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Volumn 98, Issue 10, 2010, Pages 2290-2298

Amyloid-β fibrillogenesis seeded by interface-induced peptide misfolding and self-assembly

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EID: 77952775252     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.01.038     Document Type: Article
Times cited : (13)

References (44)
  • 1
    • 33847076858 scopus 로고    scopus 로고
    • Ganglioside G(M1)mediated amyloid-β fibrillogenesis and membrane disruption
    • Chi, E. Y., S. L. Frey, and K. Y. C. Lee. 2007. Ganglioside G(M1)mediated amyloid-β fibrillogenesis and membrane disruption. Biochemistry. 46:1913-1924.
    • (2007) Biochemistry. , vol.46 , pp. 1913-1924
    • Chi, E.Y.1    Frey, S.L.2    Lee, K.Y.C.3
  • 2
    • 4444328762 scopus 로고    scopus 로고
    • Insertion of Alzheimer's Aβ40 peptide into lipid monolayers
    • Ege, C., and K. Y. C. Lee. 2004. Insertion of Alzheimer's Aβ40 peptide into lipid monolayers. Biophys. J. 87:1732-1740.
    • (2004) Biophys. J. , vol.87 , pp. 1732-1740
    • Ege, C.1    Lee, K.Y.C.2
  • 3
    • 20544466133 scopus 로고    scopus 로고
    • Evidence of the existence of micelles in the fibrillogenesis of β-amyloid peptide
    • Sabaté, R., and J. Estelrich. 2005. Evidence of the existence of micelles in the fibrillogenesis of β-amyloid peptide. J. Phys. Chem. B. 109:11027-11032.
    • (2005) J. Phys. Chem. B. , vol.109 , pp. 11027-11032
    • Sabaté, R.1    Estelrich, J.2
  • 4
    • 0032796425 scopus 로고    scopus 로고
    • Amyloid-β-sheet formation at the air-water interface
    • Schladitz, C, E. P. Vieira, ..., H. Möhwald. 1999. Amyloid-β-sheet formation at the air-water interface. Biophys. J. 77:3305-3310.
    • (1999) Biophys. J. , vol.77 , pp. 3305-3310
    • Schladitz, C.1    Vieira, E.P.2    Möhwald, H.3
  • 5
    • 0027988116 scopus 로고
    • Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation
    • Soreghan, B., J. Kosmoski, and C. Glabe. 1994. Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation. J. Biol. Chem. 269:28551-28554.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28551-28554
    • Soreghan, B.1    Kosmoski, J.2    Glabe, C.3
  • 6
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin, A., D. S. Chung, ..., D. B. Teplow. 1996. On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Prot: Natl. Acad. Sci. USA. 93:1125-1129.
    • (1996) Prot: Natl. Acad. Sci. USA. , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Teplow, D.B.3
  • 7
    • 0026646605 scopus 로고
    • Isolation and quantification, of soluble Alzheimer's β-peptide from biological, fluids
    • Seubert, P., C. Vigo-Pelfrey, ..., D. Schenk. 1992. Isolation and quantification, of soluble Alzheimer's β-peptide from biological, fluids. Nature. 359:325-327.
    • (1992) Nature. , vol.359 , pp. 325-327
    • Seubert, P.1    Vigo-Pelfrey, C.2    Schenk, D.3
  • 8
    • 0025779179 scopus 로고
    • Solution structures of β peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow, C. J., and M. G. Zagorski. 1991. Solution structures of β peptide and its constituent fragments: relation to amyloid deposition. Science. 253:179-182.
    • (1991) Science. , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 9
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde, M., and C. Blake. 1997. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50: 123-159.
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 10
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease. Analysis of circular dichroism spectra
    • Barrow, C. J., A. Yasuda, ..., M. G. Zagorski. 1992. Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease. Analysis of circular dichroism spectra. J. Mol. Biol. 225:1075-1093.
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Zagorski, M.G.3
  • 11
    • 10744219665 scopus 로고    scopus 로고
    • Solution NMR studies of the Aβ (1-40) and Aβ (1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation
    • Hou, L. M., H. Y. Shao, ..., M. G. Zagorski. 2004. Solution NMR studies of the Aβ (1-40) and Aβ (1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation. J. Am. Chem. Soc. 126:1992-2005.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1992-2005
    • Hou, L.M.1    Shao, H.Y.2    Zagorski, M.G.3
  • 12
    • 34247234602 scopus 로고    scopus 로고
    • The Alzheimer's peptides Aβ4O and 42 adopt distinct conformations in water: A combined MD/NMR study
    • Sgourakis, N. G., Y. L. Yan, ...., A. E. Garcia. 2007. The Alzheimer's peptides Aβ4O and 42 adopt distinct conformations in water: a combined MD/NMR study. J. Mol. Biol. 368:1448-1457.
