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Volumn 105, Issue 21, 2008, Pages 7462-7466

Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy

Author keywords

Alzheimer's disease; Amyloid ; Electron cryomicroscopy; Neurodegeneration; Protein folding

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; AMYLOID; AMYLOID BETA PROTEIN; PEPTIDE FRAGMENT;

EID: 44949250850     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0712290105     Document Type: Article
Times cited : (183)

References (35)
  • 1
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen F, Kelly J (2003) Therapeutic approaches to protein-misfolding diseases. Nature 426:905-909.
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.1    Kelly, J.2
  • 2
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson MP (2004) Pathways towards and away from Alzheimer's disease. Nature 430:631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 3
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson C (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.2
  • 4
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • Serpell LC (2000) Alzheimer's amyloid fibrils: Structure and assembly. Biochim Biophys Acta 1502:16-30.
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 5
    • 1642433249 scopus 로고    scopus 로고
    • High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
    • Jaroniec C, et al. (2004) High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc Natl Acad Sci USA 101:711-716.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 711-716
    • Jaroniec, C.1
  • 7
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-beta spines reveal varied steric zippers
    • Sawaya M, et al. (2007) Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447:453-457.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.1
  • 8
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova A, et al. (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.1
  • 9
    • 28444442999 scopus 로고    scopus 로고
    • Three-dimensional structure of Alzheimer's amyloid-β(1-42) fibrils
    • Lührs T, et al. (2005) Three-dimensional structure of Alzheimer's amyloid-β(1-42) fibrils. Proc Natl Acad Sci USA 102:17342-17347.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17342-17347
    • Lührs, T.1
  • 10
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • Kodali R, Wetzel R (2007) Polymorphism in the intermediates and products of amyloid assembly. Curr Opin Struct Biol 17:48-57.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 11
    • 0033849965 scopus 로고    scopus 로고
    • Studies on the in vitro assembly of a beta 1-40: Implications for the search for a beta fibril formation inhibitors
    • Goldsbury C, et al. (2000) Studies on the in vitro assembly of a beta 1-40: Implications for the search for a beta fibril formation inhibitors. J Struct Biol 130:217-231.
    • (2000) J Struct Biol , vol.130 , pp. 217-231
    • Goldsbury, C.1
  • 12
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • Petkova A, et al. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307:262-265.
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.1
  • 13
    • 0037047118 scopus 로고    scopus 로고
    • The protofilament structure of insulin amyloid fibrils
    • Jimenez J, et al. (2002) The protofilament structure of insulin amyloid fibrils. Proc Natl Acad Sci USA 99:9196-9201.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9196-9201
    • Jimenez, J.1
  • 14
    • 33747789637 scopus 로고    scopus 로고
    • Quaternary structure of a mature amyloid fibril from Alzheimer's A(1-40) peptide
    • Sachse C, et al. (2006) Quaternary structure of a mature amyloid fibril from Alzheimer's A(1-40) peptide. J Mol Biol 362:347-354.
    • (2006) J Mol Biol , vol.362 , pp. 347-354
    • Sachse, C.1
  • 15
    • 34447649588 scopus 로고    scopus 로고
    • High-resolution electron microscopy of helical specimens:Afresh look at tobacco mosaic virus
    • Sachse C, et al. (2007) High-resolution electron microscopy of helical specimens:Afresh look at tobacco mosaic virus. J Mol Biol 371:812-835.
    • (2007) J Mol Biol , vol.371 , pp. 812-835
    • Sachse, C.1
  • 16
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fändrich M, Dobson C (2002) The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J 21:5682-5690.
    • (2002) EMBO J , vol.21 , pp. 5682-5690
    • Fändrich, M.1    Dobson, C.2
  • 17
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of Alzheimer's beta(1-40) amyloid: Protofilament assembly of tubular fibrils
    • Malinchik SB, Inouye H, Szumowski KE, Kirschner DA (1998) Structural analysis of Alzheimer's beta(1-40) amyloid: Protofilament assembly of tubular fibrils. Biophys J 74:537-545.
    • (1998) Biophys J , vol.74 , pp. 537-545
    • Malinchik, S.B.1    Inouye, H.2    Szumowski, K.E.3    Kirschner, D.A.4
