메뉴 건너뛰기




Volumn 79, Issue 6, 2000, Pages 3282-3293

Ultrastructural organization of amyloid fibrils by atomic force microscopy

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; LYSOZYME; PHOSPHATIDYLINOSITOL 3 KINASE; PREALBUMIN;

EID: 0033637078     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76560-X     Document Type: Article
Times cited : (181)

References (72)
  • 1
    • 0028800177 scopus 로고
    • Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin
    • Bauer, H. H., U. Aebi, M. Haner, R. Hermann, M. Muller, and H. P. Merkle. 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    Merkle, H.P.6
  • 4
    • 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 L. Serpell. 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.2
  • 6
    • 0027191192 scopus 로고
    • Solution structure and ligand-binding site of the SH3 domain of the p85 α subunit of phosphatidylinositol 3′-kinase
    • Booker, G. W., I. Gout, A. K. Downing, P. C. Driscoll, J. Boyd, M. D. Waterfield, and I. D. Campbell. 1993. Solution structure and ligand-binding site of the SH3 domain of the p85 α 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
  • 8
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta amyloid neurotoxicity
    • Busciglio, J., A. Lorenzo, and B. A. Yankner. 1992. Methodological variables in the assessment of beta amyloid neurotoxicity. Neurobiol. Aging. 13:609-612.
    • (1992) Neurobiol. Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 9
    • 0033580657 scopus 로고    scopus 로고
    • Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants
    • Canet, D., M. Sunde, A. M. Last, A. Miranker, A. Spencer, C. V. Robinson, and C. M. Dobson. 1999. Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants. Biochemistry. 38:6419-6427.
    • (1999) Biochemistry , vol.38 , pp. 6419-6427
    • Canet, D.1    Sunde, M.2    Last, A.M.3    Miranker, A.4    Spencer, A.5    Robinson, C.V.6    Dobson, C.M.7
  • 10
    • 0031593854 scopus 로고    scopus 로고
    • Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease
    • Chaney, M. O., S. D. Webster, Y. M. Kuo, and A. E. Roher. 1998. Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease. Protein Eng. 11:761-767.
    • (1998) Protein Eng. , vol.11 , pp. 761-767
    • Chaney, M.O.1    Webster, S.D.2    Kuo, Y.M.3    Roher, A.E.4
  • 12
    • 0000844417 scopus 로고
    • Electron microscopy of amyloid
    • J. R. Harris, editor. Academic Press, New York
    • Cohen, A. S., T. Shirahama, and M. Skinner. 1982. Electron microscopy of amyloid. In Electron Microscopy of Proteins. J. R. Harris, editor. Academic Press, New York. 165-205.
    • (1982) Electron Microscopy of Proteins , pp. 165-205
    • Cohen, A.S.1    Shirahama, T.2    Skinner, M.3
  • 13
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease
    • Conway, K. A., J. D. Harper, and P. T. Lansbury. 1998. Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease. Nature Med. 4:1318-2130.
    • (1998) Nature Med. , vol.4 , pp. 1318-2130
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 14
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 15
    • 0033602221 scopus 로고    scopus 로고
    • Atomic force microscopy: A forceful way with single molecules
    • Engel, A., H. E. Gaub, and D. J. Muller. 1999. Atomic force microscopy: a forceful way with single molecules. Curr. Biol. 9:R133-R-136.
    • (1999) Curr. Biol. , vol.9
    • Engel, A.1    Gaub, H.E.2    Muller, D.J.3
  • 17
    • 0028937108 scopus 로고
    • Sequential assembly of collagen revealed by atomic force microscopy
    • Gale, M., M. S. Pollanen, P. Markiewicz, and M. C. Goh. 1995. Sequential assembly of collagen revealed by atomic force microscopy. Biophys. J. 68:2124-2128.
    • (1995) Biophys. J. , vol.68 , pp. 2124-2128
    • Gale, M.1    Pollanen, M.S.2    Markiewicz, P.3    Goh, M.C.4
  • 19
    • 0033534397 scopus 로고    scopus 로고
    • Watching amyloid fibrils grow by time-lapse atomic force microscopy
    • Goldsbury, C., J. Kistler, U. Aebi, T. Arvinte, and G. J. S. Cooper. 1999. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J. Mol. Biol. 285:33-39.
