메뉴 건너뛰기




Volumn 10, Issue 3, 2009, Pages 1226-1260

Physiological and pathological role of alpha-synuclein in parkinson's disease through iron mediated oxidative stress; the role of a putative iron-responsive element

Author keywords

syn: Alpha synuclein; 5 utr: 5' untranslated region; 6 ohda: 6 hydroxydopamine; Aa: Amino acid(s); Ad: Alzheimer's disease; Cns: Central nervous system; Da: Dopamine; Dat: Dopamine transporter; Dlb: Dementia with lewy bodies; Er: Endoplasmatic reticulum; Gcis: Glial cytoplasmic inclusions; Gsh: Reduced gluthatione; Ire:iron responsive element; Irps: Interacting binding proteins; Lbs: Lewy bodies; Lns: Lewy neurites; Mptp: 1 methyl 4 phenyl 1, 2, 3, 6 tetrapyridine; Nac: Non amyloidogenic component; Nt: Nucleotide(s); Pd: Parkinson's disease; Pld2: Phospholipase d2; Pm: Plasmatic membrane; Ros: Reactive oxygen species; Tfr: Transferrin receptor; Th: Tyrosine hydroxylase; Wt: Wild type

Indexed keywords

ALPHA SYNUCLEIN; AMANTADINE; APOMORPHINE; BENSERAZIDE PLUS LEVODOPA; BENZATROPINE; BIPERIDEN; BROMOCRIPTINE; CAFFEINE; CARBEGOLINE; CARBIDOPA PLUS LEVODOPA; CREATINE; DIPHENHYDRAMINE; DOPAMINE RECEPTOR STIMULATING AGENT; ENTACAPONE; ESTRADIOL; GANGLIOSIDE GM1; GPI 1485; LEVODOPA; LISURIDE; ORPHENADRINE; PERGOLIDE; PRAMIPEXOLE; PROCYCLIDINE; PROFENAMINE; ROPINIROLE; SELEGILINE; TOLCAPONE; TRIHEXYPHENIDYL; UBIDECARENONE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 63449129338     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms10031226     Document Type: Review
Times cited : (71)

References (186)
  • 2
    • 0035956501 scopus 로고    scopus 로고
    • Parkinsonism in Ontario: Increased mortality compared with controls in a large cohort study
    • Guttman, M.; Slaughter, P.M.; Theriault, M.E.; DeBoer, D.P.; Naylor, C.D. Parkinsonism in Ontario: increased mortality compared with controls in a large cohort study. Neurology 2001, 57 (12), 2278-2282.
    • (2001) Neurology , vol.57 , Issue.12 , pp. 2278-2282
    • Guttman, M.1    Slaughter, P.M.2    Theriault, M.E.3    DeBoer, D.P.4    Naylor, C.D.5
  • 4
    • 14344263884 scopus 로고    scopus 로고
    • The role of alpha-synuclein in neurodegenerative diseases
    • Bennett, M.C. The role of alpha-synuclein in neurodegenerative diseases. Pharmacol. Ther. 2005, 105 (3), 311-331.
    • (2005) Pharmacol. Ther , vol.105 , Issue.3 , pp. 311-331
    • Bennett, M.C.1
  • 5
    • 23744443327 scopus 로고    scopus 로고
    • Nosology of Parkinson's disease: Looking for the way out of a quagmire
    • Forman, M.S.; Lee, V.M. and Trojanowski, J.Q. Nosology of Parkinson's disease: looking for the way out of a quagmire. Neuron 2005, 47 (4), 479-482.
    • (2005) Neuron , vol.47 , Issue.4 , pp. 479-482
    • Forman, M.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 6
    • 0033849550 scopus 로고    scopus 로고
    • Autosomal recessive early-onset parkinsonism with diurnal fluctuation: Clinicopathologic characteristics and molecular genetic identification
    • Yamamura, Y.; Hattori, N.; Matsumine, H.; Kuzuhara, S.; Mizuno, Y. Autosomal recessive early-onset parkinsonism with diurnal fluctuation: clinicopathologic characteristics and molecular genetic identification. Brain Dev. 2000, 22 (Suppl 1), S87-S91.
    • (2000) Brain Dev , vol.22 , Issue.SUPPL. 1
    • Yamamura, Y.1    Hattori, N.2    Matsumine, H.3    Kuzuhara, S.4    Mizuno, Y.5
  • 7
    • 33749240943 scopus 로고    scopus 로고
    • Mechanisms of Parkinson's disease linked to pathological alphasynuclein:new targets for drug discovery
    • Lee, V.M. ; Trojanowski, J.Q. Mechanisms of Parkinson's disease linked to pathological alphasynuclein:new targets for drug discovery. Neuron 2006, 52 (1), 33-38.
    • (2006) Neuron , vol.52 , Issue.1 , pp. 33-38
    • Lee, V.M.1    Trojanowski, J.Q.2
  • 8
    • 0037039267 scopus 로고    scopus 로고
    • Miyasaki, J.M.; Martin, W.; Suchowersky, O.; Weiner, W.J.; Lang, A.E. Practice parameter:initiation of treatment for Parkinson's disease: an evidence-based review: report of the Quality Standards Subcommittee of the American Academy of Neurology. Neurology 2002, 58 (1), 11-17.
    • Miyasaki, J.M.; Martin, W.; Suchowersky, O.; Weiner, W.J.; Lang, A.E. Practice parameter:initiation of treatment for Parkinson's disease: an evidence-based review: report of the Quality Standards Subcommittee of the American Academy of Neurology. Neurology 2002, 58 (1), 11-17.
  • 9
    • 20544476874 scopus 로고    scopus 로고
    • The 'magic' of L-dopa: Why is it the gold standard Parkinson's disease therapy?
    • Mercuri, N.B.; Bernardi, G. The 'magic' of L-dopa: Why is it the gold standard Parkinson's disease therapy? Trends Pharmacol. Sci. 2005, 26 (7), 341-344.
    • (2005) Trends Pharmacol. Sci , vol.26 , Issue.7 , pp. 341-344
    • Mercuri, N.B.1    Bernardi, G.2
  • 10
    • 0037418066 scopus 로고    scopus 로고
    • Current concepts in the diagnosis and management of Parkinson's disease
    • Guttman, M.; Kish, S.J.; Furukawa, Y. Current concepts in the diagnosis and management of Parkinson's disease. CMAJ 2003, 168 (3), 293-301.
    • (2003) CMAJ , vol.168 , Issue.3 , pp. 293-301
    • Guttman, M.1    Kish, S.J.2    Furukawa, Y.3
  • 11
    • 0006647256 scopus 로고    scopus 로고
    • Verhagen Metman, L.; Del Dotto, P.; van den Munckhof, P.; Fang, J.; Mouradian, M.M.; Chase, T.N. Amantadine as treatment for dyskinesias and motor fluctuations in Parkinson's disease. Neurology 1998, 50 (5), 1323-1326. 12. Quinn, N.; Parkes, D.; Janota, I.; Marsden, C. D. Preservation of the substantia nigra and locus coeruleus in a patient receiving levodopa (2 kg) plus decarboxylase inhibitor over a four-year period. Mov. Disord. 1986, 1 (1), 65-68.
    • Verhagen Metman, L.; Del Dotto, P.; van den Munckhof, P.; Fang, J.; Mouradian, M.M.; Chase, T.N. Amantadine as treatment for dyskinesias and motor fluctuations in Parkinson's disease. Neurology 1998, 50 (5), 1323-1326. 12. Quinn, N.; Parkes, D.; Janota, I.; Marsden, C. D. Preservation of the substantia nigra and locus coeruleus in a patient receiving levodopa (2 kg) plus decarboxylase inhibitor over a four-year period. Mov. Disord. 1986, 1 (1), 65-68.
  • 12
    • 0030984046 scopus 로고    scopus 로고
    • Is levodopa toxic to human substantia nigra?
    • Rajput, A.H.; Fenton, M.; Birdi, S.; Macaulay, R. Is levodopa toxic to human substantia nigra? Mov. Disord. 1997, 12 (5), 634-638.
    • (1997) Mov. Disord , vol.12 , Issue.5 , pp. 634-638
    • Rajput, A.H.1    Fenton, M.2    Birdi, S.3    Macaulay, R.4
  • 13
    • 0021183217 scopus 로고
    • Long-term therapy of the Parkinson syndrome]
    • Ludin, H.P. [Long-term therapy of the Parkinson syndrome]. Schweiz. Med. Wochenschr. 1984, 114 (33), 1131-1136.
    • (1984) Schweiz. Med. Wochenschr , vol.114 , Issue.33 , pp. 1131-1136
    • Ludin, H.P.1
  • 14
    • 0033800614 scopus 로고    scopus 로고
    • The early treatment of Parkinson's disease: Levodopa, dopamine agonists or both
    • Stern, M.B. The early treatment of Parkinson's disease: levodopa, dopamine agonists or both. Parkinsonism Relat. Disord. 2000, 7 (1), 27-33.
    • (2000) Parkinsonism Relat. Disord , vol.7 , Issue.1 , pp. 27-33
    • Stern, M.B.1
  • 15
    • 0027470879 scopus 로고
    • Early combination therapy (bromocriptine and levodopa) does not prevent motor fluctuations in Parkinson's disease
    • Weiner, W.J.; Factor, S.A.; Sanchez-Ramos, J.R.; Singer, C.; Sheldon, C.; Cornelius, L.; Ingenito, A. Early combination therapy (bromocriptine and levodopa) does not prevent motor fluctuations in Parkinson's disease. Neurology 1993, 43 (1), 21-27.
    • (1993) Neurology , vol.43 , Issue.1 , pp. 21-27
    • Weiner, W.J.1    Factor, S.A.2    Sanchez-Ramos, J.R.3    Singer, C.4    Sheldon, C.5    Cornelius, L.6    Ingenito, A.7
  • 16
    • 0034682308 scopus 로고    scopus 로고
    • A five-year study of the incidence of dyskinesia in patients with early Parkinson's disease who were treated with ropinirole or levodopa. 056 Study Group
    • Rascol, O.; Brooks, D.J.; Korczyn, A.D.; De Deyn, P.P.; Clarke, C.E.; Lang, A. E. A five-year study of the incidence of dyskinesia in patients with early Parkinson's disease who were treated with ropinirole or levodopa. 056 Study Group. N. Engl. J. Med. 2000, 342 (20), 1484-1491.
