메뉴 건너뛰기




Volumn 3, Issue 3, 2013, Pages 703-732

Biophysical characterization of α-synuclein and rotenone interaction

Author keywords

Agrochemical; Environmental toxin; Fibrillation; Intrinsically disordered protein; Misfolding; Parkinson's disease; Pesticide; Rotenone; synuclein

Indexed keywords

ALPHA SYNUCLEIN; ROTENONE;

EID: 85019505446     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom3030703     Document Type: Article
Times cited : (28)

References (124)
  • 1
    • 25844524877 scopus 로고    scopus 로고
    • Neurodegenerative diseases: An overview of environmental risk factors
    • Brown, R.C.; Lockwood, A.H.; Sonawane, B.R. Neurodegenerative diseases: An overview of environmental risk factors. Environ. Health Perspect. 2005, 113, 1250-1256.
    • (2005) Environ. Health Perspect , vol.113 , pp. 1250-1256
    • Brown, R.C.1    Lockwood, A.H.2    Sonawane, B.R.3
  • 2
    • 34548819028 scopus 로고    scopus 로고
    • The economic impact of Parkinson's disease
    • Findley, L.J. The economic impact of Parkinson's disease. Parkinsonism Relat. Disord. 2007, 13, S8-S12.
    • (2007) Parkinsonism Relat. Disord , vol.13
    • Findley, L.J.1
  • 3
    • 67249152339 scopus 로고    scopus 로고
    • Neuropathology and neurochemistry of Parkinson's disease: The never-ending story or the story with no beginning?
    • Uversky, V.N. Neuropathology and neurochemistry of Parkinson's disease: The never-ending story or the story with no beginning? Minerva Psichiatr. 2009, 50, 1-26.
    • (2009) Minerva Psichiatr , vol.50 , pp. 1-26
    • Uversky, V.N.1
  • 4
    • 5444248216 scopus 로고    scopus 로고
    • Biophysical Properties of Human Alpha-Synuclein and its Role in Parkinson's Disease
    • Pandalai, S.G., Ed.; Transworld Research Network: Kerala, India
    • Uversky, V.N.; Fink, A.L. Biophysical Properties of Human Alpha-Synuclein and its Role in Parkinson's Disease. In Recent Research Developments in Proteins; Pandalai, S.G., Ed.; Transworld Research Network: Kerala, India, 2002; pp. 153-186.
    • (2002) Recent Research Developments In Proteins , pp. 153-186
    • Uversky, V.N.1    Fink, A.L.2
  • 5
    • 0029937494 scopus 로고    scopus 로고
    • Epidemiology of Parkinson's disease
    • Tanner, C.M.; Goldman, S.M. Epidemiology of Parkinson's disease. Neurol. Clin. 1996, 14, 317-335.
    • (1996) Neurol. Clin , vol.14 , pp. 317-335
    • Tanner, C.M.1    Goldman, S.M.2
  • 6
    • 0005444118 scopus 로고
    • Parkinson's disease in a chemist working with 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine
    • Langston, J.W.; Ballard, P.A., Jr. Parkinson's disease in a chemist working with 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine. N. Engl. J. Med. 1983, 309, 310.
    • (1983) N. Engl. J. Med , vol.309 , pp. 310
    • Langston, J.W.1    Ballard Jr., P.A.2
  • 7
    • 0020680904 scopus 로고
    • Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston, J.W.; Ballard, P.; Tetrud, J.W.; Irwin, I. Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 1983, 219, 979-980.
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 8
    • 0000412998 scopus 로고
    • Cohort analysis of Parkinson's syndrome: Evidence for a single etiology related to subclinical infection about 1920
    • Poskanzer, D.C.; Schwab, R.S. Cohort analysis of Parkinson's syndrome: Evidence for a single etiology related to subclinical infection about 1920. J. Chron. Dis. 1963, 16, 961-973.
    • (1963) J. Chron. Dis , vol.16 , pp. 961-973
    • Poskanzer, D.C.1    Schwab, R.S.2
  • 12
    • 42349111633 scopus 로고    scopus 로고
    • Characterization of alpha-synuclein interactions with selected aggregation-inhibiting small molecules
    • Rao, J.N.; Dua, V.; Ulmer, T.S. Characterization of alpha-synuclein interactions with selected aggregation-inhibiting small molecules. Biochemistry 2008, 47, 4651-4656.
    • (2008) Biochemistry , vol.47 , pp. 4651-4656
    • Rao, J.N.1    Dua, V.2    Ulmer, T.S.3
  • 14
    • 34547174917 scopus 로고    scopus 로고
    • Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins
    • Munishkina, L.A.; Fink, A.L. Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins. Biochim. Biophys. Acta 2007, 1768, 1862-1885.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1862-1885
    • Munishkina, L.A.1    Fink, A.L.2
  • 15
    • 0038727850 scopus 로고    scopus 로고
    • Parkinson's disease and related alpha-synucleinopathies are brain amyloidoses
    • Trojanowski, J.Q.; Lee, V.M. Parkinson's disease and related alpha-synucleinopathies are brain amyloidoses. Ann. N. Y. Acad. Sci. 2003, 991, 107-110.
