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Volumn 38, Issue 8, 2009, Pages 1135-1140

Dehydration stability of amyloid fibrils studied by AFM

Author keywords

AFM; Aggregation; Amyloid; Peptide; Protein

Indexed keywords

AMYLOID; POLYPEPTIDE;

EID: 70349682422     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-009-0526-x     Document Type: Article
Times cited : (26)

References (32)
  • 1
    • 0842307665 scopus 로고    scopus 로고
    • Amyloidosis of Alzheimer's Aβ peptides: Solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies
    • DOI 10.1002/mrc.1341
    • O Antzutkin 2004 Amyloidosis of alzheimer's a beta peptides: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies Magn Reson Chem 42 2 231 246 14745804 10.1002/mrc.1341 1:CAS:528:DC%2BD2cXhtFKhtrc%3D (Pubitemid 38178093)
    • (2004) Magnetic Resonance in Chemistry , vol.42 , Issue.2 , pp. 231-246
    • Antzutkin, O.N.1
  • 2
    • 23444450012 scopus 로고    scopus 로고
    • Fine structure study of a beta(1-42) fibrillogenesis with atomic force microscopy
    • 15919759 1:CAS:528:DC%2BD2MXntlaqsLY%3D
    • M Arimon I Diez-Perez M Kogan N Durany E Giralt F Sanz X Fernandez-Busquets 2005 Fine structure study of a beta(1-42) fibrillogenesis with atomic force microscopy FASEB J 19 7 1344 1346 15919759 1:CAS:528:DC%2BD2MXntlaqsLY%3D
    • (2005) FASEB J , vol.19 , Issue.7 , pp. 1344-1346
    • Arimon, M.1    Diez-Perez, I.2    Kogan, M.3    Durany, N.4    Giralt, E.5    Sanz, F.6    Fernandez-Busquets, X.7
  • 3
    • 0024413349 scopus 로고
    • Localization of islet amyloid peptide in lipofuscin bodies and secretory granules of human b-cells and in islets of type-2 diabetic subjects
    • 2546670 10.1007/BF00221649 1:CAS:528:DyaL1MXltlWhtLY%3D
    • A Clark C Edwards L Ostle R Sutton J Rothbard J Morris R Turner 1989 Localization of islet amyloid peptide in lipofuscin bodies and secretory granules of human b-cells and in islets of type-2 diabetic subjects Cell Tissue Res 257 1 179 185 2546670 10.1007/BF00221649 1:CAS:528:DyaL1MXltlWhtLY%3D
    • (1989) Cell Tissue Res , vol.257 , Issue.1 , pp. 179-185
    • Clark, A.1    Edwards, C.2    Ostle, L.3    Sutton, R.4    Rothbard, J.5    Morris, J.6    Turner, R.7
  • 4
    • 0022435132 scopus 로고
    • Image-reconstruction of the alzheimer paired helical filament
    • 2419127 1:STN:280:DyaL287js1Sjuw%3D%3D
    • R Crowther C Wischik 1985 Image-reconstruction of the alzheimer paired helical filament EMBO J 4 13B 3661 3665 2419127 1:STN:280:DyaL287js1Sjuw%3D%3D
    • (1985) EMBO J , vol.4 , pp. 3661-3665
    • Crowther, R.1    Wischik, C.2
  • 6
    • 33644813233 scopus 로고    scopus 로고
    • A native to amyloidogenic transition regulated by a backbone trigger
    • DOI 10.1038/nsmb1068, PII N1068
    • C Eakin A Berman A Miranker 2006 A native to amyloidogenic transition regulated by a backbone trigger Nat Struct Mol Biol 13 3 202 208 16491088 10.1038/nsmb1068 1:CAS:528:DC%2BD28XhvFOltrw%3D (Pubitemid 43348505)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.3 , pp. 202-208
    • Eakin, C.M.1    Berman, A.J.2    Miranker, A.D.3