    • (2000) N. Engl. J. Med , vol.342 , Issue.20 , pp. 1484-1491
    • Rascol, O.1    Brooks, D.J.2    Korczyn, A.D.3    De Deyn, P.P.4    Clarke, C.E.5    Lang, A.E.6
  • 17
    • 0030897345 scopus 로고    scopus 로고
    • Attenuation of levodopa-induced toxicity in mesencephalic cultures by pramipexole
    • Carvey, P.M.; Pieri, S.; Ling, Z.D. Attenuation of levodopa-induced toxicity in mesencephalic cultures by pramipexole. J. Neural Transm. 1997, 104 (2-3), 209-28.
    • (1997) J. Neural Transm , vol.104 , Issue.2-3 , pp. 209-228
    • Carvey, P.M.1    Pieri, S.2    Ling, Z.D.3
  • 18
    • 0027752367 scopus 로고
    • The effect of pergolide and MDL 72974 on rat brain CuZn superoxide dismutase
    • Clow, A.; Freestone, C.; Lewis, E.; Dexter, D.; Sandler, M.; Glover, V. The effect of pergolide and MDL 72974 on rat brain CuZn superoxide dismutase. Neurosci. Lett. 1993, 164 (1-2), 41-43.
    • (1993) Neurosci. Lett , vol.164 , Issue.1-2 , pp. 41-43
    • Clow, A.1    Freestone, C.2    Lewis, E.3    Dexter, D.4    Sandler, M.5    Glover, V.6
  • 20
    • 0028068121 scopus 로고
    • Bromocriptine protects mice against 6-hydroxydopamine and scavenges hydroxyl free radicals in vitro
    • Ogawa, N.; Tanaka, K.; Asanuma, M.; Kawai, M.; Masumizu, T.; Kohno, M. and Mori, A. Bromocriptine protects mice against 6-hydroxydopamine and scavenges hydroxyl free radicals in vitro. Brain Res. 1994, 657 (1-2), 207-213.
    • (1994) Brain Res , vol.657 , Issue.1-2 , pp. 207-213
    • Ogawa, N.1    Tanaka, K.2    Asanuma, M.3    Kawai, M.4    Masumizu, T.5    Kohno, M.6    Mori, A.7
  • 21
    • 37149018270 scopus 로고    scopus 로고
    • Role of tolcapone in the treatment of Parkinson's disease
    • Leegwater-Kim, J.; Waters, C. Role of tolcapone in the treatment of Parkinson's disease. Expert Rev. Neurother. 2007, 7 (12), 1649-1657.
    • (2007) Expert Rev. Neurother , vol.7 , Issue.12 , pp. 1649-1657
    • Leegwater-Kim, J.1    Waters, C.2
  • 22
    • 0034106475 scopus 로고    scopus 로고
    • Inhibition of catechol-O-methyltransferase. Optimizing dopaminergic therapy in idiopathic Parkinson syndrome with entacapone]
    • Arnold, G.; Kupsch, A. [Inhibition of catechol-O-methyltransferase. Optimizing dopaminergic therapy in idiopathic Parkinson syndrome with entacapone]. Nervenarzt. 2000, 71 (2), 78-83.
    • (2000) Nervenarzt , vol.71 , Issue.2 , pp. 78-83
    • Arnold, G.1    Kupsch, A.2
  • 23
    • 0037461309 scopus 로고    scopus 로고
    • Neuroprotective agents for clinical trials in Parkinson's disease: A systematic assessment
    • Ravina, B.M.; Fagan, S.C.; Hart, R.G.; Hovinga, C.A.; Murphy, D.D.; Dawson, T.M.; Marler, J.R. Neuroprotective agents for clinical trials in Parkinson's disease: a systematic assessment. Neurology 2003, 60 (8), 1234-1240.
    • (2003) Neurology , vol.60 , Issue.8 , pp. 1234-1240
    • Ravina, B.M.1    Fagan, S.C.2    Hart, R.G.3    Hovinga, C.A.4    Murphy, D.D.5    Dawson, T.M.6    Marler, J.R.7
  • 24
  • 25
    • 0032568534 scopus 로고    scopus 로고
    • 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 (11), 6469-6473.
    • 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 (11), 6469-6473.
  • 26
    • 0030882856 scopus 로고    scopus 로고
    • Spillantini, M.G.; Schmidt, M.L.; Lee, V.M.; Trojanowski, J.Q.; Jakes, R.; Goedert, M. Alphasynuclein in Lewy bodies. Nature 1997, 388 (6645), 839-840.
    • Spillantini, M.G.; Schmidt, M.L.; Lee, V.M.; Trojanowski, J.Q.; Jakes, R.; Goedert, M. Alphasynuclein in Lewy bodies. Nature 1997, 388 (6645), 839-840.
  • 27
    • 0034661820 scopus 로고    scopus 로고
    • Duda, J.E.; Lee, V.M.; Trojanowski, J.Q. Neuropathology of synuclein aggregates. J. Neurosci. Res. 2000, 61 (2), 121-127. 29. Polymeropoulos, M.H. Autosomal dominant Parkinson's disease and alpha-synuclein. Ann. Neurol. 1998, 44 (Suppl 1), S63-S64.
    • Duda, J.E.; Lee, V.M.; Trojanowski, J.Q. Neuropathology of synuclein aggregates. J. Neurosci. Res. 2000, 61 (2), 121-127. 29. Polymeropoulos, M.H. Autosomal dominant Parkinson's disease and alpha-synuclein. Ann. Neurol. 1998, 44 (Suppl 1), S63-S64.
  • 31
    • 33646896726 scopus 로고    scopus 로고
    • Brandis, K.A.; Holmes, I.F.; England, S.J.; Sharma, N.; Kukreja, L.; DebBurman, S.K. alpha-Synuclein fission yeast model: concentration-dependent aggregation without plasma membrane localization or toxicity. J. Mol. Neurosci. 2006, 28 (2), 179-191.
    • Brandis, K.A.; Holmes, I.F.; England, S.J.; Sharma, N.; Kukreja, L.; DebBurman, S.K. alpha-Synuclein fission yeast model: concentration-dependent aggregation without plasma membrane localization or toxicity. J. Mol. Neurosci. 2006, 28 (2), 179-191.
  • 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., Lansbury, P.T., Jr. Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 2000, 39 (10), 2552-2563.
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury Jr., P.T.3
  • 33
    • 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, P.T., Jr. 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. USA 2000, 97 (2), 571-576.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.2 , 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
  • 34
    • 2342556414 scopus 로고    scopus 로고
    • Fibrillization of alpha-synuclein and tau in familial Parkinson's disease caused by the A53T alpha-synuclein mutation
    • Kotzbauer, P.T.; Giasson, B.I.; Kravitz, A.V.; Golbe, L.I.; Mark, M.H.; Trojanowski, J.Q.; Lee, V.M. Fibrillization of alpha-synuclein and tau in familial Parkinson's disease caused by the A53T alpha-synuclein mutation. Exp. Neurol. 2004, 187(2), 279-288.
    • (2004) Exp. Neurol , vol.187 , Issue.2 , pp. 279-288
    • Kotzbauer, P.T.1    Giasson, B.I.2    Kravitz, A.V.3    Golbe, L.I.4    Mark, M.H.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 36
    • 33846462040 scopus 로고    scopus 로고
    • Identification of a risk haplotype of the alpha-synuclein gene in Japanese with sporadic Parkinson's disease
    • Kobayashi, H.; Ujike, H.; Hasegawa, J.; Yamamoto, M.; Kanzaki, A. and Sora, I. Identification of a risk haplotype of the alpha-synuclein gene in Japanese with sporadic Parkinson's disease. Mov. Disord. 2006, 21 (12), 2157-2164.
    • (2006) Mov. Disord , vol.21 , Issue.12 , pp. 2157-2164
    • Kobayashi, H.1    Ujike, H.2    Hasegawa, J.3    Yamamoto, M.4    Kanzaki, A.5    Sora, I.6
  • 37
    • 0242300619 scopus 로고    scopus 로고
    • Singleton, A.B.; Farrer, M.; Johnson, J.; Singleton, A.; Hague, S.; Kachergus, J.; Hulihan, M.; Peuralinna, T.; Dutra, A.; Nussbaum, R.; Lincoln, S.; Crawley, A.; Hanson, M.; Maraganore, D.; Adler, C.; Cookson, M.R.; Muenter, M.; Baptista, M.; Miller, D.; Blancato, J.; Hardy, J.; Gwinn-Hardy, K. alpha-Synuclein locus triplication causes Parkinson's disease. Science 2003, 302 (5646), 841.
    • Singleton, A.B.; Farrer, M.; Johnson, J.; Singleton, A.; Hague, S.; Kachergus, J.; Hulihan, M.; Peuralinna, T.; Dutra, A.; Nussbaum, R.; Lincoln, S.; Crawley, A.; Hanson, M.; Maraganore, D.; Adler, C.; Cookson, M.R.; Muenter, M.; Baptista, M.; Miller, D.; Blancato, J.; Hardy, J.; Gwinn-Hardy, K. alpha-Synuclein locus triplication causes Parkinson's disease. Science 2003, 302 (5646), 841.
  • 38
    • 33745847479 scopus 로고    scopus 로고
    • Diagnosis and treatment of Parkinson disease: Molecules to medicine
    • Savitt, J.M.; Dawson, V.L.; Dawson, T.M. Diagnosis and treatment of Parkinson disease: Molecules to medicine. J. Clin. Invest. 2006, 116 (7), 1744-1754.
    • (2006) J. Clin. Invest , vol.116 , Issue.7 , pp. 1744-1754
    • Savitt, J.M.1    Dawson, V.L.2    Dawson, T.M.3
  • 39
    • 0037130450 scopus 로고    scopus 로고
    • Dawson, T.; Mandir, A.; Lee, M. Animal models of PD: Pieces of the same puzzle? Neuron 2002, 35 (2), 219-222. 42. Abeliovich, A.; Schmitz, Y.; Farinas, I.; Choi-Lundberg, D.; Ho, W.H.; Castillo, P.E.; Shinsky, N.; Verdugo, J.M.; Armanini, M.; Ryan, A.; Hynes, M.; Phillips, H.; Sulzer, D. and Rosenthal, A. Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system. Neuron 2000, 25 (1), 239-252.
