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Volumn 38, Issue 1, 2008, Pages 99-110

Effects of oxidation, pH and lipids on amyloidogenic peptide structure: Implications for fibril formation?

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID PROTEIN; APOLIPOPROTEIN C2; METHIONINE; PHOSPHOLIPID; THIOFLAVINE;

EID: 55349140721     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-008-0363-3     Document Type: Article
Times cited : (30)

References (60)
  • 2
    • 33846324298 scopus 로고    scopus 로고
    • The structure of the Alzheimer amyloid beta 10-35 peptide probed through replica-exchange molecular dynamics simulations in explicit solvent
    • 10.1016/j.jmb.2006.11.015
    • A Baumketner J-E Shea 2007 The structure of the Alzheimer amyloid beta 10-35 peptide probed through replica-exchange molecular dynamics simulations in explicit solvent J Mol Biol 366 275 285 10.1016/j.jmb.2006.11.015
    • (2007) J Mol Biol , vol.366 , pp. 275-285
    • Baumketner, A.1    Shea, J.-E.2
  • 3
    • 33748121600 scopus 로고    scopus 로고
    • Folding landscapes of the Alzheimer amyloid-beta(12-28) peptide
    • 10.1016/j.jmb.2006.07.032
    • A Baumketner JE Shea 2006 Folding landscapes of the Alzheimer amyloid-beta(12-28) peptide J Mol Biol 362 567 579 10.1016/j.jmb.2006.07.032
    • (2006) J Mol Biol , vol.362 , pp. 567-579
    • Baumketner, A.1    Shea, J.E.2
  • 5
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • O Berger O Edholm F Jahnig 1997 Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature Biophys J 72 2002 2013
    • (1997) Biophys J , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 6
    • 34548317095 scopus 로고    scopus 로고
    • Oxidation reduces the fibrillation but not the neurotoxicity of the prion peptide PrP106-126
    • 10.1016/j.bbapap.2007.06.016
    • AL Bergstrom J Chabry L Bastholm PMH Heegaard 2007 Oxidation reduces the fibrillation but not the neurotoxicity of the prion peptide PrP106-126 Biochim Biophys Acta Prot Proteomics 1774 1118 1127 10.1016/j.bbapap.2007.06.016
    • (2007) Biochim Biophys Acta Prot Proteomics , vol.1774 , pp. 1118-1127
    • Bergstrom, A.L.1    Chabry, J.2    Bastholm, L.3    Heegaard, P.M.H.4
  • 7
    • 55349130730 scopus 로고    scopus 로고
    • Breaking up amyloid fibrils: Methionine oxidation dissociates preformed amyloid fibrils
    • KJ Binger MD Griffin GJ Howlett 2008 Breaking up amyloid fibrils: methionine oxidation dissociates preformed amyloid fibrils FEBS J 275 442
    • (2008) FEBS J , vol.275 , pp. 442
    • Binger, K.J.1    Griffin, M.D.2    Howlett, G.J.3
  • 8
    • 17844362202 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the aggregation of the core-recognition motif of the islet amylolid polypeptide in explicit water
    • 10.1002/prot.20426
    • G Colombo I Daidone E Gazit A Amadei A Di Nola 2005 Molecular dynamics simulation of the aggregation of the core-recognition motif of the islet amylolid polypeptide in explicit water Proteins 59 519 527 10.1002/prot.20426
    • (2005) Proteins , vol.59 , pp. 519-527
    • Colombo, G.1    Daidone, I.2    Gazit, E.3    Amadei, A.4    Di Nola, A.5
  • 9
    • 17844406143 scopus 로고    scopus 로고
    • Thermodynamic and kinetic characterization of a beta-hairpin peptide in solution: An extended phase space sampling by molecular dynamics simulations in explicit water
