메뉴 건너뛰기




Volumn 48, Issue 31, 2009, Pages 7465-7472

A triple-emission fluorescent probe reveals distinctive amyloid fibrillar polymorphism of wild-type α-synuclein and its familial Parkinson's disease mutants

Author keywords

[No Author keywords available]

Indexed keywords

3-HYDROXYFLAVONE; AMYLOID FIBRIL; EMISSION BANDS; EXCITATION-EMISSION SPECTRA; FLUORESCENCE SPECTRA; FLUORESCENT PROBES; HYDROGEN BONDINGS; IN-VITRO; LOCAL DIELECTRIC CONSTANT; NEURODEGENERATIVE DISORDERS; PARKINSON'S DISEASE; POINT MUTATIONS; PRESYNAPTIC; PROTON TRANSFER REACTIONS; RATIOMETRIC; SPECTROSCOPIC SIGNATURES; STRUCTURAL FEATURE; STRUCTURE-FUNCTION RELATIONSHIP; SUPRAMOLECULAR STRUCTURE; SYNUCLEIN; TAUTOMERIC EQUILIBRIA; TWO-DIMENSIONAL; WILD TYPES;

EID: 68249093598     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9003843     Document Type: Article
Times cited : (50)

References (43)
  • 2
    • 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
  • 3
    • 33845637320 scopus 로고    scopus 로고
    • From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity
    • Kreplak, L., and Aebi, U. (2006) From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity. Adv. Protein Chem. 73, 217-233.
    • (2006) Adv. Protein Chem. , vol.73 , pp. 217-233
    • Kreplak, L.1    Aebi, U.2
  • 4
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien, P., Weissman, J. S., and DePace, A. H. (2004) Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 73, 617-656.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 5
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • Kodali, R., and Wetzel, R. (2007) Polymorphism in the intermediates and products of amyloid assembly. Curr. Opin. Struct. Biol. 17, 48-57.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 7
    • 33744954409 scopus 로고    scopus 로고
    • Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay
    • Novitskaya, V.,Makarava, N.,Bellon, A., Bocharova, O.V.,Bronstein, I. B., Williamson, R. A., and Baskakov, I. V. (2006) Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay. J. Biol. Chem. 281, 15536-15545.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15536-15545
    • Novitskaya, V.1    Makarava, N.2    Bellon, A.3    Bocharova, O.V.4    Bronstein, I.B.5    Williamson, R.A.6    Baskakov, I.V.7
  • 8
    • 67649365665 scopus 로고    scopus 로고
    • Parkinson's disease: The syndrome, the pathogenesis and pathophysiology
    • doi 10.1016/j.cortex.2008.11.010
    • Bartels, A. L., and Leenders, K. L. (2008) Parkinson's disease: The syndrome, the pathogenesis and pathophysiology. Cortex (doi 10.1016/j.cortex. 2008.11.010).
    • (2008) Cortex
    • Bartels, A.L.1    Leenders, K.L.2
  • 10
    • 34548620297 scopus 로고    scopus 로고
    • Neuropathology, biochemistry, and biophysics of α-synuclein aggregation
    • Uversky, V. N. (2007) Neuropathology, biochemistry, and biophysics of α-synuclein aggregation. J. Neurochem. 103, 17-37.
    • (2007) J. Neurochem. , vol.103 , pp. 17-37
    • Uversky, V.N.1
  • 12
    • 24744461907 scopus 로고    scopus 로고
    • Familial mutants of α-synuclein with increased neurotoxicity have a destabilized conformation
    • Bertoncini, C. W., Fernandez, C. O., Griesinger, C., Jovin, T. M., and Zweckstetter, M. (2005) Familial mutants of α-synuclein with increased neurotoxicity have a destabilized conformation. J. Biol. Chem. 280, 30649-30652.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30649-30652
    • Bertoncini, C.W.1    Fernandez, C.O.2    Griesinger, C.3    Jovin, T.M.4    Zweckstetter, M.5
  • 13
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation
    • Serpell, L. C., Berriman, J., Jakes, R., Goedert, M., and Crowther, R. A. (2000) Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation. Proc. Natl. Acad. Sci. U.S.A. 97, 4897-4902.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 14
