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Volumn 36, Issue 4, 2011, Pages 679-689

Aggregation properties of a short peptide that mediates amyloid fibril formation in model proteins unrelated to disease

Author keywords

Amyloid fibrils; atomic force microscopy; non fibrillar structures; peptide self association; SH3 domain

Indexed keywords

AMYLOID; AMYLOID PROTEIN; ASPARTYLISOLEUCYLASPARTYLLEUCYLHISDITYLLEUCINE CARBOXYLAMIDE; ASPARTYLISOLEUCYLASPARTYLLEUCYLHISDITYLLEUCINE CARBOXYLIC ACID; MICA; PEPTIDE; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 80054979271     PISSN: 02505991     EISSN: 09737138     Source Type: Journal    
DOI: 10.1007/s12038-011-9104-3     Document Type: Article
Times cited : (8)

References (54)
  • 1
    • 33646093028 scopus 로고    scopus 로고
    • Polymorphism and ultrastructural organization of prion protein amyloid fibrils: An insight from high resolution atomic force microscopy
    • 16519898 10.1016/j.jmb.2006.02.007 1:CAS:528:DC%2BD28XjvVamtb0%3D
    • M Anderson OV Bocharova N Makarava L Breydo VV Salnikov IV Baskakov 2006 Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy J. Mol. Biol. 358 580 596 16519898 10.1016/j.jmb.2006.02.007 1:CAS:528:DC%2BD28XjvVamtb0%3D
    • (2006) J. Mol. Biol. , vol.358 , pp. 580-596
    • Anderson, M.1    Bocharova, O.V.2    Makarava, N.3    Breydo, L.4    Salnikov, V.V.5    Baskakov, I.V.6
  • 3
    • 0028800177 scopus 로고
    • Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin
    • 7577226 10.1006/jsbi.1995.1024 1:CAS:528:DyaK2MXpt1ykurs%3D
    • HH Bauer U Aebi M Haner R Hermann M Muller HP Merkle 1995 Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin J Struct Biol 115 1 15 7577226 10.1006/jsbi.1995.1024 1:CAS:528:DyaK2MXpt1ykurs%3D
    • (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
    • 0034685621 scopus 로고    scopus 로고
    • In-situ atomic force microscopy study of beta-amyloid fibrillization
    • 10801352 10.1006/jmbi.2000.3711 1:CAS:528:DC%2BD3cXivFGjtL0%3D
    • HK Blackley GH Sanders MC Davies CJ Roberts SJ Tendler MJ Wilkinson 2000 In-situ atomic force microscopy study of beta-amyloid fibrillization J. Mol. Biol. 298 833 840 10801352 10.1006/jmbi.2000.3711 1:CAS:528:DC%2BD3cXivFGjtL0%3D
    • (2000) J. Mol. Biol. , vol.298 , pp. 833-840
    • Blackley, H.K.1    Sanders, G.H.2    Davies, M.C.3    Roberts, C.J.4    Tendler, S.J.5    Wilkinson, M.J.6
  • 5
    • 0026595567 scopus 로고
    • Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs
    • 1730616 1:CAS:528:DyaK38XjvFSmtA%3D%3D
    • D Burdick B Soreghan M Kwon J Kosmoski M Knauer A Henschen J Yates C Cotman, et al. 1992 Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs J. Biol. Chem. 267 546 554 1730616 1:CAS:528:DyaK38XjvFSmtA%3D%3D
    • (1992) J. Biol. Chem. , vol.267 , pp. 546-554
    • Burdick, D.1    Soreghan, B.2    Kwon, M.3    Kosmoski, J.4    Knauer, M.5    Henschen, A.6    Yates, J.7    Cotman, C.8
  • 6
    • 60849117286 scopus 로고    scopus 로고
    • Organic solvent mediated self-association of an amyloid forming peptide from beta2-microglobulin: An atomic force microscopy study
    • 18798577 10.1002/bip.21087 1:CAS:528:DC%2BD1cXhsV2qtL3P
    • N Chaudhary S Singh R Nagaraj 2008 Organic solvent mediated self-association of an amyloid forming peptide from beta2-microglobulin: an atomic force microscopy study Biopolymers 90 783 791 18798577 10.1002/bip.21087 1:CAS:528:DC%2BD1cXhsV2qtL3P
    • (2008) Biopolymers , vol.90 , pp. 783-791
    • Chaudhary, N.1    Singh, S.2    Nagaraj, R.3