  • 18
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla A, Rousseau F, Schymkowitz J, Serrano L (2004) Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 22:1302-1306.
    • (2004) Nat Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 19
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama N, Venyaminov S, Woody R (1999) Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy. Protein Sci 8:370-380.
    • (1999) Protein Sci , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.2    Woody, R.3
  • 20
    • 20444458341 scopus 로고    scopus 로고
    • Correlation of structural elements and infectivity of the HET-s prion
    • Ritter C, et al. (2005) Correlation of structural elements and infectivity of the HET-s prion. Nature 435:844-848.
    • (2005) Nature , vol.435 , pp. 844-848
    • Ritter, C.1
  • 21
    • 15544388942 scopus 로고    scopus 로고
    • Hydrogen-deuterium (H/D) exchange mapping of Aβ 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy
    • Whittemore N, et al. (2005) Hydrogen-deuterium (H/D) exchange mapping of Aβ 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy. Biochemistry 44:4434-4441.
    • (2005) Biochemistry , vol.44 , pp. 4434-4441
    • Whittemore, N.1
  • 22
    • 33750826280 scopus 로고    scopus 로고
    • General structural motifs of amyloid protofilaments
    • Ferguson N, et al. (2006) General structural motifs of amyloid protofilaments. Proc Natl Acad Sci USA 103:16248-16253.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16248-16253
    • Ferguson, N.1
  • 23
    • 33845334180 scopus 로고    scopus 로고
    • Three-dimensional structure of amyloid protofilaments of β2-microglobulin fragment probed by solid-state NMR
    • Iwata K, et al. (2006) Three-dimensional structure of amyloid protofilaments of β2-microglobulin fragment probed by solid-state NMR. Proc Natl Acad Sci USA 103:18119-18124.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18119-18124
    • Iwata, K.1
  • 24
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils
    • Petkova AT, Yau WM, Tycko R (2006) Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry 45:498-512.
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 25
    • 10644252759 scopus 로고    scopus 로고
    • An intersheet packing interaction in A beta fibrils mapped by disulfide cross-linking
    • Shivaprasad S, Wetzel R (2004) An intersheet packing interaction in A beta fibrils mapped by disulfide cross-linking. Biochemistry 43:15310-15317.
    • (2004) Biochemistry , vol.43 , pp. 15310-15317
    • Shivaprasad, S.1    Wetzel, R.2
  • 26
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper JD, Wong SS, Lieber CM, Lansbury PT (1997) Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem Biol 4:119-125.
    • (1997) Chem Biol , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 27
    • 0035797795 scopus 로고    scopus 로고
    • Structural features of the Aβ amyloid fibril elucidated by limited proteolysis
    • Kheterpal I, Williams A, Murphy C, Bledsoe B, Wetzel R (2001) Structural features of the Aβ amyloid fibril elucidated by limited proteolysis. Biochemistry 40:11757-11767.
    • (2001) Biochemistry , vol.40 , pp. 11757-11767
    • Kheterpal, I.1    Williams, A.2    Murphy, C.3    Bledsoe, B.4    Wetzel, R.5
  • 28
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury P (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26:267-298.
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.2
  • 29
    • 34247504580 scopus 로고    scopus 로고
    • Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p
    • van der Wel PC, Lewandowski JR, Griffin RG (2007) Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p. J Am Chem Soc 129:5117-5130.
    • (2007) J Am Chem Soc , vol.129 , pp. 5117-5130
    • van der Wel, P.C.1    Lewandowski, J.R.2    Griffin, R.G.3
  • 30
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for highresolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for highresolution single-particle reconstructions. J Struct Biol 128:82-97.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 31
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, et al. (1996) SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116:190-199.
    • (1996) J Struct Biol , vol.116 , pp. 190-199
    • Frank, J.1
  • 32
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142:334-347.
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 33
    • 0035231630 scopus 로고    scopus 로고
    • Scanning transmission electron microscopy of DNA-protein complexes
    • Wall J, Simon M (2001) Scanning transmission electron microscopy of DNA-protein complexes. Methods Mol Biol 148:589-601.
    • (2001) Methods Mol Biol , vol.148 , pp. 589-601
    • Wall, J.1    Simon, M.2
  • 35
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera-A visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.