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Volumn 387, Issue 4, 2009, Pages 682-687

β-Sheet-breaking peptides inhibit the fibrillation of human α-synuclein

Author keywords

Synuclein; Conformational switch; Peptide inhibitors; Protein amyloid; Protein fibrils

Indexed keywords

ALPHA SYNUCLEIN; HEXAPEPTIDE; PROLYLGLYCYLVALYLTHREONYLALANYLVALINE; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 68549139858     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.07.083     Document Type: Article
Times cited : (29)

References (27)
  • 1
    • 33646672862 scopus 로고    scopus 로고
    • Charcot and Parkinson's disease
    • Factor S., and Weiner W. (Eds), Demos Medical Publishing, New York
    • Goetz C.G. Charcot and Parkinson's disease. In: Factor S., and Weiner W. (Eds). Parkinson's Disease Diagnosis and Clinical Management (2002), Demos Medical Publishing, New York 19-26
    • (2002) Parkinson's Disease Diagnosis and Clinical Management , pp. 19-26
    • Goetz, C.G.1
  • 5
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both α-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 α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. USA 97 (2000) 571-576
    • (2000) Proc. Natl. Acad. Sci. USA , 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
  • 6
    • 6344228684 scopus 로고    scopus 로고
    • Mutation E46K increases phospholipid binding and assembly into filaments of human α-synuclein
    • Choi W., Zibaee S., Jakes R., Serpell L.C., Davletov B., Crowther R.A., and Goedert M. Mutation E46K increases phospholipid binding and assembly into filaments of human α-synuclein. FEBS Lett. 576 (2004) 363-368
    • (2004) FEBS Lett. , vol.576 , pp. 363-368
    • Choi, W.1    Zibaee, S.2    Jakes, R.3    Serpell, L.C.4    Davletov, B.5    Crowther, R.A.6    Goedert, M.7
  • 10
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany M.B., and Bender W.W. A Drosophila model of Parkinson's disease. Nature 404 (2000) 394-398
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 11
  • 13
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: abnormal protein aggregation in neurodegeneration
    • Koo E.H., Lansbury Jr. P.T., and Kelly J.W. Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc. Natl. Acad. Sci. USA 96 (1999) 9989-9990
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury Jr., P.T.2    Kelly, J.W.3
  • 14
    • 33644945380 scopus 로고    scopus 로고
    • Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for α-synuclein fibrils in vitro
    • Ono K., and Yamada M. Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for α-synuclein fibrils in vitro. J. Neurochem. 97 (2006) 105-115
    • (2006) J. Neurochem. , vol.97 , pp. 105-115
    • Ono, K.1    Yamada, M.2
  • 15
    • 0141642253 scopus 로고    scopus 로고
    • Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease
    • Ono K., Yoshiike Y., Takashima A., Hasegawa K., Kaike H., and Yamada M. Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease. J. Neurochem. 87 (2003) 172-181
    • (2003) J. Neurochem. , vol.87 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Kaike, H.5    Yamada, M.6
  • 16
    • 0030572683 scopus 로고    scopus 로고
    • For protein misassembly, it's the "I" decade
    • Wetzel R. For protein misassembly, it's the "I" decade. Cell 86 (1996) 699-702
    • (1996) Cell , vol.86 , pp. 699-702
    • Wetzel, R.1
  • 17
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition
    • Speed M.A., Wang D.I., and King J. Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition. Nat. Biotechnol. 14 (1996) 1283-1287
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.2    King, J.3
  • 20
    • 0031873102 scopus 로고    scopus 로고
    • β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • Soto C., Sigurdsson E.M., Morelli L., Kumar R.A., Castano E.M., and Frangione B. β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy. Nat. Med. 7 (1998) 822-826
    • (1998) Nat. Med. , vol.7 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 22
    • 0033538541 scopus 로고    scopus 로고
    • Synuclein fibrillogenesis is nucleation-dependent: implications for the pathogenesis of Parkinson's disease
    • Wood S.J., Wypych J., Steavenson S., Louis J.C., Citron M., and Biere A.L. Synuclein fibrillogenesis is nucleation-dependent: implications for the pathogenesis of Parkinson's disease. J. Biol. Chem. 274 (1999) 19509-19512
    • (1999) J. Biol. Chem. , vol.274 , pp. 19509-19512
    • Wood, S.J.1    Wypych, J.2    Steavenson, S.3    Louis, J.C.4    Citron, M.5    Biere, A.L.6
  • 23
    • 39749133508 scopus 로고    scopus 로고
    • Sequence determinants regulating fibrillation of human α-synuclein
    • Koo H.-J., Lee H.-J., and Im H. Sequence determinants regulating fibrillation of human α-synuclein. Biochem. Biophys. Res. Commun. 368 (2008) 772-778
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 772-778
    • Koo, H.-J.1    Lee, H.-J.2    Im, H.3
  • 24
    • 67649213482 scopus 로고    scopus 로고
    • Aggregation-defective α-synuclein mutants inhibit the fibrillation of Parkinson's disease-linked α-synuclein variants
    • Koo H.-J., Choi M.-Y., and Im H. Aggregation-defective α-synuclein mutants inhibit the fibrillation of Parkinson's disease-linked α-synuclein variants. Biochem. Biophys. Res. Commun. 386 (2009) 165-169
    • (2009) Biochem. Biophys. Res. Commun. , vol.386 , pp. 165-169
    • Koo, H.-J.1    Choi, M.-Y.2    Im, H.3
  • 25
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of α-synuclein and its mechanism of neurotoxicity in Parkinson's disease
    • Volles M.J., and Lansbury Jr. P.T. Zeroing in on the pathogenic form of α-synuclein and its mechanism of neurotoxicity in Parkinson's disease. Biochemistry 42 (2003) 7871-7878
    • (2003) Biochemistry , vol.42 , pp. 7871-7878
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 26
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly
    • Giasson B.I., Murray I.V.J., Trojanowski J.Q., and Lee V.M.-Y. A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly. J. Biol. Chem. 276 (2001) 2380-2386
    • (2001) J. Biol. Chem. , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.J.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 27
    • 0034169203 scopus 로고    scopus 로고
    • Toxicity of non-Aβ component (NAC) of Alzheimer's disease amyloid, and N-terminal fragment thereof, correlates to formation of β-sheet structure and fibrils
    • Bodles A.M., Guthrie D.J.S., Harriott P., Campbell P., and Irvine G.B. Toxicity of non-Aβ component (NAC) of Alzheimer's disease amyloid, and N-terminal fragment thereof, correlates to formation of β-sheet structure and fibrils. Eur. J. Biochem. 267 (2000) 2186-2194
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2186-2194
    • Bodles, A.M.1    Guthrie, D.J.S.2    Harriott, P.3    Campbell, P.4    Irvine, G.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.