  • 10
    • 0033534397 scopus 로고    scopus 로고
    • Watching amyloid fibrils grow by time-lapse atomic force microscopy
    • DOI 10.1006/jmbi.1998.2299
    • C Goldsbury J Kistler U Aebi T Arvinte G Cooper 1999 Watching amyloid fibrils grow by time-lapse atomic force microscopy J Mol Biol 285 1 33 39 9878384 10.1006/jmbi.1998.2299 1:CAS:528:DyaK1MXntFCksw%3D%3D (Pubitemid 29034022)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.1 , pp. 33-39
    • Goldsbury, C.1    Kistler, J.2    Aebi, U.3    Arvinte, T.4    Cooper, G.J.S.5
  • 12
    • 24044507958 scopus 로고    scopus 로고
    • Multiple assembly pathways underlie amyloid-β fibril polymorphisms
    • DOI 10.1016/j.jmb.2005.07.029, PII S002228360500817X
    • C Goldsbury P Frey V Olivieri U Aebi S Muller 2005 Multiple assembly pathways underlie amyloid-beta fibril polymorphisms J Mol Biol 352 2 282 298 16095615 10.1016/j.jmb.2005.07.029 1:CAS:528:DC%2BD2MXpslyltrk%3D (Pubitemid 41213315)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.2 , pp. 282-298
    • Goldsbury, C.1    Frey, P.2    Olivieri, V.3    Aebi, U.4    Muller, S.A.5
  • 13
    • 23444445907 scopus 로고    scopus 로고
    • 2-microglobulin into amyloid
    • DOI 10.1016/j.jmb.2005.06.040, PII S0022283605007023
    • W Gosal I Morten E Hewitt D Smith N Thomson S Radford 2005 Competing pathways determine fibril morphology in the self-assembly of beta(2)-microglobulin into amyloid J Mol Biol 351 4 850 864 16024039 10.1016/j.jmb.2005.06.040 1:CAS:528:DC%2BD2MXntVGmt7g%3D (Pubitemid 41111901)
    • (2005) Journal of Molecular Biology , vol.351 , Issue.4 , pp. 850-864
    • Gosal, W.S.1    Morten, I.J.2    Hewitt, E.W.3    Smith, D.A.4    Thomson, N.H.5    Radford, S.E.6
  • 14
    • 0034677739 scopus 로고    scopus 로고
    • Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils
    • DOI 10.1016/S0014-5793(00)01287-4, PII S0014579300012874
    • C Higham E Jaikaran P Fraser M Gross A Clark 2000 Preparation of synthetic human islet amyloid polypeptide (iapp) in a stable conformation to enable study of conversion to amyloid-like fibrils FEBS Lett 470 1 55 60 10722845 10.1016/S0014-5793(00)01287-4 1:CAS:528:DC%2BD3cXhslalt7w%3D (Pubitemid 30155623)
    • (2000) FEBS Letters , vol.470 , Issue.1 , pp. 55-60
    • Higham, C.E.1    Jaikaran, E.T.A.S.2    Fraser, P.E.3    Gross, M.4    Clark, A.5
  • 15
    • 9144267018 scopus 로고    scopus 로고
    • Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling
    • DOI 10.1074/jbc.M406853200
    • S Jayasinghe R Langen 2004 Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling J Biol Chem 279 46 48,420 48,425 10.1074/jbc.M406853200 1:CAS:528:DC%2BD2cXptl2msrc%3D (Pubitemid 39540999)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 48420-48425
    • Jayasinghe, S.A.1    Langen, R.2
  • 16
    • 33645148331 scopus 로고    scopus 로고
    • Oriented sols for fiber diffraction from limited quantities or hazardous materials
    • 10.1107/S0021889805033455 1:CAS:528:DC%2BD28XmvVOqsg%3D%3D