    • (2007) J. Mol. Biol. , vol.368 , pp. 1448-1457
    • Sgourakis, N.G.1    Yan, Y.L.2    Garcia, A.E.3
  • 13
    • 0033863220 scopus 로고    scopus 로고
    • Activation barriers to structural transition determine deposition, rates of Alzheimer's disease Aβ amyloid
    • Esler, W. P., A. M. Felix, ..., J. E. Maggio. 2000. Activation barriers to structural transition determine deposition, rates of Alzheimer's disease Aβ amyloid. J. Struct. Biol. 130:174-183.
    • (2000) J. Struct. Biol. , vol.130 , pp. 174-183
    • Esler, W.P.1    Felix, A.M.2    Maggio, J.E.3
  • 14
    • 0037020259 scopus 로고    scopus 로고
    • Kinetic studies of amyloid β-protein fibril assembly. Differential effects of α-helix stabilization
    • Fezoui, Y., and D. B. Teplow. 2002. Kinetic studies of amyloid β-protein fibril assembly. Differential effects of α-helix stabilization. J. Biol. Chem. 277:36948-36954.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36948-36954
    • Fezoui, Y.1    Teplow, D.B.2
  • 15
    • 17644397372 scopus 로고    scopus 로고
    • Aβ40-Lac- Tam(D23/K28) models a conformation highly favorable for nucleation of amyloid
    • Sciarretta, K. L., D. J. Gordon, ..., S. C. Meredith. 2005. Aβ40-Lac- tam(D23/K28) models a conformation highly favorable for nucleation of amyloid. Biochemistry. 44:6003-6014.
    • (2005) Biochemistry. , vol.44 , pp. 6003-6014
    • Sciarretta, K.L.1    Gordon, D.J.2    Meredith, S.C.3
  • 16
    • 21244462685 scopus 로고    scopus 로고
    • Protein structural perturbation and aggregation on homogeneous surfaces
    • Sethuraman, A., and G. Belfort. 2005. Protein structural perturbation and aggregation on homogeneous surfaces. Biophys. J. 88:1322-1333.
    • (2005) Biophys. J. , vol.88 , pp. 1322-1333
    • Sethuraman, A.1    Belfort, G.2
  • 17
    • 14344262955 scopus 로고    scopus 로고
    • Heterogeneous nucleation-controlled particulate formation of recombinant human platelet-activating factor acetylhydrolase in pharmaceutical formulation
    • Chi, E. Y., J. Weickmann, ...,T. W. Randolph. 2005. Heterogeneous nucleation-controlled particulate formation of recombinant human platelet-activating factor acetylhydrolase in pharmaceutical formulation. J. Pharm. Sci. 94:256-274.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 256-274
    • Chi, E.Y.1    Weickmann, J.2    Randolph, T.W.3
  • 18
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation
    • Kowalewski, T., and D. M. Holtzman. 1999. In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: new insights into mechanism of β-sheet formation. Proc. Natl. Acad. Sci. USA. 96:3688-3693.
    • (1999) Proc. Natl. Acad. Sci. USA. , vol.96 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.M.2
  • 19
    • 24144499832 scopus 로고    scopus 로고
    • Amyloid-β aggregates formed at polar-nonpolar interfaces differ from amyloid-β protofibrils produced in aqueous buffers
    • Nichols, M. R., M. A. Moss, ..., T. L. Rosenberry. 2005. Amyloid-β aggregates formed at polar-nonpolar interfaces differ from amyloid-β protofibrils produced in aqueous buffers. Microsc. Res. Tech, 67: 164-174.
    • (2005) Microsc. Res. Tech , vol.67 , pp. 164-174
    • Nichols, M.R.1    Moss, M.A.2    Rosenberry, T.L.3
  • 20
    • 0035943343 scopus 로고    scopus 로고
    • Cholesterol, a modulator of membrane-associated Aβ-fibrillogenesis and neurotoxicity
    • Yip, C. M., E. A. Elton, ..., J. McLaurin. 2001. Cholesterol, a modulator of membrane-associated Aβ-fibrillogenesis and neurotoxicity. J. Mol. Biol. 311:723-734.
