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Volumn 8, Issue 3, 2013, Pages

Site-Specific Perturbations of Alpha-Synuclein Fibril Structure by the Parkinson's Disease Associated Mutations A53T and E46K

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALPHA SYNUCLEIN; GLUTAMIC ACID; LYSINE; TRYPTOPHAN;

EID: 84874680352     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049750     Document Type: Article
Times cited : (55)

References (44)
  • 2
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, et al. (1997) Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276: 2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5
  • 3
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • Kruger R, Kuhn W, Muller T, Woitalla D, Graeber M, et al. (1998) Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat Genet 18: 106-108.
    • (1998) Nat Genet , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5
  • 4
    • 10744230149 scopus 로고    scopus 로고
    • The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia
    • Zarranz JJ, Alegre J, Gomez-Esteban JC, Lezcano E, Ros R, et al. (2004) The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia. Ann Neurol 55: 164-173.
    • (2004) Ann Neurol , vol.55 , pp. 164-173
    • Zarranz, J.J.1    Alegre, J.2    Gomez-Esteban, J.C.3    Lezcano, E.4    Ros, R.5
  • 5
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alpha-synuclein in its free and lipid-associated states
    • Eliezer D, Kutluay E, Bussell R, Browne G, (2001) Conformational properties of alpha-synuclein in its free and lipid-associated states. J Mol Biol 307: 1061-1073.
    • (2001) J Mol Biol , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell, R.3    Browne, G.4
  • 6
    • 0035824545 scopus 로고    scopus 로고
    • Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein
    • Bussell R, Eliezer D, (2001) Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein. J Biol Chem 276: 45996-46003.
    • (2001) J Biol Chem , vol.276 , pp. 45996-46003
    • Bussell, R.1    Eliezer, D.2
  • 7
    • 34250796802 scopus 로고    scopus 로고
    • The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states
    • Fredenburg RA, Rospigliosi C, Meray RK, Kessler JC, Lashuel HA, et al. (2007) The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states. Biochemistry 46: 7107-7118.
    • (2007) Biochemistry , vol.46 , pp. 7107-7118
    • Fredenburg, R.A.1    Rospigliosi, C.2    Meray, R.K.3    Kessler, J.C.4    Lashuel, H.A.5
  • 8
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • Conway KA, Harper JD, Lansbury PT, (1998) Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat Med 4: 1318-1320.
    • (1998) Nat Med , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 9
    • 0033515471 scopus 로고    scopus 로고
    • Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation
    • Narhi L, Wood SJ, Steavenson S, Jiang YJ, Wu GM, et al. (1999) Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation. J Biol Chem 274: 9843-9846.
    • (1999) J Biol Chem , vol.274 , pp. 9843-9846
    • Narhi, L.1    Wood, S.J.2    Steavenson, S.3    Jiang, Y.J.4    Wu, G.M.5
  • 10
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR
    • Heise H, Hoyer W, Becker S, Andronesi OC, Riedel D, et al. (2005) Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. Proc Natl Acad Sci USA 102: 15871-15876.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5
  • 11
    • 78049396749 scopus 로고    scopus 로고
    • Supramolecular interactions probed by 13C-13C solid-state NMR spectroscopy
    • Loquet A, Giller K, Becker S, Lange A, (2010) Supramolecular interactions probed by 13C-13C solid-state NMR spectroscopy. J Am Chem Soc 132: 15164-15166.
    • (2010) J Am Chem Soc , vol.132 , pp. 15164-15166
    • Loquet, A.1    Giller, K.2    Becker, S.3    Lange, A.4
  • 12
    • 80051672851 scopus 로고    scopus 로고
    • Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites
    • Comellas G, Lemkau LR, Nieuwkoop AJ, Kloepper KD, Ladror DT, et al. (2011) Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites. J Mol Biol 411: 881-895.
