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Volumn 18, Issue 4, 1999, Pages 815-821

Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

Author keywords

Amyloid fibrils; Cryo electron microscopy; Protein misfolding; SH3 domain; Single particle analysis

Indexed keywords

AMYLOID; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN SUBUNIT;

EID: 0042847751     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.4.815     Document Type: Article
Times cited : (465)

References (36)
  • 1
    • 0028800177 scopus 로고
    • Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin
    • Bauer,H.H., Aebi, U., Haner, M., Hermann, R., Muller, M., Arvinte, T. and Merkle, H.P. (1995) Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. J. Struct. Biol., 115, 1-15.
    • (1995) J. Struct. Biol. , vol.115 , pp. 1-15
    • Bauer, H.H.1    Aebi, U.2    Haner, M.3    Hermann, R.4    Muller, M.5    Arvinte, T.6    Merkle, H.P.7
  • 2
    • 0027292152 scopus 로고
    • The crystal structure of alkaline protease
    • Baumann, U., Wu, S., Flaherty, K.M. and McKay, D.B. (1993) The crystal structure of alkaline protease. EMBO J., 12, 3357-3364.
    • (1993) EMBO J. , vol.12 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 3
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • Blake, C. and Serpell, L.C. (1996) Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure, 4, 989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.C.2
  • 4
    • 0024163316 scopus 로고
    • The reconstruction of helical particles with variable pitch
    • Bluemke, D.A., Carragher, B. and Josephs, R. (1988) The reconstruction of helical particles with variable pitch. Ultramicroscopy, 26, 255-270.
    • (1988) Ultramicroscopy , vol.26 , pp. 255-270
    • Bluemke, D.A.1    Carragher, B.2    Josephs, R.3
  • 5
    • 0029905402 scopus 로고    scopus 로고
    • Stacked bilayer helices: A new structural organization of amphiphilic molecules
    • Boettcher, C., Stark, H. and van Heel, M. (1996) Stacked bilayer helices: a new structural organization of amphiphilic molecules. Ultramicroscopy, 62, 133-139.
    • (1996) Ultramicroscopy , vol.62 , pp. 133-139
    • Boettcher, C.1    Stark, H.2    Van Heel, M.3
  • 6
    • 0027191192 scopus 로고
    • Solution structure and ligand binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase
    • Booker, G.W., Gout, I., Downing, A.K., Driscoll, P.C., Boyd, J., Waterfield, M.D. and Campbell, I.D. (1993) Solution structure and ligand binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase. Cell 73, 813-822.
    • (1993) Cell , vol.73 , pp. 813-822
    • Booker, G.W.1    Gout, I.2    Downing, A.K.3    Driscoll, P.C.4    Boyd, J.5    Waterfield, M.D.6    Campbell, I.D.7
  • 7
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth, D.R. et al. (1997) Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature, 385, 787-793.
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1
  • 10
    • 0000844417 scopus 로고
    • Electron microscopy of amyloid
    • Harris, J.R. (ed.), Academic Press, London, UK
    • Cohen, A.S., Shirahama, T. and Skinner, M. (1982) Electron microscopy of amyloid. In Harris, J.R. (ed.), Electron Microscopy of Proteins, Vol. 3. Academic Press, London, UK, pp. 165-205.
    • (1982) Electron Microscopy of Proteins , vol.3 , pp. 165-205
    • Cohen, A.S.1    Shirahama, T.2    Skinner, M.3
  • 11
    • 0016287131 scopus 로고
    • Selective staining as a function of amyloid composition and structure: Histochemical analysis of the alkaline Congo red, standardized toluidine blue and iodine methods
    • Cooper, J.H. (1974) Selective staining as a function of amyloid composition and structure: histochemical analysis of the alkaline Congo red, standardized toluidine blue and iodine methods. Lab. Invest., 31, 232-238.
    • (1974) Lab. Invest. , vol.31 , pp. 232-238
    • Cooper, J.H.1
  • 12
    • 0022435132 scopus 로고
    • Image reconstruction of the Alzheimer paired helical filament
    • Crowther, R.A. and Wischik, C. (1985) Image reconstruction of the Alzheimer paired helical filament. EMBO J., 4, 3661-3665.
    • (1985) EMBO J. , vol.4 , pp. 3661-3665
    • Crowther, R.A.1    Wischik, C.2
  • 13
    • 0014945329 scopus 로고
    • Reconstruction of the three-dimensional image from electron micrographs of structures with helical symmetry
    • DeRosier, D.J. and Moore, P.B. (1970) Reconstruction of the three-dimensional image from electron micrographs of structures with helical symmetry. J. Mol. Biol., 52, 355-369.
    • (1970) J. Mol. Biol. , vol.52 , pp. 355-369
    • DeRosier, D.J.1    Moore, P.B.2
  • 14
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. (1997) An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J. Mol. Graphics, 15, 132-134.