    • 10.1002/prot.20427
    • I Daidone A Amadei A Di Nola 2005 Thermodynamic and kinetic characterization of a beta-hairpin peptide in solution: an extended phase space sampling by molecular dynamics simulations in explicit water Proteins 59 510 518 10.1002/prot.20427
    • (2005) Proteins , vol.59 , pp. 510-518
    • Daidone, I.1    Amadei, A.2    Di Nola, A.3
  • 10
    • 4444267407 scopus 로고    scopus 로고
    • Beta-hairpin conformation of fibrillogenic peptides: Structure and alpha-beta transition mechanism revealed by molecular dynamics simulations
    • 10.1002/prot.20178
    • I Daidone F Simona D Roccatano RA Broglia G Tiana G Colombo 2004 beta-hairpin conformation of fibrillogenic peptides: structure and alpha-beta transition mechanism revealed by molecular dynamics simulations Proteins 57 198 204 10.1002/prot.20178
    • (2004) Proteins , vol.57 , pp. 198-204
    • Daidone, I.1    Simona, F.2    Roccatano, D.3    Broglia, R.A.4    Tiana, G.5    Colombo, G.6
  • 11
    • 33846823909 scopus 로고
    • Particle Mesh Ewald-an N.Log(N) method for Ewald sums in large systems
    • 10.1063/1.464397
    • T Darden D York L Pedersen 1993 Particle Mesh Ewald-an N.Log(N) method for Ewald sums in large systems J Chem Phys 98 10089 10092 10.1063/1.464397
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 12
    • 0037102362 scopus 로고    scopus 로고
    • Getting out of shape
    • 10.1038/418729a
    • CM Dobson 2002 Getting out of shape Nature 418 729 730 10.1038/418729a
    • (2002) Nature , vol.418 , pp. 729-730
    • Dobson, C.M.1
  • 13
    • 33749841522 scopus 로고    scopus 로고
    • The aggregation and fibrillation of alpha-synuclein
    • 10.1021/ar050073t
    • AL Fink 2006 The aggregation and fibrillation of alpha-synuclein Acc Chem Res 39 628 634 10.1021/ar050073t
    • (2006) Acc Chem Res , vol.39 , pp. 628-634
    • Fink, A.L.1
  • 14
    • 30344461291 scopus 로고    scopus 로고
    • Misfolding of the amyloid beta-protein: A molecular dynamics study
    • 10.1002/prot.20683
    • D Flock S Colacino G Colombo A Di Nola 2006 Misfolding of the amyloid beta-protein: a molecular dynamics study Proteins 62 183 192 10.1002/prot.20683
    • (2006) Proteins , vol.62 , pp. 183-192
    • Flock, D.1    Colacino, S.2    Colombo, G.3    Di Nola, A.4
  • 15
    • 33751089074 scopus 로고    scopus 로고
    • Aggregation of small peptides studied by molecular dynamics simulations
    • 10.1002/prot.21168
    • D Flock G Rossetti I Daidone A Amadei A Di Nola 2006 Aggregation of small peptides studied by molecular dynamics simulations Proteins 65 914 921 10.1002/prot.21168
    • (2006) Proteins , vol.65 , pp. 914-921
    • Flock, D.1    Rossetti, G.2    Daidone, I.3    Amadei, A.4    Di Nola, A.5
  • 16
    • 34547316314 scopus 로고    scopus 로고
    • Self-assembled peptide nanostructures: The design of molecular building blocks and their technological utilization
    • 10.1039/b605536m
    • E Gazit 2007 Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization Chem Soc Rev 36 1263 1269 10.1039/b605536m
    • (2007) Chem Soc Rev , vol.36 , pp. 1263-1269
    • Gazit, E.1
  • 17
    • 1842611408 scopus 로고    scopus 로고
    • Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using C-13-enhanced Fourier transform infrared spectroscopy
    • 10.1110/ps.03407704