  • 7
    • 70449721154 scopus 로고    scopus 로고
    • Morphology of self-assembled structures formed by short peptides from the amyloidogenic protein tau depends on the solvent in which the peptides are dissolved
    • 19714684 10.1002/psc.1172 1:CAS:528:DC%2BD1MXhtFSnsbbE
    • N Chaudhary S Singh R Nagaraj 2009 Morphology of self-assembled structures formed by short peptides from the amyloidogenic protein tau depends on the solvent in which the peptides are dissolved J. Pept. Sci. 15 675 684 19714684 10.1002/psc.1172 1:CAS:528:DC%2BD1MXhtFSnsbbE
    • (2009) J. Pept. Sci. , vol.15 , pp. 675-684
    • Chaudhary, N.1    Singh, S.2    Nagaraj, R.3
  • 8
    • 0344875516 scopus 로고    scopus 로고
    • 2-microglobulin
    • DOI 10.1074/jbc.M304473200
    • T Chiba Y Hagihara T Higurashi K Hasegawa H Naiki Y Goto 2003 Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of beta2-microglobulin J. Biol. Chem. 278 47016 47024 12958308 10.1074/jbc.M304473200 1:CAS:528:DC%2BD3sXovFKktrc%3D (Pubitemid 37452285)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 47016-47024
    • Chiba, T.1    Hagihara, Y.2    Higurashi, T.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 9
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin. Even an ordinary globular protein can assume a rogue guise if conditions are right
    • DOI 10.1038/35065514
    • M Fandrich MA Fletcher CM Dobson 2001 Amyloid fibrils from muscle myoglobin Nature (London) 410 165 166 10.1038/35065514 1:CAS:528: DC%2BD3MXitVyktb4%3D (Pubitemid 32216577)
    • (2001) Nature , vol.410 , Issue.6825 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 11
    • 0033669788 scopus 로고    scopus 로고
    • A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils
    • 11101888 10.1038/81937 1:CAS:528:DC%2BD3cXovVahsLo%3D
    • Y Fezoui DM Hartley DM Walsh DJ Selkoe JJ Osterhout DB Teplow 2000 A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils Nat. Struct. Biol. 7 1095 1099 11101888 10.1038/81937 1:CAS:528:DC%2BD3cXovVahsLo%3D
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1095-1099
    • Fezoui, Y.1    Hartley, D.M.2    Walsh, D.M.3    Selkoe, D.J.4    Osterhout, J.J.5    Teplow, D.B.6
  • 12
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly
    • 11060312 10.1074/jbc.M008919200 1:CAS:528:DC%2BD3MXhtVGjsrw%3D
    • BI Giasson IV Murray JQ Trojanowski VM Lee 2001 A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly J. Biol. Chem. 276 2380 2386 11060312 10.1074/jbc.M008919200 1:CAS:528:DC%2BD3MXhtVGjsrw%3D
    • (2001) J. Biol. Chem. , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 13
    • 33644536691 scopus 로고    scopus 로고
    • Atomic-level description of amyloid beta-dimer formation
    • 16478138 10.1021/ja0548337 1:CAS:528:DC%2BD28XoslGrug%3D%3D
    • S Gnanakaran R Nussinov AE Garcia 2006 Atomic-level description of amyloid beta-dimer formation J. Am. Chem. Soc. 128 2158 2159 16478138 10.1021/ja0548337 1:CAS:528:DC%2BD28XoslGrug%3D%3D
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2158-2159
    • Gnanakaran, S.1    Nussinov, R.2    Garcia, A.E.3
  • 14
    • 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 SA Muller 2005 Multiple assembly pathways underlie amyloid-beta fibril polymorphisms J. Mol. Biol. 352 282 298 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
  • 15
    • 0035802949 scopus 로고    scopus 로고
    • Nanotube formation by hydrophobic dipeptides
    • Gorbitz CH 2001 Nanotube formation by hydrophobic dipeptides. Chemistry - Eur. J. 7 5153-5159
