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Volumn 9, Issue 2, 2012, Pages 464-476

Erratum to: A Novel "Molecular Tweezer" Inhibitor of α-Synuclein Neurotoxicity In Vitro and In Vivo (Neurotherapeutics, 10.1007/s13311-012-0105-1);A Novel "Molecular Tweezer" Inhibitor of α-Synuclein Neurotoxicity in Vitro and in Vivo

Author keywords

amyloid; neuroprotection; Parkinson's disease; synucleinopathy; zebrafish

Indexed keywords

ALPHA SYNUCLEIN; CLR 01; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 84859708060     PISSN: 19337213     EISSN: 18787479     Source Type: Journal    
DOI: 10.1007/s13311-012-0120-2     Document Type: Erratum
Times cited : (143)

References (56)
  • 1
    • 0030768929 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease
    • Nussbaum, R. L. and M. H. Polymeropoulos, Genetics of Parkinson's disease. Hum Mol Genet, 1997. 6(10): p. 1687-91.
    • (1997) Hum Mol Genet , vol.6 , Issue.10 , pp. 1687-1691
    • Nussbaum, R.L.1    Polymeropoulos, M.H.2
  • 2
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease
    • Kruger, R., Kuhn, W, Muller, T, et al., Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease. Nat Genet, 1998. 18(2): p. 106-8.
    • (1998) Nat Genet , vol.18 , Issue.2 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3
  • 3
    • 0031762949 scopus 로고    scopus 로고
    • Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia
    • Trojanowski, J. Q., Goedert, M., Iwatsubo, T., and Lee, V. M. Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia. Cell Death Differ, 1998. 5(10): p. 832-7.
    • (1998) Cell Death Differ , vol.5 , Issue.10 , pp. 832-837
    • Trojanowski, J.Q.1    Goedert, M.2    Iwatsubo, T.3    Lee, V.M.4
  • 5
    • 10744227740 scopus 로고    scopus 로고
    • Comparison of kindreds with parkinsonism and α-synuclein genomic multiplications
    • Farrer, M., Kachergus, J., Forno, L., et al., Comparison of kindreds with parkinsonism and α-synuclein genomic multiplications. Ann Neurol, 2004. 55(2): p. 174-9.
    • (2004) Ann Neurol , vol.55 , Issue.2 , pp. 174-179
    • Farrer, M.1    Kachergus, J.2    Forno, L.3
  • 6
    • 33745612296 scopus 로고    scopus 로고
    • Intersecting pathways to neurodegeneration in Parkinson's disease: Effects of the pesticide rotenone on DJ-1, α-synuclein, and the ubiquitin-proteasome system
    • Betarbet, R., Canet-Aviles, R. M., Sherer, T. B. et al., Intersecting pathways to neurodegeneration in Parkinson's disease: Effects of the pesticide rotenone on DJ-1, α-synuclein, and the ubiquitin-proteasome system. Neurobiol Dis, 2006. 22(2): p. 404-20.
    • (2006) Neurobiol Dis , vol.22 , Issue.2 , pp. 404-420
    • Betarbet, R.1    Canet-Aviles, R.M.2    Sherer, T.B.3
  • 7
    • 58049200137 scopus 로고    scopus 로고
    • Ziram causes dopaminergic cell damage by inhibiting E1 ligase of the proteasome
    • Chou, A. P., Maidment, N., Klintenberg, R. et al., Ziram causes dopaminergic cell damage by inhibiting E1 ligase of the proteasome. The Journal of biological chemistry, 2008. 283(50): p. 34696-703.
    • (2008) The Journal of biological chemistry , vol.283 , Issue.50 , pp. 34696-34703
    • Chou, A.P.1    Maidment, N.2    Klintenberg, R.3
  • 8
    • 70349481750 scopus 로고    scopus 로고
    • Enhanced α-synuclein expression in human neurodegenerative diseases: Pathogenetic and therapeutic implications
    • McCormack, A. L. and D. A. Di Monte, Enhanced α-synuclein expression in human neurodegenerative diseases: pathogenetic and therapeutic implications. Current protein & peptide science, 2009. 10(5): p. 476-82.
    • (2009) Current protein & peptide science , vol.10 , Issue.5 , pp. 476-482
    • McCormack, A.L.1    Di Monte, D.A.2
  • 10
    • 80055020556 scopus 로고    scopus 로고
    • Lysine-specific molecular tweezers are broadspectrum inhibitors of assembly and toxicity of amyloid proteins
    • Sinha, S., Lopes, D.H., Du, Z. et al., Lysine-specific molecular tweezers are broadspectrum inhibitors of assembly and toxicity of amyloid proteins. Journal of the American Chemical Society, 2011. 133(42): p. 16958-69.