    • LM Gordon PW Mobley W Lee S Eskandari YN Kaznessis MA Sherman 2004 Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using C-13-enhanced Fourier transform infrared spectroscopy Protein Sci 13 1012 1030 10.1110/ps.03407704
    • (2004) Protein Sci , vol.13 , pp. 1012-1030
    • Gordon, L.M.1    Mobley, P.W.2    Lee, W.3    Eskandari, S.4    Kaznessis, Y.N.5    Sherman, M.A.6
  • 18
    • 36348996602 scopus 로고    scopus 로고
    • Phospholipid interaction induces molecular-level polymorphism in apolipoprotein C-II amyloid fibrils via alternative assembly pathways
    • MDW Griffin MLY Mok LM Wilson CLL Pham LJ Waddington MA Perugini 2008 Phospholipid interaction induces molecular-level polymorphism in apolipoprotein C-II amyloid fibrils via alternative assembly pathways J Mol Biol 375 240 256
    • (2008) J Mol Biol , vol.375 , pp. 240-256
    • Griffin, M.D.W.1    Mok, M.L.Y.2    Wilson, L.M.3    Pham, C.L.L.4    Waddington, L.J.5    Perugini, M.A.6
  • 20
    • 33846228438 scopus 로고    scopus 로고
    • Molecular dynamics studies of hexamers of amyloid-beta peptide (16-35) and its mutants: Influence of charge states on amyloid formation
    • 10.1002/prot.21232
    • W Han YD Wu 2007 Molecular dynamics studies of hexamers of amyloid-beta peptide (16-35) and its mutants: influence of charge states on amyloid formation Proteins 66 575 587 10.1002/prot.21232
    • (2007) Proteins , vol.66 , pp. 575-587
    • Han, W.1    Wu, Y.D.2
  • 21
    • 0036520326 scopus 로고    scopus 로고
    • The structural basis for amyloid formation by plasma apolipoproteins: A review
    • DM Hatters GJ Howlett 2002 The structural basis for amyloid formation by plasma apolipoproteins: a review Eur Biophys J Biophys Lett 31 2 8
    • (2002) Eur Biophys J Biophys Lett , vol.31 , pp. 2-8
    • Hatters, D.M.1    Howlett, G.J.2
  • 22
    • 0035853448 scopus 로고    scopus 로고
    • Sub-micellar phospholipid accelerates amyloid formation by apolipoprotein C-II
    • 10.1016/S0014-5793(01)02355-9
    • DM Hatters LJ Lawrence GJ Howlett 2001 Sub-micellar phospholipid accelerates amyloid formation by apolipoprotein C-II FEBS Lett 494 220 224 10.1016/S0014-5793(01)02355-9
    • (2001) FEBS Lett , vol.494 , pp. 220-224
    • Hatters, D.M.1    Lawrence, L.J.2    Howlett, G.J.3
  • 23
    • 0034682559 scopus 로고    scopus 로고
    • Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops
    • 10.1021/bi000002w
    • DM Hatters CE MacPhee LJ Lawrence WH Sawyer GJ Howlett 2000 Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops Biochemistry 39 8276 8283 10.1021/bi000002w
    • (2000) Biochemistry , vol.39 , pp. 8276-8283
    • Hatters, D.M.1    MacPhee, C.E.2    Lawrence, L.J.3    Sawyer, W.H.4    Howlett, G.J.5
  • 24
    • 0037040878 scopus 로고    scopus 로고
    • Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II
    • 10.1074/jbc.M110429200
    • DM Hatters AP Minton GJ Howlett 2002 Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II J Biol Chem 277 7824 7830 10.1074/jbc.M110429200
    • (2002) J Biol Chem , vol.277 , pp. 7824-7830
    • Hatters, D.M.1    Minton, A.P.2    Howlett, G.J.3
  • 25
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • 10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H