    • (2011) J Mol Biol , vol.411 , pp. 881-895
    • Comellas, G.1    Lemkau, L.R.2    Nieuwkoop, A.J.3    Kloepper, K.D.4    Ladror, D.T.5
  • 13
    • 68249093598 scopus 로고    scopus 로고
    • A Triple-Emission Fluorescent Probe Reveals Distinctive Amyloid Fibrillar Polymorphism of Wild-Type alpha-Synuclein and Its Familial Parkinson's Disease Mutants
    • Celej MS, Caarls W, Demchenko AP, Jovin TM, (2009) A Triple-Emission Fluorescent Probe Reveals Distinctive Amyloid Fibrillar Polymorphism of Wild-Type alpha-Synuclein and Its Familial Parkinson's Disease Mutants. Biochemistry 48: 7465-7472.
    • (2009) Biochemistry , vol.48 , pp. 7465-7472
    • Celej, M.S.1    Caarls, W.2    Demchenko, A.P.3    Jovin, T.M.4
  • 14
    • 1642433249 scopus 로고    scopus 로고
    • High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
    • Jaroniec CP, MacPhee CE, Bajaj VS, McMahon MT, Dobson CM, et al. (2004) High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc Natl Acad Sci USA 101: 711-716.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 711-716
    • Jaroniec, C.P.1    MacPhee, C.E.2    Bajaj, V.S.3    McMahon, M.T.4    Dobson, C.M.5
  • 16
    • 33845334180 scopus 로고    scopus 로고
    • 3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR
    • Iwata K, Fujiwara T, Matsuki Y, Akutsu H, Takahashi S, et al. (2006) 3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR. Proc Natl Acad Sci USA 103: 18119-18124.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18119-18124
    • Iwata, K.1    Fujiwara, T.2    Matsuki, Y.3    Akutsu, H.4    Takahashi, S.5
  • 17
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core
    • Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, et al. (2008) Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 319: 1523-1526.
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5
  • 18
    • 77957324146 scopus 로고    scopus 로고
    • Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy
    • van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, et al. (2010) Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy. J Am Chem Soc 132: 13765-13775.
    • (2010) J Am Chem Soc , vol.132 , pp. 13765-13775
    • van Melckebeke, H.1    Wasmer, C.2    Lange, A.3    Ab, E.4    Loquet, A.5
  • 19
    • 84859514070 scopus 로고    scopus 로고
    • A30P alpha-synuclein adopts the wild-type fibrils structure, despite slower fibrillation kinetics
    • Lemkau LR, Comellas G, Kloepper KD, Woods WS, George JM, et al. (2012) A30P alpha-synuclein adopts the wild-type fibrils structure, despite slower fibrillation kinetics. J Biol Chem 287: 11526-11532.
    • (2012) J Biol Chem , vol.287 , pp. 11526-11532
    • Lemkau, L.R.1    Comellas, G.2    Kloepper, K.D.3    Woods, W.S.4    George, J.M.5
  • 20
    • 51749125627 scopus 로고    scopus 로고
    • Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein
    • Heise H, Celej MS, Becker S, Riede D, Pelah A, et al. (2008) Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-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    Riede, D.4    Pelah, A.5
  • 21
    • 33646878753 scopus 로고    scopus 로고
    • Preparation of alpha-synuclein fibrils for solid-state NMR: Expression, purification, and incubation of wild-type and mutant forms
    • Kloepper KD, Woods WS, Winter KA, George JM, Rienstra CM, (2006) Preparation of alpha-synuclein fibrils for solid-state NMR: Expression, purification, and incubation of wild-type and mutant forms. Protein Expr Purif 48: 112-117.
    • (2006) Protein Expr 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
    • 0001211725 scopus 로고
    • NMR cross-polarization by adiabatic passage through the Hartmann-Hahn condition (APHH)
    • Hediger S, Meier BH, Kurur ND, Bodenhausen G, Ernst RR, (1994) NMR cross-polarization by adiabatic passage through the Hartmann-Hahn condition (APHH). Chem Phys Lett 223: 283-288.
