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Volumn 53, Issue 39, 2014, Pages 6252-6263

High stability and cooperative unfolding of α-Synuclein Oligomers

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; NEURODEGENERATIVE DISEASES;

EID: 84907854533     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5007833     Document Type: Article
Times cited : (68)

References (87)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75, 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 79952748803 scopus 로고    scopus 로고
    • Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation
    • Giehm, L., Svergun, D. I., Otzen, D. E., and Vestergaard, B. (2011) Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation Proc. Natl. Acad. Sci. U.S.A. 108, 3246-3251
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3246-3251
    • Giehm, L.1    Svergun, D.I.2    Otzen, D.E.3    Vestergaard, B.4
  • 3
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., and Lansbury, P. T., Jr. (2002) Neurodegenerative disease: Amyloid pores from pathogenic mutations Nature 418, 291
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 4
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway, K. A., Lee, S. J., Rochet, J. C., Ding, T. T., Williamson, R. E., and Lansbury, P. T., Jr. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy Proc. Natl. Acad. Sci. U.S.A. 97, 571-576
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 6
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - A decade of discovery
    • Walsh, D. M. and Selkoe, D. J. (2007) A beta oligomers-a decade of discovery J. Neurochem. 101, 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 11
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
    • Volles, M. J., Lee, S. J., Rochet, J. C., Shtilerman, M. D., Ding, T. T., Kessler, J. C., and Lansbury, P. T., Jr. (2001) Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease Biochemistry 40, 7812-7819
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Volles, M.J.1    Lee, S.J.2    Rochet, J.C.3    Shtilerman, M.D.4    Ding, T.T.5    Kessler, J.C.6    Lansbury, P.T.7
  • 12
    • 67650403403 scopus 로고    scopus 로고
    • Amyloid protofibrils of lysozyme nucleate and grow via oligomer fusion
    • Hill, S. E., Robinson, J., Matthews, G., and Muschol, M. (2009) Amyloid protofibrils of lysozyme nucleate and grow via oligomer fusion Biophys. J. 96, 3781-3790
    • (2009) Biophys. J. , vol.96 , pp. 3781-3790
    • Hill, S.E.1    Robinson, J.2    Matthews, G.3    Muschol, M.4
  • 15
    • 11244309572 scopus 로고    scopus 로고
    • Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry
    • Kardos, J., Yamamoto, K., Hasegawa, K., Naiki, H., and Goto, Y. (2004) Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry J. Biol. Chem. 279, 55308-55314
    • (2004) J. Biol. Chem. , vol.279 , pp. 55308-55314
    • Kardos, J.1    Yamamoto, K.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 16
    • 38149142280 scopus 로고    scopus 로고
    • Seed-dependent accelerated fibrillation of alpha-synuclein induced by periodic ultrasonication treatment
    • Kim, H. J., Chatani, E., Goto, Y., and Paik, S. R. (2007) Seed-dependent accelerated fibrillation of alpha-synuclein induced by periodic ultrasonication treatment J. Microbiol. Biotechnol. 17, 2027-2032
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 2027-2032
    • Kim, H.J.1    Chatani, E.2    Goto, Y.3    Paik, S.R.4
  • 17
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
    • Morris, A. M., Watzky, M. A., and Finke, R. G. (2009) Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature Biochim. Biophys. Acta 1794, 375-397
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 19
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • e321
    • Collins, S. R., Douglass, A., Vale, R. D., and Weissman, J. S. (2004) Mechanism of prion propagation: Amyloid growth occurs by monomer addition PLoS Biol. 2 e321
    • (2004) PLoS Biol. , vol.2