    • (2003) Ann. N. Y. Acad. Sci , vol.991 , pp. 107-110
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 16
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M.; Dobson, C.M. Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. (Berl.) 2003, 81, 678-699.
    • (2003) J. Mol. Med. (Berl.) , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 18
    • 69149103558 scopus 로고    scopus 로고
    • Intrinsic disorder in proteins associated with neurodegenerative diseases
    • Uversky, V.N. Intrinsic disorder in proteins associated with neurodegenerative diseases. Front. Biosci. 2009, 14, 5188-5238.
    • (2009) Front. Biosci , vol.14 , pp. 5188-5238
    • Uversky, V.N.1
  • 20
    • 0031941058 scopus 로고    scopus 로고
    • Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies
    • Baba, M.; Nakajo, S.; Tu, P.H.; Tomita, T.; Nakaya, K.; Lee, V.M.; Trojanowski, J.Q.; Iwatsubo, T. Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. Am. J. Pathol. 1998, 152, 879-884.
    • (1998) Am. J. Pathol , vol.152 , pp. 879-884
    • Baba, M.1    Nakajo, S.2    Tu, P.H.3    Tomita, T.4    Nakaya, K.5    Lee, V.M.6    Trojanowski, J.Q.7    Iwatsubo, T.8
  • 27
    • 84940364788 scopus 로고    scopus 로고
    • Alpha-synuclein and the Lewy body disorders
    • Dickson, D.W. Alpha-synuclein and the Lewy body disorders. Curr. Opin. Neurol. 2001, 14, 423-432.
    • (2001) Curr. Opin. Neurol , vol.14 , pp. 423-432
    • Dickson, D.W.1
  • 28
    • 0035031135 scopus 로고    scopus 로고
    • Parkinson's disease and other alpha-synucleinopathies
    • Goedert, M. Parkinson's disease and other alpha-synucleinopathies. Clin. Chem. Lab. Med. 2001, 39, 308-312.
    • (2001) Clin. Chem. Lab. Med , vol.39 , pp. 308-312
    • Goedert, M.1
  • 29
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert, M. Alpha-synuclein and neurodegenerative diseases. Nat. Rev. Neurosci. 2001, 2, 492-501.
    • (2001) Nat. Rev. Neurosci , vol.2 , pp. 492-501
    • Goedert, M.1
  • 31
    • 0031910093 scopus 로고    scopus 로고
    • Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: Implications for the pathogenesis of Parkinson disease and Lewy body dementia
    • Trojanowski, J.Q.; Lee, V.M. Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: Implications for the pathogenesis of Parkinson disease and Lewy body dementia. Arch. Neurol. 1998, 55, 151-152.
    • (1998) Arch. Neurol , vol.55 , pp. 151-152
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 32
    • 34548620297 scopus 로고    scopus 로고
    • Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation
    • Uversky, V.N. Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation. J. Neurochem. 2007, 103, 17-37.
    • (2007) J. Neurochem , vol.103 , pp. 17-37
    • Uversky, V.N.1
  • 33
    • 70349503591 scopus 로고    scopus 로고
    • Biophysics of Parkinson's disease: Structure and aggregation of alpha-synuclein
    • Uversky, V.N.; Eliezer, D. Biophysics of Parkinson's disease: Structure and aggregation of alpha-synuclein. Curr. Protein Pept. Sci. 2009, 10, 483-499.
    • (2009) Curr. Protein Pept. Sci , vol.10 , pp. 483-499
    • Uversky, V.N.1    Eliezer, D.2
  • 34
    • 77956072590 scopus 로고    scopus 로고
    • Metalloproteomics and metal toxicology of alpha-synuclein
    • Santner, A.; Uversky, V.N. Metalloproteomics and metal toxicology of alpha-synuclein. Metallomics 2010, 2, 378-392.
    • (2010) Metallomics , vol.2 , pp. 378-392
    • Santner, A.1    Uversky, V.N.2
  • 35
    • 83455202793 scopus 로고    scopus 로고
    • Alpha-synuclein misfolding and Parkinson's disease
    • Breydo, L.; Wu, J.W.; Uversky, V.N. Alpha-synuclein misfolding and Parkinson's disease. Biochim. Biophys. Acta 2012, 1822, 261-285.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 261-285
    • Breydo, L.1    Wu, J.W.2    Uversky, V.N.3
  • 36
    • 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.; Goedert, M. Alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. Proc. Natl. Acad. Sci. USA 1998, 95, 6469-6473.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 37
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • Masliah, E.; Rockenstein, E.; Veinbergs, I.; Mallory, M.; Hashimoto, M.; Takeda, A.; Sagara, Y.; Sisk, A.; Mucke, L. Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders. Science 2000, 287, 1265-1269.
