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Volumn 469, Issue 3, 2016, Pages 529-534

α-Synuclein aggregation, seeding and inhibition by scyllo-inositol

Author keywords

Parkinson's disease; Protein misfolding; scyllo Inositol; Seeding; Synuclein

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID PROTEIN; CHIROINOSITOL; INOSITOL DERIVATIVE; MONOMER; PROTEIN INHIBITOR; SCYLLOINOSITOL; UNCLASSIFIED DRUG; INOSITOL; MULTIPROTEIN COMPLEX; PROTEIN BINDING; SCYLLITOL;

EID: 84953636182     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.12.043     Document Type: Article
Times cited : (23)

References (22)
  • 2
    • 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
    • K.A. Conway, S.J. Lee, J.C. Rochet, T.T. Ding, R.E. Williamson, and P.T. Lansbury 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. 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, P.T.6
  • 3
    • 0033538541 scopus 로고    scopus 로고
    • Alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease
    • S.J. Wood, J. Wypych, S. Steavenson, J.C. Louis, M. Citron, and A.L. Biere alpha-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
  • 9
    • 80051521167 scopus 로고    scopus 로고
    • Structural role of compensatory amino acid replacements in the alpha-synuclein protein
    • V. Losasso, A. Pietropaolo, C. Zannoni, S. Gustincich, and P. Carloni Structural role of compensatory amino acid replacements in the alpha-synuclein protein Biochemistry 50 2011 6994 7001
    • (2011) Biochemistry , vol.50 , pp. 6994-7001
    • Losasso, V.1    Pietropaolo, A.2    Zannoni, C.3    Gustincich, S.4    Carloni, P.5
  • 10
    • 80052087039 scopus 로고    scopus 로고
    • The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse alpha-synuclein
    • L. Kang, K.P. Wu, M. Vendruscolo, and J. Baum The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse alpha-synuclein J. Am. Chem. Soc. 133 2011 13465 13470
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 13465-13470
    • Kang, L.1    Wu, K.P.2    Vendruscolo, M.3    Baum, J.4
  • 11
    • 84860110592 scopus 로고    scopus 로고
    • Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure
    • M.S. Celej, R. Sarroukh, E. Goormaghtigh, G.D. Fidelio, J.M. Ruysschaert, and V. Raussens Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure Biochem. J. 443 2012 719 726
    • (2012) Biochem. J. , vol.443 , pp. 719-726
    • Celej, M.S.1    Sarroukh, R.2    Goormaghtigh, E.3    Fidelio, G.D.4    Ruysschaert, J.M.5    Raussens, V.6
  • 13
    • 65549102934 scopus 로고    scopus 로고
    • Inducible over-expression of wild type alpha-synuclein in human neuronal cells leads to caspase-dependent non-apoptotic death
    • K. Vekrellis, M. Xilouri, E. Emmanouilidou, and L. Stefanis Inducible over-expression of wild type alpha-synuclein in human neuronal cells leads to caspase-dependent non-apoptotic death J. Neurochem. 109 2009 1348 1362
    • (2009) J. Neurochem. , vol.109 , pp. 1348-1362
    • Vekrellis, K.1    Xilouri, M.2    Emmanouilidou, E.3    Stefanis, L.4
  • 14
    • 0034674785 scopus 로고    scopus 로고
    • Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid beta peptide and inhibit abeta -induced toxicity
    • J. McLaurin, R. Golomb, A. Jurewicz, J.P. Antel, and P.E. Fraser Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid beta peptide and inhibit abeta -induced toxicity J. Biol. Chem. 275 2000 18495 18502
    • (2000) J. Biol. Chem. , vol.275 , pp. 18495-18502
    • McLaurin, J.1    Golomb, R.2    Jurewicz, A.3    Antel, J.P.4    Fraser, P.E.5
  • 16
    • 0034609561 scopus 로고    scopus 로고
    • Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein
    • J.C. Rochet, K.A. Conway, and P.T. Lansbury Jr. Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein Biochemistry 39 2000 10619 10626
    • (2000) Biochemistry , vol.39 , pp. 10619-10626
    • Rochet, J.C.1    Conway, K.A.2    Lansbury, P.T.3
  • 17
    • 84907033533 scopus 로고    scopus 로고
    • Addition of exogenous alpha-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous alpha-synuclein to Lewy body and Lewy neurite-like aggregates
    • L.A. Volpicelli-Daley, K.C. Luk, and V.M. Lee Addition of exogenous alpha-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous alpha-synuclein to Lewy body and Lewy neurite-like aggregates Nat. Protoc. 9 2014 2135 2146
    • (2014) Nat. Protoc. , vol.9 , pp. 2135-2146
    • Volpicelli-Daley, L.A.1    Luk, K.C.2    Lee, V.M.3
  • 20
    • 84886728386 scopus 로고    scopus 로고
    • Hsp90 inhibits alpha-synuclein aggregation by interacting with soluble oligomers
    • S. Daturpalli, C.A. Waudby, S. Meehan, and S.E. Jackson Hsp90 inhibits alpha-synuclein aggregation by interacting with soluble oligomers J. Mol. Biol. 425 2013 4614 4628
    • (2013) J. Mol. Biol. , vol.425 , pp. 4614-4628
    • Daturpalli, S.1    Waudby, C.A.2    Meehan, S.3    Jackson, S.E.4
  • 21
    • 84899422309 scopus 로고    scopus 로고
    • Anti-amyloid compounds inhibit alpha-synuclein aggregation induced by protein misfolding cyclic amplification (PMCA)
    • M.E. Herva, S. Zibaee, G. Fraser, R.A. Barker, M. Goedert, and M.G. Spillantini Anti-amyloid compounds inhibit alpha-synuclein aggregation induced by protein misfolding cyclic amplification (PMCA) J. Biol. Chem. 289 2014 11897 11905
    • (2014) J. Biol. Chem. , vol.289 , pp. 11897-11905
    • Herva, M.E.1    Zibaee, S.2    Fraser, G.3    Barker, R.A.4    Goedert, M.5    Spillantini, M.G.6
  • 22
    • 84879137514 scopus 로고    scopus 로고
    • Binding mechanism of inositol stereoisomers to monomers and aggregates of Abeta(16-22)
    • G. Li, and R. Pomes Binding mechanism of inositol stereoisomers to monomers and aggregates of Abeta(16-22) J. Phys. Chem. B 117 2013 6603 6613
    • (2013) J. Phys. Chem. B , vol.117 , pp. 6603-6613
    • Li, G.1    Pomes, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.