    • (2001) Chemistry - Eur. J. , vol.7 , pp. 5153-5159
    • Gorbitz, C.H.1
  • 18
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • 7540054 10.1002/bip.360370404 1:CAS:528:DyaK2MXlvFarurg%3D
    • PI Haris D Chapman 1995 The conformational analysis of peptides using Fourier transform IR spectroscopy Biopolymers 37 251 263 7540054 10.1002/bip.360370404 1:CAS:528:DyaK2MXlvFarurg%3D
    • (1995) Biopolymers , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 19
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of Aβ amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
    • DOI 10.1021/bi9904149
    • JD Harper SS Wong CM Lieber PT Lansbury Jr 1999 Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease Biochemistry 38 8972 8980 10413470 10.1021/bi9904149 1:CAS:528:DyaK1MXjsl2jtLo%3D (Pubitemid 29334658)
    • (1999) Biochemistry , vol.38 , Issue.28 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury Jr., P.T.4
  • 20
    • 0035933540 scopus 로고    scopus 로고
    • Amyloid-like fibrils from an 18-residue peptide analogue of a part of the central domain of the B-family of silkmoth chorion proteins
    • DOI 10.1016/S0014-5793(01)02510-8, PII S0014579301025108
    • Iconomidou VA, Chryssikos GD, Gionis V, Vriend G, Hoenger A and Hamodrakas SJ 2001 Amyloid-like fibrils from an 18-residue peptide analogue of a part of the central domain of the B-family of silkmoth chorion proteins. FEBS Lett. 499 268-273 (Pubitemid 32553877)
    • (2001) FEBS Letters , vol.499 , Issue.3 , pp. 268-273
    • Iconomidou, V.A.1    Chryssikos, G.D.2    Gionis, V.3    Vriend, G.4    Hoenger, A.5    Hamodrakas, S.J.6
  • 21
    • 0034683126 scopus 로고    scopus 로고
    • Amyloids protect the silkmoth oocyte and embryo
    • DOI 10.1016/S0014-5793(00)01888-3, PII S0014579300018883
    • Iconomidou VA, Vriend G and Hamodrakas SJ 2000 Amyloids protect the silkmoth oocyte and embryo. FEBS Lett. 479 141-145 (Pubitemid 30616422)
    • (2000) FEBS Letters , vol.479 , Issue.3 , pp. 141-145
    • Iconomidou, V.A.1    Vriend, G.2    Hamodrakas, S.J.3
  • 23
    • 33645240208 scopus 로고    scopus 로고
    • A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments
    • Ivanova MI, Thompson MJ and Eisenberg D 2006 A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments. Proc. Natl. Acad. Sci. USA 103 4079-4082
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4079-4082
    • Ivanova, M.I.1    Thompson, M.J.2    Eisenberg, D.3
  • 24
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • 7656562 10.3109/10409239509085140 1:CAS:528:DyaK2MXlvFGnsrw%3D
    • M Jackson HH Mantsch 1995 The use and misuse of FTIR spectroscopy in the determination of protein structure Crit. Rev. Biochem. Mol. Biol. 30 95 120 7656562 10.3109/10409239509085140 1:CAS:528:DyaK2MXlvFGnsrw%3D
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 25
    • 17144426174 scopus 로고    scopus 로고
    • Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy
    • DOI 10.1529/biophysj.104.048843
    • R Jansen W Dzwolak R Winter 2005 Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy Biophys. J. 88 1344 1353 15574704 10.1529/biophysj.104.048843 1:CAS:528:DC%2BD2MXhtlyjtL0%3D (Pubitemid 40975961)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 1344-1353
    • Jansen, R.1    Dzwolak, W.2    Winter, R.3
  • 26
    • 0027296226 scopus 로고
    • X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin
    • DOI 10.1006/bbrc.1993.1514