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6    Sagara, Y.7    Sisk, A.8    Mucke, L.9
  • 38
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany, M.B.; Bender, W.W. A Drosophila model of Parkinson's disease. Nature 2000, 404, 394-398.
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 39
    • 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.; Lee, V.M. Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem. 1999, 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
  • 40
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • Uversky, V.N.; Li, J.; Fink, A.L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem. 2001, 276, 10737-10744.
    • (2001) J. Biol. Chem , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 41
    • 5444255433 scopus 로고    scopus 로고
    • Neurotoxicant-induced animal models of Parkinson's disease: Understanding the role of rotenone, maneb and paraquat in neurodegeneration
    • Uversky, V.N. Neurotoxicant-induced animal models of Parkinson's disease: Understanding the role of rotenone, maneb and paraquat in neurodegeneration. Cell Tissue Res. 2004, 318, 225-241.
    • (2004) Cell Tissue Res , vol.318 , pp. 225-241
    • Uversky, V.N.1
  • 43
    • 0024546234 scopus 로고
    • The role of environmental toxins in the etiology of Parkinson's disease
    • Tanner, C.M. The role of environmental toxins in the etiology of Parkinson's disease. Trends Neurosci. 1989, 12, 49-54.
    • (1989) Trends Neurosci , vol.12 , pp. 49-54
    • Tanner, C.M.1
  • 44
    • 0042521076 scopus 로고    scopus 로고
    • The environment and Parkinson's disease: Is the nigrostriatal system preferentially targeted by neurotoxins?
    • Di Monte, D.A. The environment and Parkinson's disease: Is the nigrostriatal system preferentially targeted by neurotoxins? Lancet Neurol. 2003, 2, 531-538.
    • (2003) Lancet Neurol , vol.2 , pp. 531-538
    • Di, M.D.A.1
  • 45
  • 46
  • 47
    • 0037127197 scopus 로고    scopus 로고
    • The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: Paraquat and alpha-synuclein
    • Manning-Bog, A.B.; McCormack, A.L.; Li, J.; Uversky, V.N.; Fink, A.L.; Di Monte, D.A. The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: Paraquat and alpha-synuclein. J. Biol. Chem. 2002, 277, 1641-1644.
    • (2002) J. Biol. Chem , vol.277 , pp. 1641-1644
    • Manning-Bog, A.B.1    McCormack, A.L.2    Li, J.3    Uversky, V.N.4    Fink, A.L.5    Di Monte, D.A.6
  • 49
    • 0035690443 scopus 로고    scopus 로고
    • Current evidence for neuroprotective effects of nicotine and caffeine against Parkinson's disease
    • Ross, G.W.; Petrovitch, H. Current evidence for neuroprotective effects of nicotine and caffeine against Parkinson's disease. Drugs Aging 2001, 18, 797-806.
    • (2001) Drugs Aging , vol.18 , pp. 797-806
    • Ross, G.W.1    Petrovitch, H.2
  • 51
    • 0026034279 scopus 로고
    • Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: An X-ray microanalysis
    • Hirsch, E.C.; Brandel, J.P.; Galle, P.; Javoy-Agid, F.; Agid, Y. Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: An X-ray microanalysis. J. Neurochem. 1991, 56, 446-451.
    • (1991) J Neurochem , vol.56 , pp. 446-451
    • Hirsch, E.C.1    Brandel, J.P.2    Galle, P.3    Javoy-Agid, F.4    Agid, Y.5
  • 52
    • 0026454505 scopus 로고
    • Calcium, magnesium and aluminum concentrations in Parkinson's disease
    • Yasui, M.; Kihira, T.; Ota, K. Calcium, magnesium and aluminum concentrations in Parkinson's disease. Neurotoxicology 1992, 13, 593-600.
    • (1992) Neurotoxicology , vol.13 , pp. 593-600
    • Yasui, M.1    Kihira, T.2    Ota, K.3
  • 53
    • 0026746512 scopus 로고
    • Neuromelanin-containing neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: A LAMMA study
    • Good, P.F.; Olanow, C.W.; Perl, D.P. Neuromelanin-containing neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: A LAMMA study. Brain Res. 1992, 593, 343-346.
    • (1992) Brain Res , vol.593 , pp. 343-346
    • Good, P.F.1    Olanow, C.W.2    Perl, D.P.3
  • 56
    • 0033153770 scopus 로고    scopus 로고
    • Aluminum-containing antacids as a cause of idiopathic Parkinson's disease
    • Altschuler, E. Aluminum-containing antacids as a cause of idiopathic Parkinson's disease. Med. Hypotheses 1999, 53, 22-23.