    • Dawson, T.; Mandir, A.; Lee, M. Animal models of PD: Pieces of the same puzzle? Neuron 2002, 35 (2), 219-222. 42. Abeliovich, A.; Schmitz, Y.; Farinas, I.; Choi-Lundberg, D.; Ho, W.H.; Castillo, P.E.; Shinsky, N.; Verdugo, J.M.; Armanini, M.; Ryan, A.; Hynes, M.; Phillips, H.; Sulzer, D. and Rosenthal, A. Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system. Neuron 2000, 25 (1), 239-252.
  • 41
    • 33645833848 scopus 로고    scopus 로고
    • Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease
    • El-Agnaf, O.M.; Salem, S.A.; Paleologou, K.E.; Curran, M.D.; Gibson, M.J.; Court, J.A.; Schlossmacher, M.G.; Allsop, D. Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease. FASEB J. 2006, 20 (3), 419-425.
    • (2006) FASEB J , vol.20 , Issue.3 , pp. 419-425
    • El-Agnaf, O.M.1    Salem, S.A.2    Paleologou, K.E.3    Curran, M.D.4    Gibson, M.J.5    Court, J.A.6    Schlossmacher, M.G.7    Allsop, D.8
  • 42
    • 5444260407 scopus 로고    scopus 로고
    • Synucleins and their relationship to Parkinson's disease
    • von Bohlen Und Halbach, O. Synucleins and their relationship to Parkinson's disease. Cell Tissue Res. 2004, 318 (1), 163-174.
    • (2004) Cell Tissue Res , vol.318 , Issue.1 , pp. 163-174
    • von Bohlen Und Halbach, O.1
  • 43
    • 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.; 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 1995, 14 (2), 467-475.
    • (1995) Neuron , vol.14 , Issue.2 , 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
  • 44
    • 0028061989 scopus 로고
    • Localization of phosphoneuroprotein 14 (PNP 14) and its mRNA expression in rat brain determined by immunocytochemistry and in situ hybridization
    • Nakajo, S.; Shioda, S.; Nakai, Y.; Nakaya, K. Localization of phosphoneuroprotein 14 (PNP 14) and its mRNA expression in rat brain determined by immunocytochemistry and in situ hybridization. Brain Res. Mol. Brain Res. 1994, 27 (1), 81-86.
    • (1994) Brain Res. Mol. Brain Res , vol.27 , Issue.1 , pp. 81-86
    • Nakajo, S.1    Shioda, S.2    Nakai, Y.3    Nakaya, K.4
  • 45
    • 0031763264 scopus 로고    scopus 로고
    • The synuclein family
    • Lavedan, C. The synuclein family. Genome Res. 1998, 8 (9), 871-80.
    • (1998) Genome Res , vol.8 , Issue.9 , pp. 871-880
    • Lavedan, C.1
  • 46
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alphasynuclein in its free and lipid-associated states
    • Eliezer, D.; Kutluay, E.; Bussell, R., Jr.; Browne, G. Conformational properties of alphasynuclein in its free and lipid-associated states. J. Mol. Biol. 2001, 307 (4), 1061-1073.
    • (2001) J. Mol. Biol , vol.307 , Issue.4 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell Jr., R.3    Browne, G.4
  • 47
    • 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 2001, 40 (38), 11604-11613.
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 49
    • 0036150971 scopus 로고    scopus 로고
    • The synucleins
    • Reviews3002
    • George, J.M. The synucleins. Genome Biol. 2002, 3 (1), Reviews3002.
    • (2002) Genome Biol , vol.3 , Issue.1
    • George, J.M.1
  • 50
    • 0036326067 scopus 로고    scopus 로고
    • Structure/function of alpha-synuclein in health and disease: Rational development of animal models for Parkinson's and related diseases
    • Kahle, P.J.; Haass, C.; Kretzschmar, H.A., Neumann, M. Structure/function of alpha-synuclein in health and disease: Rational development of animal models for Parkinson's and related diseases. J. Neurochem. 2002, 82 (3), 449-457.
    • (2002) J. Neurochem , vol.82 , Issue.3 , pp. 449-457
    • Kahle, P.J.1    Haass, C.2    Kretzschmar, H.A.3    Neumann, M.4
  • 51
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W.S.; Jonas, A.; Clayton, D.F.; George, J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 1998, 273 (16), 9443-9449.
    • (1998) J. Biol. Chem , vol.273 , Issue.16 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 52
    • 0037016741 scopus 로고    scopus 로고
    • Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form
    • Lee, H. J.; Choi, C. and Lee, S. J. Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. J. Biol. Chem. 2002, 277(1), 671-678.
    • (2002) J. Biol. Chem , vol.277 , Issue.1 , pp. 671-678
    • Lee, H.J.1    Choi, C.2    Lee, S.J.3
  • 53
    • 0038054286 scopus 로고    scopus 로고
    • A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins
    • Bussell, R., Jr.; Eliezer, D. A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins. J. Mol. Biol. 2003, 329 (4), 763-778.
    • (2003) J. Mol. Biol , vol.329 , Issue.4 , pp. 763-778
    • Bussell Jr., R.1    Eliezer, D.2
  • 54
    • 0027489773 scopus 로고    scopus 로고
    • Ueda, K.; Fukushima, H.; Masliah, E.; Xia, Y.; Iwai, A.; Yoshimoto, M.; Otero, D. A.; Kondo, J.; Ihara, Y.; Saitoh, T. Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. Proc. Natl. Acad. Sci. USA 1993, 90 (23), 11282-11286. 58. el-Agnaf, O.M.; Irvine, G.B. Aggregation and neurotoxicity of alpha-synuclein and related peptides. Biochem. Soc. Trans. 2002, 30 (4), 559-565.
    • Ueda, K.; Fukushima, H.; Masliah, E.; Xia, Y.; Iwai, A.; Yoshimoto, M.; Otero, D. A.; Kondo, J.; Ihara, Y.; Saitoh, T. Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. Proc. Natl. Acad. Sci. USA 1993, 90 (23), 11282-11286. 58. el-Agnaf, O.M.; Irvine, G.B. Aggregation and neurotoxicity of alpha-synuclein and related peptides. Biochem. Soc. Trans. 2002, 30 (4), 559-565.
  • 55
    • 0029257497 scopus 로고
    • The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: Is NAC a common trigger or target in neurodegenerative disease?
    • Han, H.; Weinreb, P.H.; Lansbury, P.T., Jr. The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: Is NAC a common trigger or target in neurodegenerative disease? Chem. Biol. 1995, 2 (3), 163-169.
    • (1995) Chem. Biol , vol.2 , Issue.3 , pp. 163-169
    • Han, H.1    Weinreb, P.H.2    Lansbury Jr., P.T.3
  • 56
    • 0032573597 scopus 로고    scopus 로고
    • Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments
    • El-Agnaf, O.M.; Jakes, R.; Curran, M.D.; Middleton, D.; Ingenito, R.; Bianchi, E.; Pessi, A.; Neill, D.; Wallace, A. Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments. FEBS Lett. 1998, 440 (1-2), 71-75.
    • (1998) FEBS Lett , vol.440 , Issue.1-2 , pp. 71-75
    • El-Agnaf, O.M.1    Jakes, R.2    Curran, M.D.3    Middleton, D.4    Ingenito, R.5    Bianchi, E.6    Pessi, A.7    Neill, D.8    Wallace, A.9
  • 57
    • 0036484302 scopus 로고    scopus 로고
    • Multiple phosphorylation of alpha-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation
    • Negro, A.; Brunati, A.M.; Donella-Deana, A.; Massimino, M.L.; Pinna, L.A. Multiple phosphorylation of alpha-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation. FASEB J. 2002, 16 (2), 210-212.
    • (2002) FASEB J , vol.16 , Issue.2 , pp. 210-212
    • Negro, A.1    Brunati, A.M.2    Donella-Deana, A.3    Massimino, M.L.4    Pinna, L.A.5
  • 58
    • 0037137224 scopus 로고    scopus 로고
    • Structural and functional implications of C-terminal regions of alpha-synuclein
    • Kim, T.D.; Paik, S.R.; Yang, C.H. Structural and functional implications of C-terminal regions of alpha-synuclein. Biochemistry 2002, 41 (46), 13782-13790.
    • (2002) Biochemistry , vol.41 , Issue.46 , pp. 13782-13790
    • Kim, T.D.1    Paik, S.R.2    Yang, C.H.3
  • 59
    • 0033565874 scopus 로고    scopus 로고
    • Ostrerova, N.; Petrucelli, L.; Farrer, M.; Mehta, N.; Choi, P.; Hardy, J.; Wolozin, B. alpha-Synuclein shares physical and functional homology with 14-3-3 proteins. J. Neurosci. 1999, 19 (14), 5782-5791.
    • Ostrerova, N.; Petrucelli, L.; Farrer, M.; Mehta, N.; Choi, P.; Hardy, J.; Wolozin, B. alpha-Synuclein shares physical and functional homology with 14-3-3 proteins. J. Neurosci. 1999, 19 (14), 5782-5791.
  • 60
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Yuan, J.; Yankner, B.A. Apoptosis in the nervous system. Nature 2000, 407 (6805), 802-809.
    • (2000) Nature , vol.407 , Issue.6805 , pp. 802-809
    • Yuan, J.1    Yankner, B.A.2
  • 61
    • 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.; Yankner, B.A. Dopamine-dependent neurotoxicity of alpha-synuclein: A mechanism for selective neurodegeneration in Parkinson disease. Nat. Med. 2002, 8 (6), 600-606.
    • (2002) Nat. Med , vol.8 , Issue.6 , 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
  • 62
    • 0037092442 scopus 로고    scopus 로고
    • A role for alpha-synuclein in the regulation of dopamine biosynthesis
    • Perez, R.G.; Waymire, J.C.; Lin, E.; Liu, J.J.; Guo, F.; Zigmond, M.J. A role for alpha-synuclein in the regulation of dopamine biosynthesis. J. Neurosci. 2002, 22 (8), 3090-3099.
    • (2002) J. Neurosci , vol.22 , Issue.8 , pp. 3090-3099
    • Perez, R.G.1    Waymire, J.C.2    Lin, E.3    Liu, J.J.4    Guo, F.5    Zigmond, M.J.6
  • 63
    • 33747769942 scopus 로고    scopus 로고
    • Alpha-synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers
    • Beyer, K. Alpha-synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers. Acta Neuropathol. 2006, 112 (3), 237-251.