    • B Hess H Bekker HJC Berendsen JGEM Fraaije 1997 LINCS: a linear constraint solver for molecular simulations J Comput Chem 18 1463 1472 10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Jgem, F.4
  • 26
    • 0037174835 scopus 로고    scopus 로고
    • Methionine 35 oxidation reduces fibril assembly of the amyloid a beta-(1-42) peptide of Alzheimer's disease
    • 10.1074/jbc.C200338200
    • LM Hou I Kang RE Marchant MG Zagorski 2002 Methionine 35 oxidation reduces fibril assembly of the amyloid A beta-(1-42) peptide of Alzheimer's disease J Biol Chem 277 40173 40176 10.1074/jbc.C200338200
    • (2002) J Biol Chem , vol.277 , pp. 40173-40176
    • Hou, L.M.1    Kang, I.2    Marchant, R.E.3    Zagorski, M.G.4
  • 28
    • 33646155955 scopus 로고    scopus 로고
    • Structure of core domain of fibril-forming PHF/Tau fragments
    • H Inouye D Sharma WJ Goux DA Kirschner 2006 Structure of core domain of fibril-forming PHF/Tau fragments Biophys J 90 1774 1789
    • (2006) Biophys J , vol.90 , pp. 1774-1789
    • Inouye, H.1    Sharma, D.2    Goux, W.J.3    Kirschner, D.A.4
  • 29
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure-pattern-recognition of hydrogen-bonded and geometrical features
    • 10.1002/bip.360221211
    • W Kabsch C Sander 1983 Dictionary of protein secondary structure-pattern-recognition of hydrogen-bonded and geometrical features Biopolymers 22 2577 2637 10.1002/bip.360221211
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 30
    • 34249818803 scopus 로고    scopus 로고
    • Folding of the 25 residue a beta(12-36) peptide in TFE/water: Temperature-dependent transition from a funneled free-energy landscape to a rugged one
    • 10.1021/jp067075v
    • N Kamiya D Mitomo JE Shea J Higo 2007 Folding of the 25 residue A beta(12-36) peptide in TFE/water: temperature-dependent transition from a funneled free-energy landscape to a rugged one J Phys Chem B 111 5351 5356 10.1021/jp067075v
    • (2007) J Phys Chem B , vol.111 , pp. 5351-5356
    • Kamiya, N.1    Mitomo, D.2    Shea, J.E.3    Higo, J.4
  • 31
    • 33845478722 scopus 로고    scopus 로고
    • Exploring atomistic details of pH-dependent peptide folding
    • 10.1073/pnas.0605216103
    • J Khandogin JH Chen CL Brooks 2006 Exploring atomistic details of pH-dependent peptide folding PNAS USA 103 18546 18550 10.1073/pnas.0605216103
    • (2006) PNAS USA , vol.103 , pp. 18546-18550
    • Khandogin, J.1    Chen, J.H.2    Brooks, C.L.3
  • 32
    • 34248352704 scopus 로고    scopus 로고
    • Conformational diversity of the fibrillogenic fusion peptide B18 in different environments from molecular dynamics simulations
    • 10.1021/jp0659204
    • V Knecht H Mohwald R Lipowsky 2007 Conformational diversity of the fibrillogenic fusion peptide B18 in different environments from molecular dynamics simulations J Phys Chem B 111 4161 4170 10.1021/jp0659204
    • (2007) J Phys Chem B , vol.111 , pp. 4161-4170
    • Knecht, V.1    Mohwald, H.2    Lipowsky, R.3
  • 33
    • 34848871860 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fibrillogenic peptide derived from apolipoprotein C-II
    • 10.1016/j.bpc.2007.08.002
    • ES Legge H Treutlein GJ Howlett I Yarovsky 2007 Molecular dynamics simulations of a fibrillogenic peptide derived from apolipoprotein C-II Biophys Chem 130 102 113 10.1016/j.bpc.2007.08.002
    • (2007) Biophys Chem , vol.130 , pp. 102-113
