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Volumn 47, Issue 3, 2015, Pages 583-593

Studies of Polymorphism of Amyloid-β42 Peptide from Different Suppliers

Author keywords

Alzheimer's disease; amyloid fibril; A 42 peptide; electron microscopy; mass spectroscopy; oligomer; prion like behavior; protofibril

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN[1-42]; PROTEIN AGGREGATE; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT; PRION; RECOMBINANT PROTEIN;

EID: 84938699749     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-150147     Document Type: Article
Times cited : (30)

References (35)
  • 1
    • 33444474195 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms underlying synaptic degeneration and neuronal death in Alzheimers disease
    • Mattson MP, ed. Humana Press, Totowa, NJ
    • Mattson MP (2001) Cellular and molecular mechanisms underlying synaptic degeneration and neuronal death in Alzheimers disease. In Pathogenesis of Neurodegenerative Disorders, Mattson MP, ed. Humana Press, Totowa, NJ, pp. 113-138.
    • (2001) Pathogenesis of Neurodegenerative Disorders , pp. 113-138
    • Mattson, M.P.1
  • 2
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M, Blake C (1997) The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv Protein Chem 50, 123-159.
    • (1997) Adv Protein Chem , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 4
    • 0021256895 scopus 로고
    • Alzheimers disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW (1984) Alzheimers disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120, 885-890.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 5
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimers disease
    • Hardy J, Allsop D (1991) Amyloid deposition as the central event in the aetiology of Alzheimers disease. Trends Pharmacol Sci 12, 383-388.
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 7
    • 34249862316 scopus 로고    scopus 로고
    • The role of tau phosphorylation and cleavage in neuronal cell death
    • Chun W, Johnson GVW (2007) The role of tau phosphorylation and cleavage in neuronal cell death. Front Biosci J Virtual Libr 12, 733-756.
    • (2007) Front Biosci J Virtual Libr , vol.12 , pp. 733-756
    • Chun, W.1    Gvw, J.2
  • 9
    • 84877581156 scopus 로고    scopus 로고
    • Novel mechanistic insight into the molecular basis of amyloid polymorphism and secondary nucleation during amyloid formation
    • Jeong JS, Ansaloni A, Mezzenga R, Lashuel HA, Dietler G (2013) Novel mechanistic insight into the molecular basis of amyloid polymorphism and secondary nucleation during amyloid formation. J Mol Biol 425, 1765-1781.
    • (2013) J Mol Biol , vol.425 , pp. 1765-1781
    • Jeong, J.S.1    Ansaloni, A.2    Mezzenga, R.3    Lashuel, H.A.4    Dietler, G.5
  • 11
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: The examples of Alzheimers and Parkinsons diseases
    • Selkoe DJ (2004) Cell biology of protein misfolding: The examples of Alzheimers and Parkinsons diseases. Nat Cell Biol 6, 1054-1061.
    • (2004) Nat Cell Biol , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 12
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloidbeta peptides differentially affect neuronal viability
    • Dahlgren KN, Manelli AM, Stine WB, Baker LK, Krafft GA, LaDu MJ (2002) Oligomeric and fibrillar species of amyloidbeta peptides differentially affect neuronal viability. J Biol Chem 277, 32046-32053.
    • (2002) J Biol Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.3    Baker, L.K.4    Krafft, G.A.5    LaDu, M.J.6
  • 13
    • 0030611858 scopus 로고    scopus 로고
    • Soluble amyloid Abeta-(1-40) exists as a stable dimer at low concentrations
    • Garzon-Rodriguez W, Sepulveda-Becerra M, Milton S, Glabe CG (1997) Soluble amyloid Abeta-(1-40) exists as a stable dimer at low concentrations. J Biol Chem 272, 21037-21044.
    • (1997) J Biol Chem , vol.272 , pp. 21037-21044
    • Garzon-Rodriguez, W.1    Sepulveda-Becerra, M.2    Milton, S.3    Glabe, C.G.4
  • 14
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of A beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimers disease
    • Harper JD, Wong SS, Lieber CM, Lansbury PT (1999) Assembly of A beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimers disease. Biochemistry (Mosc) 38, 8972-8980.
    • (1999) Biochemistry (Mosc) , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 17
    • 0027195933 scopus 로고
    • Seeding one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimers disease and scrapie?
    • Jarrett JT, Lansbury PT (1993) Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimers disease and scrapie? Cell 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 18
    • 24044518189 scopus 로고    scopus 로고
    • Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism
    • Carrotta R, Manno M, Bulone D, Martorana V, San Biagio PL (2005) Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism. J Biol Chem 280, 30001-30008.