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 20
    • 79951607134 scopus 로고    scopus 로고
    • Defining the pathway of worm-like amyloid fibril formation by the mouse prion protein by delineation of the productive and unproductive oligomerization reactions
    • Jain, S. and Udgaonkar, J. B. (2011) Defining the pathway of worm-like amyloid fibril formation by the mouse prion protein by delineation of the productive and unproductive oligomerization reactions Biochemistry 50, 1153-1161
    • (2011) Biochemistry , vol.50 , pp. 1153-1161
    • Jain, S.1    Udgaonkar, J.B.2
  • 21
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula, M., Kayed, R., Milton, S., and Glabe, C. G. (2007) Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct J. Biol. Chem. 282, 10311-10324
    • (2007) J. Biol. Chem. , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 22
    • 0037066715 scopus 로고    scopus 로고
    • Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH
    • Souillac, P. O., Uversky, V. N., Millett, I. S., Khurana, R., Doniach, S., and Fink, A. L. (2002) Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH J. Biol. Chem. 277, 12666-12679
    • (2002) J. Biol. Chem. , vol.277 , pp. 12666-12679
    • Souillac, P.O.1    Uversky, V.N.2    Millett, I.S.3    Khurana, R.4    Doniach, S.5    Fink, A.L.6
  • 24
    • 79951638042 scopus 로고    scopus 로고
    • Characterization of the non-fibrillar alpha-synuclein oligomers
    • Hong, D. P., Han, S., Fink, A. L., and Uversky, V. N. (2011) Characterization of the non-fibrillar alpha-synuclein oligomers Protein Pept. Lett. 18, 230-240
    • (2011) Protein Pept. Lett. , vol.18 , pp. 230-240
    • Hong, D.P.1    Han, S.2    Fink, A.L.3    Uversky, V.N.4
  • 29
    • 1542613781 scopus 로고    scopus 로고
    • Alpha-Synuclein A53T substitution associated with Parkinson disease also marks the divergence of Old World and New World primates
    • Hamilton, B. A. (2004) alpha-Synuclein A53T substitution associated with Parkinson disease also marks the divergence of Old World and New World primates Genomics 83, 739-742
    • (2004) Genomics , vol.83 , pp. 739-742
    • Hamilton, B.A.1
  • 34
    • 27544507306 scopus 로고    scopus 로고
    • Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration
    • Chandra, S., Gallardo, G., Fernandez-Chacon, R., Schluter, O. M., and Sudhof, T. C. (2005) Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration Cell 123, 383-396
    • (2005) Cell , vol.123 , pp. 383-396
    • Chandra, S.1    Gallardo, G.2    Fernandez-Chacon, R.3    Schluter, O.M.4    Sudhof, T.C.5
  • 36
    • 19444388207 scopus 로고    scopus 로고
    • Alpha-synuclein overexpression in oligodendrocytic cells results in impaired adhesion to fibronectin and cell death
    • Tsuboi, K., Grzesiak, J. J., Bouvet, M., Hashimoto, M., Masliah, E., and Shults, C. W. (2005) Alpha-synuclein overexpression in oligodendrocytic cells results in impaired adhesion to fibronectin and cell death Mol. Cell. Neurosci. 29, 259-268
    • (2005) Mol. Cell. Neurosci. , vol.29 , pp. 259-268
    • Tsuboi, K.1    Grzesiak, J.J.2    Bouvet, M.3    Hashimoto, M.4    Masliah, E.5    Shults, C.W.6
  • 37
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels, T., Choi, J. G., and Selkoe, D. J. (2011) alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation Nature 477, 107-110
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 40
    • 84874769548 scopus 로고    scopus 로고
    • In vivo cross-linking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells
    • Dettmer, U., Newman, A. J., Luth, E. S., Bartels, T., and Selkoe, D. (2013) In vivo cross-linking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells J. Biol. Chem. 288, 6371-6385
    • (2013) J. Biol. Chem. , vol.288 , pp. 6371-6385
    • Dettmer, U.1    Newman, A.J.2    Luth, E.S.3    Bartels, T.4    Selkoe, D.5
  • 41
    • 84866671599 scopus 로고    scopus 로고
    • Bacterial in-cell NMR of human alpha-synuclein: A disordered monomer by nature?