    • (1999) Med. Hypotheses , vol.53 , pp. 22-23
    • Altschuler, E.1
  • 57
    • 0030012558 scopus 로고    scopus 로고
    • Possible environmental, occupational, and other etiologic factors for Parkinson's disease: A case-control study in Germany
    • Seidler, A.; Hellenbrand, W.; Robra, B.P.; Vieregge, P.; Nischan, P.; Joerg, J.; Oertel, W.H.; Ulm, G.; Schneider, E. Possible environmental, occupational, and other etiologic factors for Parkinson's disease: A case-control study in Germany. Neurology 1996, 46, 1275-1284.
    • (1996) Neurology , vol.46 , pp. 1275-1284
    • Seidler, A.1    Hellenbrand, W.2    Robra, B.P.3    Vieregge, P.4    Nischan, P.5    Joerg, J.6    Oertel, W.H.7    Ulm, G.8    Schneider, E.9
  • 58
    • 0033436303 scopus 로고    scopus 로고
    • Parkinsonism from methanol poisoning: Benefit from treatment with anti-Parkinson drugs
    • Davis, L.E.; Adair, J.C. Parkinsonism from methanol poisoning: Benefit from treatment with anti-Parkinson drugs. Mov. Disord. 1999, 14, 520-522.
    • (1999) Mov. Disord , vol.14 , pp. 520-522
    • Davis, L.E.1    Adair, J.C.2
  • 59
    • 0032895184 scopus 로고    scopus 로고
    • Parkinsonism, pyramidal signs, polyneuropathy, and cognitive decline after long-term occupational solvent exposure
    • Hageman, G.; van der Hoek, J.; van Hout, M.; van der Laan, G.; Steur, E.J.; de Bruin, W.; Herholz, K. Parkinsonism, pyramidal signs, polyneuropathy, and cognitive decline after long-term occupational solvent exposure. J. Neurol. 1999, 246, 198-206.
    • (1999) J. Neurol , vol.246 , pp. 198-206
    • Hageman, G.1    van der Hoek, J.2    van Hout, M.3    van der Laan, G.4    Steur, E.J.5    de Bruin, W.6    Herholz, K.7
  • 62
    • 0020037126 scopus 로고
    • A pure parkinsonian syndrome following acute carbon monoxide intoxication
    • Klawans, H.L.; Stein, R.W.; Tanner, C.M.; Goetz, C.G. A pure parkinsonian syndrome following acute carbon monoxide intoxication. Arch. Neurol. 1982, 39, 302-304.
    • (1982) Arch. Neurol , vol.39 , pp. 302-304
    • Klawans, H.L.1    Stein, R.W.2    Tanner, C.M.3    Goetz, C.G.4
  • 63
    • 0031843721 scopus 로고    scopus 로고
    • The risk of Parkinson's disease with exposure to pesticides, farming, well water, and rural living
    • Gorell, J.M.; Johnson, C.C.; Rybicki, B.A.; Peterson, E.L.; Richardson, R.J. The risk of Parkinson's disease with exposure to pesticides, farming, well water, and rural living. Neurology 1998, 50, 1346-1350.
    • (1998) Neurology , vol.50 , pp. 1346-1350
    • Gorell, J.M.1    Johnson, C.C.2    Rybicki, B.A.3    Peterson, E.L.4    Richardson, R.J.5
  • 64
    • 0032924712 scopus 로고    scopus 로고
    • Nutritional and occupational factors influencing the risk of Parkinson's disease: A case-control study in southeastern Sweden
    • Fall, P.A.; Fredrikson, M.; Axelson, O.; Granerus, A.K. Nutritional and occupational factors influencing the risk of Parkinson's disease: A case-control study in southeastern Sweden. Mov. Disord. 1999, 14, 28-37.
    • (1999) Mov. Disord , vol.14 , pp. 28-37
    • Fall, P.A.1    Fredrikson, M.2    Axelson, O.3    Granerus, A.K.4
  • 65
    • 0027256104 scopus 로고
    • Parkinson's disease: A test of the multifactorial etiologic hypothesis
    • Semchuk, K.M.; Love, E.J.; Lee, R.G. Parkinson's disease: A test of the multifactorial etiologic hypothesis. Neurology 1993, 43, 1173-1180.
    • (1993) Neurology , vol.43 , pp. 1173-1180
    • Semchuk, K.M.1    Love, E.J.2    Lee, R.G.3
  • 66
    • 0026711037 scopus 로고
    • Parkinson's disease and exposure to agricultural work and pesticide chemicals
    • Semchuk, K.M.; Love, E.J.; Lee, R.G. Parkinson's disease and exposure to agricultural work and pesticide chemicals. Neurology 1992, 42, 1328-1335.