    • A Kendall G Stubbs 2006 Oriented sols for fiber diffraction from limited quantities or hazardous materials J Appl Crystallogr 39 Part 1 39 41 10.1107/S0021889805033455 1:CAS:528:DC%2BD28XmvVOqsg%3D%3D
    • (2006) J Appl Crystallogr , vol.39 , Issue.PART 1 , pp. 39-41
    • Kendall, A.1    Stubbs, G.2
  • 18
    • 0036669903 scopus 로고    scopus 로고
    • Examining the structure of the mature amyloid fibril
    • 12196128 1:CAS:528:DC%2BD38XntVent7w%3D
    • O Makin L Serpell 2002 Examining the structure of the mature amyloid fibril Biochem Soc Trans 30 Part 4 521 525 12196128 1:CAS:528: DC%2BD38XntVent7w%3D
    • (2002) Biochem Soc Trans , vol.30 , Issue.PART 4 , pp. 521-525
    • Makin, O.1    Serpell, L.2
  • 19
    • 0347284249 scopus 로고    scopus 로고
    • Structural Characterisation of Islet Amyloid Polypeptide Fibrils
    • DOI 10.1016/j.jmb.2003.11.048
    • O Makin L Serpell 2004 Structural characterisation of islet amyloid polypeptide fibrils J Mol Biol 335 5 1279 1288 10.1016/j.jmb.2003.11.048 (Pubitemid 38077245)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.5 , pp. 1279-1288
    • Makin, O.S.1    Serpell, L.C.2
  • 20
    • 33748520925 scopus 로고    scopus 로고
    • Diffraction to study protein and peptide assemblies
    • DOI 10.1016/j.cbpa.2006.08.009, PII S1367593106001153, Analytical Techniques/Mechanisms
    • OS Makin P Sikorski LC Serpell 2006 Diffraction to study protein and peptide assemblies Curr Opin Chem Biol 10 5 417 422 16931111 10.1016/j.cbpa.2006.08.009 1:CAS:528:DC%2BD28Xps1Oltbs%3D (Pubitemid 44375062)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 417-422
    • Makin, O.S.1    Sikorski, P.2    Serpell, L.C.3
  • 21
    • 38349164999 scopus 로고    scopus 로고
    • Enclosed chambers for humidity control and sample containment in fiber diffraction
    • 10.1107/S0021889807060803 1:CAS:528:DC%2BD1cXmvFymsg%3D%3D
    • M McDonald A Kendalla M Tanaka JS Weissman G Stubbs 2008 Enclosed chambers for humidity control and sample containment in fiber diffraction J Appl Crystallogr 41 206 209 10.1107/S0021889807060803 1:CAS:528: DC%2BD1cXmvFymsg%3D%3D
    • (2008) J Appl Crystallogr , vol.41 , pp. 206-209
    • McDonald, M.1    Kendalla, A.2    Tanaka, M.3    Weissman, J.S.4    Stubbs, G.5
  • 22
    • 34347234780 scopus 로고    scopus 로고
    • Morphology and mechanical stability of amyloid-like peptide fibrils
    • DOI 10.1007/s10856-006-0075-0, Special Section: Selected Papers from the EUROMAT 2005 Conference, Prague, September 2005
    • P Mesquida CK Riener CE MacPhee RA McKendry 2007 Morphology and mechanical stability of amyloid-like peptide fibrils J Mater Sci Mater Med 18 7 1325 1331 17221316 10.1007/s10856-006-0075-0 1:CAS:528:DC%2BD2sXmvFSmu7k%3D (Pubitemid 46999018)
    • (2007) Journal of Materials Science: Materials in Medicine , vol.18 , Issue.7 , pp. 1325-1331
    • Mesquida, P.1    Riener, C.K.2    MacPhee, C.E.3    McKendry, R.A.4
  • 23
    • 0347949620 scopus 로고    scopus 로고
    • Characterization by atomic force microscopy of Alzheimer paired helical filaments under physiological conditions
    • 14695296 10.1016/S0006-3495(04)74130-2 1:CAS:528:DC%2BD2cXlsV2ktg%3D%3D