    • Legge, E.S.1    Treutlein, H.2    Howlett, G.J.3    Yarovsky, I.4
  • 34
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • E Lindahl B Hess D van der Spoel 2001 GROMACS 3.0: a package for molecular simulation and trajectory analysis J Mol Model 7 306 317
    • (2001) J Mol Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 35
    • 33645396508 scopus 로고    scopus 로고
    • All-atom molecular dynamics studies of the full-length beta-amyloid peptides
    • 10.1016/j.chemphys.2005.08.071
    • E Luttmann G Fels 2006 All-atom molecular dynamics studies of the full-length beta-amyloid peptides Chem Phys 323 138 147 10.1016/j.chemphys.2005. 08.071
    • (2006) Chem Phys , vol.323 , pp. 138-147
    • Luttmann, E.1    Fels, G.2
  • 36
    • 0037195098 scopus 로고    scopus 로고
    • Stabilities and conformations of Alzheimer's beta-amyloid peptide oligomers (A beta(16-22') a beta(16-35 ') and a beta(10-35)): Sequence effects
    • 10.1073/pnas.212206899
    • BY Ma R Nussinov 2002 Stabilities and conformations of Alzheimer's beta-amyloid peptide oligomers (A beta(16-22') A beta(16-35 ') and A beta(10-35)): sequence effects PNAS USA 99 14126 14131 10.1073/pnas.212206899
    • (2002) PNAS USA , vol.99 , pp. 14126-14131
    • Ma, B.Y.1    Nussinov, R.2
  • 37
    • 0035826625 scopus 로고    scopus 로고
    • NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate
    • 10.1021/bi002821m
    • CA MacRaild DM Hatters GJ Howlett PR Gooley 2001 NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate Biochemistry 40 5414 5421 10.1021/bi002821m
    • (2001) Biochemistry , vol.40 , pp. 5414-5421
    • MacRaild, C.A.1    Hatters, D.M.2    Howlett, G.J.3    Gooley, P.R.4
  • 38
    • 3042655091 scopus 로고    scopus 로고
    • The structure and interactions of human apolipoprotein C-II in dodecyl phosphocholine
    • 10.1021/bi049817l
    • CA MacRaild GJ Howlett PR Gooley 2004 The structure and interactions of human apolipoprotein C-II in dodecyl phosphocholine Biochemistry 43 8084 8093 10.1021/bi049817l
    • (2004) Biochemistry , vol.43 , pp. 8084-8093
    • MacRaild, C.A.1    Howlett, G.J.2    Gooley, P.R.3
  • 39
    • 0037199994 scopus 로고    scopus 로고
    • Regulated expression of the apolipoprotein E/C-I/C-IV/C-II gene cluster in murine and human macrophages-a critical role for nuclear liver X receptors alpha and beta
    • 10.1074/jbc.M202993200
    • PA Mak BA Laffitte C Desrumaux SB Joseph LK Curtiss DJ Mangelsdorf 2002 Regulated expression of the apolipoprotein E/C-I/C-IV/C-II gene cluster in murine and human macrophages-a critical role for nuclear liver X receptors alpha and beta J Biol Chem 277 31900 31908 10.1074/jbc.M202993200
    • (2002) J Biol Chem , vol.277 , pp. 31900-31908
    • Mak, P.A.1    Laffitte, B.A.2    Desrumaux, C.3    Joseph, S.B.4    Curtiss, L.K.5    Mangelsdorf, D.J.6
  • 40
    • 12244285938 scopus 로고    scopus 로고
    • Molecular basis for amyloid fibril formation and stability
    • 10.1073/pnas.0406847102
    • OS Makin E Atkins P Sikorski J Johansson LC Serpell 2005 Molecular basis for amyloid fibril formation and stability PNAS USA 102 315 320 10.1073/pnas.0406847102
    • (2005) PNAS USA , vol.102 , pp. 315-320
    • Makin, O.S.1    Atkins, E.2    Sikorski, P.3    Johansson, J.4    Serpell, L.C.5
  • 41
    • 33751112217 scopus 로고    scopus 로고