    • (1999) J. Mol. Biol. , vol.285 , pp. 33-39
    • Goldsbury, C.1    Kistler, J.2    Aebi, U.3    Arvinte, T.4    Cooper, G.J.S.5
  • 20
    • 0032570543 scopus 로고    scopus 로고
    • Folding kinetics of the SH3 domain of PI3′-kinase by real-time NMR combined with optical spectroscopy
    • Guijarro, J. I., C. J. Morton, K. W. Plaxco, I. D. Campbell, and C. M. Dobson. 1998a. Folding kinetics of the SH3 domain of PI3′-kinase by real-time NMR combined with optical spectroscopy. J. Mol. Biol. 276: 657-667.
    • (1998) J. Mol. Biol. , vol.276 , pp. 657-667
    • Guijarro, J.I.1    Morton, C.J.2    Plaxco, K.W.3    Campbell, I.D.4    Dobson, C.M.5
  • 22
    • 0025801516 scopus 로고
    • Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro
    • Gustavsson, A., U. Engstrom, and P. Westermark. 1991. Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro. Biochem. Biophys. Res. Commun. 175:1159-1164.
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 1159-1164
    • Gustavsson, A.1    Engstrom, U.2    Westermark, P.3
  • 23
    • 0028364295 scopus 로고
    • Biomolecular imaging with the atomic force microscope
    • Hansma, H. G., and J. H. Hoh. 1994. Biomolecular imaging with the atomic force microscope. Annu. Rev. Biophys. Biomol. Struct. 23: 115-139.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 115-139
    • Hansma, H.G.1    Hoh, J.H.2
  • 24
    • 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., C. M. Lieber, and P. T. Lansbury. 1997a. 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
  • 25
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper, J. D., S. S. Wong, C. M. Lieber, and P. T. Lansbury. 1997b. 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
  • 26
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of Aβ amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
    • Harper, J. D., S. S. Wong, C. M. Lieber, and P. T. Lansbury. 1999. Assembly of Aβ amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry. 38:8972-8980.
    • (1999) Biochemistry , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 27
    • 0033121032 scopus 로고    scopus 로고
    • Spatially resolved force spectroscopy of biological surfaces using the atomic force microscope
    • Heinz, W. F., and J. H. Hoh. 1999. Spatially resolved force spectroscopy of biological surfaces using the atomic force microscope. Trends Biotechnol. 17:143-150.
    • (1999) Trends Biotechnol. , vol.17 , pp. 143-150
    • Heinz, W.F.1    Hoh, J.H.2
  • 28
    • 0026784795 scopus 로고
    • Actin filament dynamics in living glial cells imaged by atomic force microscopy
    • Henderson, E., P. G. Haydon, and D. S. Sakaguchi. 1992. Actin filament dynamics in living glial cells imaged by atomic force microscopy. Science. 257:1944-1946.
    • (1992) Science , vol.257 , pp. 1944-1946
    • Henderson, E.1    Haydon, P.G.2    Sakaguchi, D.S.3
  • 29
    • 0029868555 scopus 로고    scopus 로고
    • A high resolution ultrastructural study of experimental murine AA amyloid
    • Inoue, S., and R. Kisilevsky. 1996. A high resolution ultrastructural study of experimental murine AA amyloid. Lab. Invest. 74:670-683.
    • (1996) Lab. Invest. , vol.74 , pp. 670-683
    • Inoue, S.1    Kisilevsky, R.2
  • 30
    • 0031450347 scopus 로고    scopus 로고
    • Ultrastructural organization of hemodialysis-associated β2-microglobulin amyloid fibrils
    • Inoue, S., M. Kuroiwa, K. Ohashi, M. Hara, and R. Kisilevsky. 1997. Ultrastructural organization of hemodialysis-associated β2-microglobulin amyloid fibrils. Kidney Int. 52:1543-1549.
    • (1997) Kidney Int. , vol.52 , pp. 1543-1549
    • Inoue, S.1    Kuroiwa, M.2    Ohashi, K.3    Hara, M.4    Kisilevsky, R.5
  • 31
    • 0032447486 scopus 로고    scopus 로고
    • Ultrastructure of familial amyloid polyneuropathy amyloid fibrils: Examination with high-resolution electron microscopy
    • Inoue, S., M. Kuroiwa, M. J. Saraiva, A. Guimaraes, and R. Kisilevsky. 1998a. Ultrastructure of familial amyloid polyneuropathy amyloid fibrils: examination with high-resolution electron microscopy. J. Struct. Biol. 124:1-12.
