    Rosenblum, W.M.4    Mays, J.W.5
  • 52
    • 0029862811 scopus 로고    scopus 로고
    • Assembly of the gigantic hemoglobin of the earthworm Lumbricus terrestris-roles of subunit equilibria, non-globin linker chains, and valence of the heme iron
    • Zhu H., Ownby D.W., Riggs C.K., Nolasco N.J., Stoops J.K., and Riggs A.F. Assembly of the gigantic hemoglobin of the earthworm Lumbricus terrestris-roles of subunit equilibria, non-globin linker chains, and valence of the heme iron. J. Biol. Chem. 271 (1996) 300007-300021
    • (1996) J. Biol. Chem. , vol.271 , pp. 300007-300021
    • Zhu, H.1    Ownby, D.W.2    Riggs, C.K.3    Nolasco, N.J.4    Stoops, J.K.5    Riggs, A.F.6
  • 53
    • 0042849714 scopus 로고
    • Apparatus and methods for measurement and interpretation of the angular variation of light scattering; preliminary results on polystyrene solutions
    • Zimm B.H. Apparatus and methods for measurement and interpretation of the angular variation of light scattering; preliminary results on polystyrene solutions. J. Chem. Phys. 16 (1948) 1099-1116
    • (1948) J. Chem. Phys. , vol.16 , pp. 1099-1116
    • Zimm, B.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.