    • 34548359337 scopus 로고    scopus 로고
    • Investigation of α-synuclein fibril structure by site-directed spin labeling
    • Chen, M., Margittai, M., Chen, J., and Langen, R. (2007) Investigation of α-synuclein fibril structure by site-directed spin labeling. J. Biol. Chem. 282, 24970-24979.
    • (2007) J. Biol. Chem. , vol.282 , pp. 24970-24979
    • Chen, M.1    Margittai, M.2    Chen, J.3    Langen, R.4
  • 15
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solidstate NMR
    • Heise, H., Hoyer, W., Becker, S., Andronesi, O. C., Riedel, D., and Baldus, M. (2005) Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solidstate NMR. Proc. Natl. Acad. Sci. U.S.A. 102, 15871-15876.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 17
    • 0036386364 scopus 로고    scopus 로고
    • Dependence of α-synuclein aggregate morphology on solution conditions
    • Hoyer, W., Antony, T., Cherny, D., Heim, G., Jovin, T. M., and Subramaniam, V. (2002) Dependence of α-synuclein aggregate morphology on solution conditions. J. Mol. Biol. 322, 383-393.
    • (2002) J. Mol. Biol. , vol.322 , pp. 383-393
    • Hoyer, W.1    Antony, T.2    Cherny, D.3    Heim, G.4    Jovin, T.M.5    Subramaniam, V.6
  • 18
    • 0033583215 scopus 로고    scopus 로고
    • Mutant and wild type human α-synucleins assemble into elongated filaments with distinct morphologies in vitro
    • Giasson, B. I., Uryu, K., Trojanowski, J. Q., and Lee, V. M. (1999) Mutant and wild type human α-synucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem. 274, 7619-7622.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7619-7622
    • Giasson, B.I.1    Uryu, K.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 19
    • 33845358566 scopus 로고    scopus 로고
    • Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from α-synuclein mutants
    • van Raaij, M. E., Segers-Nolten, I. M., and Subramaniam, V. (2006) Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from α-synuclein mutants. Biophys. J. 91, L96-L98.
    • (2006) Biophys. J. , vol.91
    • Van Raaij, M.E.1    Segers-Nolten, I.M.2    Subramaniam, V.3
  • 20
    • 65549150887 scopus 로고    scopus 로고
    • Conversion of wild-type α-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant
    • Yonetani, M., Nonaka, T., Masuda, M., Inukai, Y., Oikawa, T., Hisanaga, S. I., and Hasegawa, M. (2009) Conversion of wild-type α-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant. J. Biol. Chem. 284, 7940-7950.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7940-7950
    • Yonetani, M.1    Nonaka, T.2    Masuda, M.3    Inukai, Y.4    Oikawa, T.5    Hisanaga, S.I.6    Hasegawa, M.7
  • 21
    • 33646878753 scopus 로고    scopus 로고
    • Preparation of α-synuclein fibrils for solidstateNMR: Expression, purification, and incubation of wild-type and mutant forms
    • Kloepper, K. D., Woods, W. S., Winter, K. A., George, J. M., and Rienstra, C. M. (2006) Preparation of α-synuclein fibrils for solidstateNMR: Expression, purification, and incubation of wild-type and mutant forms. Protein Expression Purif. 48, 112-117.
    • (2006) Protein Expression Purif. , vol.48 , pp. 112-117
    • Kloepper, K.D.1    Woods, W.S.2    Winter, K.A.3    George, J.M.4    Rienstra, C.M.5
  • 22
    • 51749125627 scopus 로고    scopus 로고
    • Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant α-synuclein
    • Heise, H., Celej, M. S., Becker, S., Riedel, D., Pelah, A., Kumar, A., Jovin, T. M., and Baldus, M. (2008) Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant α-synuclein. J. Mol. Biol. 380, 444-450.
    • (2008) J. Mol. Biol. , vol.380 , pp. 444-450
    • Heise, H.1    Celej, M.S.2    Becker, S.3    Riedel, D.4    Pelah, A.5    Kumar, A.6    Jovin, T.M.7    Baldus, M.8
  • 23
    • 45849128342 scopus 로고    scopus 로고
    • Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-synuclein
    • Celej,M. S., Jares-Erijman, E. A., and Jovin, T.M. (2008) Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of α-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
  • 24
    • 42649135877 scopus 로고    scopus 로고
    • Multiparametric fluorescence detection of early stages in the amyloid protein aggregation of pyrene-labeled α-synuclein
    • Thirunavukkuarasu, S., Jares-Erijman, E. A., and Jovin, T. M. (2008) Multiparametric fluorescence detection of early stages in the amyloid protein aggregation of pyrene-labeled α-synuclein. J. Mol. Biol. 378, 1064-1073.
    • (2008) J. Mol. Biol. , vol.378 , pp. 1064-1073
    • Thirunavukkuarasu, S.1    Jares-Erijman, E.A.2    Jovin, T.M.3
  • 25
    • 0142125377 scopus 로고    scopus 로고
    • Modulation of the solvent-dependent dual emission in 3-hydroxychromone by substituents
    • Klymchenko, A. S., Pivovarenko, V. G., Ozturk, T., and Demchenko, A. P. (2003) Modulation of the solvent-dependent dual emission in 3-hydroxychromone by substituents. New J. Chem. 27, 1336-1343.
    • (2003) New J. Chem. , vol.27 , pp. 1336-1343
    • Klymchenko, A.S.1    Pivovarenko, V.G.2    Ozturk, T.3    Demchenko, A.P.4
  • 26
    • 0037208160 scopus 로고    scopus 로고
    • Multiparametric probing of intermolecular interactions with fluorescent dye exhibiting excited state intramolecular proton transfer
    • Klymchenko, A. S., and Demchenko, A. P. (2003) Multiparametric probing of intermolecular interactions with fluorescent dye exhibiting excited state intramolecular proton transfer. Phys. Chem. Chem. Phys. 5, 461-468.
    • (2003) Phys. Chem. Chem. Phys. , vol.5 , pp. 461-468
    • Klymchenko, A.S.1    Demchenko, A.P.2
  • 27
    • 6344287943 scopus 로고    scopus 로고
    • Dynamics of intermolecular hydrogen bonds in the excited states of 4-dialkylamino-3-hydroxyflavones. On the pathway to an ideal fluorescent hydrogen bonding sensor
    • Shynkar, V. V.,Klymchenko, A. S., Piémont, E., Demchenko, A. P., and Mély, Y. (2004) Dynamics of intermolecular hydrogen bonds in the excited states of 4-dialkylamino-3-hydroxyflavones. On the pathway to an ideal fluorescent hydrogen bonding sensor. J. Phys. Chem. A 108, 8151-8159.
    • (2004) J. Phys. Chem. , vol.108 , pp. 8151-8159
    • Shynkar, V.V.1    Klymchenko, A.S.2    Piémont, E.3    Demchenko, A.P.4    Mély, Y.5
  • 28
    • 2142812408 scopus 로고    scopus 로고
    • Bimodal Distribution and Fluorescence Response of Environment-Sensitive Probes in Lipid Bilayers
    • Klymchenko, A. S., Duportail, G., Demchenko, A. P., and Mely, Y. (2004) Bimodal distribution and fluorescence response of environment- sensitive probes in lipid bilayers. Biophys. J. 86, 2929-2941. (Pubitemid 38552697)
    • (2004) Biophysical Journal , vol.86 , Issue.5 , pp. 2929-2941
    • Klymchenko, A.S.1    Duportail, G.2    Demchenko, A.P.3    Mely, Y.4
  • 29
    • 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 Jr., P.T.5
  • 30
    • 36849108026 scopus 로고
    • Band shapes of the electronic spectra of complex molecules
    • Siano, D. B., and Metzler, D. E. (1969) Band shapes of the electronic spectra of complex molecules. J. Chem. Phys. 51, 1856-1861.
    • (1969) J. Chem. Phys. , vol.51 , pp. 1856-1861
    • Siano, D.B.1    Metzler, D.E.2
  • 31
    • 0036363969 scopus 로고    scopus 로고
    • The red-edge effects: 30 years of exploration
    • Demchenko, A. P. (2002) The red-edge effects: 30 years of exploration. Luminescence 17, 19-42.
    • (2002) Luminescence , vol.17 , pp. 19-42
    • Demchenko, A.P.1
  • 32
    • 4644251757 scopus 로고    scopus 로고
    • Simultaneous probing of hydration and polarity of lipid bilayers with 3-hydroxyflavone fluorescent dyes