    • Binolfi, A., Theillet, F. X., and Selenko, P. (2012) Bacterial in-cell NMR of human alpha-synuclein: a disordered monomer by nature? Biochem. Soc. Trans. 40, 950-954
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 950-954
    • Binolfi, A.1    Theillet, F.X.2    Selenko, P.3
  • 43
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., and Lansbury, P. T., Jr. (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded Biochemistry 35, 13709-13715
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, P.T.5
  • 44
    • 0032568534 scopus 로고    scopus 로고
    • Alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies
    • Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., and Goedert, M. (1998) alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies Proc. Natl. Acad. Sci. U.S.A. 95, 6469-6473
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 45
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink, A. L. (1998) Protein aggregation: Folding aggregates, inclusion bodies and amyloid Folding Des. 3, R9-23
    • (1998) Folding Des. , vol.3 , pp. 9-23
    • Fink, A.L.1
  • 46
    • 84860110592 scopus 로고    scopus 로고
    • Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure
    • Celej, M. S., Sarroukh, R., Goormaghtigh, E., Fidelio, G. D., Ruysschaert, J. M., and Raussens, V. (2012) Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure Biochem. J. 443, 719-726
    • (2012) Biochem. J. , vol.443 , pp. 719-726
    • Celej, M.S.1    Sarroukh, R.2    Goormaghtigh, E.3    Fidelio, G.D.4    Ruysschaert, J.M.5    Raussens, V.6
  • 49
    • 84876891740 scopus 로고    scopus 로고
    • Alpha-synuclein oligomers: An amyloid pore? Insights into mechanisms of alpha-synuclein oligomer-lipid interactions
    • Stockl, M. T., Zijlstra, N., and Subramaniam, V. (2013) Alpha-synuclein oligomers: an amyloid pore? Insights into mechanisms of alpha-synuclein oligomer-lipid interactions Mol. Neurobiol. 47, 613-621
    • (2013) Mol. Neurobiol. , vol.47 , pp. 613-621
    • Stockl, M.T.1    Zijlstra, N.2    Subramaniam, V.3
  • 50
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of alpha-synuclein: From structure and toxicity to therapeutic target
    • Lashuel, H. A., Overk, C. R., Oueslati, A., and Masliah, E. (2013) The many faces of alpha-synuclein: from structure and toxicity to therapeutic target Nat. Rev. Neurosci. 14, 38-48
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 51
    • 84875415994 scopus 로고    scopus 로고
    • Alpha-Synuclein oligomers and clinical implications for Parkinson disease
    • Kalia, L. V., Kalia, S. K., McLean, P. J., Lozano, A. M., and Lang, A. E. (2013) alpha-Synuclein oligomers and clinical implications for Parkinson disease Ann. Neurol. 73, 155-169
    • (2013) Ann. Neurol. , vol.73 , pp. 155-169
    • Kalia, L.V.1    Kalia, S.K.2    McLean, P.J.3    Lozano, A.M.4    Lang, A.E.5
  • 53
    • 78650763561 scopus 로고    scopus 로고
    • Membrane Permeabilization by Oligomeric alpha-Synuclein: In Search of the Mechanism
    • e14292
    • van Rooijen, B. D., Claessens, M. M., and Subramaniam, V. (2010) Membrane Permeabilization by Oligomeric alpha-Synuclein: In Search of the Mechanism PloS One 5 e14292
    • (2010) PloS One , vol.5
    • Van Rooijen, B.D.1    Claessens, M.M.2    Subramaniam, V.3
  • 54
    • 65549114936 scopus 로고    scopus 로고
    • Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core
    • van Rooijen, B. D., Claessens, M. M., and Subramaniam, V. (2009) Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core Biochim. Biophys. Acta 1788, 1271-1278
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1271-1278
    • Van Rooijen, B.D.1    Claessens, M.M.2    Subramaniam, V.3
  • 58
    • 77954358960 scopus 로고    scopus 로고
    • Mysterious oligomerization of the amyloidogenic proteins
    • Uversky, V. N. (2010) Mysterious oligomerization of the amyloidogenic proteins FEBS J. 277, 2940-2953
    • (2010) FEBS J. , vol.277 , pp. 2940-2953
    • Uversky, V.N.1
  • 59
    • 84863986886 scopus 로고    scopus 로고
    • Oligomeric intermediates in amyloid formation: Structure determination and mechanisms of toxicity
    • Fandrich, M. (2012) Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity J. Mol. Biol. 421, 427-440
    • (2012) J. Mol. Biol. , vol.421 , pp. 427-440
    • Fandrich, M.1
  • 60
    • 84904515491 scopus 로고    scopus 로고