    • JA Jarvis DJ Craik MC Wilce 1993 X-ray diffraction studies of fibrils formed from peptide fragments of transthyretin Biochem. Biophys. Res. Commun. 192 991 998 8507211 10.1006/bbrc.1993.1514 1:CAS:528:DyaK3sXkvV2gsbo%3D (Pubitemid 23218512)
    • (1993) Biochemical and Biophysical Research Communications , vol.192 , Issue.3 , pp. 991-998
    • Jarvis, J.A.1    Craik, D.J.2    Wilce, M.C.J.3
  • 27
    • 0037227173 scopus 로고    scopus 로고
    • 2-microglobulin - Insights into the mechanism of fibril formation in vitro
    • DOI 10.1016/S0022-2836(02)01227-5
    • S Jones J Manning NM Kad SE Radford 2003 Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro J. Mol. Biol. 325 249 257 12488093 10.1016/S0022-2836(02)01227-5 1:CAS:528:DC%2BD38XpsFyitLY%3D (Pubitemid 36062686)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.2 , pp. 249-257
    • Jones, S.1    Manning, J.2    Kad, N.M.3    Radford, S.E.4
  • 28
    • 0035955555 scopus 로고    scopus 로고
    • 2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro
    • DOI 10.1006/jmbi.2001.5071
    • NM Kad NH Thomson DP Smith DA Smith SE Radford 2001 Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro J. Mol. Biol. 313 559 571 11676539 10.1006/jmbi.2001.5071 1:CAS:528:DC%2BD3MXnslCrtrw%3D (Pubitemid 33052287)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.3 , pp. 559-571
    • Kad, N.M.1    Thomson, N.H.2    Smith, D.P.3    Smith, D.A.4    Radford, S.E.5
  • 31
    • 0034646562 scopus 로고    scopus 로고
    • Similarities between the spectrin SH3 domain denatured state and its folding transition state
    • 10764585 10.1006/jmbi.2000.3618 1:CAS:528:DC%2BD3cXitl2rtb0%3D
    • T Kortemme MJ Kelly LE Kay J Forman-Kay L Serrano 2000 Similarities between the spectrin SH3 domain denatured state and its folding transition state J. Mol. Biol. 297 1217 1229 10764585 10.1006/jmbi.2000.3618 1:CAS:528:DC%2BD3cXitl2rtb0%3D
    • (2000) J. Mol. Biol. , vol.297 , pp. 1217-1229
    • Kortemme, T.1    Kelly, M.J.2    Kay, L.E.3    Forman-Kay, J.4    Serrano, L.5
  • 32
    • 0037059764 scopus 로고    scopus 로고
    • 2-microglobulin by Achromobacter protease I
    • DOI 10.1074/jbc.M108753200
    • GV Kozhukh Y Hagihara T Kawakami K Hasegawa H Naiki Y Goto 2002 Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I J. Biol. Chem. 277 1310 1315 11687582 10.1074/jbc.M108753200 1:CAS:528:DC%2BD38XnvFOrsw%3D%3D (Pubitemid 34968884)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 1310-1315
    • Kozhukh, G.V.1    Hagihara, Y.2    Kawakami, T.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 34
    • 33749464823 scopus 로고    scopus 로고
    • β-amyloid fibril formation is promoted by step edges of highly oriented pyrolytic graphite
    • DOI 10.1002/bip.20549
    • D Losic LL Martin MI Aguilar DH Small 2006 Beta-amyloid fibril formation is promoted by step edges of highly oriented pyrolytic graphite Biopolymers 84 519 526 16752395 10.1002/bip.20549 1:CAS:528:DC%2BD28XhtVChur%2FN (Pubitemid 44519211)
    • (2006) Biopolymers - Peptide Science Section , vol.84 , Issue.5 , pp. 519-526
    • Losic, D.1    Martin, L.L.2    Aguilar, M.-I.3    Small, D.H.4
  • 35
    • 30744477442 scopus 로고    scopus 로고
    • A single mutation induces amyloid aggregation in the α-spectrin SH3 domain: Analysis of the early stages of fibril formation
    • DOI 10.1016/j.jmb.2005.11.062, PII S0022283605014658
    • B Morel S Casares F Conejero-Lara 2006 A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation J. Mol. Biol. 356 453 468 16375922 10.1016/j.jmb.2005.11.062 1:CAS:528:DC%2BD28XmsFWrtw%3D%3D (Pubitemid 43099983)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.2 , pp. 453-468