    • (1998) J. Struct. Biol. , vol.124 , pp. 1-12
    • Inoue, S.1    Kuroiwa, M.2    Saraiva, M.J.3    Guimaraes, A.4    Kisilevsky, R.5
  • 32
    • 0032087441 scopus 로고    scopus 로고
    • A high resolution ultrastructural comparison of isolated and in situ murine AA amyloid fibrils
    • Inoue, S., M. Kuroiwa, R. Tan, and R. Kisilevsky. 1998b. A high resolution ultrastructural comparison of isolated and in situ murine AA amyloid fibrils. Amyloid. 5:99-110.
    • (1998) Amyloid , vol.5 , pp. 99-110
    • Inoue, S.1    Kuroiwa, M.2    Tan, R.3    Kisilevsky, R.4
  • 33
    • 0032150739 scopus 로고    scopus 로고
    • Analysis of x-ray diffraction patterns from amyloid of biopsied vitreous humor and kidney of transthyretin (TTR) Met30 familial amyloidotic polyneuropathy (FAP) patients: Axially arrayed TIK monomers constitute the protofilament
    • Inouye, H., F. S. Domingues, A. M. Damas, M. J. Saraiva, E. Lundgren, O. Sandgren, and D. A. Kirschner. 1998. Analysis of x-ray diffraction patterns from amyloid of biopsied vitreous humor and kidney of transthyretin (TTR) Met30 familial amyloidotic polyneuropathy (FAP) patients: axially arrayed TIK monomers constitute the protofilament. Amyloid. 5:163-174.
    • (1998) Amyloid , vol.5 , pp. 163-174
    • Inouye, H.1    Domingues, F.S.2    Damas, A.M.3    Saraiva, M.J.4    Lundgren, E.5    Sandgren, O.6    Kirschner, D.A.7
  • 34
    • 0031547975 scopus 로고    scopus 로고
    • X-ray diffraction analysis of scrapie prion: Intermediate and folded structures in a peptide containing two putative α-helices
    • Inouye, H., and D. A. Kirschner. 1997. X-ray diffraction analysis of scrapie prion: intermediate and folded structures in a peptide containing two putative α-helices. J. Mol. Biol. 268:375-389.
    • (1997) J. Mol. Biol. , vol.268 , pp. 375-389
    • Inouye, H.1    Kirschner, D.A.2
  • 36
    • 0027296226 scopus 로고
    • X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin
    • Jarvis, J. A., D. J. Craik, and M. C. Wilce. 1993. X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin. Biochem. Biophys. Res. Commun. 192:991-998.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 991-998
    • Jarvis, J.A.1    Craik, D.J.2    Wilce, M.C.3
  • 37
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jiménez, J. L., J. I. Guijarro, E. Orlova, J. Zurdo, C. M. Dobson, M. Sunde, and H. R. Saibil. 1999. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18: 815-821.
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jiménez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 38
    • 0027403020 scopus 로고
    • Observation of living cells using the atomic force microscope
    • Kasas, S., V. Gotzos, and M. R. Celio. 1993. Observation of living cells using the atomic force microscope. Biophys. J. 64:539-544.
    • (1993) Biophys. J. , vol.64 , pp. 539-544
    • Kasas, S.1    Gotzos, V.2    Celio, M.R.3
  • 40
    • 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
  • 41
    • 0032447487 scopus 로고    scopus 로고
    • In vitro amyloid fibril formation by synthetic peptides corresponding to the amino terminus of apoSAA isoforms from amyloid-susceptible and amyloid-resistant mice
    • Kirschner, D. A., R. Elliott-Bryant, K. E. Szumowski, W. A. Gonnerman, M. S. Kindy, J. D. Sipe, and E. S. Cathcart. 1998. In vitro amyloid fibril formation by synthetic peptides corresponding to the amino terminus of apoSAA isoforms from amyloid-susceptible and amyloid-resistant mice. J. Struct. Biol. 124:88-98.
    • (1998) J. Struct. Biol. , vol.124 , pp. 88-98
    • Kirschner, D.A.1    Elliott-Bryant, R.2    Szumowski, K.E.3    Gonnerman, W.A.4    Kindy, M.S.5    Sipe, J.D.6    Cathcart, E.S.7
  • 42
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo, E. H., P. T. Lansbury, and J. W. Kelly. 1999. Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc. Natl. Acad. Sci. U.S.A. 96:9989-9990.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury, P.T.2    Kelly, J.W.3
  • 43
    • 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. U.S.A. 96:3688-3693.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.M.2
  • 44
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
    • Lansbury, P. T. 1999. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl. Acad. Sci. U.S.A. 96:3342-3344.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3342-3344
    • Lansbury, P.T.1
  • 46
    • 0033040551 scopus 로고    scopus 로고
    • An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments
    • Li, L., T. A. Darden, L. Bartolotti, D. Kominos, and L. G. Pedersen. 1999. An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments. Biophys. J. 76:2871-2878.