    • Co-existence of two different α-synuclein oligomers with different core structures determined by Hydrogen/Deuterium Exchange Mass Spectrometry
    • Paslawski, W., Mysling, S., Thomsen, K., Jørgensen, T. J. D., and Otzen, D. E. (2014) Co-existence of two different α-synuclein oligomers with different core structures determined by Hydrogen/Deuterium Exchange Mass Spectrometry Angew. Chem., Int. Ed. Engl. 53, 7560-7563 10.1002/anie.201400491
    • (2014) Angew. Chem., Int. Ed. Engl. , vol.53 , pp. 7560-7563
    • Paslawski, W.1    Mysling, S.2    Thomsen, K.3    Jørgensen, T.J.D.4    Otzen, D.E.5
  • 62
    • 84892794505 scopus 로고    scopus 로고
    • The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes
    • Lorenzen, N., Lemminger, L., Pedersen, J. N., Nielsen, S. B., and Otzen, D. E. (2013) The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes FEBS Lett. 588, 497-502
    • (2013) FEBS Lett. , vol.588 , pp. 497-502
    • Lorenzen, N.1    Lemminger, L.2    Pedersen, J.N.3    Nielsen, S.B.4    Otzen, D.E.5
  • 63
    • 22244456042 scopus 로고    scopus 로고
    • Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy
    • Lindgren, M., Sorgjerd, K., and Hammarstrom, P. (2005) Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy Biophys. J. 88, 4200-4212
    • (2005) Biophys. J. , vol.88 , pp. 4200-4212
    • Lindgren, M.1    Sorgjerd, K.2    Hammarstrom, P.3
  • 64
    • 20444412385 scopus 로고    scopus 로고
    • A new method for purification of recombinant human alpha-synuclein in Escherichia coli
    • Huang, C., Ren, G., Zhou, H., and Wang, C. C. (2005) A new method for purification of recombinant human alpha-synuclein in Escherichia coli Protein Expression Purif. 42, 173-177
    • (2005) Protein Expression Purif. , vol.42 , pp. 173-177
    • Huang, C.1    Ren, G.2    Zhou, H.3    Wang, C.C.4
  • 65
    • 79952188071 scopus 로고    scopus 로고
    • Assays for alpha-synuclein aggregation
    • Giehm, L., Lorenzen, N., and Otzen, D. E. (2011) Assays for alpha-synuclein aggregation Methods 53, 295-305
    • (2011) Methods , vol.53 , pp. 295-305
    • Giehm, L.1    Lorenzen, N.2    Otzen, D.E.3
  • 66
    • 77950689601 scopus 로고    scopus 로고
    • Strategies to increase the reproducibility of protein fibrillization in plate reader assays
    • Giehm, L. and Otzen, D. E. (2010) Strategies to increase the reproducibility of protein fibrillization in plate reader assays Anal. Biochem. 400, 270-281
    • (2010) Anal. Biochem. , vol.400 , pp. 270-281
    • Giehm, L.1    Otzen, D.E.2
  • 67
    • 56449127663 scopus 로고    scopus 로고
    • Kinetic partitioning between aggregation and vesicle permeabilization by modified ADan
    • Nesgaard, L., Vad, B., Christiansen, G., and Otzen, D. (2009) Kinetic partitioning between aggregation and vesicle permeabilization by modified ADan Biochim. Biophys. Acta 1794, 84-93
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 84-93
    • Nesgaard, L.1    Vad, B.2    Christiansen, G.3    Otzen, D.4
  • 69
    • 0027378450 scopus 로고
    • Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants
    • Royer, C. A., Mann, C. J., and Matthews, C. R. (1993) Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants Protein Sci. 2, 1844-1852
    • (1993) Protein Sci. , vol.2 , pp. 1844-1852
    • Royer, C.A.1    Mann, C.J.2    Matthews, C.R.3
  • 70
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131, 266-279
    • (1986) Methods Enzymol. , vol.131 , pp. 266-279
    • Pace, C.N.1
  • 71
    • 1642283195 scopus 로고    scopus 로고
    • Elimination of an off-pathway folding intermediate by a single point mutation
    • Mogensen, J. E., Ibsen, H., Lund, J., and Otzen, D. E. (2004) Elimination of an off-pathway folding intermediate by a single point mutation Biochemistry 43, 3357-3367
    • (2004) Biochemistry , vol.43 , pp. 3357-3367
    • Mogensen, J.E.1    Ibsen, H.2    Lund, J.3    Otzen, D.E.4
  • 72
    • 3442880149 scopus 로고    scopus 로고
    • A flux- and background-optimized version of the NanoSTAR small-angle X-ray scattering camera for solution scattering
    • Pedersen, J. S. (2004) A flux- and background-optimized version of the NanoSTAR small-angle X-ray scattering camera for solution scattering J. Appl. Crystallogr. 37, 368-380
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 368-380
    • Pedersen, J.S.1
  • 73
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300, 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 74
    • 45849128342 scopus 로고    scopus 로고
    • Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of alpha-synuclein
    • Celej, M. S., Jares-Erijman, E. A., and Jovin, T. M. (2008) Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of alpha-synuclein Biophys. J. 94, 4867-4879
    • (2008) Biophys. J. , vol.94 , pp. 4867-4879
    • Celej, M.S.1    Jares-Erijman, E.A.2    Jovin, T.M.3
  • 76
    • 22244456042 scopus 로고    scopus 로고
    • Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy
    • Lindgren, M., Sörgjerd, K., and Hammarström, P. (2005) Detection and Characterization of Aggregates, Prefibrillar Amyloidogenic Oligomers, and Protofibrils Using Fluorescence Spectroscopy Biophys. J. 88, 4200-4212
    • (2005) Biophys. J. , vol.88 , pp. 4200-4212
    • Lindgren, M.1    Sörgjerd, K.2    Hammarström, P.3
  • 77
    • 0037592927 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence
    • Ban, T., Hamada, D., Hasegawa, K., Naiki, H., and Goto, Y. (2003) Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence J. Biol. Chem. 278, 16462-16465
    • (2003) J. Biol. Chem. , vol.278 , pp. 16462-16465
    • Ban, T.1    Hamada, D.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 78
    • 33644527256 scopus 로고    scopus 로고
    • Characterization of oligomers during α-synuclein aggregation using intrinsic tryptophan fluorescence
    • Dusa, A., Kaylor, J., Edridge, S., Bodner, N., Hong, D. P., and Fink, A. L. (2006) Characterization of oligomers during α-synuclein aggregation using intrinsic tryptophan fluorescence Biochemistry 45, 2752-2760
    • (2006) Biochemistry , vol.45 , pp. 2752-2760
    • Dusa, A.1    Kaylor, J.2    Edridge, S.3    Bodner, N.4    Hong, D.P.5    Fink, A.L.6
  • 79
    • 0037432332 scopus 로고    scopus 로고
    • Conformational behavior and aggregation of α-synuclein in organic solvents: Modeling the effects of membranes
    • Munishkina, L. A., Phelan, C., Uversky, V. N., and Fink, A. L. (2003) Conformational behavior and aggregation of α-synuclein in organic solvents: Modeling the effects of membranes Biochemistry 42, 2720-2730
    • (2003) Biochemistry , vol.42 , pp. 2720-2730
    • Munishkina, L.A.1    Phelan, C.2    Uversky, V.N.3    Fink, A.L.4
  • 80
    • 35848966149 scopus 로고    scopus 로고
    • Sensitive fluorescence polarization technique for rapid screening of α-synuclein oligomerization/fibrillization inhibitors
    • Luk, K. C., Hyde, E. G., Trojanowski, J. Q., and Lee, V. M. (2007) Sensitive fluorescence polarization technique for rapid screening of α-synuclein oligomerization/fibrillization inhibitors Biochemistry 46, 12522-12529
    • (2007) Biochemistry , vol.46 , pp. 12522-12529
    • Luk, K.C.1    Hyde, E.G.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 81
    • 33749841522 scopus 로고    scopus 로고
    • The aggregation and fibrillation of α-synuclein
    • Fink, A. L. (2006) The aggregation and fibrillation of α-synuclein Acc. Chem. Res. 39, 628-634
    • (2006) Acc. Chem. Res. , vol.39 , pp. 628-634
    • Fink, A.L.1
  • 84
    • 4344569643 scopus 로고    scopus 로고
    • Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro
    • McLean, P. J., Klucken, J., Shin, Y., and Hyman, B. T. (2004) Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro Biochem. Biophys. Res. Commun. 321, 665-669
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 665-669
    • McLean, P.J.1    Klucken, J.2    Shin, Y.3    Hyman, B.T.4
  • 85
    • 77649305375 scopus 로고    scopus 로고
    • 17-AAG induces cytoplasmic alpha-synuclein aggregate clearance by induction of autophagy
    • e8753
    • Riedel, M., Goldbaum, O., Schwarz, L., Schmitt, S., and Richter-Landsberg, C. (2010) 17-AAG induces cytoplasmic alpha-synuclein aggregate clearance by induction of autophagy PloS One 5 e8753
    • (2010) PloS One , vol.5
    • Riedel, M.1    Goldbaum, O.2    Schwarz, L.3    Schmitt, S.4    Richter-Landsberg, C.5
  • 87
    • 82955194531 scopus 로고    scopus 로고
    • Black tea theaflavins inhibit formation of toxic amyloid-β and α-synuclein fibrils
    • Grelle, G., Otto, A., Lorenz, M., Frank, R. F., Wanker, E. E., and Bieschke, J. (2011) Black tea theaflavins inhibit formation of toxic amyloid-β and α-synuclein fibrils Biochemistry 50, 10624-10636
    • (2011) Biochemistry , vol.50 , pp. 10624-10636
    • Grelle, G.1    Otto, A.2    Lorenz, M.3    Frank, R.F.4    Wanker, E.E.5    Bieschke, J.6


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