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Volumn 391, Issue 3, 2010, Pages 1415-1420

Residue Glu83 plays a major role in negatively regulating α-synuclein amyloid formation

Author keywords

Synuclein; Amyloid; Parkinson disease

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; DOPAMINE; EPIGALLOCATECHIN GALLATE; GLUTAMIC ACID;

EID: 73949119538     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.12.079     Document Type: Article
Times cited : (16)

References (58)
  • 1
    • 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. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35 (1996) 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
  • 2
    • 0028985267 scopus 로고
    • The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • Iwai A., Masliah E., Yoshimoto M., Ge N., Flanagan L., De Silva H.A., Kittel A., and Saitoh T. The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 14 (1995) 467-475
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    Ge, N.4    Flanagan, L.5    De Silva, H.A.6    Kittel, A.7    Saitoh, T.8
  • 3
    • 0033215063 scopus 로고    scopus 로고
    • Synucleins in synaptic plasticity and neurodegenerative disorders
    • Clayton D.F., and George J.M. Synucleins in synaptic plasticity and neurodegenerative disorders. J. Neurosci. Res. 58 (1999) 120-129
    • (1999) J. Neurosci. Res. , vol.58 , pp. 120-129
    • Clayton, D.F.1    George, J.M.2
  • 4
    • 2642514788 scopus 로고    scopus 로고
    • Alpha-synuclein: normal function and role in neurodegenerative diseases
    • Norris E.H., Giasson B.I., and Lee V.M. Alpha-synuclein: normal function and role in neurodegenerative diseases. Curr. Top. Dev. Biol. 60 (2004) 17-54
    • (2004) Curr. Top. Dev. Biol. , vol.60 , pp. 17-54
    • Norris, E.H.1    Giasson, B.I.2    Lee, V.M.3
  • 6
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons
    • Murphy D.D., Rueter S.M., Trojanowski J.Q., and Lee V.M.Y. Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J. Neurosci. 20 (2000) 3214-3220
    • (2000) J. Neurosci. , vol.20 , pp. 3214-3220
    • Murphy, D.D.1    Rueter, S.M.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 8
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert M. Alpha-synuclein and neurodegenerative diseases. Nat. Rev. Neurosci. 2 (2001) 492-501
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 492-501
    • Goedert, M.1
  • 10
  • 11
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies
    • Spillantini M.G., Crowther R.A., Jakes R., Cairns N.J., Lantos P.L., and Goedert M. Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies. Neurosci. Lett. 251 (1998) 205-208
    • (1998) Neurosci. Lett. , vol.251 , pp. 205-208
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Cairns, N.J.4    Lantos, P.L.5    Goedert, M.6
  • 18
    • 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 L.C., Davletov B., Crowther R.A., and Goedert M. Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein. FEBS Lett. 576 (2004) 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    Crowther, R.A.6    Goedert, M.7
  • 19
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • Conway K.A., Harper J.D., and Lansbury P.T. Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat. Med. 4 (1998) 1318-1320
    • (1998) Nat. Med. , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 20
    • 0033583215 scopus 로고    scopus 로고
    • Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro
    • Giasson B.I., Uryu K., Trojanowski J.Q., and Lee V.M.Y. Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem. 274 (1999) 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.Y.4
  • 22
    • 0037469147 scopus 로고    scopus 로고
    • The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation
    • Kessler J.C., Rochet J.C., and Lansbury Jr. P.T. The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation. Biochemistry 42 (2003) 672-678
    • (2003) Biochemistry , vol.42 , pp. 672-678
    • Kessler, J.C.1    Rochet, J.C.2    Lansbury Jr., P.T.3
  • 25
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation
    • Serpell L.C., Berriman J., Jakes R., Goedert M., and Crowther R.A. Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc. Natl. Acad. Sci. USA 97 (2000) 4897-4902
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 26
    • 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 B.I., Murray I.V., Trojanowski J.Q., and Lee V.M.Y. A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. J. Biol. Chem. 276 (2001) 2380-2386
    • (2001) J. Biol. Chem. , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 27
    • 70350041314 scopus 로고    scopus 로고
    • Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization
    • Waxman E.A., Mazzulli J.R., and Giasson B.I. Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization. Biochemistry 48 (2009) 9227-9436
    • (2009) Biochemistry , vol.48 , pp. 9227-9436
    • Waxman, E.A.1    Mazzulli, J.R.2    Giasson, B.I.3
  • 30
    • 0042848693 scopus 로고    scopus 로고
    • A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein
    • Du H.N., Tang L., Luo X.Y., Li H.T., Hu J., Zhou J.W., and Hu H.Y. A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein. Biochemistry 42 (2003) 8870-8878
    • (2003) Biochemistry , vol.42 , pp. 8870-8878
    • Du, H.N.1    Tang, L.2    Luo, X.Y.3    Li, H.T.4    Hu, J.5    Zhou, J.W.6    Hu, H.Y.7
  • 32
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • Conway K.A., Harper J.D., and Lansbury P.T. Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 39 (2000) 2552-2563
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 34
    • 20444401187 scopus 로고    scopus 로고
    • Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations
    • Norris E.H., Giasson B.I., Hodara R., Xu S., Trojanowski J.Q., Ischiropoulos H., and Lee V.M. Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations. J. Biol. Chem. 280 (2005) 21212-21219
    • (2005) J. Biol. Chem. , vol.280 , pp. 21212-21219
    • Norris, E.H.1    Giasson, B.I.2    Hodara, R.3    Xu, S.4    Trojanowski, J.Q.5    Ischiropoulos, H.6    Lee, V.M.7
  • 35
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway K.A., Rochet J.C., Bieganski R.M., and Lansbury Jr. P.T. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294 (2001) 1346-1349