    • (1992) Neurology , vol.42 , pp. 1328-1335
    • Semchuk, K.M.1    Love, E.J.2    Lee, R.G.3
  • 67
    • 0030878320 scopus 로고    scopus 로고
    • Environmental risk factors and Parkinson's disease: A case-control study in Taiwan
    • Liou, H.H.; Tsai, M.C.; Chen, C.J.; Jeng, J.S.; Chang, Y.C.; Chen, S.Y.; Chen, R.C. Environmental risk factors and Parkinson's disease: A case-control study in Taiwan. Neurology 1997, 48, 1583-1588.
    • (1997) Neurology , vol.48 , pp. 1583-1588
    • Liou, H.H.1    Tsai, M.C.2    Chen, C.J.3    Jeng, J.S.4    Chang, Y.C.5    Chen, S.Y.6    Chen, R.C.7
  • 69
    • 0036777847 scopus 로고    scopus 로고
    • Synergistic effects of pesticides and metals on the fibrillation of alpha-synuclein: Implications for Parkinson's disease
    • Uversky, V.N.; Li, J.; Bower, K.; Fink, A.L. Synergistic effects of pesticides and metals on the fibrillation of alpha-synuclein: Implications for Parkinson's disease. Neurotoxicology 2002, 23, 527-536.
    • (2002) Neurotoxicology , vol.23 , pp. 527-536
    • Uversky, V.N.1    Li, J.2    Bower, K.3    Fink, A.L.4
  • 70
    • 0035816404 scopus 로고    scopus 로고
    • Pesticides directly accelerate the rate of alpha-synuclein fibril formation: A possible factor in Parkinson's disease
    • Uversky, V.N.; Li, J.; Fink, A.L. Pesticides directly accelerate the rate of alpha-synuclein fibril formation: A possible factor in Parkinson's disease. FEBS Lett. 2001, 500, 105-108.
    • (2001) FEBS Lett , vol.500 , pp. 105-108
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 71
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky, V.N.; Fink, A.L. Conformational constraints for amyloid fibrillation: The importance of being unfolded. Biochim. Biophys. Acta 2004, 1698, 131-153.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 72
    • 77954358960 scopus 로고    scopus 로고
    • Mysterious oligomerization of the amyloidogenic proteins
    • Uversky, V.N. Mysterious oligomerization of the amyloidogenic proteins. FEBS J. 2010, 277, 2940-2953.
    • (2010) FEBS J , vol.277 , pp. 2940-2953
    • Uversky, V.N.1
  • 73
    • 0038404977 scopus 로고    scopus 로고
    • Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers
    • Yamin, G.; Uversky, V.N.; Fink, A.L. Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers. FEBS Lett. 2003, 542, 147-152.
    • (2003) FEBS Lett , vol.542 , pp. 147-152
    • Yamin, G.1    Uversky, V.N.2    Fink, A.L.3
  • 74
    • 52049098478 scopus 로고    scopus 로고
    • Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein
    • Hong, D.P.; Fink, A.L.; Uversky, V.N. Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein. J. Mol. Biol. 2008, 383, 214-223.
    • (2008) J. Mol. Biol , vol.383 , pp. 214-223
    • Hong, D.P.1    Fink, A.L.2    Uversky, V.N.3
  • 75
    • 58149199681 scopus 로고    scopus 로고
    • Smoking and Parkinson's disease: Does nicotine affect alpha-synuclein fibrillation?
    • Hong, D.P.; Fink, A.L.; Uversky, V.N. Smoking and Parkinson's disease: Does nicotine affect alpha-synuclein fibrillation? Biochim. Biophys. Acta 2009, 1794, 282-290.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 282-290
    • Hong, D.P.1    Fink, A.L.2    Uversky, V.N.3
  • 76
    • 69249141470 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the flavonoid-induced inhibition of alpha-synuclein fibrillation
    • Meng, X.; Munishkina, L.A.; Fink, A.L.; Uversky, V.N. Molecular mechanisms underlying the flavonoid-induced inhibition of alpha-synuclein fibrillation. Biochemistry 2009, 48, 8206-8224.
    • (2009) Biochemistry , vol.48 , pp. 8206-8224
    • Meng, X.1    Munishkina, L.A.2    Fink, A.L.3    Uversky, V.N.4
  • 77
    • 64649090221 scopus 로고    scopus 로고
    • At low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to alpha-synuclein and prevents its fibrillation
    • Zhou, W.; Gallagher, A.; Hong, D.P.; Long, C.; Fink, A.L.; Uversky, V.N. At low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to alpha-synuclein and prevents its fibrillation. J. Mol. Biol. 2009, 388, 597-610.
