메뉴 건너뛰기




Volumn 1794, Issue 2, 2009, Pages 282-290

Smoking and Parkinson's disease: Does nicotine affect α-synuclein fibrillation?

Author keywords

synuclein; Fibrillation; Hydroquinone; Intrinsically disordered protein; Misfolding; Nicotine; Parkinson's disease; Smoking

Indexed keywords

ALPHA SYNUCLEIN; ANABASINE; COTININE; HYDROQUINONE; NICOTINE; NORNICOTINE; THIOFLAVINE;

EID: 58149199681     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.09.026     Document Type: Article
Times cited : (88)

References (46)
  • 1
    • 0032936755 scopus 로고    scopus 로고
    • Etiology and pathogenesis of Parkinson's disease
    • Olanow C.W., and Tatton W.G. Etiology and pathogenesis of Parkinson's disease. Annu. Rev. Neurosci. 22 (1999) 123-144
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 123-144
    • Olanow, C.W.1    Tatton, W.G.2
  • 2
    • 0001509014 scopus 로고
    • Lewandowski M. (Ed), Springer, Berlin
    • Lewy F.H. In: Lewandowski M. (Ed). Handbuch der Neurologie (1912), Springer, Berlin 920-933
    • (1912) Handbuch der Neurologie , pp. 920-933
    • Lewy, F.H.1
  • 3
    • 0029981526 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease
    • Forno L.S. Neuropathology of Parkinson's disease. J. Neuropathol. Exp. Neurol. 55 (1996) 259-272
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 259-272
    • Forno, L.S.1
  • 4
    • 0031762949 scopus 로고    scopus 로고
    • Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia
    • Trojanowski J.Q., Goedert M., Iwatsubo T., and Lee V.M. Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia. Cell Death Differ. 5 (1998) 832-837
    • (1998) Cell Death Differ. , vol.5 , pp. 832-837
    • Trojanowski, J.Q.1    Goedert, M.2    Iwatsubo, T.3    Lee, V.M.4
  • 5
    • 0038727850 scopus 로고    scopus 로고
    • Parkinson's disease and related alpha-synucleinopathies are brain amyloidoses
    • Trojanowski J.Q., and Lee V.M. Parkinson's disease and related alpha-synucleinopathies are brain amyloidoses. Ann. N. Y. Acad. Sci. 991 (2003) 107-110
    • (2003) Ann. N. Y. Acad. Sci. , vol.991 , pp. 107-110
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 6
    • 0141677840 scopus 로고    scopus 로고
    • A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders
    • Uversky V.N. A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders. J. Biomol. Struct. Dyn. 21 (2003) 211-234
    • (2003) J. Biomol. Struct. Dyn. , vol.21 , pp. 211-234
    • Uversky, V.N.1
  • 7
    • 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. 103 (2007) 17-37
    • (2007) J. Neurochem. , vol.103 , pp. 17-37
    • Uversky, V.N.1
  • 8
    • 0038460184 scopus 로고    scopus 로고
    • Part II: alpha-synuclein and its molecular pathophysiological role in neurodegenerative disease
    • Dev K.K., Hofele K., Barbieri S., Buchman V.L., and van der Putten H. Part II: alpha-synuclein and its molecular pathophysiological role in neurodegenerative disease. Neuropharmacology 45 (2003) 14-44
    • (2003) Neuropharmacology , vol.45 , pp. 14-44
    • Dev, K.K.1    Hofele, K.2    Barbieri, S.3    Buchman, V.L.4    van der Putten, H.5
  • 9
    • 33749841522 scopus 로고    scopus 로고
    • The aggregation and fibrillation of alpha-synuclein
    • Fink A.L. The aggregation and fibrillation of alpha-synuclein. Acc. Chem. Res. 39 (2006) 628-634
    • (2006) Acc. Chem. Res. , vol.39 , pp. 628-634
    • Fink, A.L.1
  • 11
    • 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 Jr. 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 Jr., P.T.5
  • 12
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • Uversky V.N., Li J., and Fink A.L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem. 276 (2001) 10737-10744
    • (2001) J. Biol. Chem. , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 13
    • 0023722437 scopus 로고
    • Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
    • Maroteaux L., Campanelli J.T., and Scheller R.H. Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci. 8 (1988) 2804-2815
    • (1988) J. Neurosci. , vol.8 , pp. 2804-2815
    • Maroteaux, L.1    Campanelli, J.T.2    Scheller, R.H.3
  • 14
    • 0037014618 scopus 로고    scopus 로고
    • Amino acid determinants of alpha-synuclein aggregation: putting together pieces of the puzzle
    • Uversky V.N., and Fink A.L. Amino acid determinants of alpha-synuclein aggregation: putting together pieces of the puzzle. FEBS Lett. 522 (2002) 9-13
    • (2002) FEBS Lett. , vol.522 , pp. 9-13
    • Uversky, V.N.1    Fink, A.L.2
  • 18
    • 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 V.N., and Fink A.L. Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry 40 (2001) 11604-11613
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 20
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
    • Conway K.A., Lee S.J., Rochet J.C., Ding T.T., Williamson R.E., and Lansbury Jr. P.T. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 571-576
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury Jr., P.T.6
  • 21
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease
    • Xu J., Kao S.Y., Lee F.J., Song W., Jin L.W., and Yankner B.A. Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nat. Med. 8 (2002) 600-606
    • (2002) Nat. Med. , vol.8 , pp. 600-606
    • Xu, J.1    Kao, S.Y.2    Lee, F.J.3    Song, W.4    Jin, L.W.5    Yankner, B.A.6
  • 22
    • 0033842094 scopus 로고    scopus 로고