    • (1994) Chem Phys Lett , vol.223 , pp. 283-288
    • Hediger, S.1    Meier, B.H.2    Kurur, N.D.3    Bodenhausen, G.4    Ernst, R.R.5
  • 23
    • 0033629304 scopus 로고    scopus 로고
    • An improved broadband decoupling sequence for liquid crystals and solids
    • Fung BM, Khitrin AK, Ermolaev K, (2000) An improved broadband decoupling sequence for liquid crystals and solids. J Magn Reson 142: 97-101.
    • (2000) J Magn Reson , vol.142 , pp. 97-101
    • Fung, B.M.1    Khitrin, A.K.2    Ermolaev, K.3
  • 24
    • 79953204569 scopus 로고    scopus 로고
    • Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR
    • Comellas G, Lopez JJ, Nieuwkoop AJ, Lemkau LR, Rienstra CM, (2011) Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR. J Magn Reson 209: 131-135.
    • (2011) J Magn Reson , vol.209 , pp. 131-135
    • Comellas, G.1    Lopez, J.J.2    Nieuwkoop, A.J.3    Lemkau, L.R.4    Rienstra, C.M.5
  • 25
    • 0000368822 scopus 로고    scopus 로고
    • Cross polarization in the tilted frame: assignment and spectral simplification in heteronuclear spin systems
    • Baldus M, Petkova AT, Herzfeld J, Griffin RG, (1998) Cross polarization in the tilted frame: assignment and spectral simplification in heteronuclear spin systems. Mol Phys 95: 1197-1207.
    • (1998) Mol Phys , vol.95 , pp. 1197-1207
    • Baldus, M.1    Petkova, A.T.2    Herzfeld, J.3    Griffin, R.G.4
  • 26
    • 0000953276 scopus 로고    scopus 로고
    • C-13-H-1 dipolar-assisted rotational resonance in magic-angle spinning NMR
    • Takegoshi K, Nakamura S, Terao T, (2001) C-13-H-1 dipolar-assisted rotational resonance in magic-angle spinning NMR. Chem Phys Lett 344: 631-637.
    • (2001) Chem Phys Lett , vol.344 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 27
    • 0042995329 scopus 로고    scopus 로고
    • Chemical shift referencing in MAS solid state NMR
    • Morcombe CR, Zilm KW, (2003) Chemical shift referencing in MAS solid state NMR. J Magn Reson 162: 479-486.
    • (2003) J Magn Reson , vol.162 , pp. 479-486
    • Morcombe, C.R.1    Zilm, K.W.2
  • 28
    • 0029400480 scopus 로고
    • Nmrpipe: a Multidimensional Spectral Processing System Based On Unix Pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) Nmrpipe: a Multidimensional Spectral Processing System Based On Unix Pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 29
    • 84874713480 scopus 로고    scopus 로고
    • 8.1.13 ed. Newark: One Moon Scientific, Inc
    • Johnson B (2007) NMRViewJ. 8.1.13 ed. Newark: One Moon Scientific, Inc.
    • (2007) NMRViewJ
    • Johnson, B.1
  • 30
    • 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 alpha-synuclein
    • Li J, Uversky VN, Fink AL, (2001) Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry 40: 11604-11613.
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 31
    • 2942592408 scopus 로고    scopus 로고
    • Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy
    • Hoyer WG, Cherny D, Subramaniam V, Jovin TM, (2004) Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy. J Mol Biol 340: 127-139.
    • (2004) J Mol Biol , vol.340 , pp. 127-139
    • Hoyer, W.G.1    Cherny, D.2    Subramaniam, V.3    Jovin, T.M.4
  • 32
    • 6344228684 scopus 로고    scopus 로고
    • Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein
    • Choi W, Zibaee S, Jakes R, Serpell LC, Davletov B, et al. (2004) Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein. FEBS Lett 576: 363-368.