    • (2006) Acta Neuropathol , vol.112 , Issue.3 , pp. 237-251
    • Beyer, K.1
  • 64
    • 0030965452 scopus 로고    scopus 로고
    • Phosphorylation of a vesicular monoamine transporter by casein kinase II
    • Krantz, D.E.; Peter, D.; Liu, Y.; Edwards, R.H. Phosphorylation of a vesicular monoamine transporter by casein kinase II. J. Biol. Chem. 1997, 272 (10), 6752-6759.
    • (1997) J. Biol. Chem , vol.272 , Issue.10 , pp. 6752-6759
    • Krantz, D.E.1    Peter, D.2    Liu, Y.3    Edwards, R.H.4
  • 65
    • 0034714204 scopus 로고    scopus 로고
    • Synucleins are a novel class of substrates for G protein-coupled receptor kinases
    • Pronin, A.N.; Morris, A.J.; Surguchov, A.; Benovic, J.L. Synucleins are a novel class of substrates for G protein-coupled receptor kinases. J. Biol. Chem. 2000, 275 (34), 26515-26522.
    • (2000) J. Biol. Chem , vol.275 , Issue.34 , pp. 26515-26522
    • Pronin, A.N.1    Morris, A.J.2    Surguchov, A.3    Benovic, J.L.4
  • 66
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • Chen, L.; Feany, M.B. Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat. Neurosci. 2005, 8 (5), 657-663.
    • (2005) Nat. Neurosci , vol.8 , Issue.5 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 67
    • 0036174010 scopus 로고    scopus 로고
    • Fujiwara, H.; Hasegawa, M.; Dohmae, N.; Kawashima, A.; Masliah, E.; Goldberg, M.S.; Shen, J.; Takio, K.; Iwatsubo, T. alpha-Synuclein is phosphorylated in synucleinopathy lesions. Nat. Cell Biol. 2002, 4 (2), 160-164.
    • Fujiwara, H.; Hasegawa, M.; Dohmae, N.; Kawashima, A.; Masliah, E.; Goldberg, M.S.; Shen, J.; Takio, K.; Iwatsubo, T. alpha-Synuclein is phosphorylated in synucleinopathy lesions. Nat. Cell Biol. 2002, 4 (2), 160-164.
  • 69
    • 5444249974 scopus 로고    scopus 로고
    • Yamada, M.; Iwatsubo, T.; Mizuno, Y. and Mochizuki, H. Overexpression of alpha-synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of alpha-synuclein and activation of caspase-9: Resemblance to pathogenetic changes in Parkinson's disease. J. Neurochem. 2004, 91 (2), 451-461. 74. Souza, J.M.; Giasson, B.I.; Chen, Q.; Lee, V.M.; Ischiropoulos, H. Dityrosine cross-linking promotes formation of stable alpha -synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J. Biol. Chem. 2000, 275 (24), 18344-18349.
    • Yamada, M.; Iwatsubo, T.; Mizuno, Y. and Mochizuki, H. Overexpression of alpha-synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of alpha-synuclein and activation of caspase-9: Resemblance to pathogenetic changes in Parkinson's disease. J. Neurochem. 2004, 91 (2), 451-461. 74. Souza, J.M.; Giasson, B.I.; Chen, Q.; Lee, V.M.; Ischiropoulos, H. Dityrosine cross-linking promotes formation of stable alpha -synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J. Biol. Chem. 2000, 275 (24), 18344-18349.
  • 70
    • 9144229591 scopus 로고    scopus 로고
    • Functional consequences of alpha-synuclein tyrosine nitration: Diminished binding to lipid vesicles and increased fibril formation
    • Hodara, R.; Norris, E.H.; Giasson, B.I.; Mishizen-Eberz, A.J.; Lynch, D.R.; Lee, V.M.; Ischiropoulos, H. Functional consequences of alpha-synuclein tyrosine nitration: Diminished binding to lipid vesicles and increased fibril formation. J. Biol. Chem. 2004, 279 (46),47746-47753.
    • (2004) J. Biol. Chem , vol.279 , Issue.46 , pp. 47746-47753
    • Hodara, R.1    Norris, E.H.2    Giasson, B.I.3    Mishizen-Eberz, A.J.4    Lynch, D.R.5    Lee, V.M.6    Ischiropoulos, H.7
  • 72
    • 0037205095 scopus 로고    scopus 로고
    • Tyrosine 125 of alphasynuclein plays a critical role for dimerization following nitrative stress
    • Takahashi, T.; Yamashita, H.; Nakamura, T.; Nagano, Y.; Nakamura, S. Tyrosine 125 of alphasynuclein plays a critical role for dimerization following nitrative stress. Brain Res. 2002, 938 (1-2), 73-80.
    • (2002) Brain Res , vol.938 , Issue.1-2 , pp. 73-80
    • Takahashi, T.1    Yamashita, H.2    Nakamura, T.3    Nagano, Y.4    Nakamura, S.5
  • 74
    • 0035976835 scopus 로고    scopus 로고
    • Tofaris, G.K.; Layfield, R.; Spillantini, M.G. alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 2001, 509 (1), 22-26.
    • Tofaris, G.K.; Layfield, R.; Spillantini, M.G. alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 2001, 509 (1), 22-26.
  • 76
    • 0038307156 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alphasynucleinopathies
    • Sampathu, D.M.; Giasson, B.I.; Pawlyk, A.C.; Trojanowski, J.Q.; Lee, V.M. Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alphasynucleinopathies. Am. J. Pathol. 2003, 163 (1), 91-100.
    • (2003) Am. J. Pathol , vol.163 , Issue.1 , pp. 91-100
    • Sampathu, D.M.1    Giasson, B.I.2    Pawlyk, A.C.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 77
    • 0038051352 scopus 로고    scopus 로고
    • The cast of molecular characters in Parkinson's disease: Felons, conspirators, and suspects
    • Lim, K.L.; Dawson, V.L.; Dawson, T.M. The cast of molecular characters in Parkinson's disease: Felons, conspirators, and suspects. Ann. N. Y. Acad. Sci. 2003, 99, 80-92.
    • (2003) Ann. N. Y. Acad. Sci , vol.99 , pp. 80-92
    • Lim, K.L.1    Dawson, V.L.2    Dawson, T.M.3
  • 78
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M.; Rogers, S.W. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 1996, 21 (7), 267-271.
    • (1996) Trends Biochem. Sci , vol.21 , Issue.7 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 79
    • 38649119157 scopus 로고    scopus 로고
    • Identification and characterization of a new alpha-synuclein isoform and its role in Lewy body diseases
    • Beyer, K.; Domingo-Sabat, M.; Lao, J.I.; Carrato, C.; Ferrer, I.; Ariza, A. Identification and characterization of a new alpha-synuclein isoform and its role in Lewy body diseases. Neurogenetics 2008, 9 (1), 15-23.
    • (2008) Neurogenetics , vol.9 , Issue.1 , pp. 15-23
    • Beyer, K.1    Domingo-Sabat, M.2    Lao, J.I.3    Carrato, C.4    Ferrer, I.5    Ariza, A.6
  • 80
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis
    • Perrin, R.J.; Woods, W.S.; Clayton, D.F. and George, J.M. Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis. J. Biol. Chem. 2000, 275 (44), 34393-34398.
    • (2000) J. Biol. Chem , vol.275 , Issue.44 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 81
    • 0031728689 scopus 로고    scopus 로고
    • Synthetic filaments assembled from Cterminally truncated alpha-synuclein
    • Crowther, R.A.; Jakes, R.; Spillantini, M.G.; Goedert, M. Synthetic filaments assembled from Cterminally truncated alpha-synuclein. FEBS Lett. 1998, 436 (3), 309-312.
    • (1998) FEBS Lett , vol.436 , Issue.3 , pp. 309-312
    • Crowther, R.A.1    Jakes, R.2    Spillantini, M.G.3    Goedert, M.4
  • 82
    • 9444233904 scopus 로고    scopus 로고
    • Beyer, K.; Lao, J.I.; Carrato, C.; Mate, J.L.; Lopez, D.; Ferrer, I.; Ariza, A. Differential expression of alpha-synuclein isoforms in dementia with Lewy bodies. Neuropathol. Appl. Neurobiol. 2004, 30 (6), 601-607. 88. McLean, P.J.; Kawamata, H.; Ribich, S.; Hyman, B.T. Membrane association and protein conformation of alpha-synuclein in intact neurons. Effect of Parkinson's disease-linked mutations. J. Biol. Chem. 2000, 275 (12), 8812-8816.
    • Beyer, K.; Lao, J.I.; Carrato, C.; Mate, J.L.; Lopez, D.; Ferrer, I.; Ariza, A. Differential expression of alpha-synuclein isoforms in dementia with Lewy bodies. Neuropathol. Appl. Neurobiol. 2004, 30 (6), 601-607. 88. McLean, P.J.; Kawamata, H.; Ribich, S.; Hyman, B.T. Membrane association and protein conformation of alpha-synuclein in intact neurons. Effect of Parkinson's disease-linked mutations. J. Biol. Chem. 2000, 275 (12), 8812-8816.
  • 83
    • 0141841634 scopus 로고    scopus 로고
    • Gene expression changes presage neurodegeneration in a Drosophila model of Parkinson's disease
    • Scherzer, C.R.; Jensen, R.V.; Gullans, S.R.; Feany, M.B. Gene expression changes presage neurodegeneration in a Drosophila model of Parkinson's disease. Hum. Mol. Genet. 2003, 12 (19), 2457-2466.
    • (2003) Hum. Mol. Genet , vol.12 , Issue.19 , pp. 2457-2466
    • Scherzer, C.R.1    Jensen, R.V.2    Gullans, S.R.3    Feany, M.B.4
  • 84
    • 0037456578 scopus 로고    scopus 로고
    • The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease
    • Sharon, R.; Bar-Joseph, I.; Frosch, M.P.; Walsh, D.M.; Hamilton, J.A.; Selkoe, D.J. The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease. Neuron 2003, 37 (4), 583-595.
    • (2003) Neuron , vol.37 , Issue.4 , pp. 583-595
    • Sharon, R.1    Bar-Joseph, I.2    Frosch, M.P.3    Walsh, D.M.4    Hamilton, J.A.5    Selkoe, D.J.6
  • 87
    • 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.; van der Putten, H. Part II: alpha-Synuclein and its molecular pathophysiological role in neurodegenerative disease. Neuropharmacology 2003, 45 (1), 14-44.