    • Smoking and Parkinson's and Alzheimer's disease: review of the epidemiological studies
    • Fratiglioni L., and Wang H.X. Smoking and Parkinson's and Alzheimer's disease: review of the epidemiological studies. Behav. Brain Res. 113 (2000) 117-120
    • (2000) Behav. Brain Res. , vol.113 , pp. 117-120
    • Fratiglioni, L.1    Wang, H.X.2
  • 23
    • 4344698859 scopus 로고    scopus 로고
    • Smoking, nicotine and Parkinson's disease
    • Quik M. Smoking, nicotine and Parkinson's disease. Trends Neurosci. 27 (2004) 561-568
    • (2004) Trends Neurosci. , vol.27 , pp. 561-568
    • Quik, M.1
  • 24
    • 0030751425 scopus 로고    scopus 로고
    • Nicotinic system involvement in Alzheimer's and Parkinson's diseases. Implications for therapeutics
    • Newhouse P.A., Potter A., and Levin E.D. Nicotinic system involvement in Alzheimer's and Parkinson's diseases. Implications for therapeutics. Drugs Aging 11 (1997) 206-228
    • (1997) Drugs Aging , vol.11 , pp. 206-228
    • Newhouse, P.A.1    Potter, A.2    Levin, E.D.3
  • 28
    • 0037165646 scopus 로고    scopus 로고
    • Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro
    • Uversky V.N., Yamin G., Souillac P.O., Goers J., Glaser C.B., and Fink A.L. Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro. FEBS Lett. 517 (2002) 239-244
    • (2002) FEBS Lett. , vol.517 , pp. 239-244
    • Uversky, V.N.1    Yamin, G.2    Souillac, P.O.3    Goers, J.4    Glaser, C.B.5    Fink, A.L.6
  • 29
    • 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., and Fink A.L. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40 (2001) 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
  • 31
    • 0035104574 scopus 로고    scopus 로고
    • Dopamine agonist-induced dyskinesias are correlated to both firing pattern and frequency alterations of pallidal neurones in the MPTP-treated monkey
    • Boraud T., Bezard E., Bioulac B., and Gross C.E. Dopamine agonist-induced dyskinesias are correlated to both firing pattern and frequency alterations of pallidal neurones in the MPTP-treated monkey. Brain 124 (2001) 546-557
    • (2001) Brain , vol.124 , pp. 546-557
    • Boraud, T.1    Bezard, E.2    Bioulac, B.3    Gross, C.E.4
  • 32
    • 33847105184 scopus 로고    scopus 로고
    • Advances in the treatment of Parkinson's disease
    • Singh N., Pillay V., and Choonara Y.E. Advances in the treatment of Parkinson's disease. Prog. Neurobiol. 81 (2007) 29-44
    • (2007) Prog. Neurobiol. , vol.81 , pp. 29-44
    • Singh, N.1    Pillay, V.2    Choonara, Y.E.3
  • 33
    • 34248572482 scopus 로고    scopus 로고
    • Anti-fibrillogenic and fibril-destabilizing activity of nicotine in vitro: implications for the prevention and therapeutics of Lewy body diseases
    • Ono K., Hirohata M., and Yamada M. Anti-fibrillogenic and fibril-destabilizing activity of nicotine in vitro: implications for the prevention and therapeutics of Lewy body diseases. Exp. Neurol. 205 (2007) 414-424
    • (2007) Exp. Neurol. , vol.205 , pp. 414-424
    • Ono, K.1    Hirohata, M.2    Yamada, M.3
  • 36
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • Lashuel H.A., Petre B.M., Wall J., Simon M., Nowak R.J., Walz T., and Lansbury Jr. P.T. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 322 (2002) 1089-1102
    • (2002) J. Mol. Biol. , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury Jr., P.T.7
  • 37
  • 38
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease
    • Lansbury Jr. P.T. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 3342-3344
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 3342-3344
    • Lansbury Jr., P.T.1
  • 39
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg M.S., and Lansbury Jr. P.T. Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?. Nat. Cell Biol. 2 (2000) E115-E119
    • (2000) Nat. Cell Biol. , vol.2
    • Goldberg, M.S.1    Lansbury Jr., P.T.2
  • 40
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley D.M., Walsh D.M., Ye C.P., Diehl T., Vasquez S., Vassilev P.M., Teplow D.B., and Selkoe D.J. Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19 (1999) 8876-8884
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 41
    • 0033048453 scopus 로고    scopus 로고
    • The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles
    • Janson J., Ashley R.H., Harrison D., McIntyre S., and Butler P.C. The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes 48 (1999) 491-498
    • (1999) Diabetes , vol.48 , pp. 491-498
    • Janson, J.1    Ashley, R.H.2    Harrison, D.3    McIntyre, S.4    Butler, P.C.5
  • 44
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury P.T., and Lashuel H.A. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443 (2006) 774-779
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 45
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • Lashuel H.A., and Lansbury Jr. P.T. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?. Q. Rev. Biophys. 39 (2006) 167-201
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury Jr., P.T.2
  • 46
    • 52049098478 scopus 로고    scopus 로고
    • Structural characteristics of the alpha-synuclein oligomers stabilized by the flavonoid baicalein
    • Hong D.-P., Fink Jr. A.L., and Uversky V.N. Structural characteristics of the 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 Jr., A.L.2    Uversky, V.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.