    • (2011) Journal of the American Chemical Society , vol.133 , Issue.42 , pp. 16958-16969
    • Sinha, S.1    Lopes, D.H.2    Du, Z.3
  • 12
    • 80055101575 scopus 로고    scopus 로고
    • Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides
    • Rahimi, F., P. Maiti, and G. Bitan, Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides. Journal of visualized experiments: J Vis Exp. 2009 (23): http://www. jove. com/index/details. stp?id=1071.
    • (2009) Journal of visualized experiments: J Vis Exp , vol.23
    • Rahimi, F.1    Maiti, P.2    Bitan, G.3
  • 13
    • 33745143950 scopus 로고    scopus 로고
    • Inhibitory effects of pesticides on proteasome activity: Implication in Parkinson's disease
    • Wang, X.-F., Li, S., Chou, A. P. and Bronstein, J. M. Inhibitory effects of pesticides on proteasome activity: Implication in Parkinson's disease. Neurobiology of Disease, 2006. 23(1): p. 198-205.
    • (2006) Neurobiology of Disease , vol.23 , Issue.1 , pp. 198-205
    • Wang, X.-F.1    Li, S.2    Chou, A.P.3    Bronstein, J.M.4
  • 16
    • 2342471959 scopus 로고    scopus 로고
    • Correction of multi-gene deficiency in vivo using a single 'self-cleaving' 2A peptide-based retroviral vector
    • Szymczak, A. L., Workman, C. J., Wang, Y., et al., Correction of multi-gene deficiency in vivo using a single 'self-cleaving' 2A peptide-based retroviral vector. Nat Biotechnol, 2004. 22(5): p. 589-94.
    • (2004) Nat Biotechnol , vol.22 , Issue.5 , pp. 589-594
    • Szymczak, A.L.1    Workman, C.J.2    Wang, Y.3
  • 17
    • 0036803294 scopus 로고    scopus 로고
    • I-SceI meganuclease mediates highly efficient transgenesis in fish
    • Thermes, V., Grabher, C., Ristoratore, F., et al., I-SceI meganuclease mediates highly efficient transgenesis in fish. Mech Dev, 2002. 118(1-2): p. 91-8.
    • (2002) Mech Dev , vol.118 , Issue.1-2 , pp. 91-98
    • Thermes, V.1    Grabher, C.2    Ristoratore, F.3
  • 18
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N. F., R. M. Sampat, and R. R. Kopito, Impairment of the ubiquitin-proteasome system by protein aggregation. Science, 2001. 292(5521): p. 1552-5.
    • (2001) Science , vol.292 , Issue.5521 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 19
    • 0024347761 scopus 로고
    • Dark-induced changes in activity and compartmentalization of retinal calmodulin kinase in the rat
    • Bronstein, J., Wasterlain, C. G., Lasher, R., and Farber, D. B. Dark-induced changes in activity and compartmentalization of retinal calmodulin kinase in the rat. Brain Res, 1989. 495(1): p. 83-8.
    • (1989) Brain Res , vol.495 , Issue.1 , pp. 83-88
    • Bronstein, J.1    Wasterlain, C.G.2    Lasher, R.3    Farber, D.B.4
  • 20
    • 57049147881 scopus 로고    scopus 로고
    • Characterization of housekeeping genes in zebrafish: Male-female differences and effects of tissue type, developmental stage and chemical treatment
    • McCurley, A. T. and G. V. Callard, Characterization of housekeeping genes in zebrafish: male-female differences and effects of tissue type, developmental stage and chemical treatment. BMC molecular biology, 2008. 9: p. 102.
    • (2008) BMC molecular biology , vol.9 , pp. 102
    • McCurley, A.T.1    Callard, G.V.2
  • 22
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
    • Desplats, P., Lee, H. J., Bae, E. J., et al., Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein. Proceedings of the National Academy of Sciences USA, 2009. 106(31): p. 13010-5.
    • (2009) Proceedings of the National Academy of Sciences USA , vol.106 , Issue.31 , pp. 13010-13015
    • Desplats, P.1    Lee, H.J.2    Bae, E.J.3
  • 23
    • 72149119358 scopus 로고    scopus 로고
    • Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells
    • Luk, K. C., Song, C., O'Brien, P., et al., Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Proceedings of the National Academy of Sciences USA, 2009. 106(47): p. 20051-6.
