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Volumn 16, Issue 5, 2010, Pages 1011-1020

Effect of pathogenic mutations on the structure and dynamics of Alzheimer's Aβ42-amyloid oligomers

Author keywords

Energetic analysis; Fibrillation; Glutamate 22; Molecular dynamics; Oligomerisation; Protein interaction

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; OLIGOMER; AMYLOID; AMYLOID PRECURSOR PROTEIN; CELL SURFACE RECEPTOR; PROTEASE NEXINS;

EID: 77953944835     PISSN: 16102940     EISSN: 09485023     Source Type: Journal    
DOI: 10.1007/s00894-009-0611-1     Document Type: Article
Times cited : (30)

References (52)
  • 1
    • 0000293742 scopus 로고
    • Über eine eigenartige Erkrankung der Hirnrinde
    • Alzheimer A (1907) Über eine eigenartige Erkrankung der Hirnrinde. Allg Z Psychiat Psych-Gerichtl Med 64:146-148.
    • (1907) Allg Z Psychiat Psych-Gerichtl Med , vol.64 , pp. 146-148
    • Alzheimer, A.1
  • 3
    • 0019440757 scopus 로고
    • Regional pattern of degeneration in Alzheimer's disease: neuronal loss and histopathological grading
    • Brun A, Englund E (1981) Regional pattern of degeneration in Alzheimer's disease: neuronal loss and histopathological grading. Histopathology 5:549-564.
    • (1981) Histopathology , vol.5 , pp. 549-564
    • Brun, A.1    Englund, E.2
  • 4
    • 0035168927 scopus 로고    scopus 로고
    • Pathologic correlates of nondemented aging, mild cognitive impairment, and early-stage Alzheimer's disease
    • Morris JC, Price AL (2001) Pathologic correlates of nondemented aging, mild cognitive impairment, and early-stage Alzheimer's disease. J Mol Neurosci 17:101-118.
    • (2001) J Mol Neurosci , vol.17 , pp. 101-118
    • Morris, J.C.1    Price, A.L.2
  • 8
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils
    • Petkova AT, Yau WM, Tycko R (2006) Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry 45:498-512.
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 10
    • 33748689799 scopus 로고    scopus 로고
    • Simulations as analytical tools to understand protein aggregation and predict amyloid conformation
    • Ma B, Nussinov R (2006) Simulations as analytical tools to understand protein aggregation and predict amyloid conformation. Curr Opin Chem Biol 10:445-452.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 445-452
    • Ma, B.1    Nussinov, R.2
  • 12
    • 44049099816 scopus 로고    scopus 로고
    • Protofibril assemblies of the arctic, Dutch, and Flemish mutants of the Alzheimer's Abeta1-40 peptide
    • Fawzi NL, Kohlstedt KL, Okabe Y, Head-Gordon T (2008) Protofibril assemblies of the arctic, Dutch, and Flemish mutants of the Alzheimer's Abeta1-40 peptide. Biophys J 94:2007-2016.
    • (2008) Biophys J , vol.94 , pp. 2007-2016
    • Fawzi, N.L.1    Kohlstedt, K.L.2    Okabe, Y.3    Head-Gordon, T.4
  • 13
    • 36148983867 scopus 로고    scopus 로고
    • Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities
    • Zheng J, Jang H, Ma B, Tsai CJ, Nussinov R (2007) Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities. Biophys J 93:3046-3057.
    • (2007) Biophys J , vol.93 , pp. 3046-3057
    • Zheng, J.1    Jang, H.2    Ma, B.3    Tsai, C.J.4    Nussinov, R.5
  • 14
    • 42649088020 scopus 로고    scopus 로고
    • Molecular dynamics simulations of Alzheimer Abeta40 elongation and lateral association
    • Zheng J, Ma B, Chang Y, Nussinov R (2008) Molecular dynamics simulations of Alzheimer Abeta40 elongation and lateral association. Front Biosci 13:3919-3930.
    • (2008) Front Biosci , vol.13 , pp. 3919-3930
    • Zheng, J.1    Ma, B.2    Chang, Y.3    Nussinov, R.4
  • 15
    • 46749113483 scopus 로고    scopus 로고
    • Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42
    • Zheng J, Jang H, Ma B, Nussinov R (2008) Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42. J Phys Chem B 112:6856-6865.
    • (2008) J Phys Chem B , vol.112 , pp. 6856-6865
    • Zheng, J.1    Jang, H.2    Ma, B.3    Nussinov, R.4