    • (2003) Neuropharmacology , vol.45 , Issue.1 , pp. 14-44
    • Dev, K.K.1    Hofele, K.2    Barbieri, S.3    Buchman, V.L.4    van der Putten, H.5
  • 88
    • 0032492689 scopus 로고    scopus 로고
    • Regulation of phospholipase D2: Selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleins
    • Jenco, J.M.; Rawlingson, A.; Daniels, B.; Morris, A.J. Regulation of phospholipase D2: Selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleins. Biochemistry 1998, 37 (14), 4901-4909.
    • (1998) Biochemistry , vol.37 , Issue.14 , pp. 4901-4909
    • Jenco, J.M.1    Rawlingson, A.2    Daniels, B.3    Morris, A.J.4
  • 90
    • 27544507306 scopus 로고    scopus 로고
    • Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration
    • Chandra, S.; Gallardo, G.; Fernandez-Chacon, R.; Schluter, O.M.; Sudhof, T.C. Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration. Cell 2005, 123 (3), 383-396.
    • (2005) Cell , vol.123 , Issue.3 , pp. 383-396
    • Chandra, S.1    Gallardo, G.2    Fernandez-Chacon, R.3    Schluter, O.M.4    Sudhof, T.C.5
  • 92
    • 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 (47), 44284-44296.
    • (2001) J. Biol. Chem , vol.276 , Issue.47 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 93
    • 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 (3), 105-108.
    • (2001) FEBS Lett , vol.500 , Issue.3 , pp. 105-108
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 94
    • 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 (47), 43495-43498.
    • (2001) J. Biol. Chem , vol.276 , Issue.47 , pp. 43495-43498
    • Uversky, V.N.1    Lee, H.J.2    Li, J.3    Fink, A.L.4    Lee, S.J.5
  • 95
    • 0035815664 scopus 로고    scopus 로고
    • Uversky, V.N.; Li, J.; Fink, A.L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem. 2001, 276 (14), 10737-10744. 102. Munishkina, L.A.; Henriques, J.; Uversky, V.N.; Fink, A.L. Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation. Biochemistry 2004, 43 (11), 3289-3300.
    • Uversky, V.N.; Li, J.; Fink, A.L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem. 2001, 276 (14), 10737-10744. 102. Munishkina, L.A.; Henriques, J.; Uversky, V.N.; Fink, A.L. Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation. Biochemistry 2004, 43 (11), 3289-3300.
  • 96
    • 0037072284 scopus 로고    scopus 로고
    • Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
    • Ding, T.T.; Lee, S.J.; Rochet, J.C.; Lansbury, P.T., Jr. Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry 2002, 41 (32), 10209-10217.
    • (2002) Biochemistry , vol.41 , Issue.32 , pp. 10209-10217
    • Ding, T.T.1    Lee, S.J.2    Rochet, J.C.3    Lansbury Jr., P.T.4
  • 97
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism
    • Volles, M.J.; Lansbury, P.T., Jr. Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism. Biochemistry 2002, 41 (14), 4595-4602.
    • (2002) Biochemistry , vol.41 , Issue.14 , pp. 4595-4602
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 98
    • 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 (1), 17-37.
    • (2007) J Neurochem , vol.103 , Issue.1 , pp. 17-37
    • Uversky, V.N.1
  • 102
    • 0029125857 scopus 로고
    • Aging, energy, and oxidative stress in neurodegenerative diseases
    • Beal, M.F. Aging, energy, and oxidative stress in neurodegenerative diseases. Ann. Neurol. 1995, 38 (3), 357-366.
    • (1995) Ann. Neurol , vol.38 , Issue.3 , pp. 357-366
    • Beal, M.F.1
  • 103
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman, E.R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 1993, 62, 797-821.
    • (1993) Annu. Rev. Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 104
    • 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.; Fink, A.L. Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro. FEBS Lett. 2002, 517 (1-3), 239-244.
    • (2002) FEBS Lett , vol.517 , Issue.1-3 , 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
  • 105
    • 0034025513 scopus 로고    scopus 로고
    • Dopamine-induced apoptosis is mediated by oxidative stress and Is enhanced by cyanide in differentiated PC12 cells
    • Jones, D.C.; Gunasekar, P.G.; Borowitz, J.L.; Isom, G.E. Dopamine-induced apoptosis is mediated by oxidative stress and Is enhanced by cyanide in differentiated PC12 cells. J. Neurochem. 2000, 74 (6), 2296-2304.
    • (2000) J. Neurochem , vol.74 , Issue.6 , pp. 2296-2304
    • Jones, D.C.1    Gunasekar, P.G.2    Borowitz, J.L.3    Isom, G.E.4
  • 106
    • 0037040491 scopus 로고    scopus 로고
    • Human alpha-synuclein over-expression increases intracellular reactive oxygen species levels and susceptibility to dopamine
    • Junn, E.; Mouradian, M.M. Human alpha-synuclein over-expression increases intracellular reactive oxygen species levels and susceptibility to dopamine. Neurosci. Lett. 2002, 320 (3), 146-150.
    • (2002) Neurosci. Lett , vol.320 , Issue.3 , pp. 146-150
    • Junn, E.1    Mouradian, M.M.2
  • 107
    • 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.; Lansbury, P.T., Jr. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 2001, 294 (5545), 1346-1349.
    • (2001) Science , vol.294 , Issue.5545 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 108
    • 0141940629 scopus 로고    scopus 로고
    • What have we learnt from CDNA microarray gene expression studies about the role of iron in MPTP induced neurodegeneration and Parkinson's disease?
    • Youdim, M.B. What have we learnt from CDNA microarray gene expression studies about the role of iron in MPTP induced neurodegeneration and Parkinson's disease? J. Neural. Transm. Suppl. 2003, 65, 73-88.
    • (2003) J. Neural. Transm. Suppl , vol.65 , pp. 73-88
    • Youdim, M.B.1
  • 109
    • 2342496196 scopus 로고    scopus 로고
    • Sidhu, A.; Wersinger, C.; Vernier, P. alpha-Synuclein regulation of the dopaminergic transporter: A possible role in the pathogenesis of Parkinson's disease. FEBS Lett. 2004, 565 (1-3), 1-5. 117. Kaur, D.; Andersen, J. Does cellular iron dysregulation play a causative role in Parkinson's disease? Ageing Res. Rev. 2004, 3 (3), 327-343.
    • Sidhu, A.; Wersinger, C.; Vernier, P. alpha-Synuclein regulation of the dopaminergic transporter: A possible role in the pathogenesis of Parkinson's disease. FEBS Lett. 2004, 565 (1-3), 1-5. 117. Kaur, D.; Andersen, J. Does cellular iron dysregulation play a causative role in Parkinson's disease? Ageing Res. Rev. 2004, 3 (3), 327-343.
  • 110
    • 20444471551 scopus 로고    scopus 로고
    • Overexpression of superoxide dismutase or glutathione peroxidase protects against the paraquat + maneb-induced Parkinson disease phenotype
    • Thiruchelvam, M.; Prokopenko, O.; Cory-Slechta, D.A.; Buckley, B.; Mirochnitchenko, O. Overexpression of superoxide dismutase or glutathione peroxidase protects against the paraquat + maneb-induced Parkinson disease phenotype. J. Biol. Chem. 2005, 280 (23), 22530-22539.
    • (2005) J. Biol. Chem , vol.280 , Issue.23 , pp. 22530-22539
    • Thiruchelvam, M.1    Prokopenko, O.2    Cory-Slechta, D.A.3    Buckley, B.4    Mirochnitchenko, O.5
  • 111
    • 0642364992 scopus 로고    scopus 로고
    • Modulation of dopamine transporter function by alpha-synuclein is altered by impairment of cell adhesion and by induction of oxidative stress
    • Wersinger, C.; Prou, D.; Vernier, P.; Sidhu, A. Modulation of dopamine transporter function by alpha-synuclein is altered by impairment of cell adhesion and by induction of oxidative stress. FASEB J 2003, 17 (14), 2151-2153.
    • (2003) FASEB J , vol.17 , Issue.14 , pp. 2151-2153
    • Wersinger, C.1    Prou, D.2    Vernier, P.3    Sidhu, A.4
  • 113
    • 0027981759 scopus 로고
    • Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans
    • Multhaup, G. Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans. Biochimie 1994, 76 (3-4), 304-311.
    • (1994) Biochimie , vol.76 , Issue.3-4 , pp. 304-311
    • Multhaup, G.1
  • 114
    • 0037022186 scopus 로고    scopus 로고
    • Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro
    • Cohlberg, J.A.; Li, J.; Uversky, V.N.; Fink, A.L. Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro. Biochemistry 2002, 41 (5), 1502-1511.
    • (2002) Biochemistry , vol.41 , Issue.5 , pp. 1502-1511
    • Cohlberg, J.A.1    Li, J.2    Uversky, V.N.3    Fink, A.L.4
  • 115
  • 116
    • 0037378356 scopus 로고    scopus 로고
    • Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro
    • Goers, J.; Uversky, V.N.; Fink, A.L. Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro. Protein. Sci. 2003, 12 (4), 702-707.
    • (2003) Protein. Sci , vol.12 , Issue.4 , pp. 702-707
    • Goers, J.1    Uversky, V.N.2    Fink, A.L.3
  • 117
    • 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 (3), 1641-1644.
    • (2002) J. Biol. Chem , vol.277 , Issue.3 , 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
  • 118
    • 4644336256 scopus 로고    scopus 로고
    • Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson's disease
    • Andringa, G.; Lam, K.Y.; Chegary, M.; Wang, X.; Chase, T.N. and Bennett, M.C. Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson's disease. FASEB J. 2004, 18 (7), 932-934.