    • (2009) J. Mol. Biol , vol.388 , pp. 597-610
    • Zhou, W.1    Gallagher, A.2    Hong, D.P.3    Long, C.4    Fink, A.L.5    Uversky, V.N.6
  • 78
    • 79951638042 scopus 로고    scopus 로고
    • Characterization of the non-fibrillar alpha-synuclein oligomers
    • Hong, D.P.; Han, S.; Fink, A.L.; Uversky, V.N. Characterization of the non-fibrillar alpha-synuclein oligomers. Protein Pept. Lett. 2011, 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
  • 79
    • 74849125564 scopus 로고    scopus 로고
    • Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions
    • Zhou, W.; Long, C.; Reaney, S.H.; di Monte, D.A.; Fink, A.L.; Uversky, V.N. Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions. Biochim. Biophys. Acta 2010, 1802, 322-330.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 322-330
    • Zhou, W.1    Long, C.2    Reaney, S.H.3    di Monte, D.A.4    Fink, A.L.5    Uversky, V.N.6
  • 82
    • 1242271236 scopus 로고    scopus 로고
    • Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
    • Militello, V.; Casarino, C.; Emanuele, A.; Giostra, A.; Pullara, F.; Leone, M. Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Biophys. Chem. 2004, 107, 175-187.
    • (2004) Biophys. Chem , vol.107 , pp. 175-187
    • Militello, V.1    Casarino, C.2    Emanuele, A.3    Giostra, A.4    Pullara, F.5    Leone, M.6
  • 83
    • 67149087384 scopus 로고    scopus 로고
    • Accelerated fibrillation of alpha-synuclein induced by the combined action of macromolecular crowding and factors inducing partial folding
    • Munishkina, L.A.; Fink, A.L.; Uversky, V.N. Accelerated fibrillation of alpha-synuclein induced by the combined action of macromolecular crowding and factors inducing partial folding. Curr. Alzheimer Res. 2009, 6, 252-260.
    • (2009) Curr. Alzheimer Res , vol.6 , pp. 252-260
    • Munishkina, L.A.1    Fink, A.L.2    Uversky, V.N.3
  • 84
    • 84881029374 scopus 로고    scopus 로고
    • Agrochemicals, alpha-synuclein, and Parkinson's disease
    • Silva, B.A.; Breydo, L.; Fink, A.L.; Uversky, V.N. Agrochemicals, alpha-synuclein, and Parkinson's disease. Mol. Neurobiol. 2013, 47, 598-612.
    • (2013) Mol. Neurobiol , vol.47 , pp. 598-612
    • Silva, B.A.1    Breydo, L.2    Fink, A.L.3    Uversky, V.N.4
  • 85
    • 0037186773 scopus 로고    scopus 로고
    • Chlorpyrifos targets developing glia: Effects on glial fibrillary acidic protein
    • Garcia, S.J.; Seidler, F.J.; Qiao, D.; Slotkin, T.A. Chlorpyrifos targets developing glia: Effects on glial fibrillary acidic protein. Brain Res. Dev. Brain Res. 2002, 133, 151-161.
    • (2002) Brain Res. Dev. Brain Res , vol.133 , pp. 151-161
    • Garcia, S.J.1    Seidler, F.J.2    Qiao, D.3    Slotkin, T.A.4
  • 86
    • 27244437782 scopus 로고    scopus 로고
    • Effect of metals on herbicides-alpha-synuclein association: A possible factor in neurodegenerative disease studied by capillary electrophoresis
    • Andre, C.; Truong, T.T.; Robert, J.F.; Guillaume, Y.C. Effect of metals on herbicides-alpha-synuclein association: A possible factor in neurodegenerative disease studied by capillary electrophoresis. Electrophoresis 2005, 26, 3256-3264.
    • (2005) Electrophoresis , vol.26 , pp. 3256-3264
    • Andre, C.1    Truong, T.T.2    Robert, J.F.3    Guillaume, Y.C.4
  • 87
    • 0034088395 scopus 로고    scopus 로고
    • Parkinson's disease mortality and pesticide exposure in California 1984-1994
    • Ritz, B.; Yu, F. Parkinson's disease mortality and pesticide exposure in California 1984-1994. Int. J. Epidemiol. 2000, 29, 323-329.
    • (2000) Int. J. Epidemiol , vol.29 , pp. 323-329
    • Ritz, B.1    Yu, F.2
  • 90
    • 0032831759 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in analysis of protein deposits
    • Seshadri, S.; Khurana, R.; Fink, A.L. Fourier transform infrared spectroscopy in analysis of protein deposits. Methods Enzymol. 1999, 309, 559-576.
    • (1999) Methods Enzymol , vol.309 , pp. 559-576
    • Seshadri, S.1    Khurana, R.2    Fink, A.L.3
  • 91
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth, A.; Zscherp, C. What vibrations tell us about proteins. Q Rev. Biophys. 2002, 35, 369-430.
    • (2002) Q Rev. Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 92
    • 0032818805 scopus 로고    scopus 로고
    • FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media
    • Haris, P.I.; Severcan, F. FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. J. Mol. Catal. B Enzym. 1999, 7, 207-221.