  • 16
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe DJ (1991) The molecular pathology of Alzheimer's disease. Neuron 6:487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 17
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 19
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8:101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 20
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 267-298.
    • (2003) Annu Rev Neurosci , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 21
    • 0242580170 scopus 로고    scopus 로고
    • Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease
    • Murakami K, Irie K, Morimoto A, Ohigashi H, ShindoM, NagaoM, Shimizu T, Shirasawa T (2003) Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease. J Biol Chem 278:46179-46187.
    • (2003) J Biol Chem , vol.278 , pp. 46179-46187
    • Murakami, K.1    Irie, K.2    Morimoto, A.3    Ohigashi, H.4    Shindo, M.5    Nagao, M.6    Shimizu, T.7    Shirasawa, T.8
  • 24
    • 41749084194 scopus 로고    scopus 로고
    • Amyloid-beta E22Delta variant induces synaptic alteration in mouse hippocampal slices
    • Takuma H, Teraoka R, Mori H, Tomiyama T (2008) Amyloid-beta E22Delta variant induces synaptic alteration in mouse hippocampal slices. NeuroReport 19:615-619.
    • (2008) NeuroReport , vol.19 , pp. 615-619
    • Takuma, H.1    Teraoka, R.2    Mori, H.3    Tomiyama, T.4
  • 26
    • 33644851439 scopus 로고    scopus 로고
    • The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy
    • Olofsson A, Sauer-Eriksson AE, Ohman A (2006) The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy. J Biol Chem 281:477-483.
    • (2006) J Biol Chem , vol.281 , pp. 477-483
    • Olofsson, A.1    Sauer-Eriksson, A.E.2    Ohman, A.3
  • 27
    • 58149376285 scopus 로고    scopus 로고
    • Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance
    • Olofsson A, Sauer-Eriksson AE, Ohman A (2009) Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance. Anal Biochem 385:374-376.
    • (2009) Anal Biochem , vol.385 , pp. 374-376
    • Olofsson, A.1    Sauer-Eriksson, A.E.2    Ohman, A.3
  • 28
    • 77954761465 scopus 로고
    • St. Louis, MO
    • Tripos (1991-2008) Sybyl7.3. St. Louis, MO.
    • (1991) Sybyl7.3
    • Tripos1
  • 31
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, Simmerling C (2006) Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 65:712-725.
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 33
    • 0032922174 scopus 로고    scopus 로고
    • A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat
    • Cheatham TE 3rd, Cieplak P, Kollman PA (1999) A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat. J Biomol Struct Dyn 16:845-862.
    • (1999) J Biomol Struct Dyn , vol.16 , pp. 845-862
    • Cheatham III, T.E.1    Cieplak, P.2    Kollman, P.A.3
  • 34
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang J, Cieplak P, Kollman PA (2000) How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J Comput Chem 21:1049-1074.
    • (2000) J Comput Chem , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 36
    • 33846823909 scopus 로고
    • Particle Mesh Ewald. An N.log(N) method for Ewald sums in large systems
    • Darden TA, York DM, Pedersen LG (1993) Particle Mesh Ewald. An N.log(N) method for Ewald sums in large systems. J Chem Phys 98:10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.A.1    York, D.M.2    Pedersen, L.G.3
  • 38
    • 36649006642 scopus 로고    scopus 로고
    • Clustering molecular dynamics trajectories: 1. Characterizing the performance of different clustering altorithms
    • Shao J, Tanner SW, Thompson N, Cheatham TE III (2007) Clustering molecular dynamics trajectories: 1. Characterizing the performance of different clustering altorithms. J Chem Theory Comput 3:2312-2334.
    • (2007) J Chem Theory Comput , vol.3 , pp. 2312-2334
    • Shao, J.1    Tanner, S.W.2    Thompson, N.3    Cheatham III, T.E.4
  • 40
    • 0029878720 scopus 로고    scopus 로고