    • (2001) J. Mol. Biol. , vol.311 , pp. 723-734
    • Yip, C.M.1    Elton, E.A.2    McLaurin, J.3
  • 21
    • 0030892291 scopus 로고    scopus 로고
    • Characterization of the interactions of Alzheimer β-amyloid peptides with phospholipid membranes
    • McLaurin, J., and A. Chakrabartty. 1997. Characterization of the interactions of Alzheimer β-amyloid peptides with phospholipid membranes. Eur. J. Biochem. 245:355-363.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 355-363
    • McLaurin, J.1    Chakrabartty, A.2
  • 22
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes
    • Terzi, E., G. Hölzemann, and J. Seelig. 1997. Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes. Biochemistry. 36:14845-14852.
    • (1997) Biochemistry. , vol.36 , pp. 14845-14852
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 23
    • 44949154514 scopus 로고    scopus 로고
    • Lipid membrane templates the ordering and induces the fibrillogenesis of Alzheimer's disease amyloid-β peptide
    • Chi, E. Y., C. Ege, ..., K. Y. Lee. 2008. Lipid membrane templates the ordering and induces the fibrillogenesis of Alzheimer's disease amyloid-β peptide. Proteins. 72:1-24.
    • (2008) Proteins. , vol.72 , pp. 1-24
    • Chi, E.Y.1    Ege, C.2    Lee, K.Y.3
  • 24
    • 15044365726 scopus 로고    scopus 로고
    • Templating effect of lipid membranes on Alzheimer's amyloid β peptide
    • Ege, C., J. Majewski, ..., K. Y. Lee. 2005. Templating effect of lipid membranes on Alzheimer's amyloid β peptide. ChemPhysChem. 6:226-229.
    • (2005) ChemPhysChem. , vol.6 , pp. 226-229
    • Ege, C.1    Majewski, J.2    Lee, K.Y.3
  • 25
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • Tycko, R. 2006. Molecular structure of amyloid fibrils: insights from solid-state NMR. Q. Rev. Biophys. 39:1-55.
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 1-55
    • Tycko, R.1
  • 26
    • 33846703726 scopus 로고    scopus 로고
    • Adsorption of amyloid-β (1-40) peptide at liquid interfaces
    • Brezesinski, G., E. Maltseva, and H. Mohwald. 2007. Adsorption of amyloid-β (1-40) peptide at liquid interfaces. Z. Phys. Chem. 221: 95-111.
    • (2007) Z. Phys. Chem. , vol.221 , pp. 95-111
    • Brezesinski, G.1    Maltseva, E.2    Mohwald, H.3
  • 27
    • 77957063705 scopus 로고    scopus 로고
    • Structural properties and interactions of thin films at the air-liquid interface explored by synchrotron x-ray scattering
    • D. Mobius and R. Miller, editors. Elsevier Science, Amsterdam
    • Jensen, T. R., and K. Kjaer. 2001, Structural properties and interactions of thin films at the air-liquid interface explored by synchrotron x-ray scattering. In Novel Methods to Study Interfacial Layers. D. Mobius and R. Miller, editors. Elsevier Science, Amsterdam. 205-254.
    • (2001) Novel Methods to Study Interfacial Layers , pp. 205-254
    • Jensen, T.R.1    Kjaer, K.2
  • 28
    • 0032049616 scopus 로고    scopus 로고
    • Apparatus for the continuous monitoring of surface morphology via fluorescence microscopy during monolayer transfer to substrates
    • Lee, K. Y. C., M. M. Lipp, ..., A. J. Waring. 1998. Apparatus for the continuous monitoring of surface morphology via fluorescence microscopy during monolayer transfer to substrates. Langmuir: 14:2567-2572.
    • (1998) Langmuir , vol.14 , pp. 2567-2572
    • Lee, K.Y.C.1    Lipp, M.M.2    Waring, A.J.3
  • 29
    • 66149153044 scopus 로고    scopus 로고
    • Float and compress: Honeycomb-like array of a highly stable protein scaffold
    • Heyman, A., I. Medalsy, ...,O. Shoseyov. 2009. Float and compress: honeycomb-like array of a highly stable protein scaffold. Langmuir. 25:5226-5229.
    • (2009) Langmuir. , vol.25 , pp. 5226-5229
    • Heyman, A.1    Medalsy, I.2    Shoseyov, O.3
  • 30
    • 17744363305 scopus 로고    scopus 로고
    • Silicone oil induced aggregation, of proteins
    • Jones, L. S., A. Kaufmann, and C. R. Middaugh. 2005. Silicone oil induced aggregation, of proteins. J. Pharm. Sci. 94:918-927.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 918-927
    • Jones, L.S.1    Kaufmann, A.2    Middaugh, C.R.3
  • 31
    • 0036872542 scopus 로고    scopus 로고
    • Study of β-amyloid peptide (Aβ40) insertion into phospholipid membranes using monolayer technique
    • Ji, S. R., Y. Wu, and S. F. Sui. 2002. Study of β-amyloid peptide (Aβ40) insertion into phospholipid membranes using monolayer technique. Biochemistry (Mosc). 67:1283-1288.