    • (2004) FEBS Lett , vol.576 , pp. 363-368
    • Choi, W.1    Zibaee, S.2    Jakes, R.3    Serpell, L.C.4    Davletov, B.5
  • 34
    • 33845358566 scopus 로고    scopus 로고
    • Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from alpha-synuclein mutants
    • van Raaij ME, Segers-Nolten IM, Subramaniam V, (2006) Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from alpha-synuclein mutants. Biophysical Journal 91: L96-98.
    • (2006) Biophysical Journal , vol.91
    • van Raaij, M.E.1    Segers-Nolten, I.M.2    Subramaniam, V.3
  • 35
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation
    • Serpell LC, Berriman J, Jakes R, Goedert M, Crowther RA, (2000) Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta 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
  • 36
    • 0026410969 scopus 로고
    • Relationship Between Nuclear-Magnetic-Resonance Chemical-Shift and Protein Secondary Structure
    • Wishart DS, Sykes BD, Richards FM, (1991) Relationship Between Nuclear-Magnetic-Resonance Chemical-Shift and Protein Secondary Structure. J Mol Biol 222: 311-333.
    • (1991) J Mol Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 37
    • 0028673594 scopus 로고
    • Chemical-Shifts as a Tool for Structure Determination
    • Wishart DS, Sykes BD, (1994) Chemical-Shifts as a Tool for Structure Determination. Methods in Enzymol 239: 363-392.
    • (1994) Methods in Enzymol , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 38
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart DS, Sykes BD, (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4: 171-180.
    • (1994) J Biomol NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 39
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G, Delaglio F, Bax A, (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13: 289-302.
    • (1999) J Biomol NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 40
    • 0036025444 scopus 로고    scopus 로고
    • Chemical shifts in amino acids, peptides, and protiens: From Quantum Chemistry to Drug Design
    • Oldfield E, (2002) Chemical shifts in amino acids, peptides, and protiens: From Quantum Chemistry to Drug Design. Ann Rev Phys Chem 53: 349-378.
    • (2002) Ann Rev Phys Chem , vol.53 , pp. 349-378
    • Oldfield, E.1
  • 41
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly
    • Giasson BI, Murray IVJ, Trojanowski JQ, Lee VMY, (2001) A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. J Biol Chem 276: 2380-2386.
    • (2001) J Biol Chem , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.J.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 42
    • 68349093958 scopus 로고    scopus 로고
    • TALOS plus: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen Y, Delaglio F, Cornilescu G, Bax A, (2009) TALOS plus: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44: 213-223.
    • (2009) J Biomol NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 43
    • 75749093356 scopus 로고    scopus 로고
    • Differential Phospholipid Binding of alpha-Synuclein Variants Implicated in Parkinson's Disease Revealed by Solution NMR Spectroscopy
    • Bodner CR, Maltsev AS, Dobson CM, Bax A, (2010) Differential Phospholipid Binding of alpha-Synuclein Variants Implicated in Parkinson's Disease Revealed by Solution NMR Spectroscopy. Biochemistry 49: 862-871.
    • (2010) Biochemistry , vol.49 , pp. 862-871
    • Bodner, C.R.1    Maltsev, A.S.2    Dobson, C.M.3    Bax, A.4
  • 44
    • 84858627029 scopus 로고    scopus 로고
    • Unique structural intermediates during alpha-synuclein fibrillogenesis on phospholipid vesicles
    • Comellas G, Lemkau LR, Zhou DH, George JM, Rienstra CM, (2012) Unique structural intermediates during alpha-synuclein fibrillogenesis on phospholipid vesicles. J Am Chem Soc 134: 5090-5099.
    • (2012) J Am Chem Soc , vol.134 , pp. 5090-5099
    • Comellas, G.1    Lemkau, L.R.2    Zhou, D.H.3    George, J.M.4    Rienstra, C.M.5


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