    • (2009) Proceedings of the National Academy of Sciences USA , vol.106 , Issue.47 , pp. 20051-20056
    • Luk, K.C.1    Song, C.2    O'Brien, P.3
  • 24
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by α-synuclein oligomers provides evidence for spreading of α-synuclein pathology
    • Danzer, K. M., Krebs, S. K., Wolff, M., Birk, G., and Hengerer, B. Seeding induced by α-synuclein oligomers provides evidence for spreading of α-synuclein pathology. Journal of Neurochemistry, 2009. 111(1): p. 192-203.
    • (2009) Journal of Neurochemistry , vol.111 , Issue.1 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3    Birk, G.4    Hengerer, B.5
  • 25
    • 0035910347 scopus 로고    scopus 로고
    • The teleostean (zebrafish) dopaminergic system ascending to the subpallium (striatum) is located in the basal diencephalon (posterior tuberculum)
    • Rink, E. and M. F. Wullimann, The teleostean (zebrafish) dopaminergic system ascending to the subpallium (striatum) is located in the basal diencephalon (posterior tuberculum). Brain Res, 2001. 889(1-2): p. 316-30.
    • (2001) Brain Res , vol.889 , Issue.1-2 , pp. 316-330
    • Rink, E.1    Wullimann, M.F.2
  • 26
    • 77957334868 scopus 로고    scopus 로고
    • Sex reversal in zebrafish fancl mutants is caused by Tp53-mediated germ cell apoptosis
    • Rodriguez-Mari, A., Canestro, C., Bremiller, R. A. et al., Sex reversal in zebrafish fancl mutants is caused by Tp53-mediated germ cell apoptosis. PLoS Genetics, 2010. 6(7): p. e1001034.
    • (2010) PLoS Genetics , vol.6 , Issue.7 , pp. 1001034
    • Rodriguez-Mari, A.1    Canestro, C.2    Bremiller, R.A.3
  • 27
    • 0038413759 scopus 로고    scopus 로고
    • Aggregated and Monomeric α -Synuclein Bind to the S6' Proteasomal Protein and Inhibit Proteasomal Function
    • Snyder, H., Aggregated and Monomeric α -Synuclein Bind to the S6' Proteasomal Protein and Inhibit Proteasomal Function. Journal of Biological Chemistry, 2003. 278(14): p. 11753-11759.
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 11753-11759
    • Snyder, H.1
  • 28
    • 45749101292 scopus 로고    scopus 로고
    • Design of an N-methylated peptide inhibitor of α-synuclein aggregation guided by solid-state NMR
    • Madine, J., A. J. Doig, and D. A. Middleton, Design of an N-methylated peptide inhibitor of α-synuclein aggregation guided by solid-state NMR. Journal of the American Chemical Society, 2008. 130(25): p. 7873-81.
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.25 , pp. 7873-7881
    • Madine, J.1    Doig, A.J.2    Middleton, D.A.3
  • 30
    • 8844224948 scopus 로고    scopus 로고
    • Rifampicin inhibits α-synuclein fibrillation and disaggregates fibrils
    • Li, J., Zhu, M., Rajamani, S., Uversky, V. N. and Fink, A. L Rifampicin inhibits α-synuclein fibrillation and disaggregates fibrils. Chemistry & biology, 2004. 11(11): p. 1513-21.
    • (2004) Chemistry & biology , vol.11 , Issue.11 , pp. 1513-1521
    • Li, J.1    Zhu, M.2    Rajamani, S.3    Uversky, V.N.4    Fink, A.L.5
  • 32
    • 33646570598 scopus 로고    scopus 로고
    • Small molecule inhibitors of α-synuclein filament assembly
    • Masuda, M., Suzuki, N., Taniguchi, S., et al., Small molecule inhibitors of α-synuclein filament assembly. Biochemistry, 2006. 45(19): p. 6085-94.
    • (2006) Biochemistry , vol.45 , Issue.19 , pp. 6085-6094
    • Masuda, M.1    Suzuki, N.2    Taniguchi, S.3
  • 33
    • 59849083504 scopus 로고    scopus 로고
    • Inhibition of α-synuclein fibril assembly by small molecules: Analysis using epitope-specific antibodies
    • Masuda, M., Hasegawa, M., Nonaka, T. et al., Inhibition of α-synuclein fibril assembly by small molecules: analysis using epitope-specific antibodies. FEBS Letters, 2009. 583(4): p. 787-91.
