메뉴 건너뛰기




Volumn 6, Issue 12, 2010, Pages 702-706

Erratum: Cell-to-cell transmission of non-prion protein aggregates (Nature Reviews Neurology (2010) 6 (702-706) DOI: 10.1038/nrneurol.2010.145));Cell-to-cell transmission of non-prion protein aggregates

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID A PROTEIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN A2; HUNTINGTIN; POLYGLUTAMINE; TAU PROTEIN;

EID: 78649907008     PISSN: 17594758     EISSN: 17594766     Source Type: Journal    
DOI: 10.1038/nrneurol.2010.191     Document Type: Erratum
Times cited : (268)

References (43)
  • 1
    • 7044238416 scopus 로고    scopus 로고
    • Neurodegenerative diseases: A decade of discoveries paves the way for therapeutic breakthroughs
    • Forman, M. S., Trojanowski, J. Q. & Lee, V. M. Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs. Nat. Med. 10, 1055-1063 (2004).
    • (2004) Nat. Med. , vol.10 , pp. 1055-1063
    • Forman, M.S.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 2
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury, P. T. & Lashuel, H. A. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443, 774-779 (2006).
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 3
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe, C. G. Structural classification of toxic amyloid oligomers. J. Biol. Chem. 283, 29639-29643 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 4
    • 52349111812 scopus 로고    scopus 로고
    • Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases
    • Tsigelny, I. F. et al. Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases. PLoS ONE 3, e3135 (2008).
    • (2008) PLoS ONE , vol.3
    • Tsigelny, I.F.1
  • 6
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak, H. & Braak, E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 82, 239-259 (1991).
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 7
    • 0037333666 scopus 로고    scopus 로고
    • Staging of brain pathology related to sporadic Parkinson's disease
    • Braak, H. et al. Staging of brain pathology related to sporadic Parkinson's disease. Neurobiol. Aging 24, 197-211 (2003).
    • (2003) Neurobiol. Aging , vol.24 , pp. 197-211
    • Braak, H.1
  • 8
    • 34547465506 scopus 로고    scopus 로고
    • Amyloidogenic potential of foie gras
    • Solomon, A. et al. Amyloidogenic potential of foie gras. Proc. Natl Acad. Sci. USA 104, 10998-11001 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10998-11001
    • Solomon, A.1
  • 9
    • 53749094342 scopus 로고    scopus 로고
    • AA-amyloidosis can be transferred by peripheral blood monocytes
    • Sponarova, J., Nystrom, S. N. & Westermark, G. T. AA-amyloidosis can be transferred by peripheral blood monocytes. PLoS ONE 3, e3308 (2008).
    • (2008) PLoS ONE , vol.3
    • Sponarova, J.1    Nystrom, S.N.2    Westermark, G.T.3
  • 10
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A. & Poirier, M. A. Protein aggregation and neurodegenerative disease. Nat. Med. 10 (Suppl.), S10-S17 (2004).
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 11
    • 0027195933 scopus 로고
    • Seeding "onedimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T. & Lansbury, P. T. Jr. Seeding "onedimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058 (1993).
    • (1993) Cell. , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 12
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecularlevel polymorphism in Alzheimer's β-amyloid fibrils
    • Petkova, A. T. et al. Self-propagating, molecularlevel polymorphism in Alzheimer's β-amyloid fibrils. Science 307, 262-265 (2005).
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1
  • 13
    • 65549150887 scopus 로고    scopus 로고
    • Conversion of wild-type α-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant
    • Yonetani, M. et al. Conversion of wild-type α-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant. J. Biol. Chem. 284, 7940-7950 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 7940-7950
    • Yonetani, M.1
  • 14
    • 63649160214 scopus 로고    scopus 로고
    • Conformational diversity of wild-type Tau fibrils specified by templated conformation change
    • Frost, B., Ollesch, J., Wille, H. & Diamond, M. I. Conformational diversity of wild-type Tau fibrils specified by templated conformation change. J. Biol. Chem. 284, 3546-3551 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 3546-3551