    • Oxidation inhibits amyloid fibril formation of transthyretin
    • 10.1111/j.1742-4658.2006.05532.x
    • SD Maleknia N Reixach JN Buxbaum 2006 Oxidation inhibits amyloid fibril formation of transthyretin FEBS J 273 5400 5406 10.1111/j.1742-4658.2006.05532.x
    • (2006) FEBS J , vol.273 , pp. 5400-5406
    • Maleknia, S.D.1    Reixach, N.2    Buxbaum, J.N.3
  • 42
    • 33748447891 scopus 로고    scopus 로고
    • Amyloid formation may involve alpha- to beta sheet interconversion via peptide plane flipping
    • 10.1016/j.str.2006.06.016
    • EJ Milner-White JD Watson GY Qi S Hayward 2006 Amyloid formation may involve alpha- to beta sheet interconversion via peptide plane flipping Structure 14 1369 1376 10.1016/j.str.2006.06.016
    • (2006) Structure , vol.14 , pp. 1369-1376
    • Milner-White, E.J.1    Watson, J.D.2    Qi, G.Y.3    Hayward, S.4
  • 43
    • 0842307662 scopus 로고    scopus 로고
    • Structural diversity of amyloid fibril formed in human calcitonin as revealed by site-directed C-13 solid-state NMR spectroscopy
    • 10.1002/mrc.1323
    • A Naito M Kamihira R Inoue H Saito 2004 Structural diversity of amyloid fibril formed in human calcitonin as revealed by site-directed C-13 solid-state NMR spectroscopy Magn Reson Chem 42 247 257 10.1002/mrc.1323
    • (2004) Magn Reson Chem , vol.42 , pp. 247-257
    • Naito, A.1    Kamihira, M.2    Inoue, R.3    Saito, H.4
  • 44
    • 33645995764 scopus 로고    scopus 로고
    • Recent atomic models of amyloid fibril structure
    • 10.1016/j.sbi.2006.03.007
    • R Nelson D Eisenberg 2006 Recent atomic models of amyloid fibril structure Curr Opin Struct Biol 16 260 265 10.1016/j.sbi.2006.03.007
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 260-265
    • Nelson, R.1    Eisenberg, D.2
  • 45
    • 25844438392 scopus 로고    scopus 로고
    • Structures of a peptide fragment of beta(2)-microglobulin studied by replica-exchange molecular dynamics simulations-towards the understanding of the mechanism of amyloid formation
    • 10.1016/j.febslet.2005.08.068
    • M Nishino Y Sugita T Yoda Y Okamoto 2005 Structures of a peptide fragment of beta(2)-microglobulin studied by replica-exchange molecular dynamics simulations-towards the understanding of the mechanism of amyloid formation FEBS Lett 579 5425 5429 10.1016/j.febslet.2005.08.068
    • (2005) FEBS Lett , vol.579 , pp. 5425-5429
    • Nishino, M.1    Sugita, Y.2    Yoda, T.3    Okamoto, Y.4
  • 46
    • 0037205434 scopus 로고    scopus 로고
    • Oxidation of methionine 35 attenuates formation of amyloid beta-peptide 1-40 oligomers
    • 10.1074/jbc.M112218200
    • M Palmblad A Westlind-Danielsson J Bergquist 2002 Oxidation of methionine 35 attenuates formation of amyloid beta-peptide 1-40 oligomers J Biol Chem 277 19506 19510 10.1074/jbc.M112218200
    • (2002) J Biol Chem , vol.277 , pp. 19506-19510
    • Palmblad, M.1    Westlind-Danielsson, A.2    Bergquist, J.3
  • 47
    • 33846352795 scopus 로고    scopus 로고
    • Serpin acceleration of amyloid fibril formation: A role for accessory proteins
    • 10.1016/j.jmb.2006.11.062
    • GA Powers CLL Pham MC Pearce GJ Howlett SP Bottomley 2007 Serpin acceleration of amyloid fibril formation: a role for accessory proteins J Mol Biol 366 666 676 10.1016/j.jmb.2006.11.062
    • (2007) J Mol Biol , vol.366 , pp. 666-676