    • (2009) FEBS Letters , vol.583 , Issue.4 , pp. 787-791
    • Masuda, M.1    Hasegawa, M.2    Nonaka, T.3
  • 34
    • 42349111633 scopus 로고    scopus 로고
    • Characterization of α-synuclein interactions with selected aggregation-inhibiting small molecules
    • Rao, J. N., V. Dua, and T. S. Ulmer, Characterization of α-synuclein interactions with selected aggregation-inhibiting small molecules. Biochemistry, 2008. 47(16): p. 4651-6.
    • (2008) Biochemistry , vol.47 , Issue.16 , pp. 4651-4656
    • Rao, J.N.1    Dua, V.2    Ulmer, T.S.3
  • 35
  • 36
    • 44849087785 scopus 로고    scopus 로고
    • EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
    • Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A. et al., EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nature structural & molecular biology, 2008. 15(6): p. 558-66.
    • (2008) Nature structural & molecular biology , vol.15 , Issue.6 , pp. 558-566
    • Ehrnhoefer, D.E.1    Bieschke, J.2    Boeddrich, A.3
  • 37
    • 39349111263 scopus 로고    scopus 로고
    • Aggregator compounds confound amyloid fibrillization assay
    • Rishton, G. M., Aggregator compounds confound amyloid fibrillization assay. Nature Chemical Biology, 2008. 4(3): p. 159-60.
    • (2008) Nature Chemical Biology , vol.4 , Issue.3 , pp. 159-160
    • Rishton, G.M.1
  • 38
    • 39349094523 scopus 로고    scopus 로고
    • Small-molecule aggregates inhibit amyloid polymerization
    • Feng, B. Y., Toyama, B. H., Wille, H. et al., Small-molecule aggregates inhibit amyloid polymerization. Nature Chemical Biology, 2008. 4(3): p. 197-9.
    • (2008) Nature Chemical Biology , vol.4 , Issue.3 , pp. 197-199
    • Feng, B.Y.1    Toyama, B.H.2    Wille, H.3
  • 40
    • 70350338222 scopus 로고    scopus 로고
    • Pre-fibrillar α-synuclein variants with impaired β-structure increase neurotoxicity in Parkinson's disease models
    • Karpinar, D. P., Balija, M. B., Kugler, S. et al., Pre-fibrillar α-synuclein variants with impaired β-structure increase neurotoxicity in Parkinson's disease models. The EMBO journal, 2009. 28(20): p. 3256-68.
    • (2009) The EMBO journal , vol.28 , Issue.20 , pp. 3256-3268
    • Karpinar, D.P.1    Balija, M.B.2    Kugler, S.3
  • 41
    • 55949092886 scopus 로고    scopus 로고
    • α-synuclein misfolding and neurodegenerative diseases
    • Uversky, V. N., α-synuclein misfolding and neurodegenerative diseases. Current protein & peptide science, 2008. 9(5): p. 507-40.
    • (2008) Current protein & peptide science , vol.9 , Issue.5 , pp. 507-540
    • Uversky, V.N.1
  • 42
    • 77951976610 scopus 로고    scopus 로고
    • Cell-produced α-synuclein oligomers are targeted to, and impair, the 26S proteasome
    • Emmanouilidou, E., L. Stefanis, and K. Vekrellis, Cell-produced α-synuclein oligomers are targeted to, and impair, the 26S proteasome. Neurobiology of Aging, 2010. 31(6): p. 953-968.
    • (2010) Neurobiology of Aging , vol.31 , Issue.6 , pp. 953-968
    • Emmanouilidou, E.1    Stefanis, L.2    Vekrellis, K.3
  • 43
    • 50649112184 scopus 로고    scopus 로고
    • α-Synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: Understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis
    • Zhang, N. Y., Z. Tang, and C. W. Liu, α-Synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis. The Journal of biological chemistry, 2008. 283(29): p. 20288-98.
    • (2008) The Journal of biological chemistry , vol.283 , Issue.29 , pp. 20288-20298
    • Zhang, N.Y.1    Tang, Z.2    Liu, C.W.3
  • 45
    • 34548462199 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome pathway is a downstream endoplasmic reticulum stress response induced by extracellular human islet amyloid polypeptide and contributes to pancreatic β-cell apoptosis
    • Casas, S., Gomis, R., Gribble, F. M., Altirriba, J., Knuutila, S., and Novials, A. Impairment of the ubiquitin-proteasome pathway is a downstream endoplasmic reticulum stress response induced by extracellular human islet amyloid polypeptide and contributes to pancreatic β-cell apoptosis. Diabetes, 2007. 56(9): p. 2284-94.