    • (2004) FASEB J , vol.18 , Issue.7 , pp. 932-934
    • Andringa, G.1    Lam, K.Y.2    Chegary, M.3    Wang, X.4    Chase, T.N.5    Bennett, M.C.6
  • 119
    • 0037452813 scopus 로고    scopus 로고
    • Tissue transglutaminase-induced aggregation of alpha-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies
    • Junn, E.; Ronchetti, R.D.; Quezado, M.M.; Kim, S.Y.; Mouradian, M.M. Tissue transglutaminase-induced aggregation of alpha-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies. Proc. Natl. Acad. Sci. USA 2003, 100 (4), 2047-2052.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.4 , pp. 2047-2052
    • Junn, E.1    Ronchetti, R.D.2    Quezado, M.M.3    Kim, S.Y.4    Mouradian, M.M.5
  • 120
    • 0036135523 scopus 로고    scopus 로고
    • Protein crosslinking, tissue transglutaminase, alternative splicing and neurodegeneration
    • Citron, B.A.; Suo, Z.; SantaCruz, K.; Davies, P.J.; Qin, F.; Festoff, B.W. Protein crosslinking, tissue transglutaminase, alternative splicing and neurodegeneration. Neurochem. Int. 2002, 40 (1), 69-78.
    • (2002) Neurochem. Int , vol.40 , Issue.1 , pp. 69-78
    • Citron, B.A.1    Suo, Z.2    SantaCruz, K.3    Davies, P.J.4    Qin, F.5    Festoff, B.W.6
  • 121
    • 0034602296 scopus 로고    scopus 로고
    • Jo, E.; McLaurin, J.; Yip, C.M.; St George-Hyslop, P.; Fraser, P.E. alpha-Synuclein membrane interactions and lipid specificity. J. Biol. Chem. 2000, 275 (44), 34328-33434.
    • Jo, E.; McLaurin, J.; Yip, C.M.; St George-Hyslop, P.; Fraser, P.E. alpha-Synuclein membrane interactions and lipid specificity. J. Biol. Chem. 2000, 275 (44), 34328-33434.
  • 122
    • 0033583215 scopus 로고    scopus 로고
    • Giasson, B.I.; Uryu, K.; Trojanowski, J.Q.; Lee, V.M. Mutant and wild type human alphasynucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem. 1999, 274 (12), 7619-7622. 131. Lindersson, E.; Lundvig, D.; Petersen, C.; Madsen, P.; Nyengaard, J.R.; Hojrup, P.; Moos, T.; Otzen, D.; Gai, W.P.; Blumbergs, P.C.; Jensen, P.H. p25alpha Stimulates alpha-synuclein aggregation and is co-localized with aggregated alpha-synuclein in alpha-synucleinopathies. J. Biol. Chem. 2005, 280 (7),5703-5715.
    • Giasson, B.I.; Uryu, K.; Trojanowski, J.Q.; Lee, V.M. Mutant and wild type human alphasynucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem. 1999, 274 (12), 7619-7622. 131. Lindersson, E.; Lundvig, D.; Petersen, C.; Madsen, P.; Nyengaard, J.R.; Hojrup, P.; Moos, T.; Otzen, D.; Gai, W.P.; Blumbergs, P.C.; Jensen, P.H. p25alpha Stimulates alpha-synuclein aggregation and is co-localized with aggregated alpha-synuclein in alpha-synucleinopathies. J. Biol. Chem. 2005, 280 (7),5703-5715.
  • 123
  • 125
    • 0035076647 scopus 로고    scopus 로고
    • Iwata, A.; Miura, S.; Kanazawa, I.; Sawada, M.; Nukina, N. alpha-Synuclein forms a complex with transcription factor Elk-1. J. Neurochem. 2001, 77 (1), 239-252.
    • Iwata, A.; Miura, S.; Kanazawa, I.; Sawada, M.; Nukina, N. alpha-Synuclein forms a complex with transcription factor Elk-1. J. Neurochem. 2001, 77 (1), 239-252.
  • 126
    • 11244258633 scopus 로고    scopus 로고
    • Lindersson, E.K.; Hojrup, P.; Gai, W.P.; Locker, D.; Martin, D.; Jensen, P.H. alpha-Synuclein filaments bind the transcriptional regulator HMGB-1. Neuroreport 2004, 15 (18), 2735-2739.
    • Lindersson, E.K.; Hojrup, P.; Gai, W.P.; Locker, D.; Martin, D.; Jensen, P.H. alpha-Synuclein filaments bind the transcriptional regulator HMGB-1. Neuroreport 2004, 15 (18), 2735-2739.
  • 127
    • 0036846119 scopus 로고    scopus 로고
    • TorsinA and heat shock proteins act as molecular chaperones: Suppression of alpha-synuclein aggregation
    • McLean, P.J.; Kawamata, H.; Shariff, S.; Hewett, J.; Sharma, N.; Ueda, K.; Breakefield, X.O.; Hyman, B.T. TorsinA and heat shock proteins act as molecular chaperones: Suppression of alpha-synuclein aggregation. J. Neurochem. 2002, 83 (4), 846-854.
    • (2002) J. Neurochem , vol.83 , Issue.4 , pp. 846-854
    • McLean, P.J.1    Kawamata, H.2    Shariff, S.3    Hewett, J.4    Sharma, N.5    Ueda, K.6    Breakefield, X.O.7    Hyman, B.T.8
  • 128
    • 0033215063 scopus 로고    scopus 로고
    • Synucleins in synaptic plasticity and neurodegenerative disorders
    • Clayton, D.F.; George, J.M. Synucleins in synaptic plasticity and neurodegenerative disorders. J. Neurosci. Res. 1999, 58 (1), 120-129.
    • (1999) J. Neurosci. Res , vol.58 , Issue.1 , pp. 120-129
    • Clayton, D.F.1    George, J.M.2
  • 129
    • 0037023699 scopus 로고    scopus 로고
    • Biophysical properties of the synucleins and their propensities to fibrillate: Inhibition of alphasynuclein assembly by beta- and gamma-synucleins
    • Uversky, V.N.; Li, J.; Souillac, P.; Millett, I.S.; Doniach, S.; Jakes, R.; Goedert, M.; Fink, A.L. Biophysical properties of the synucleins and their propensities to fibrillate: Inhibition of alphasynuclein assembly by beta- and gamma-synucleins. J. Biol. Chem. 2002, 277 (14), 11970-11978.
    • (2002) J. Biol. Chem , vol.277 , Issue.14 , pp. 11970-11978
    • Uversky, V.N.1    Li, J.2    Souillac, P.3    Millett, I.S.4    Doniach, S.5    Jakes, R.6    Goedert, M.7    Fink, A.L.8
  • 131
    • 0035950270 scopus 로고    scopus 로고
    • Hashimoto, M.; Rockenstein, E.; Mante, M.; Mallory, M.; Masliah, E. beta-Synuclein inhibits alpha-synuclein aggregation: A possible role as an anti-parkinsonian factor. Neuron 2001, 32 (2), 213-223.
    • Hashimoto, M.; Rockenstein, E.; Mante, M.; Mallory, M.; Masliah, E. beta-Synuclein inhibits alpha-synuclein aggregation: A possible role as an anti-parkinsonian factor. Neuron 2001, 32 (2), 213-223.
  • 133
    • 0030830270 scopus 로고    scopus 로고
    • Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly
    • Ii, K.; Ito, H.; Tanaka, K.; Hirano, A. Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly. J. Neuropathol. Exp. Neurol. 1997, 56 (2), 125-131.
    • (1997) J. Neuropathol. Exp. Neurol , vol.56 , Issue.2 , pp. 125-131
    • Ii, K.1    Ito, H.2    Tanaka, K.3    Hirano, A.4
  • 136
    • 2942620074 scopus 로고    scopus 로고
    • Klucken, J.; Shin, Y.; Masliah, E.; Hyman, B.T.; McLean, P.J. Hsp70 Reduces alpha-Synuclein Aggregation and Toxicity. J. Biol. Chem. 2004, 279 (24), 25497-25502. 146. Paleologou, K.E.; Irvine, G.B.; El-Agnaf, O.M. Alpha-synuclein aggregation in neurodegenerative diseases and its inhibition as a potential therapeutic strategy. Biochem. Soc. Trans. 2005, 33 (Pt 5), 1106-1110.
    • Klucken, J.; Shin, Y.; Masliah, E.; Hyman, B.T.; McLean, P.J. Hsp70 Reduces alpha-Synuclein Aggregation and Toxicity. J. Biol. Chem. 2004, 279 (24), 25497-25502. 146. Paleologou, K.E.; Irvine, G.B.; El-Agnaf, O.M. Alpha-synuclein aggregation in neurodegenerative diseases and its inhibition as a potential therapeutic strategy. Biochem. Soc. Trans. 2005, 33 (Pt 5), 1106-1110.
  • 137
    • 0026034279 scopus 로고    scopus 로고
    • 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 (2), 446-451.
    • 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 (2), 446-451.
  • 139
    • 0034660568 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of alpha-synuclein in the presence of Copper(II) and hydrogen peroxide
    • Paik, S.R.; Shin, H.J. and Lee, J.H. Metal-catalyzed oxidation of alpha-synuclein in the presence of Copper(II) and hydrogen peroxide. Arch. Biochem. Biophys. 2000, 378 (2), 269-277.
    • (2000) Arch. Biochem. Biophys , vol.378 , Issue.2 , pp. 269-277
    • Paik, S.R.1    Shin, H.J.2    Lee, J.H.3
  • 140
    • 0031571624 scopus 로고    scopus 로고
    • Aluminum-induced structural alterations of the precursor of the non-A beta component of Alzheimer's disease amyloid
    • Paik, S.R.; Lee, J.H.; Kim, D.H.; Chang, C.S.; Kim, J. Aluminum-induced structural alterations of the precursor of the non-A beta component of Alzheimer's disease amyloid. Arch. Biochem. Biophys. 1997, 344 (2), 325-334.
    • (1997) Arch. Biochem. Biophys , vol.344 , Issue.2 , pp. 325-334
    • Paik, S.R.1    Lee, J.H.2    Kim, D.H.3    Chang, C.S.4    Kim, J.5
  • 141
    • 34447629079 scopus 로고    scopus 로고
    • Interactions between metals and alpha-synuclein-function or artefact?
    • Brown, D.R. Interactions between metals and alpha-synuclein-function or artefact? FEBS J. 2007, 274 (15), 3766-3774.
    • (2007) FEBS J , vol.274 , Issue.15 , pp. 3766-3774
    • Brown, D.R.1
  • 142
    • 0041845349 scopus 로고    scopus 로고
    • Certain metals trigger fibrillation of methionine-oxidized alpha-synuclein
    • Yamin, G.; Glaser, C.B.; Uversky, V.N. and Fink, A.L. Certain metals trigger fibrillation of methionine-oxidized alpha-synuclein. J. Biol. Chem. 2003, 278 (30), 27630-27635.