    • (1999) J. Mol. Catal. B Enzym , vol.7 , pp. 207-221
    • Haris, P.I.1    Severcan, F.2
  • 93
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • Barth, A. The infrared absorption of amino acid side chains. Progr. Biophys. Mol. Biol. 2000, 74, 141-173.
    • (2000) Progr. Biophys. Mol. Biol , vol.74 , pp. 141-173
    • Barth, A.1
  • 94
    • 0027752676 scopus 로고
    • Solvent influence on the conformation of cyclosporin. An FT-IR study
    • Shaw, R.A.; Mantsch, H.H. Solvent influence on the conformation of cyclosporin. An FT-IR study. Can. J. Chem. 1993, 7, 1334-1339.
    • (1993) Can. J. Chem , vol.7 , pp. 1334-1339
    • Shaw, R.A.1    Mantsch, H.H.2
  • 95
    • 0023776215 scopus 로고
    • Fourier transform infrared techniques for probing membrane protein structure
    • Braiman, M.S.; Rothschild, K.J. Fourier transform infrared techniques for probing membrane protein structure. Annu. Rev. Biophys. Biophys. Chem. 1988, 17, 541-570.
    • (1988) Annu. Rev. Biophys. Biophys. Chem , vol.17 , pp. 541-570
    • Braiman, M.S.1    Rothschild, K.J.2
  • 96
    • 5344241257 scopus 로고    scopus 로고
    • Toxicity of dipyridyl compounds and related compounds
    • Li, S.; Crooks, P.A.; Wei, X.; de Leon, J. Toxicity of dipyridyl compounds and related compounds. Crit. Rev. Toxicol. 2004, 34, 447-460.
    • (2004) Crit. Rev. Toxicol , vol.34 , pp. 447-460
    • Li, S.1    Crooks, P.A.2    Wei, X.3    de Leon, J.4
  • 98
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • Ulmer, T.S.; Bax, A.; Cole, N.B.; Nussbaum, R.L. Structure and dynamics of micelle-bound human alpha-synuclein. J. Biol. Chem. 2005, 280, 9595-9603.
    • (2005) J. Biol. Chem , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 100
    • 0037424245 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production
    • Li, N.; Ragheb, K.; Lawler, G.; Sturgis, J.; Rajwa, B.; Melendez, J.A.; Robinson, J.P. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J. Biol. Chem. 2003, 278, 8516-8525.
    • (2003) J. Biol. Chem , vol.278 , pp. 8516-8525
    • Li, N.1    Ragheb, K.2    Lawler, G.3    Sturgis, J.4    Rajwa, B.5    Melendez, J.A.6    Robinson, J.P.7
  • 101
    • 79955066685 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease
    • 2011, Article ID 716871, 18 pages
    • Keane, P.C.; Kurzawa, M.; Blain, P.G.; Morris, C.M. Mitochondrial dysfunction in Parkinson's disease. Parkinson's Disease. 2011, 2011, Article ID 716871, 18 pages.
    • (2011) Parkinson's Disease
    • Keane, P.C.1    Kurzawa, M.2    Blain, P.G.3    Morris, C.M.4
  • 103
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky, V.N.; Li, J.; Fink, A.L. Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. J. Biol. Chem. 2001, 276, 44284-44296.
    • (2001) J. Biol. Chem , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 105
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, D.M.; Susi, H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 1986, 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 106
    • 0025613794 scopus 로고
    • spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands
    • Venyaminov, S.; Kalnin, N.N. Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers 1990, 30, 1243-1257.
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.1    Kalnin, N.N.2    Quantitative, I.R.3
  • 107
    • 0035941305 scopus 로고    scopus 로고
    • Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations
    • Uversky, V.N.; Lee, H.J.; Li, J.; Fink, A.L.; Lee, S.J. Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations. J. Biol. Chem. 2001, 276, 43495-43498.
    • (2001) J. Biol. Chem , vol.276 , pp. 43495-43498
    • Uversky, V.N.1    Lee, H.J.2    Li, J.3    Fink, A.L.4    Lee, S.J.5
  • 108
    • 8844224948 scopus 로고    scopus 로고
    • Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils
    • Li, J.; Zhu, M.; Rajamani, S.; Uversky, V.N.; Fink, A.L. Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils. Chem. Biol. 2004, 11, 1513-1521.
    • (2004) Chem. Biol , vol.11 , pp. 1513-1521
    • Li, J.1    Zhu, M.2    Rajamani, S.3    Uversky, V.N.4    Fink, A.L.5
  • 109
    • 0028260192 scopus 로고
    • Nativelike secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR
    • Oberg, K.; Chrunyk, B.A.; Wetzel, R.; Fink, A.L. Nativelike secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR. Biochemistry 1994, 33, 2628-2634.