    • (1999) Biophys. J. , vol.76 , pp. 2871-2878
    • Li, L.1    Darden, T.A.2    Bartolotti, L.3    Kominos, D.4    Pedersen, L.G.5
  • 47
    • 0033600590 scopus 로고    scopus 로고
    • 2+-sensitive channel in reconstituted lipid vesicles
    • 2+-sensitive channel in reconstituted lipid vesicles. Biochemistry. 38:11189-11196.
    • (1999) Biochemistry , vol.38 , pp. 11189-11196
    • Lin, H.1    Zhu, Y.J.2    Lal, R.3
  • 48
    • 0034646573 scopus 로고    scopus 로고
    • Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin
    • MacPhee, C. E., and C. M. Dobson. 2000. Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin. J. Mol. Biol. 297:1203-1215.
    • (2000) J. Mol. Biol. , vol.297 , pp. 1203-1215
    • MacPhee, C.E.1    Dobson, C.M.2
  • 49
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of Alzheimer's β(1-40) amyloid: Protofilament assembly of tubular fibrils
    • Malinchik, S. B., H. Inouye, K. E. Szumowski, and D. A. Kirschner. 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
  • 50
    • 0028263333 scopus 로고
    • Amyloid fibril formation in gelsolin-derived amyloidosis: Definition of the amyloidogenic region and evidence of accelerated amyloid formation of mutant Asn-187 and Tyr-187 gelsolin peptides
    • Maury, C. P., E. L. Nurmiaho-Lassila, and H. Rossi. 1994. Amyloid fibril formation in gelsolin-derived amyloidosis: definition of the amyloidogenic region and evidence of accelerated amyloid formation of mutant Asn-187 and Tyr-187 gelsolin peptides. Lab. Invest. 70:558-564.
    • (1994) Lab. Invest. , vol.70 , pp. 558-564
    • Maury, C.P.1    Nurmiaho-Lassila, E.L.2    Rossi, H.3
  • 53
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Müller, D. J., M. Amrein, and A. Engel. 1997. Adsorption of biological molecules to a solid support for scanning probe microscopy. J. Struct. Biol. 119:172-188.
    • (1997) J. Struct. Biol. , vol.119 , pp. 172-188
    • Müller, D.J.1    Amrein, M.2    Engel, A.3
  • 54
    • 0031834932 scopus 로고    scopus 로고
    • Fibrous long spacing collagen ultrastructure elucidated by atomic force microscopy
    • Paige, M. F., J. K. Rainey, and M. C. Goh. 1998. Fibrous long spacing collagen ultrastructure elucidated by atomic force microscopy. Biophys. J. 74:3211-3216.
    • (1998) Biophys. J. , vol.74 , pp. 3211-3216
    • Paige, M.F.1    Rainey, J.K.2    Goh, M.C.3
  • 55
    • 0033533380 scopus 로고    scopus 로고
    • Disulfide bonds in the outer layer of keratin fibers confer higher mechanical rigidity: Correlative nano-indentation and elasticity measurement with an AFM
    • Parbhu, A. N., W. G. Bryson, and R. Lal. 1999. Disulfide bonds in the outer layer of keratin fibers confer higher mechanical rigidity: correlative nano-indentation and elasticity measurement with an AFM. Biochemistry. 38:11755-11761.
    • (1999) Biochemistry , vol.38 , pp. 11755-11761
    • Parbhu, A.N.1    Bryson, W.G.2    Lal, R.3
  • 57
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • Perutz, M. F. 1999. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 24:58-63.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 58
    • 0030635801 scopus 로고    scopus 로고
    • Paired helical filaments are twisted ribbons composed of two parallel and aligned components: Image reconstruction and modeling of filament structure using atomic force microscopy
    • Pollanen, M. S., P. Markiewicz, and M. C. Goh. 1997. Paired helical filaments are twisted ribbons composed of two parallel and aligned components: image reconstruction and modeling of filament structure using atomic force microscopy. J. Neuropathol. Exp. Neurol. 56:79-85.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 79-85
    • Pollanen, M.S.1    Markiewicz, P.2    Goh, M.C.3
  • 60
    • 0031170886 scopus 로고    scopus 로고
    • The toxicity of the Alzheimer's β-amyloid peptide correlates with a distinct fiber morphology
    • Seilheimer, B., B. Bohrmann, L. Bondolfi, F. Muller, D. Stuber, and H. Dobeli. 1997. The toxicity of the Alzheimer's β-amyloid peptide correlates with a distinct fiber morphology. J. Struct. Biol. 119:59-71.