    • (2005) J Biol Chem , vol.280 , pp. 30001-30008
    • Carrotta, R.1    Manno, M.2    Bulone, D.3    Martorana, V.4    San Biagio, P.L.5
  • 19
    • 61849148857 scopus 로고    scopus 로고
    • Mechanism of zinc (II) -promoted amyloid formation: Zinc (II) binding facilitates the transition from the partially alpha-helical conformer to aggregates of amyloid beta protein (1-28)
    • Talmard C, Leuma Yona R, Faller P (2009) Mechanism of zinc (II) -promoted amyloid formation: zinc (II) binding facilitates the transition from the partially alpha-helical conformer to aggregates of amyloid beta protein (1-28) . J Biol Inorg Chem 14, 449-455.
    • (2009) J Biol Inorg Chem , vol.14 , pp. 449-455
    • Talmard, C.1    Leuma Yona, R.2    Faller, P.3
  • 21
    • 14944344493 scopus 로고    scopus 로고
    • Targeting amyloid-degrading enzymes as therapeutic strategies in neurodegeneration
    • Turner AJ, Fisk L, Nalivaeva NN (2004) Targeting amyloid-degrading enzymes as therapeutic strategies in neurodegeneration. Ann N Y Acad Sci 1035, 1-20.
    • (2004) Ann N y Acad Sci , vol.1035 , pp. 1-20
    • Turner, A.J.1    Fisk, L.2    Nalivaeva, N.N.3
  • 24
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, Hayer-Hartl M (2009) Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 16, 574-581.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 25
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg AL (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 26
    • 84893833627 scopus 로고    scopus 로고
    • How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. I. Modeling the amyloid protofibril formation
    • Dovidchenko NV, Finkelstein AV, Galzitskaya OV (2014) How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. I. Modeling the amyloid protofibril formation. J Phys Chem B 118, 1189-1197.
    • (2014) J Phys Chem B , vol.118 , pp. 1189-1197
    • Dovidchenko, N.V.1    Finkelstein, A.V.2    Galzitskaya, O.V.3
  • 27
    • 84893867894 scopus 로고    scopus 로고
    • How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. II. Experimental application for insulin and LysPro insulin: Aggregation morphology, kinetics, and sizes of nuclei
    • Selivanova OM, Suvorina MY, Dovidchenko NV, Eliseeva IA, Surin AK, Finkelstein AV, Schmatchenko VV, Galzitskaya OV (2014) How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. II. Experimental application for insulin and LysPro insulin: Aggregation morphology, kinetics, and sizes of nuclei. J Phys Chem B 118, 1198-1206.
    • (2014) J Phys Chem B , vol.118 , pp. 1198-1206
    • Selivanova, O.M.1    Suvorina, M.Y.2    Dovidchenko, N.V.3    Eliseeva, I.A.4    Surin, A.K.5    Finkelstein, A.V.6    Schmatchenko, V.V.7    Galzitskaya, O.V.8
  • 28
    • 84877258447 scopus 로고    scopus 로고
    • Polymorph-specific kinetics and thermodynamics ofβ-Amyloid fibril growth
    • Qiang W, Kelley K, Tycko R (2013) Polymorph-specific kinetics and thermodynamics ofβ-Amyloid fibril growth.JAm Chem Soc 135, 6860-6871.
    • (2013) JAm Chem Soc , vol.135 , pp. 6860-6871
    • Qiang, W.1    Kelley, K.2    Tycko, R.3
  • 29
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimers beta-Amyloid fibrils
    • Petkova AT, Leapman RD, Guo Z, Yau W-M, Mattson MP, Tycko R (2005) Self-propagating, molecular-level polymorphism in Alzheimers 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
  • 32
    • 0011246323 scopus 로고    scopus 로고
    • Electron microscopy of prefibrillar structures and amyloid fibrils
    • Nielsen EH, Nybo M, Svehag SE (1999) Electron microscopy of prefibrillar structures and amyloid fibrils. Methods Enzymol 309, 491-496.
    • (1999) Methods Enzymol , vol.309 , pp. 491-496
    • Nielsen, E.H.1    Nybo, M.2    Svehag, S.E.3
  • 33
    • 84861470082 scopus 로고    scopus 로고
    • Methionine-35 of aβ (1-42) : Importance for oxidative stress in Alzheimer disease
    • Butterfield DA, Sultana R (2011) Methionine-35 of aβ (1-42) : Importance for oxidative stress in Alzheimer disease. J Amino Acids 2011, 198430.
    • (2011) J Amino Acids , vol.2011 , pp. 198430
    • Butterfield, D.A.1    Sultana, R.2
  • 34
    • 70349568356 scopus 로고    scopus 로고
    • Structural polymorphism of Alzheimer Abeta and other amyloid fibrils
    • Fändrich M, Meinhardt J, Grigorieff N (2009) Structural polymorphism of Alzheimer Abeta and other amyloid fibrils. Prion 3, 89-93.
    • (2009) Prion , vol.3 , pp. 89-93
    • Fändrich, M.1    Meinhardt, J.2    Grigorieff, N.3
  • 35
    • 84884217594 scopus 로고    scopus 로고
    • Molecular structure of β-Amyloid fibrils in Alzheimers disease brain tissue
    • Lu J-X, Qiang W, Yau W-M, Schwieters CD, Meredith SC, Tycko R (2013) Molecular structure of β-Amyloid fibrils in Alzheimers disease brain tissue. Cell 154, 1257-1268.
    • (2013) Cell , vol.154 , pp. 1257-1268
    • Lu, J.-X.1    Qiang, W.2    Yau, W.-M.3    Schwieters, C.D.4    Meredith, S.C.5    Tycko, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.