메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages

Simultaneous Measurement of Amyloid Fibril Formation by Dynamic Light Scattering and Fluorescence Reveals Complex Aggregation Kinetics

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; POLYGLUTAMINE; THIOFLAVINE;

EID: 84872568036     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0054541     Document Type: Article
Times cited : (70)

References (33)
  • 2
    • 23844525922 scopus 로고    scopus 로고
    • Huntington's Disease Genetics
    • Myers RH, (2004) Huntington's Disease Genetics. NeuroRX 1: 255-262.
    • (2004) NeuroRX , vol.1 , pp. 255-262
    • Myers, R.H.1
  • 3
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti F, Dobson CM, (2009) Amyloid formation by globular proteins under native conditions. Nat Chem Biol 5: 15-22.
    • (2009) Nat Chem Biol , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 0031446233 scopus 로고    scopus 로고
    • Intranuclear Neuronal Inclusions: A Common Pathogenic Mechanism for Glutamine-Repeat Neurodegenerative Diseases?
    • Ross CA, (1997) Intranuclear Neuronal Inclusions: A Common Pathogenic Mechanism for Glutamine-Repeat Neurodegenerative Diseases? Neuron 19: 1147-1150.
    • (1997) Neuron , vol.19 , pp. 1147-1150
    • Ross, C.A.1
  • 5
    • 77954379810 scopus 로고    scopus 로고
    • Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool
    • Olshina MA, Angley LM, Ramdzan YM, Tang J, Bailey MF, et al. (2010) Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool. J Biol Chem 285: 21807-21816.
    • (2010) J Biol Chem , vol.285 , pp. 21807-21816
    • Olshina, M.A.1    Angley, L.M.2    Ramdzan, Y.M.3    Tang, J.4    Bailey, M.F.5
  • 6
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin Spheroids and Protofibrils as Precursors in Polyglutamine Fibrilization
    • Poirier MA, Li H, Macosko J, Cai S, Amzel M, et al. (2002) Huntingtin Spheroids and Protofibrils as Precursors in Polyglutamine Fibrilization. Journal of Biological Chemistry 277: 41032-41037.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    Macosko, J.3    Cai, S.4    Amzel, M.5
  • 7
    • 64049119303 scopus 로고    scopus 로고
    • Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
    • Thakur AK, Jayaraman M, Mishra R, Thakur M, Chellgren VM, et al. (2009) Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. Nat Struct Mol Biol 16: 380-389.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 380-389
    • Thakur, A.K.1    Jayaraman, M.2    Mishra, R.3    Thakur, M.4    Chellgren, V.M.5
  • 8
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Academic Press
    • Ferrone F, Ronald W (1999) Analysis of protein aggregation kinetics. Methods in Enzymology: Academic Press. 256-274.
    • (1999) Methods in Enzymology , pp. 256-274
    • Ferrone, F.1    Ronald, W.2
  • 9
    • 0033551063 scopus 로고    scopus 로고
    • Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: Implications for Huntington's disease pathology
    • Scherzinger E, Sittler A, Schweiger K, Heiser V, Lurz R, et al. (1999) Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: Implications for Huntington's disease pathology. Proceedings of the National Academy of Sciences 96: 4604-4609.
    • (1999) Proceedings of the National Academy of Sciences , vol.96 , pp. 4604-4609
    • Scherzinger, E.1    Sittler, A.2    Schweiger, K.3    Heiser, V.4    Lurz, R.5
  • 11
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, et al. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416: 507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5
  • 12
    • 18544400323 scopus 로고    scopus 로고
    • Huntingtin-Encoded Polyglutamine Expansions Form Amyloid-like Protein Aggregates In Vitro and In Vivo
    • Scherzinger E, Lurz R, Turmaine M, Mangiarini L, Hollenbach B, et al. (1997) Huntingtin-Encoded Polyglutamine Expansions Form Amyloid-like Protein Aggregates In Vitro and In Vivo. Cell 90: 549-558.
    • (1997) Cell , vol.90 , pp. 549-558
    • Scherzinger, E.1    Lurz, R.2    Turmaine, M.3    Mangiarini, L.4    Hollenbach, B.5
  • 13
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S, (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431: 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 14
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin Acts in the Nucleus to Induce Apoptosis but Death Does Not Correlate with the Formation of Intranuclear Inclusions
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME, (1998) Huntingtin Acts in the Nucleus to Induce Apoptosis but Death Does Not Correlate with the Formation of Intranuclear Inclusions. Cell 95: 55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 17
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant
    • Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, et al. (2000) Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant. Science 289: 1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5
  • 19
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • Xue W-F, Homans SW, Radford SE, (2008) Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proceedings of the National Academy of Sciences 105: 8926-8931.
    • (2008) Proceedings of the National Academy of Sciences , vol.105 , pp. 8926-8931
    • Xue, W.-F.1    Homans, S.W.2    Radford, S.E.3
  • 20
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin P, Melki R, Kopito R, (2010) Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 11: 301-307.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 21
    • 79952189175 scopus 로고    scopus 로고
    • Assays for studying nucleated aggregation of polyglutamine proteins
    • Jayaraman M, Thakur AK, Kar K, Kodali R, Wetzel R, (2011) Assays for studying nucleated aggregation of polyglutamine proteins. Methods 53: 246-254.
    • (2011) Methods , vol.53 , pp. 246-254
    • Jayaraman, M.1    Thakur, A.K.2    Kar, K.3    Kodali, R.4    Wetzel, R.5
  • 22
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid [beta]-peptides of Alzheimer's disease: Analysis of circular dichroism spectra
    • Barrow CJ, Yasuda A, Kenny PTM, Zagorski MG, (1992) Solution conformations and aggregational properties of synthetic amyloid [beta]-peptides of Alzheimer's disease: Analysis of circular dichroism spectra. Journal of Molecular Biology 225: 1075-1093.
    • (1992) Journal of Molecular Biology , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.M.3    Zagorski, M.G.4
  • 23
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of [beta]-sheet amyloid fibril structures with thioflavin T
    • Academic Press
    • LeVine III H, Ronald W (1999) Quantification of [beta]-sheet amyloid fibril structures with thioflavin T. Methods in Enzymology: Academic Press. 274-284.
    • (1999) Methods in Enzymology , pp. 274-284
    • LeVine III, H.1    Ronald, W.2
  • 26
    • 67650403403 scopus 로고    scopus 로고
    • Amyloid Protofibrils of Lysozyme Nucleate and Grow Via Oligomer Fusion
    • Hill SE, Robinson J, Matthews G, Muschol M, (2009) Amyloid Protofibrils of Lysozyme Nucleate and Grow Via Oligomer Fusion. Biophysical Journal 96: 3781-3790.
    • (2009) Biophysical Journal , vol.96 , pp. 3781-3790
    • Hill, S.E.1    Robinson, J.2    Matthews, G.3    Muschol, M.4
  • 28
    • 0033939135 scopus 로고    scopus 로고
    • Controlled Intracellular Processing of Fusion Proteins by TEV Protease
    • Kapust RB, Waugh DS, (2000) Controlled Intracellular Processing of Fusion Proteins by TEV Protease. Protein Expression and Purification 19: 312-318.
    • (2000) Protein Expression and Purification , vol.19 , pp. 312-318
    • Kapust, R.B.1    Waugh, D.S.2
  • 29
    • 77951545940 scopus 로고    scopus 로고
    • Ostwald Ripening of Clusters during Protein Crystallization
    • Streets AM, Quake SR, (2010) Ostwald Ripening of Clusters during Protein Crystallization. Physical Review Letters 104: 178102.
    • (2010) Physical Review Letters , vol.104 , pp. 178102
    • Streets, A.M.1    Quake, S.R.2
  • 30
    • 0027596998 scopus 로고
    • Dynamic Light Scattering with single-mode and multimode recievers
    • Ricka J, (1993) Dynamic Light Scattering with single-mode and multimode recievers. Applied Optics 32: 2860-2875.
    • (1993) Applied Optics , vol.32 , pp. 2860-2875
    • Ricka, J.1
  • 31
    • 36849103950 scopus 로고
    • Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants
    • Koppel DE, (1972) Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants. Journal of Chemical Physics 57: 4814-4820.
    • (1972) Journal of Chemical Physics , vol.57 , pp. 4814-4820
    • Koppel, D.E.1
  • 32
    • 0020176708 scopus 로고
    • CONTIN: a general purpose constrained regularization program for inverting noisy linear algebraic and integral equations
    • Provencher SW, (1982) CONTIN: a general purpose constrained regularization program for inverting noisy linear algebraic and integral equations. Computer Physics Communications 27: 229-242.
    • (1982) Computer Physics Communications , vol.27 , pp. 229-242
    • Provencher, S.W.1
  • 33
    • 58149326746 scopus 로고    scopus 로고
    • Molecular Mechanism of Thioflavin-T Binding to the Surface of [beta]-Rich Peptide Self-Assemblies
    • Biancalana M, Makabe K, Koide A, Koide S, (2009) Molecular Mechanism of Thioflavin-T Binding to the Surface of [beta]-Rich Peptide Self-Assemblies. Journal of Molecular Biology 385: 1052-1063.
    • (2009) Journal of Molecular Biology , vol.385 , pp. 1052-1063
    • Biancalana, M.1    Makabe, K.2    Koide, A.3    Koide, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.