    • Klymchenko, A. S., Mely, Y., Demchenko, A. P., and Duportail, G. (2004) Simultaneous probing of hydration and polarity of lipid bilayers with 3-hydroxyflavone fluorescent dyes. Biochim. Biophys. Acta 1665, 6-19.
    • (2004) Biochim. Biophys. Acta , vol.1665 , pp. 6-19
    • Klymchenko, A.S.1    Mely, Y.2    Demchenko, A.P.3    Duportail, G.4
  • 33
    • 0037031232 scopus 로고    scopus 로고
    • Ultrasensitive fluorescent probe for the hydrophobic range of solvent polarities
    • Ercelen, S., Klymchenko, A. S., and Demchenko, A. P. (2002) Ultrasensitive fluorescent probe for the hydrophobic range of solvent polarities. Anal. Chim. Acta 464, 273-287.
    • (2002) Anal. Chim. Acta , vol.464 , pp. 273-287
    • Ercelen, S.1    Klymchenko, A.S.2    Demchenko, A.P.3
  • 34
    • 0004177513 scopus 로고    scopus 로고
    • Royal Society of Chemistry, Cambridge, U.K.
    • Suppan, P., and Ghoneim, N. (1997) Solvatochromism, Royal Society of Chemistry, Cambridge, U.K.
    • (1997) Solvatochromism
    • Suppan, P.1    Ghoneim, N.2
  • 35
    • 0037434886 scopus 로고    scopus 로고
    • Novel two-color fluorescence probe with extreme specificity to bovine serum albumin
    • DOI 10.1016/S0014-5793(03)00116-9
    • Ercelen, S., Klymchenko, A. S., and Demchenko, A. P. (2003) Novel two-color fluorescence probe with extreme specificity to bovine serum albumin. FEBS Lett. 538, 25-28. (Pubitemid 36287419)
    • (2003) FEBS Letters , vol.538 , Issue.1-3 , pp. 25-28
    • Ercelen, S.1    Klymchenko, A.S.2    Demchenko, A.P.3
  • 37
    • 24644500617 scopus 로고    scopus 로고
    • Main-chain dominated amyloid structures demonstrated by the effect of high pressure
    • Chatani, E., Kato, M., Kawai, T., Naiki, H., and Goto, Y. (2005) Main-chain dominated amyloid structures demonstrated by the effect of high pressure. J. Mol. Biol. 352, 941-951.
    • (2005) J. Mol. Biol. , vol.352 , pp. 941-951
    • Chatani, E.1    Kato, M.2    Kawai, T.3    Naiki, H.4    Goto, Y.5
  • 38
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein
    • DOI 10.1021/bi010616g
    • Li, J., Uversky, V. N., and Fink, A. L. (2001) Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein. Biochemistry 40, 11604-11613. (Pubitemid 32911305)
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 39
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: Localisation and implications
    • Krebs, M. R., Bromley, E. H., and Donald, A. M. (2005) The binding of thioflavin-T to amyloid fibrils: Localisation and implications. J. Struct. Biol. 149, 30-37.
    • (2005) J. Struct. Biol. , vol.149 , pp. 30-37
    • Krebs, M.R.1    Bromley, E.H.2    Donald, A.M.3
  • 40
    • 58149326746 scopus 로고    scopus 로고
    • Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies
    • Biancalana, M., Makabe, K., Koide, A., and Koide, S. (2009) Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies. J. Mol. Biol. 385, 1052-1063.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1052-1063
    • Biancalana, M.1    Makabe, K.2    Koide, A.3    Koide, S.4
  • 42
    • 59049099079 scopus 로고    scopus 로고
    • A comprehensive model for packing and hydration for amyloid fibrils of β2-microglobulin
    • Lee, Y. H., Chatani, E., Sasahara, K., Naiki, H., and Goto, Y. (2009) A comprehensive model for packing and hydration for amyloid fibrils of β2-microglobulin. J. Biol. Chem. 284, 2169-2175.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2169-2175
    • Lee, Y.H.1    Chatani, E.2    Sasahara, K.3    Naiki, H.4    Goto, Y.5
  • 43
    • 33847405723 scopus 로고    scopus 로고
    • Cubic equation governing the outerregion dielectric constant of globular proteins
    • Park, H., and Jeon, Y. H. (2007) Cubic equation governing the outerregion dielectric constant of globular proteins. Phys. Rev. E 75, 021916.
    • (2007) Phys. Rev. E , vol.75 , pp. 021916
    • Park, H.1    Jeon, Y.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.