    • (2003) J. Biol. Chem , vol.278 , Issue.30 , pp. 27630-27635
    • Yamin, G.1    Glaser, C.B.2    Uversky, V.N.3    Fink, A.L.4
  • 143
    • 0034663039 scopus 로고    scopus 로고
    • The A53T alphasynuclein mutation increases iron-dependent aggregation and toxicity
    • Ostrerova-Golts, N.; Petrucelli, L.; Hardy, J.; Lee, J.M.; Farer, M.; Wolozin, B. The A53T alphasynuclein mutation increases iron-dependent aggregation and toxicity. J. Neurosci. 2000, 20 (16), 6048-6054.
    • (2000) J. Neurosci , vol.20 , Issue.16 , pp. 6048-6054
    • Ostrerova-Golts, N.1    Petrucelli, L.2    Hardy, J.3    Lee, J.M.4    Farer, M.5    Wolozin, B.6
  • 144
    • 33751019425 scopus 로고    scopus 로고
    • Levels of alpha-synuclein mRNA in sporadic Parkinson disease patients
    • Chiba-Falek, O.; Lopez, G.J.; Nussbaum, R.L. Levels of alpha-synuclein mRNA in sporadic Parkinson disease patients. Mov. Disord. 2006, 21 (10), 1703-1708.
    • (2006) Mov. Disord , vol.21 , Issue.10 , pp. 1703-1708
    • Chiba-Falek, O.1    Lopez, G.J.2    Nussbaum, R.L.3
  • 145
    • 0033890821 scopus 로고    scopus 로고
    • Hsu, L.J.; Sagara, Y.; Arroyo, A.; Rockenstein, E.; Sisk, A.; Mallory, M.; Wong, J.; Takenouchi, T.; Hashimoto, M.; Masliah, E. alpha-synuclein promotes mitochondrial deficit and oxidative stress. Am. J. Pathol. 2000, 157 (2), 401-410.
    • Hsu, L.J.; Sagara, Y.; Arroyo, A.; Rockenstein, E.; Sisk, A.; Mallory, M.; Wong, J.; Takenouchi, T.; Hashimoto, M.; Masliah, E. alpha-synuclein promotes mitochondrial deficit and oxidative stress. Am. J. Pathol. 2000, 157 (2), 401-410.
  • 146
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis, L.; Larsen, K.E.; Rideout, H.J.; Sulzer, D.; Greene, L.A. Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J. Neurosci. 2001, 21 (24), 9549-9560.
    • (2001) J. Neurosci , vol.21 , Issue.24 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 147
    • 0037073748 scopus 로고    scopus 로고
    • Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion
    • Gosavi, N.; Lee, H.J.; Lee, J.S.; Patel, S.; Lee, S.J. Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion. J. Biol. Chem. 2002, 277 (50), 48984-48992.
    • (2002) J. Biol. Chem , vol.277 , Issue.50 , pp. 48984-48992
    • Gosavi, N.1    Lee, H.J.2    Lee, J.S.3    Patel, S.4    Lee, S.J.5
  • 148
    • 0036679197 scopus 로고    scopus 로고
    • Lo Bianco, C.; Ridet, J.L.; Schneider, B.L.; Deglon, N.; Aebischer, P. alpha -Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease. Proc. Natl. Acad. Sci. USA 2002, 99 (16), 10813-10818.
    • Lo Bianco, C.; Ridet, J.L.; Schneider, B.L.; Deglon, N.; Aebischer, P. alpha -Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease. Proc. Natl. Acad. Sci. USA 2002, 99 (16), 10813-10818.
  • 149
    • 0035964758 scopus 로고    scopus 로고
    • Altered expression of the synuclein family mRNA in Lewy body and Alzheimer's disease
    • Rockenstein, E.; Hansen, L.A.; Mallory, M.; Trojanowski, J.Q.; Galasko, D.; Masliah, E. Altered expression of the synuclein family mRNA in Lewy body and Alzheimer's disease. Brain Res. 2001, 914 (1-2), 48-56.
    • (2001) Brain Res , vol.914 , Issue.1-2 , pp. 48-56
    • Rockenstein, E.1    Hansen, L.A.2    Mallory, M.3    Trojanowski, J.Q.4    Galasko, D.5    Masliah, E.6
  • 150
    • 0033966487 scopus 로고    scopus 로고
    • Vila, M.; Vukosavic, S.; Jackson-Lewis, V.; Neystat, M.; Jakowec, M.; Przedborski, S. Alphasynuclein up-regulation in substantia nigra dopaminergic neurons following administration of the parkinsonian toxin MPTP. J. Neurochem. 2000, 74 (2), 721-729. 161. Talpade, D.J.; Greene, J.G.; Higgins, D.S., Jr.; Greenamyre, J.T. In vivo labeling of mitochondrial complex I (NADH:ubiquinone oxidoreductase) in rat brain using [(3)H]dihydrorotenone. J. Neurochem. 2000, 75 (6), 2611-2621.
    • Vila, M.; Vukosavic, S.; Jackson-Lewis, V.; Neystat, M.; Jakowec, M.; Przedborski, S. Alphasynuclein up-regulation in substantia nigra dopaminergic neurons following administration of the parkinsonian toxin MPTP. J. Neurochem. 2000, 74 (2), 721-729. 161. Talpade, D.J.; Greene, J.G.; Higgins, D.S., Jr.; Greenamyre, J.T. In vivo labeling of mitochondrial complex I (NADH:ubiquinone oxidoreductase) in rat brain using [(3)H]dihydrorotenone. J. Neurochem. 2000, 75 (6), 2611-2621.
  • 151
    • 2442636348 scopus 로고    scopus 로고
    • Biomedicine. Parkinson's-divergent causes, convergent mechanisms
    • Greenamyre, J.T.; Hastings, T.G. Biomedicine. Parkinson's-divergent causes, convergent mechanisms. Science 2004, 304 (5674), 1120-1122.
    • (2004) Science , vol.304 , Issue.5674 , pp. 1120-1122
    • Greenamyre, J.T.1    Hastings, T.G.2
  • 153
    • 0030790785 scopus 로고    scopus 로고
    • Iron-mediated generation of the neurotoxin 6-hydroxydopamine quinone by reaction of fatty acid hydroperoxides with dopamine: A possible contributory mechanism for neuronal degeneration in Parkinson's disease
    • Pezzella, A.; d'Ischia, M.; Napolitano, A.; Misuraca, G.; Prota, G. Iron-mediated generation of the neurotoxin 6-hydroxydopamine quinone by reaction of fatty acid hydroperoxides with dopamine: A possible contributory mechanism for neuronal degeneration in Parkinson's disease. J. Med. Chem. 1997, 40 (14), 2211-2216.
    • (1997) J. Med. Chem , vol.40 , Issue.14 , pp. 2211-2216
    • Pezzella, A.1    d'Ischia, M.2    Napolitano, A.3    Misuraca, G.4    Prota, G.5
  • 155
    • 31644435822 scopus 로고    scopus 로고
    • Metal ions and oxidative protein modification in neurological disease
    • Sayre, L.M.; Moreira, P.I.; Smith, M.A.; Perry, G. Metal ions and oxidative protein modification in neurological disease. Ann. Ist. Super. Sanita. 2005, 41 (2), 143-164.
    • (2005) Ann. Ist. Super. Sanita , vol.41 , Issue.2 , pp. 143-164
    • Sayre, L.M.1    Moreira, P.I.2    Smith, M.A.3    Perry, G.4
  • 156
    • 0041733066 scopus 로고    scopus 로고
    • Ironing out Parkinson's disease: Is therapeutic treatment with iron chelators a real possibility?
    • Kaur, D.; Andersen, J.K. Ironing out Parkinson's disease: Is therapeutic treatment with iron chelators a real possibility? Aging Cell 2002, 1 (1), 17-21.
    • (2002) Aging Cell , vol.1 , Issue.1 , pp. 17-21
    • Kaur, D.1    Andersen, J.K.2
  • 157
    • 13444274645 scopus 로고    scopus 로고
    • Iron dysregulation and Parkinson's disease
    • Andersen, J.K. Iron dysregulation and Parkinson's disease. J. Alzheimers. Dis. 2004, 6 (Suppl 6), S47-S52.
    • (2004) J. Alzheimers. Dis , vol.6 , Issue.SUPPL. 6
    • Andersen, J.K.1
  • 158
    • 0034731457 scopus 로고    scopus 로고
    • Combinatorial mRNA regulation: Iron regulatory proteins and isoiron-responsive elements (Iso-IREs)
    • Theil, E.C.; Eisenstein, R.S. Combinatorial mRNA regulation: Iron regulatory proteins and isoiron-responsive elements (Iso-IREs). J. Biol. Chem. 2000, 275 (52), 40659-40662.
    • (2000) J. Biol. Chem , vol.275 , Issue.52 , pp. 40659-40662
    • Theil, E.C.1    Eisenstein, R.S.2
  • 159
    • 0034531651 scopus 로고    scopus 로고
    • Iron regulatory proteins in pathobiology
    • Cairo, G.; Pietrangelo, A. Iron regulatory proteins in pathobiology. Biochem. J. 2000, 352 (Pt 2), 241-250.
    • (2000) Biochem. J , vol.352 , Issue.PART 2 , pp. 241-250
    • Cairo, G.1    Pietrangelo, A.2
  • 160
    • 0025736680 scopus 로고
    • Iron in brain function and dysfunction with emphasis on Parkinson's disease
    • Youdim, M.B.; Ben-Shachar, D.; Riederer, P. Iron in brain function and dysfunction with emphasis on Parkinson's disease. Eur. Neurol. 1991, 31 ( Suppl 1), 34-40.
    • (1991) Eur. Neurol , vol.31 , Issue.SUPPL. 1 , pp. 34-40
    • Youdim, M.B.1    Ben-Shachar, D.2    Riederer, P.3
  • 161
    • 0029969350 scopus 로고    scopus 로고
    • Nature of inhibition of mitochondrial respiratory complex I by 6-Hydroxydopamine
    • Glinka, Y.; Tipton, K.F.; Youdim, M.B. Nature of inhibition of mitochondrial respiratory complex I by 6-Hydroxydopamine. J. Neurochem. 1996, 66 (5), 2004-2010.