    • (1994) Biochemistry , vol.33 , pp. 2628-2634
    • Oberg, K.1    Chrunyk, B.A.2    Wetzel, R.3    Fink, A.L.4
  • 110
    • 0031933289 scopus 로고    scopus 로고
    • Discrete intermediates versus molten globule models for protein folding: Characterization of partially folded intermediates of apomyoglobin
    • Fink, A.L.; Oberg, K.A.; Seshadri, S. Discrete intermediates versus molten globule models for protein folding: Characterization of partially folded intermediates of apomyoglobin. Fold. Des. 1998, 3, 19-25.
    • (1998) Fold. Des , vol.3 , pp. 19-25
    • Fink, A.L.1    Oberg, K.A.2    Seshadri, S.3
  • 111
    • 0032005382 scopus 로고    scopus 로고
    • A new attenuated total reflectance Fourier transform infrared spectroscopy method for the study of proteins in solution
    • Oberg, K.A.; Fink, A.L. A new attenuated total reflectance Fourier transform infrared spectroscopy method for the study of proteins in solution. Anal. Biochem. 1998, 256, 92-106.
    • (1998) Anal. Biochem , vol.256 , pp. 92-106
    • Oberg, K.A.1    Fink, A.L.2
  • 112
    • 0028349385 scopus 로고
    • Thermally denatured ribonuclease A retains secondary structure as shown by FTIR
    • Seshadri, S.; Oberg, K.A.; Fink, A.L. Thermally denatured ribonuclease A retains secondary structure as shown by FTIR. Biochemistry 1994, 33, 1351-1355.
    • (1994) Biochemistry , vol.33 , pp. 1351-1355
    • Seshadri, S.1    Oberg, K.A.2    Fink, A.L.3
  • 113
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich, M.; Fletcher, M.A.; Dobson, C.M. Amyloid fibrils from muscle myoglobin. Nature 2001, 410, 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 114
    • 0036377156 scopus 로고    scopus 로고
    • Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease
    • Zerovnik, E. Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease. Eur. J. Biochem. 2002, 269, 3362-3371.
    • (2002) Eur. J. Biochem , vol.269 , pp. 3362-3371
    • Zerovnik, E.1
  • 115
    • 0029058159 scopus 로고
    • Analysis of side chain interactions and pair correlations within antiparallel b-sheets: The differences between backbone hydrogen-bonded and non-hydrrogen-bonded residue pairs
    • Wouters, M.A.; Curmi, P.M.G. Analysis of side chain interactions and pair correlations within antiparallel b-sheets: The differences between backbone hydrogen-bonded and non-hydrrogen-bonded residue pairs. Proteins Struct. Funct. Genet. 1995, 22, 119-131.
    • (1995) Proteins Struct. Funct. Genet , vol.22 , pp. 119-131
    • Wouters, M.A.1    Curmi, P.M.G.2
  • 116
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J.D.; Lansbury, P.T., Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 1997, 66, 385-407.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 117
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein
    • Harper, J.D.; Lieber, C.M.; Lansbury, P.T., Jr. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. Chem. Biol. 1997, 4, 951-959.
    • (1997) Chem. Biol , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury Jr., P.T.3
  • 118
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Abeta amyloid protofibrils by atomic force microscopy
    • Harper, J.D.; Wong, S.S.; Lieber, C.M.; Lansbury, P.T. Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem. Biol. 1997, 4, 119-125.
    • (1997) Chem. Biol , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 120
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: Localisation and implications
    • Krebs, M.R.H.; Bromley, E.H.C.; Donald, A.M. The binding of thioflavin-T to amyloid fibrils: Localisation and implications. J. Struct. Biol. 2005, 149, 30-37.
    • (2005) J. Struct. Biol , vol.149 , pp. 30-37
    • Krebs, M.R.H.1    Bromley, E.H.C.2    Donald, A.M.3
  • 122
    • 0037432332 scopus 로고    scopus 로고
    • Conformational behavior and aggregation of alpha-synuclein in organic solvents: Modeling the effects of membranes
    • Munishkina, L.A.; Phelan, C.; Uversky, V.N.; Fink, A.L. Conformational behavior and aggregation of alpha-synuclein in organic solvents: Modeling the effects of membranes. Biochemistry 2003, 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
  • 123
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • Nielsen, L.; Khurana, R.; Coats, A.; Frokjaer, S.; Brange, J.; Vyas, S.; Uversky, V.N.; Fink, A.L. Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism. Biochemistry 2001, 40, 6036-6046.
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 124
    • 4544252011 scopus 로고    scopus 로고
    • The effect of macromolecular crowding on protein aggregation and amyloid fibril formation
    • Munishkina, L.A.; Cooper, E.M.; Uversky, V.N.; Fink, A.L. The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J. Mol. Recognit. 2004, 17, 456-464.
    • (2004) J. Mol. Recognit , vol.17 , pp. 456-464
    • Munishkina, L.A.1    Cooper, E.M.2    Uversky, V.N.3    Fink, A.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.