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 36
    • 54849423681 scopus 로고    scopus 로고
    • Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region
    • Herrera F.E., Chesi A., Paleologou K.E., Schmid A., Munoz A., Vendruscolo M., Gustincich S., Lashuel H.A., and Carloni P. Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region. PLoS One 3 (2008) e3394
    • (2008) PLoS One , vol.3
    • Herrera, F.E.1    Chesi, A.2    Paleologou, K.E.3    Schmid, A.4    Munoz, A.5    Vendruscolo, M.6    Gustincich, S.7    Lashuel, H.A.8    Carloni, P.9
  • 37
    • 3042547187 scopus 로고    scopus 로고
    • The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils
    • Zhu M., Rajamani S., Kaylor J., Han S., Zhou F., and Fink A.L. The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils. J. Biol. Chem. 279 (2004) 26846-26857
    • (2004) J. Biol. Chem. , vol.279 , pp. 26846-26857
    • Zhu, M.1    Rajamani, S.2    Kaylor, J.3    Han, S.4    Zhou, F.5    Fink, A.L.6
  • 39
    • 52049098478 scopus 로고    scopus 로고
    • Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein
    • Hong D.P., Fink A.L., and Uversky V.N. Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein. J. Mol. Biol. 383 (2008) 214-223
    • (2008) J. Mol. Biol. , vol.383 , pp. 214-223
    • Hong, D.P.1    Fink, A.L.2    Uversky, V.N.3
  • 41
    • 0037166267 scopus 로고    scopus 로고
    • Biochemical characterization of the core structure of alpha-synuclein filaments
    • Miake H., Mizusawa H., Iwatsubo T., and Hasegawa M. Biochemical characterization of the core structure of alpha-synuclein filaments. J. Biol. Chem. 277 (2002) 19213-19219
    • (2002) J. Biol. Chem. , vol.277 , pp. 19213-19219
    • Miake, H.1    Mizusawa, H.2    Iwatsubo, T.3    Hasegawa, M.4
  • 42
    • 39749133508 scopus 로고    scopus 로고
    • Sequence determinants regulating fibrillation of human alpha-synuclein
    • Koo H.J., Lee H.J., and Im H. Sequence determinants regulating fibrillation of human alpha-synuclein. Biochem. Biophys. Res. Commun. 368 (2008) 772-778
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 772-778
    • Koo, H.J.1    Lee, H.J.2    Im, H.3
  • 43
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis
    • Glenner G.G. Amyloid deposits and amyloidosis. N. Engl. J. Med. 302 (1980) 1283-1292
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 44
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
    • Naiki H., Higuchi K., Hosokawa M., and Takeda T. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal. Biochem. 177 (1989) 244-249
    • (1989) Anal. Biochem. , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 45
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution
    • Levine III H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 (1993) 404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Levine III, H.1
  • 46
    • 0032867537 scopus 로고    scopus 로고
    • Screening for pharmacologic inhibitors of amyloid fibril formation
    • Levine III H., and Scholten J.D. Screening for pharmacologic inhibitors of amyloid fibril formation. Methods Enzymol. 309 (1999) 467-476
    • (1999) Methods Enzymol. , vol.309 , pp. 467-476
    • Levine III, H.1    Scholten, J.D.2
  • 47
    • 0024352110 scopus 로고
    • Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk W.E., Pettegrew J.W., and Abraham D.J. Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 37 (1989) 1273-1281
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 49
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes E.D., and Glenner G.G. X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16 (1968) 673-677
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 50
    • 0031960745 scopus 로고    scopus 로고
    • A model for structure-dependent binding of Congo red to Alzheimer beta-amyloid fibrils
    • Carter D.B., and Chou K.C. A model for structure-dependent binding of Congo red to Alzheimer beta-amyloid fibrils. Neurobiol. Aging 19 (1998) 37-40
    • (1998) Neurobiol. Aging , vol.19 , pp. 37-40
    • Carter, D.B.1    Chou, K.C.2
  • 51
    • 0029083059 scopus 로고
    • Chrysamine-G binding to Alzheimer and control brain: autopsy study of a new amyloid probe
    • Klunk W.E., Debnath M.L., and Pettegrew J.W. Chrysamine-G binding to Alzheimer and control brain: autopsy study of a new amyloid probe. Neurobiol. Aging 16 (1995) 541-548
    • (1995) Neurobiol. Aging , vol.16 , pp. 541-548
    • Klunk, W.E.1    Debnath, M.L.2    Pettegrew, J.W.3
  • 52
    • 69249141470 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the flavonoid-induced inhibition of alpha-synuclein fibrillation
    • Meng X., Munishkina L.A., Fink A.L., and Uversky V.N. Molecular mechanisms underlying the flavonoid-induced inhibition of alpha-synuclein fibrillation. Biochemistry 48 (2009) 8206-8224
    • (2009) Biochemistry , vol.48 , pp. 8206-8224
    • Meng, X.1    Munishkina, L.A.2    Fink, A.L.3    Uversky, V.N.4
  • 53
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou P.Y., and Fasman G.D. Prediction of protein conformation. Biochemistry 13 (1974) 222-245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 54
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • Chou P.Y., and Fasman G.D. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry 13 (1974) 211-222
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 55
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    • Pawar A.P., Dubay K.F., Zurdo J., Chiti F., Vendruscolo M., and Dobson C.M. Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350 (2005) 379-392
    • (2005) J. Mol. Biol. , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 56
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti F., Stefani M., Taddei N., Ramponi G., and Dobson C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424 (2003) 805-808
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 57
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: the importance of being unfolded
    • Uversky V.N., and Fink A.L. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 1698 (2004) 131-153
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2


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