    • (1996) J. Neurochem , vol.66 , Issue.5 , pp. 2004-2010
    • Glinka, Y.1    Tipton, K.F.2    Youdim, M.B.3
  • 162
    • 0025980955 scopus 로고
    • The iron chelator desferrioxamine (Desferal) retards 6-hydroxydopamine-induced degeneration of nigrostriatal dopamine neurons
    • Ben-Shachar, D.; Eshel, G.; Finberg, J.P.; Youdim, M.B. The iron chelator desferrioxamine (Desferal) retards 6-hydroxydopamine-induced degeneration of nigrostriatal dopamine neurons. J. Neurochem. 1991, 56 (4), 1441-1444.
    • (1991) J. Neurochem , vol.56 , Issue.4 , pp. 1441-1444
    • Ben-Shachar, D.1    Eshel, G.2    Finberg, J.P.3    Youdim, M.B.4
  • 163
    • 0343550312 scopus 로고    scopus 로고
    • Apomorphine protects against MPTPinduced neurotoxicity in mice
    • Grunblatt, E.; Mandel, S.; Berkuzki, T.; Youdim, M.B. Apomorphine protects against MPTPinduced neurotoxicity in mice. Mov. Disord. 1999, 14 (4), 612-618.
    • (1999) Mov. Disord , vol.14 , Issue.4 , pp. 612-618
    • Grunblatt, E.1    Mandel, S.2    Berkuzki, T.3    Youdim, M.B.4
  • 165
    • 0041952925 scopus 로고    scopus 로고
    • Crompton, D.E.; Chinnery, P.F.; Fey, C.; Curtis, A.R.; Morris, C.M.; Kierstan, J.; Burt, A.; Young, F.; Coulthard, A.; Curtis, A.; Ince, P.G.; Bates, D.; Jackson, M.J.; Burn, J. Neuroferritinopathy: A window on the role of iron in neurodegeneration. Blood Cells Mol. Dis. 2002, 29 (3), 522-531.
    • Crompton, D.E.; Chinnery, P.F.; Fey, C.; Curtis, A.R.; Morris, C.M.; Kierstan, J.; Burt, A.; Young, F.; Coulthard, A.; Curtis, A.; Ince, P.G.; Bates, D.; Jackson, M.J.; Burn, J. Neuroferritinopathy: A window on the role of iron in neurodegeneration. Blood Cells Mol. Dis. 2002, 29 (3), 522-531.
  • 168
    • 0028981059 scopus 로고
    • Role for NF-kappa B in the regulation of ferritin H by tumor necrosis factor-alpha
    • Kwak, E.L.; Larochelle, D.A.; Beaumont, C.; Torti, S.V.; Torti, F.M. Role for NF-kappa B in the regulation of ferritin H by tumor necrosis factor-alpha. J. Biol. Chem. 1995, 270 (25), 15285-15293.
    • (1995) J. Biol. Chem , vol.270 , Issue.25 , pp. 15285-15293
    • Kwak, E.L.1    Larochelle, D.A.2    Beaumont, C.3    Torti, S.V.4    Torti, F.M.5
  • 169
    • 0028799569 scopus 로고
    • Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake
    • Martins, E.A.; Robalinho, R.L.; Meneghini, R. Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake. Arch. Biochem. Biophys. 1995, 316 (1), 128-134.
    • (1995) Arch. Biochem. Biophys , vol.316 , Issue.1 , pp. 128-134
    • Martins, E.A.1    Robalinho, R.L.2    Meneghini, R.3
  • 171
    • 0036798434 scopus 로고    scopus 로고
    • Lack of up-regulation of ferritin is associated with sustained iron regulatory protein-1 binding activity in the substantia nigra of patients with Parkinson's disease
    • Faucheux, B.A.; Martin, M.E.; Beaumont, C.; Hunot, S.; Hauw, J.J.; Agid, Y.; Hirsch, E.C. Lack of up-regulation of ferritin is associated with sustained iron regulatory protein-1 binding activity in the substantia nigra of patients with Parkinson's disease. J. Neurochem. 2002, 83 (2), 320-330.
    • (2002) J. Neurochem , vol.83 , Issue.2 , pp. 320-330
    • Faucheux, B.A.1    Martin, M.E.2    Beaumont, C.3    Hunot, S.4    Hauw, J.J.5    Agid, Y.6    Hirsch, E.C.7
  • 172
    • 0035920165 scopus 로고    scopus 로고
    • Regulation of the 75-kDa subunit of mitochondrial complex I by iron
    • Lin, E.; Graziano, J.H.; Freyer, G.A. Regulation of the 75-kDa subunit of mitochondrial complex I by iron. J Biol Chem 2001, 276 (29), 27685-27692.
    • (2001) J Biol Chem , vol.276 , Issue.29 , pp. 27685-27692
    • Lin, E.1    Graziano, J.H.2    Freyer, G.A.3
  • 173
    • 0025822118 scopus 로고
    • Identification of a novel iron-responsive element in murine and human erythroid deltaaminolevulinic acid synthase mRNA
    • Dandekar, T.; Stripecke, R.; Gray, N.K.; Goossen, B.; Constable, A.; Johansson, H.E.; Hentze, M.W. Identification of a novel iron-responsive element in murine and human erythroid deltaaminolevulinic acid synthase mRNA. EMBO J. 1991, 10 (7), 1903-1909.
    • (1991) EMBO J , vol.10 , Issue.7 , pp. 1903-1909
    • Dandekar, T.1    Stripecke, R.2    Gray, N.K.3    Goossen, B.4    Constable, A.5    Johansson, H.E.6    Hentze, M.W.7
  • 174
    • 0033947467 scopus 로고    scopus 로고
    • Sequestration of iron by Lewy bodies in Parkinson's disease
    • Castellani, R.J.; Siedlak, S.L.; Perry, G.; Smith, M.A. Sequestration of iron by Lewy bodies in Parkinson's disease. Acta Neuropathol. 2000, 100 (2), 111-114.
    • (2000) Acta Neuropathol , vol.100 , Issue.2 , pp. 111-114
    • Castellani, R.J.1    Siedlak, S.L.2    Perry, G.3    Smith, M.A.4
  • 175
    • 33847320669 scopus 로고    scopus 로고
    • The 5'-untranslated region of Parkinson's disease alpha-synuclein messengerRNA contains a predicted iron responsive element
    • Friedlich, A.L.; Tanzi, R.E. and Rogers, J.T. The 5'-untranslated region of Parkinson's disease alpha-synuclein messengerRNA contains a predicted iron responsive element. Mol. Psychiatry 2007, 12 (3), 222-223.
    • (2007) Mol. Psychiatry , vol.12 , Issue.3 , pp. 222-223
    • Friedlich, A.L.1    Tanzi, R.E.2    Rogers, J.T.3
  • 177
    • 0031759964 scopus 로고    scopus 로고
    • Poly(A)-tail-promoted translation in yeast: Implications for translational control
    • Preiss, T.; Muckenthaler, M.; Hentze, M.W. Poly(A)-tail-promoted translation in yeast: Implications for translational control. RNA 1998, 4 (11), 1321-1331.
    • (1998) RNA , vol.4 , Issue.11 , pp. 1321-1331
    • Preiss, T.1    Muckenthaler, M.2    Hentze, M.W.3
  • 179
    • 26444583962 scopus 로고    scopus 로고
    • Hundsdoerfer, P.; Thoma, C.; Hentze, M.W. Eukaryotic translation initiation factor 4GI and p97 promote cellular internal ribosome entry sequence-driven translation. Proc. Natl. Acad. Sci. USA 2005, 102 (38), 13421-13426. 191. Nie, M.; Htun, H. Different modes and potencies of translational repression by sequence-specific RNA-protein interaction at the 5'-UTR. Nucleic Acids Res. 2006, 34 (19), 5528-5540.
    • Hundsdoerfer, P.; Thoma, C.; Hentze, M.W. Eukaryotic translation initiation factor 4GI and p97 promote cellular internal ribosome entry sequence-driven translation. Proc. Natl. Acad. Sci. USA 2005, 102 (38), 13421-13426. 191. Nie, M.; Htun, H. Different modes and potencies of translational repression by sequence-specific RNA-protein interaction at the 5'-UTR. Nucleic Acids Res. 2006, 34 (19), 5528-5540.
  • 181
    • 0642309509 scopus 로고    scopus 로고
    • Drug discovery targeted to the Alzheimer's APP mRNA 5'-untranslated region: The action of paroxetine and dimercaptopropanol
    • Payton, S.; Cahill, C.M.; Randall, J.D.; Gullans, S.R.; Rogers, J.T. Drug discovery targeted to the Alzheimer's APP mRNA 5'-untranslated region: The action of paroxetine and dimercaptopropanol. J. Mol. Neurosci. 2003, 20 (3), 267-275.
    • (2003) J. Mol. Neurosci , vol.20 , Issue.3 , pp. 267-275
    • Payton, S.1    Cahill, C.M.2    Randall, J.D.3    Gullans, S.R.4    Rogers, J.T.5
  • 184
    • 0035912825 scopus 로고    scopus 로고
    • Phenserine regulates translation of beta -amyloid precursor protein mRNA by a putative interleukin-1 responsive element, a target for drug development
    • Shaw, K.T.; Utsuki, T.; Rogers, J.; Yu, Q.S.; Sambamurti, K.; Brossi, A.; Ge, Y.W.; Lahiri, D.K. ; Greig, N.H. Phenserine regulates translation of beta -amyloid precursor protein mRNA by a putative interleukin-1 responsive element, a target for drug development. Proc. Natl. Acad. Sci. USA 2001, 98 (13), 7605-7610.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.13 , pp. 7605-7610
    • Shaw, K.T.1    Utsuki, T.2    Rogers, J.3    Yu, Q.S.4    Sambamurti, K.5    Brossi, A.6    Ge, Y.W.7    Lahiri, D.K.8    Greig, N.H.9
  • 186
    • 0032990543 scopus 로고    scopus 로고
    • Antibodies to alpha-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimer's disease
    • Lippa, C.F.; Schmidt, M.L.; Lee, V.M.; Trojanowski, J.Q. Antibodies to alpha-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimer's disease. Ann. Neurol. 1999, 45 (3), 353-357.
    • (1999) Ann. Neurol , vol.45 , Issue.3 , pp. 353-357
    • Lippa, C.F.1    Schmidt, M.L.2    Lee, V.M.3    Trojanowski, J.Q.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.