    • Morel, B.1    Casares, S.2    Conejero-Lara, F.3
  • 36
    • 33744831968 scopus 로고    scopus 로고
    • Polymorphic fibril formation by residues 10-40 of the Alzheimer's β-amyloid peptide
    • DOI 10.1529/biophysj.105.076927
    • AK Paravastu AT Petkova R Tycko 2006 Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide Biophys. J. 90 4618 4629 16565054 10.1529/biophysj.105.076927 1:CAS:528:DC%2BD28XlvVaksb8%3D (Pubitemid 43830905)
    • (2006) Biophysical Journal , vol.90 , Issue.12 , pp. 4618-4629
    • Paravastu, A.K.1    Petkova, A.T.2    Tycko, R.3
  • 37
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • DOI 10.1126/science.1105850
    • AT Petkova RD Leapman Z Guo WM Yau MP Mattson R Tycko 2005 Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils Science 307 262 265 15653506 10.1126/science.1105850 1:CAS:528:DC%2BD2MXisVKksA%3D%3D (Pubitemid 40116242)
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 38
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide nanotubes
    • DOI 10.1126/science.1082387
    • M Reches E Gazit 2003 Casting metal nanowires within discrete self-assembled peptide nanotubes Science 300 625 627 12714741 10.1126/science.1082387 1:CAS:528:DC%2BD3sXjtVymurk%3D (Pubitemid 36520583)
    • (2003) Science , vol.300 , Issue.5619 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 39
    • 33645522802 scopus 로고    scopus 로고
    • Designed aromatic homo-dipeptides: Formation of ordered nanostructures and potential nanotechnological applications
    • 16582461 10.1088/1478-3975/3/1/S02 1:CAS:528:DC%2BD28XjvVChtLY%3D
    • M Reches E Gazit 2006 Designed aromatic homo-dipeptides: formation of ordered nanostructures and potential nanotechnological applications Phys. Biol. 3 S10 19 16582461 10.1088/1478-3975/3/1/S02 1:CAS:528:DC%2BD28XjvVChtLY%3D
    • (2006) Phys. Biol. , vol.3 , pp. 10-19
    • Reches, M.1    Gazit, E.2
  • 40
    • 0037144424 scopus 로고    scopus 로고
    • Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin
    • 12095997 10.1074/jbc.M206039200 1:CAS:528:DC%2BD38Xnt1WmtL0%3D
    • M Reches Y Porat E Gazit 2002 Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin J. Biol. Chem. 277 35475 35480 12095997 10.1074/jbc.M206039200 1:CAS:528:DC%2BD38Xnt1WmtL0%3D
    • (2002) J. Biol. Chem. , vol.277 , pp. 35475-35480
    • Reches, M.1    Porat, Y.2    Gazit, E.3
  • 41
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • DOI 10.1021/bi00053a001
    • WK Surewicz HH Mantsch D Chapman 1993 Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment Biochemistry 32 389 394 8422346 10.1021/bi00053a001 1:CAS:528: DyaK3sXjsFahtQ%3D%3D (Pubitemid 23034873)
    • (1993) Biochemistry , vol.32 , Issue.2 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 42
    • 0034723150 scopus 로고    scopus 로고
    • Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties
    • 10656810 10.1006/jmbi.1999.3422 1:CAS:528:DC%2BD3cXotlSjtA%3D%3D
    • K Tenidis M Waldner J Bernhagen W Fischle M Bergmann M Weber ML Merkle W Voelter, et al. 2000 Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties J. Mol. Biol. 295 1055 1071 10656810 10.1006/jmbi.1999.3422 1:CAS:528:DC%2BD3cXotlSjtA%3D%3D
    • (2000) J. Mol. Biol. , vol.295 , pp. 1055-1071
    • Tenidis, K.1    Waldner, M.2    Bernhagen, J.3    Fischle, W.4    Bergmann, M.5    Weber, M.6    Merkle, M.L.7    Voelter, W.8
  • 43
    • 0034667586 scopus 로고    scopus 로고