    • VMD: visual molecular dynamics
    • Humphrey W, Dalke A, Schulten K (1996) VMD: visual molecular dynamics. J Mol Graph 14(33-38):27-38.
    • (1996) J Mol Graph , vol.14 , Issue.33-38 , pp. 27-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 41
    • 77954761348 scopus 로고    scopus 로고
    • Suite 6.0. San Diego, CA
    • Accelrys (2005) DS ViewerPro Suite 6.0. San Diego, CA.
    • (2005) DS ViewerPro
    • Accelrys1
  • 43
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic sovent models
    • Sitkoff D, Sharp K, Honig B (1994) Accurate calculation of hydration free energies using macroscopic sovent models. J Phys Chem 98:1978-1988.
    • (1994) J Phys Chem , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.2    Honig, B.3
  • 44
    • 0033568644 scopus 로고    scopus 로고
    • Computational alanine scanning to probe protein-protein interactions: A novel approach to evaluate binding free energies
    • DOI 10.1021/ja990935j
    • Massova I, Kollmann PA (1999) Computational Alanine scanning to probe protein-protein interactions: a novel approach to evaluate binding free energies. J Am Chem Soc 121:8133-8143. (Pubitemid 29444447)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.36 , pp. 8133-8143
    • Massova, I.1    Kollman, P.A.2
  • 45
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R (2005) Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307:262-265.
    • (2005) Science , vol.307 , 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
  • 46
    • 26944437967 scopus 로고    scopus 로고
    • Small non-fibrillar assemblies of amyloid beta-protein bearing the Arctic mutation induce rapid neuritic degeneration
    • Whalen BM, Selkoe DJ, Hartley DM (2005) Small non-fibrillar assemblies of amyloid beta-protein bearing the Arctic mutation induce rapid neuritic degeneration. Neurobiol Dis 20:254-266.
    • (2005) Neurobiol Dis , vol.20 , pp. 254-266
    • Whalen, B.M.1    Selkoe, D.J.2    Hartley, D.M.3
  • 47
    • 0034282630 scopus 로고    scopus 로고
    • Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells
    • Miravalle L, Tokuda T, Chiarle R, Giaccone G, Bugiani O, Tagliavini F, Frangione B, Ghiso J (2000) Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells. J Biol Chem 275:27110-27116.
    • (2000) J Biol Chem , vol.275 , pp. 27110-27116
    • Miravalle, L.1    Tokuda, T.2    Chiarle, R.3    Giaccone, G.4    Bugiani, O.5    Tagliavini, F.6    Frangione, B.7    Ghiso, J.8
  • 50
    • 2342652177 scopus 로고    scopus 로고
    • Unique physicochemical profile of beta-amyloid peptide variant Abeta1-40E22G protofibrils: conceivable neuropathogen in arctic mutant carriers
    • Päiviö A, Jarvet J, Graslund A, Lannfelt L, Westlind-Danielsson A (2004) Unique physicochemical profile of beta-amyloid peptide variant Abeta1-40E22G protofibrils: conceivable neuropathogen in arctic mutant carriers. J Mol Biol 339:145-159.
    • (2004) J Mol Biol , vol.339 , pp. 145-159
    • Päiviö, A.1    Jarvet, J.2    Graslund, A.3    Lannfelt, L.4    Westlind-Danielsson, A.5
  • 51
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: insights from solid-state NMR
    • Tycko R (2006) Molecular structure of amyloid fibrils: insights from solid-state NMR. Q Rev Biophys 39:1-55.
    • (2006) Q Rev Biophys , vol.39 , pp. 1-55
    • Tycko, R.1
  • 52
    • 0034660205 scopus 로고    scopus 로고
    • Toxicity of various amyloid beta peptide species in cultured human blood-brain barrier endothelial cells: increased toxicity of dutch-type mutant
    • Eisenhauer PB, Johnson RJ, Wells JM, Davies TA, Fine RE (2000) Toxicity of various amyloid beta peptide species in cultured human blood-brain barrier endothelial cells: increased toxicity of dutch-type mutant. J Neurosci Res 60:804-810.
    • (2000) J Neurosci Res , vol.60 , pp. 804-810
    • Eisenhauer, P.B.1    Johnson, R.J.2    Wells, J.M.3    Davies, T.A.4    Fine, R.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.