    • (2002) Biochemistry (Mosc) , vol.67 , pp. 1283-1288
    • Ji, S.R.1    Wu, Y.2    Sui, S.F.3
  • 32
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • Chi, E. Y., S. Krishnan, ..., T. W. Randolph. 2003. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci. 12:903-913.
    • (2003) Protein Sci. , vol.12 , pp. 903-913
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3
  • 33
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S. N. 1998. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem, 51:355-432.
    • (1998) Adv. Protein Chem , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 34
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 35
    • 0345217118 scopus 로고
    • Principles and applications of grazing incidence X-ray and neutron scattering from ordered molecular monolayers at the air-water interface
    • Als-Nielsen, J., D. Jacquemain, ..., L. Leiserowitz. 1994. Principles and applications of grazing incidence X-ray and neutron scattering from ordered molecular monolayers at the air-water interface. Phys. Rep. 246:251-313.
    • (1994) Phys. Rep. , vol.246 , pp. 251-313
    • Als-Nielsen, J.1    Jacquemain, D.2    Leiserowitz, L.3
  • 36
    • 0034724375 scopus 로고    scopus 로고
    • Twodimensional structure of β-amyloid( 10-35) fibrils
    • Benzinger, T. L., D. M. Gregory, ..., S. C. Meredith. 2000. Twodimensional structure of β-amyloid( 10-35) fibrils. Biochemistry. 39: 3491-3499.
    • (2000) Biochemistry. , vol.39 , pp. 3491-3499
    • Benzinger, T.L.1    Gregory, D.M.2    Meredith, S.C.3
  • 37
    • 26944494925 scopus 로고    scopus 로고
    • Adsorption of amyloid β (1-40) peptide at phospholipid monolayers
    • Maltseva, E., A. Kerth, ..., G. Brezesinski. 2005. Adsorption of amyloid β (1-40) peptide at phospholipid monolayers. ChemBioChem. 6:1817-1824.
    • (2005) ChemBioChem. , vol.6 , pp. 1817-1824
    • Maltseva, E.1    Kerth, A.2    Brezesinski, G.3
  • 38
    • 56549103100 scopus 로고    scopus 로고
    • Stochastic fitting of specular X-ray reflectivity data using StochFit
    • Danauskas, S. M., D. X. Li, ..., K. Y. C. Lee. 2008. Stochastic fitting of specular X-ray reflectivity data using StochFit. J. Appl. Cryst. 41: 1187-1193.
    • (2008) J. Appl. Cryst. , vol.41 , pp. 1187-1193
    • Danauskas, S.M.1    Li, D.X.2    Lee, K.Y.C.3
  • 39
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • Petkova, A. T., R. D. Leapman, ..., R. Tycko. 2005. Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science. 307:262-265.
    • (2005) Science. , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Tycko, R.3
  • 41
    • 66149140617 scopus 로고    scopus 로고
    • Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure
    • Paravastu, A. K., I. Qahwash, ..., R. Tycko. 2009. Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure. Prot: Natl. Acad. Sci, USA. 106:7443-7448.
    • (2009) Prot: Natl. Acad. Sci, USA. , vol.106 , pp. 7443-7448
    • Paravastu, A.K.1    Qahwash, I.2    Tycko, R.3
  • 42
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova, A. T., Y. Ishii, ..., R. Tycko. 2002. A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl, Acad. Sci, USA. 99:16742-16747.
    • (2002) Proc. Natl, Acad. Sci, USA. , vol.99 , pp. 16742-16747
    • Petkova, A.T.1    Ishii, Y.2    Tycko, R.3
  • 43
    • 0026448778 scopus 로고
    • Model for the role of macromolecular crowding in regulation, of cellular volume
    • Minton, A. P., G. C. Colclasure, and J. C. Parker. 1992. Model for the role of macromolecular crowding in regulation, of cellular volume. Proc: Natl. Acad. Sci. USA. 89:10504-10506.
    • (1992) Proc: Natl. Acad. Sci. USA. , vol.89 , pp. 10504-10506
    • Minton, A.P.1    Colclasure, G.C.2    Parker, J.C.3
  • 44
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
    • Paravastu, A. K., R. D. Leapman, ..., R. Tycko. 2008. Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils. Proc. Natl. Acad. Sci. USA. 105:18349-18354.
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Tycko, R.3


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