    • F Moreno-Herrero M Perez A Baro J Avila 2004 Characterization by atomic force microscopy of Alzheimer paired helical filaments under physiological conditions Biophys J 86 1, Part 1 517 525 14695296 10.1016/S0006-3495(04)74130-2 1:CAS:528:DC%2BD2cXlsV2ktg%3D%3D
    • (2004) Biophys J , vol.86 , Issue.PART 1 , pp. 517-525
    • Moreno-Herrero, F.1    Perez, M.2    Baro, A.3    Avila, J.4
  • 24
    • 11844249291 scopus 로고    scopus 로고
    • Rapid assembly of amyloid-β peptide at a liquid/liquid interface produces unstable β-sheet fibers
    • DOI 10.1021/bi048846t
    • M Nichols M Moss D Reed J Hoh T Rosenberry 2005 Rapid assembly of amyloid-beta peptide at a liquid/liquid interface produces unstable beta-sheet fibers Biochemistry 44 1 165 173 15628857 10.1021/bi048846t 1:CAS:528: DC%2BD2cXhtVGktrzO (Pubitemid 40095718)
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 165-173
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Hoh, J.H.4    Rosenberry, T.L.5
  • 26
    • 0033977086 scopus 로고    scopus 로고
    • Amyloid fibrillogenesis: Themes and variations
    • DOI 10.1016/S0959-440X(99)00049-4
    • J Rochet P Lansbury 2000 Amyloid fibrillogenesis: themes and variations Curr Opin Struct Biol 10 1 60 68 10679462 10.1016/S0959-440X(99)00049-4 1:CAS:528:DC%2BD3cXhs1Sltrc%3D (Pubitemid 30099328)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.1 , pp. 60-68
    • Rochet, J.-C.1    Lansbury Jr., P.T.2
  • 28
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimers-disease
    • 1673054 10.1016/0896-6273(91)90052-2 1:CAS:528:DyaK3MXltlartrk%3D
    • D Selkoe 1991 The molecular pathology of Alzheimers-disease Neuron 6 4 487 498 1673054 10.1016/0896-6273(91)90052-2 1:CAS:528:DyaK3MXltlartrk%3D
    • (1991) Neuron , vol.6 , Issue.4 , pp. 487-498
    • Selkoe, D.1
  • 29
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • 1:CAS:528:DC%2BD3cXkvFSgtb4%3D
    • L Serpell 2000 Alzheimer's amyloid fibrils: structure and assembly Biochim Biophys Acta Mol Basis Dis 1502 1 16 30 1:CAS:528:DC%2BD3cXkvFSgtb4%3D
    • (2000) Biochim Biophys Acta Mol Basis Dis , vol.1502 , Issue.1 , pp. 16-30
    • Serpell, L.1
  • 31
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • DOI 10.1006/jmbi.1997.1348
    • M Sunde L Serpell M Bartlam P Fraser M Pepys C Blake 1997 Common core structure of amyloid fibrils by synchrotron x-ray diffraction J Mol Biol 273 3 729 739 9356260 10.1006/jmbi.1997.1348 1:CAS:528:DyaK2sXnslGgurY%3D (Pubitemid 27488813)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.3 , pp. 729-739
    • Sunde, M.1    Serpell, L.C.2    Bartlam, M.3    Fraser, P.E.4    Pepys, M.B.5    Blake, C.C.F.6
  • 32
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • DOI 10.1016/j.sbi.2003.12.002
    • R Tycko 2004 Progress towards a molecular-level structural understanding of amyloid fibrils Curr Opin Struct Biol 14 1 96 103 15102455 10.1016/j.sbi.2003.12.002 1:CAS:528:DC%2BD2cXhsFWqsrg%3D (Pubitemid 38249598)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.1 , pp. 96-103
    • Tycko, R.1


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