    • Powers, G.A.1    Pham, C.L.L.2    Pearce, M.C.3    Howlett, G.J.4    Bottomley, S.P.5
  • 48
    • 23344437452 scopus 로고    scopus 로고
    • Self-assembly of peptide nanotubes and amyloid-like structures by charged-termini-capped diphenylalanine peptide analogues
    • 10.1560/5MC0-V3DX-KE0B-YF3J
    • M Reches E Gazit 2005 Self-assembly of peptide nanotubes and amyloid-like structures by charged-termini-capped diphenylalanine peptide analogues Isr J Chem 45 363 371 10.1560/5MC0-V3DX-KE0B-YF3J
    • (2005) Isr J Chem , vol.45 , pp. 363-371
    • Reches, M.1    Gazit, E.2
  • 49
    • 2442494894 scopus 로고    scopus 로고
    • Helix H1 of the prion protein is rather stable against environmental perturbations: Molecular dynamics of mutation and deletion variants of PrP(90-231)
    • 10.1007/s00018-003-3455-3
    • S Santini P Derreumaux 2004 Helix H1 of the prion protein is rather stable against environmental perturbations: molecular dynamics of mutation and deletion variants of PrP(90-231) Cell Mol Life Sci 61 951 960 10.1007/s00018-003-3455-3
    • (2004) Cell Mol Life Sci , vol.61 , pp. 951-960
    • Santini, S.1    Derreumaux, P.2
  • 50
    • 0035037143 scopus 로고    scopus 로고
    • A proposed structural model for amyloid fibril elongation: Domain swapping forms an interdigitating beta-structure polymer
    • 10.1093/protein/14.2.93
    • N Sinha CJ Tsai R Nussinov 2001 A proposed structural model for amyloid fibril elongation: domain swapping forms an interdigitating beta-structure polymer Protein Eng 14 93 103 10.1093/protein/14.2.93
    • (2001) Protein Eng , vol.14 , pp. 93-103
    • Sinha, N.1    Tsai, C.J.2    Nussinov, R.3
  • 51
    • 34948863450 scopus 로고    scopus 로고
    • Serum amyloid P colocalizes with apolipoproteins in human atheroma: Functional implications
    • 10.1194/jlr.M700098-JLR200
    • CR Stewart A Haw R Lopez TO McDonald JM Callaghan MJ McConville 2007 Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implications J Lipid Res 48 2162 2171 10.1194/jlr.M700098-JLR200
    • (2007) J Lipid Res , vol.48 , pp. 2162-2171
    • Stewart, C.R.1    Haw, A.2    Lopez, R.3    McDonald, T.O.4    Callaghan, J.M.5    McConville, M.J.6
  • 52
    • 33845570428 scopus 로고    scopus 로고
    • Dynamics of Asp23-Lys28 salt-bridge formation in a beta(10-35) monomers
    • 10.1021/ja064872y
    • B Tarus JE Straub D Thirumalai 2006 Dynamics of Asp23-Lys28 salt-bridge formation in A beta(10-35) monomers J Am Chem Soc 128 16159 16168 10.1021/ja064872y
    • (2006) J Am Chem Soc , vol.128 , pp. 16159-16168
    • Tarus, B.1    Straub, J.E.2    Thirumalai, D.3
  • 53
    • 33646145955 scopus 로고    scopus 로고
    • PK values of the ionizable groups of proteins
    • 10.1110/ps.051840806
    • RL Thurlkill GR Grimsley JM Scholtz CN Pace 2006 pK values of the ionizable groups of proteins Protein Sci 15 1214 1218 10.1110/ps.051840806
    • (2006) Protein Sci , vol.15 , pp. 1214-1218
    • Thurlkill, R.L.1    Grimsley, G.R.2    Scholtz, J.M.3    Pace, C.N.4
  • 54
    • 32344451179 scopus 로고    scopus 로고
    • The alpha-to-beta conformational transition of Alzheimer's a beta-(1-42) peptide in aqueous media is reversible: A step by step conformational analysis suggests the location of beta conformation seeding
    • 10.1002/cbic.200500223