    • (1997) J. Mol. Graphics , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 16
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M. and Leith, A. (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    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 17
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis. The β-fibrilloses (part one)
    • Glenner, G.G. (1980) Amyloid deposits and amyloidosis. The β-fibrilloses (part one). N. Engl. J. Med., 302, 1283-1292.
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 18
    • 0031170857 scopus 로고    scopus 로고
    • Polymorphic fibrillar assembly of human amylin
    • Goldsbury, C.S. et al. (1997) Polymorphic fibrillar assembly of human amylin. J. Struct. Biol., 119, 17-27.
    • (1997) J. Struct. Biol. , vol.119 , pp. 17-27
    • Goldsbury, C.S.1
  • 20
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
    • Harper, J.D., Lieber, C.M. and Lansbury, P.T. (1997) Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein. Chem. Biol., 4, 951-959.
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 21
    • 0030728039 scopus 로고    scopus 로고
    • Deadly conformations - Protein misfolding in prion disease
    • Horwich, A.L. and Weissman, J.S. (1997) Deadly conformations - protein misfolding in prion disease. Cell, 89, 499-510.
    • (1997) Cell , vol.89 , pp. 499-510
    • Horwich, A.L.1    Weissman, J.S.2
  • 22
    • 0344095509 scopus 로고
    • Department of Molecular Biology, University of Uppsala, Sweden
    • Jones, T.A. and Kjeldgaard, M. (1992) O version 5.8.1. Department of Molecular Biology, University of Uppsala, Sweden.
    • (1992) O Version 5.8.1
    • Jones, T.A.1    Kjeldgaard, M.2
  • 23
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J.W. (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol., 8, 101-106.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 24
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) Molscript - a program to produce both detailed and schematic plots of protein structures. J. Appl Crystallogr., 24, 946-950.
    • (1991) J. Appl Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of Alzheimer's β (1-40) amyloid: Protofilament assembly of tubular fibrils
    • Malinchik, S.B., Inouye, H., Szumowski, K.E. and Kirschner, D.A. (1998) Structural analysis of Alzheimer's β (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
  • 26
    • 0028057108 scopus 로고
    • Raster3d version-2.0 - A program for photorealistic molecular graphics
    • Merritt, E.A. and Murphy, M.E.P. (1994) Raster3d version-2.0 - a program for photorealistic molecular graphics. Acta Crystallogr. D, 50, 869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 27
    • 0000694354 scopus 로고    scopus 로고
    • Amyloidosis
    • Weatherall, D.J., Ledingham, J.G.G. and Warell, D.A. (eds). Oxford University Press, Oxford, UK
    • Pepys, M.B. (1996) Amyloidosis. In Weatherall, D.J., Ledingham, J.G.G. and Warell, D.A. (eds). The Oxford Textbook of Medicine, 3rd edn, Vol. 2. Oxford University Press, Oxford, UK. pp. 1512-1524.
    • (1996) The Oxford Textbook of Medicine, 3rd Edn. , vol.2 , pp. 1512-1524
    • Pepys, M.B.1
  • 29
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger, M.P., Bennett, M.J. and Eisenberg, D. (1997) Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Protein Chem., 50, 61-122.
    • (1997) Adv. Protein Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 30
  • 31
    • 0030564927 scopus 로고    scopus 로고
    • 3-dimensional structure of ncd-decorated microtubules obtained by a back-projection method
    • Sosa, H. and Milligan, R.A. (1996) 3-dimensional structure of ncd-decorated microtubules obtained by a back-projection method. J. Mol. Biol., 260, 743-755.
    • (1996) J. Mol. Biol. , vol.260 , pp. 743-755
    • Sosa, H.1    Milligan, R.A.2
  • 32
    • 0028095571 scopus 로고
    • Crystal structure of p22 tailspike protein - Interdigitated subunits in a thermostable trimer
    • Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R. and Reinemer, P. (1994) Crystal structure of p22 tailspike protein - interdigitated subunits in a thermostable trimer. Science, 265, 383-386.
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 33
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde, M. and Blake, C. (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
  • 36
    • 0027329090 scopus 로고
    • New domain motif - The structure of pectate lyase-c, a secreted plant virulence factor
    • Yoder, M.D., Keen, N.T. and Jurnak, F. (1993) New domain motif - the structure of pectate lyase-c, a secreted plant virulence factor. Science, 260, 1503-1507.
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3


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