    • (2007) Diabetes , vol.56 , Issue.9 , pp. 2284-2294
    • Casas, S.1    Gomis, R.2    Gribble, F.M.3    Altirriba, J.4    Knuutila, S.5    Novials, A.6
  • 46
    • 78751490442 scopus 로고    scopus 로고
    • β-cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency
    • Costes, S., Huang, C. J., Gurlo, T. et al., β-cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency. Diabetes, 2011. 60(1): p. 227-38.
    • (2011) Diabetes , vol.60 , Issue.1 , pp. 227-238
    • Costes, S.1    Huang, C.J.2    Gurlo, T.3
  • 48
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught, K. S. and P. Jenner, Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci Lett, 2001. 297(3): p. 191-4.
    • (2001) Neurosci Lett , vol.297 , Issue.3 , pp. 191-194
    • McNaught, K.S.1    Jenner, P.2
  • 49
  • 50
    • 33746850545 scopus 로고    scopus 로고
    • Proteasome inhibition and Parkinson's disease modeling
    • Bove, J., Zhou, C., Jackson-Lewis, V., et al., Proteasome inhibition and Parkinson's disease modeling. Annals of Neurology, 2006. 60(2): p. 260-4.
    • (2006) Annals of Neurology , vol.60 , Issue.2 , pp. 260-264
    • Bove, J.1    Zhou, C.2    Jackson-Lewis, V.3
  • 51
    • 33746851988 scopus 로고    scopus 로고
    • Failure of proteasome inhibitor administration to provide a model of Parkinson's disease in rats and monkeys
    • Kordower, J. H., Kanaan, N. M., Chu, Y., Suresh Babu, R., and Stansell, J., Failure of proteasome inhibitor administration to provide a model of Parkinson's disease in rats and monkeys. Annals of Neurology, 2006. 60(2): p. 264-8.
    • (2006) Annals of Neurology , vol.60 , Issue.2 , pp. 264-268
    • Kordower, J.H.1    Kanaan, N.M.2    Chu, Y.3    Suresh Babu, R.4    Stansell, J.5
  • 52
    • 33746791044 scopus 로고    scopus 로고
    • Lack of nigrostriatal pathology in a rat model of proteasome inhibition
    • Manning-Bog, A. B., Reaney, S. H., Chou, V. P. et al., Lack of nigrostriatal pathology in a rat model of proteasome inhibition. Annals of Neurology, 2006. 60(2): p. 256-60.
    • (2006) Annals of Neurology , vol.60 , Issue.2 , pp. 256-260
    • Manning-Bog, A.B.1    Reaney, S.H.2    Chou, V.P.3
  • 53
    • 33746839220 scopus 로고    scopus 로고
    • Proteasome inhibitor-induced model of Parkinson's disease
    • McNaught, K. S. and C. W. Olanow, Proteasome inhibitor-induced model of Parkinson's disease. Annals of Neurology, 2006. 60(2): p. 243-7.
    • (2006) Annals of Neurology , vol.60 , Issue.2 , pp. 243-247
    • McNaught, K.S.1    Olanow, C.W.2
  • 55
    • 33746851548 scopus 로고    scopus 로고
    • Reproducible nigral cell loss after systemic proteasomal inhibitor administration to rats
    • Zeng, B. Y., Bukhatwa, S., Hikima, A., Rose, S., and Jenner, P. Reproducible nigral cell loss after systemic proteasomal inhibitor administration to rats. Annals of Neurology, 2006. 60(2): p. 248-52.
    • (2006) Annals of Neurology , vol.60 , Issue.2 , pp. 248-252
    • Zeng, B.Y.1    Bukhatwa, S.2    Hikima, A.3    Rose, S.4    Jenner, P.5
  • 56
    • 38849174979 scopus 로고    scopus 로고
    • Dopamine-modified α-synuclein blocks chaperone-mediated autophagy
    • Martinez-Vicente, M., Talloczy, Z., Kaushik, S., et al., Dopamine-modified α-synuclein blocks chaperone-mediated autophagy. Journal of Clinical Investigation, 2008. 118(2): p. 777-788.
    • (2008) Journal of Clinical Investigation , vol.118 , Issue.2 , pp. 777-788
    • Martinez-Vicente, M.1    Talloczy, Z.2    Kaushik, S.3


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