    • S Tomaselli V Esposito P Vangone NAJ van Nuland AMJJ Bonvin R Guerrini 2006 The alpha-to-beta conformational transition of Alzheimer's A beta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding ChemBioChem 7 257 267 10.1002/cbic.200500223
    • (2006) ChemBioChem , vol.7 , pp. 257-267
    • Tomaselli, S.1    Esposito, V.2    Vangone, P.3    Van Nuland, N.A.J.4    Amjj, B.5    Guerrini, R.6
  • 55
    • 39849100708 scopus 로고    scopus 로고
    • Molecular dynamics study to investigate the effect of chemical substitutions of methionine 35 on the secondary structure of the amyloid beta (A beta(1-42)) monomer in aqueous solution
    • 10.1021/jp0771872
    • L Triguero R Singh R Prabhakar 2008 Molecular dynamics study to investigate the effect of chemical substitutions of methionine 35 on the secondary structure of the amyloid beta (A beta(1-42)) monomer in aqueous solution J Phys Chem B 112 2159 2167 10.1021/jp0771872
    • (2008) J Phys Chem B , vol.112 , pp. 2159-2167
    • Triguero, L.1    Singh, R.2    Prabhakar, R.3
  • 57
    • 33748473035 scopus 로고    scopus 로고
    • Effects of solvent on the structure of the Alzheimer amyloid-beta(25-35) peptide
    • 10.1529/biophysj.105.079186
    • GH Wei JE Shea 2006 Effects of solvent on the structure of the Alzheimer amyloid-beta(25-35) peptide Biophys J 91 1638 1647 10.1529/biophysj.105.079186
    • (2006) Biophys J , vol.91 , pp. 1638-1647
    • Wei, G.H.1    Shea, J.E.2
  • 58
    • 33846847762 scopus 로고    scopus 로고
    • A structural core within apolipoprotein C-II amyloid fibrils identified using hydrogen exchange and proteolysis
    • 10.1016/j.jmb.2006.12.040
    • LM Wilson YF Mok KJ Binger MDW Griffin HDT Mertens F Lin 2007 A structural core within apolipoprotein C-II amyloid fibrils identified using hydrogen exchange and proteolysis J Mol Biol 366 1639 1651 10.1016/j.jmb.2006. 12.040
    • (2007) J Mol Biol , vol.366 , pp. 1639-1651
    • Wilson, L.M.1    Mok, Y.F.2    Binger, K.J.3    Griffin, M.D.W.4    Mertens, H.D.T.5    Lin, F.6
  • 59
    • 22144448838 scopus 로고    scopus 로고
    • The role of Phe in the formation of well-ordered oligomers of amyloidogenic hexapeptide (NFGAIL) observed in molecular dynamics simulations with explicit solvent
    • 10.1529/biophysj.104.055574
    • C Wu HX Lei Y Duan 2005 The role of Phe in the formation of well-ordered oligomers of amyloidogenic hexapeptide (NFGAIL) observed in molecular dynamics simulations with explicit solvent Biophys J 88 2897 2906 10.1529/biophysj.104. 055574
    • (2005) Biophys J , vol.88 , pp. 2897-2906
    • Wu, C.1    Lei, H.X.2    Duan, Y.3
  • 60
    • 0037465469 scopus 로고    scopus 로고
    • Global structure and dynamics of human apolipoprotein CII in complex with micelles: Evidence for increased mobility of the helix involved in the activation of lipoprotein lipase
    • 10.1021/bi0267184
    • J Zdunek GV Martinez J Schleucher PO Lycksell Y Yin S Nilsson 2003 Global structure and dynamics of human apolipoprotein CII in complex with micelles: evidence for increased mobility of the helix involved in the activation of lipoprotein lipase Biochemistry 42 1872 1889 10.1021/bi0267184
    • (2003) Biochemistry , vol.42 , pp. 1872-1889
    • Zdunek, J.1    Martinez, G.V.2    Schleucher, J.3    Lycksell, P.O.4    Yin, Y.5    Nilsson, S.6


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