    • (1997) J. Struct. Biol. , vol.119 , pp. 59-71
    • Seilheimer, B.1    Bohrmann, B.2    Bondolfi, L.3    Muller, F.4    Stuber, D.5    Dobeli, H.6
  • 62
  • 63
    • 0029021712 scopus 로고
    • Progress in high resolution atomic force microscopy in biology
    • Shao, Z., and J. Yang. 1995. Progress in high resolution atomic force microscopy in biology. Q. Rev. Biophys. 28:195-251.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 195-251
    • Shao, Z.1    Yang, J.2
  • 64
    • 0029563227 scopus 로고
    • Biological atomic force microscopy: From microns to nanometers and beyond
    • Shao, Z., Yang, J., and A. P. Somlyo. 1995. Biological atomic force microscopy: from microns to nanometers and beyond. Annu. Rev. Cell. Dev. Biol. 11:241-265.
    • (1995) Annu. Rev. Cell. Dev. Biol. , vol.11 , pp. 241-265
    • Shao, Z.1    Yang, J.2    Somlyo, A.P.3
  • 65
    • 0030428377 scopus 로고    scopus 로고
    • Biological cryo atomic force microscopy: A brief review
    • Shao, Z., and Y. Zhang. 1996. Biological cryo atomic force microscopy: a brief review. Ultramicroscopy. 66:141-152.
    • (1996) Ultramicroscopy , vol.66 , pp. 141-152
    • Shao, Z.1    Zhang, Y.2
  • 66
    • 0027989805 scopus 로고
    • Effect of acid predissolution on fibril size and fibril flexibility of synthetic β-amyloid peptide
    • Shen, C. L., M. C. Fitzgerald, and R. M. Murphy. 1994. Effect of acid predissolution on fibril size and fibril flexibility of synthetic β-amyloid peptide. Biophys. J. 67:1238-12346.
    • (1994) Biophys. J. , vol.67 , pp. 1238-12346
    • Shen, C.L.1    Fitzgerald, M.C.2    Murphy, R.M.3
  • 67
    • 0029157531 scopus 로고
    • Solvent effects on self-assembly of β-amyloid peptide
    • Shen, C. L., and R. M. Murphy. 1995. Solvent effects on self-assembly of β-amyloid peptide. Biophys. J. 69:640-651.
    • (1995) Biophys. J. , vol.69 , pp. 640-651
    • Shen, C.L.1    Murphy, R.M.2
  • 68
    • 0028917968 scopus 로고
    • Two conformational states of amyloid β-peptide: Implications for the pathogenesis of Alzheimer's disease
    • Soto, C., and B. Frangione. 1995. Two conformational states of amyloid β-peptide: implications for the pathogenesis of Alzheimer's disease. Neurosci. Lett. 186:115-118.
    • (1995) Neurosci. Lett. , vol.186 , pp. 115-118
    • Soto, C.1    Frangione, B.2
  • 69
    • 0033152954 scopus 로고    scopus 로고
    • Expression, purification, and characterization of the recombinant calcium-binding equine lysozyme secreted by the filamentous fungus Aspergillus niger: Comparisons with the production of hen and human lysozymes
    • Spencer, A., L. A. Morozov-Roche, W. Noppe, D. A. MacKenzie, D. J. Jeenes, M. Joniau, C. M. Dobson, and D. B. Archer. 1999. Expression, purification, and characterization of the recombinant calcium-binding equine lysozyme secreted by the filamentous fungus Aspergillus niger: comparisons with the production of hen and human lysozymes. Prot. Exp. Purif. 16:171-180.
    • (1999) Prot. Exp. Purif. , vol.16 , pp. 171-180
    • Spencer, A.1    Morozov-Roche, L.A.2    Noppe, W.3    MacKenzie, D.A.4    Jeenes, D.J.5    Joniau, M.6    Dobson, C.M.7    Archer, D.B.8
  • 72
    • 0032573868 scopus 로고    scopus 로고
    • Carbon nanotube tips: High-resolution probes for imaging biological systems
    • Wong, S. S., J. D. Harper, P. T. Lansbury, and C. M. Lieber. 1998. Carbon nanotube tips: high-resolution probes for imaging biological systems. J. Am. Chem. Soc. 120:603-604.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 603-604
    • Wong, S.S.1    Harper, J.D.2    Lansbury, P.T.3    Lieber, C.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.