    • Amyloidogenicity and neurotoxicity of peptides corresponding to the helical regions of PrP(C)
    • 11020222 10.1002/1097-4547(20001015)62:2<293::AID-JNR14>3.0.CO;2-Y 1:CAS:528:DC%2BD3cXns1aqur8%3D
    • A Thompson AR White C McLean CL Masters R Cappai CJ Barrow 2000 Amyloidogenicity and neurotoxicity of peptides corresponding to the helical regions of PrP(C) J. Neurosci. Res. 62 293 301 11020222 10.1002/1097- 4547(20001015)62:2<293::AID-JNR14>3.0.CO;2-Y 1:CAS:528: DC%2BD3cXns1aqur8%3D
    • (2000) J. Neurosci. Res. , vol.62 , pp. 293-301
    • Thompson, A.1    White, A.R.2    McLean, C.3    Masters, C.L.4    Cappai, R.5    Barrow, C.J.6
  • 45
    • 0037044732 scopus 로고    scopus 로고
    • Charge attraction and β propensity are necessary for amyloid fibril formation from tetrapeptides
    • DOI 10.1074/jbc.M205570200
    • L Tjernberg W Hosia N Bark J Thyberg J Johansson 2002 Charge attraction and beta propensity are necessary for amyloid fibril formation from tetrapeptides J. Biol. Chem. 277 43243 43246 12215440 10.1074/jbc.M205570200 1:CAS:528:DC%2BD38Xos1ems7g%3D (Pubitemid 35285710)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 43243-43246
    • Tjernberg, L.1    Hosia, W.2    Bark, N.3    Thyberg, J.4    Johansson, J.5
  • 46
    • 10844254749 scopus 로고    scopus 로고
    • Role of aromatic interactions in amyloid formation by peptides derived from human amylin
    • DOI 10.1021/bi048812l
    • SM Tracz A Abedini M Driscoll DP Raleigh 2004 Role of aromatic interactions in amyloid formation by peptides derived from human Amylin Biochemistry 43 15901 15908 15595845 10.1021/bi048812l 1:CAS:528: DC%2BD2cXpvVGhu7c%3D (Pubitemid 39665089)
    • (2004) Biochemistry , vol.43 , Issue.50 , pp. 15901-15908
    • Tracz, S.M.1    Abedini, A.2    Driscoll, M.3    Raleigh, D.P.4
  • 49
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure
    • M von Bergen S Barghorn L Li A Marx J Biernat EM Mandelkow E Mandelkow 2001 Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure J. Biol. Chem. 276 48165 48174
    • (2001) J. Biol. Chem. , vol.276 , pp. 48165-48174
    • Von Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 51
    • 0001479670 scopus 로고
    • A simple ultraviolet spectrophotometric method for the determination of protein
    • 13346201 1:CAS:528:DyaG2sXitlSq
    • WJ Waddell 1956 A simple ultraviolet spectrophotometric method for the determination of protein J. Lab. Clin. Med. 48 311 314 13346201 1:CAS:528:DyaG2sXitlSq
    • (1956) J. Lab. Clin. Med. , vol.48 , pp. 311-314
    • Waddell, W.J.1
  • 52
    • 0021103515 scopus 로고
    • A critical reappraisal of Waddell's technique for ultraviolet spectrophotometric protein estimation
    • Wolf P 1983 A critical reappraisal of Waddell's technique for ultraviolet spectrophotometric protein estimation. Anal Biochem. 129 145-155
    • (1983) Anal Biochem. , vol.129 , pp. 145-155
    • Wolf, P.1
  • 53
    • 24644447303 scopus 로고    scopus 로고
    • Seeding-dependent propagation and maturation of amyloid fibril conformation
    • DOI 10.1016/j.jmb.2005.07.061, PII S0022283605008740
    • K Yamaguchi S Takahashi T Kawai H Naiki Y Goto 2005 Seeding-dependent propagation and maturation of amyloid fibril conformation J. Mol. Biol. 352 952 960 16126222 10.1016/j.jmb.2005.07.061 1:CAS:528:DC%2BD2MXhtVWit7nL (Pubitemid 41267080)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.4 , pp. 952-960
    • Yamaguchi, K.-I.1    Takahashi, S.2    Kawai, T.3    Naiki, H.4    Goto, Y.5


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