    • Frost, B.1    Ollesch, J.2    Wille, H.3    Diamond, M.I.4
  • 15
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost, B., Jacks, R. L. & Diamond, M. I. Propagation of tau misfolding from the outside to the inside of a cell. J. Biol. Chem. 284, 12845-12852 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 16
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren, P. H. et al. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat. Cell Biol. 11, 219-225 (2009).
    • (2009) Nat. Cell. Biol. , vol.11 , pp. 219-225
    • Ren, P.H.1
  • 17
    • 72149119358 scopus 로고    scopus 로고
    • Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells
    • Luk, K. C. et al. Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Proc. Natl Acad. Sci. USA 106, 20051-20056 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20051-20056
    • Luk, K.C.1
  • 18
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral β-amyloidogenesis is governed by agent and host
    • Meyer-Luehmann, M. et al. Exogenous induction of cerebral β-amyloidogenesis is governed by agent and host. Science 313, 1781-1784 (2006).
    • (2006) Science , vol.313 , pp. 1781-1784
    • Meyer-Luehmann, M.1
  • 19
    • 2342556414 scopus 로고    scopus 로고
    • Fibrillization of α-synuclein and tau in familial Parkinson's disease caused by the A53T α-synuclein mutation
    • Kotzbauer, P. T. et al. Fibrillization of α-synuclein and tau in familial Parkinson's disease caused by the A53T α-synuclein mutation. Exp. Neurol. 187, 279-288 (2004).
    • (2004) Exp. Neurol. , vol.187 , pp. 279-288
    • Kotzbauer, P.T.1
  • 20
    • 77950633906 scopus 로고    scopus 로고
    • Molecular cross talk between misfolded proteins in animal models of Alzheimer's and prion diseases
    • Morales, R. et al. Molecular cross talk between misfolded proteins in animal models of Alzheimer's and prion diseases. J. Neurosci. 30, 4528-4535 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 4528-4535
    • Morales, R.1
  • 21
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W. E., Morimoto, R. I., Dillin, A. & Kelly, J. W. Adapting proteostasis for disease intervention. Science 319, 916-919 (2008).
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 22
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of α-synuclein and its aggregates
    • Lee, H. J., Patel, S. & Lee, S. J. Intravesicular localization and exocytosis of α-synuclein and its aggregates. J. Neurosci. 25, 6016-6024 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 6016-6024
    • Lee, H.J.1    Patel, S.2    Lee, S.J.3
  • 23
    • 33645833848 scopus 로고    scopus 로고
    • Detection of oligomeric forms of α-synuclein protein in human plasma as a potential biomarker for Parkinson's disease
    • El-Agnaf, O. M. et al. Detection of oligomeric forms of α-synuclein protein in human plasma as a potential biomarker for Parkinson's disease. FASEB J. 20, 419-425 (2006).
    • (2006) FASEB J. , vol.20 , pp. 419-425
    • El-Agnaf, O.M.1
  • 24
    • 0027374233 scopus 로고
    • Detection of tau proteins in normal and Alzheimer's disease cerebrospinal fluid with a sensitive sandwich enzyme-linked immunosorbent assay
    • Vandermeeren, M. et al. Detection of tau proteins in normal and Alzheimer's disease cerebrospinal fluid with a sensitive sandwich enzyme-linked immunosorbent assay. J. Neurochem. 61, 1828-1834 (1993).
    • (1993) J. Neurochem. , vol.61 , pp. 1828-1834
    • Vandermeeren, M.1
  • 25
    • 44749083979 scopus 로고    scopus 로고
    • Assembly-dependent endocytosis and clearance of extracellular α-synuclein
    • Lee, H. J. et al. Assembly-dependent endocytosis and clearance of extracellular α-synuclein. Int. J. Biochem. Cell Biol. 40, 1835-1849 (2008).
    • (2008) Int. J. Biochem. Cell. Biol. , vol.40 , pp. 1835-1849
    • Lee, H.J.1
  • 26
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
    • Hu, X. et al. Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proc. Natl Acad. Sci. USA 106, 20324-20329 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20324-20329
    • Hu, X.1
  • 27
    • 3042788972 scopus 로고    scopus 로고
    • Cells release prions in association with exosomes
    • Fevrier, B. et al. Cells release prions in association with exosomes. Proc. Natl Acad. Sci. USA 101, 9683-9688 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9683-9688
    • Fevrier, B.1
  • 28
    • 61849178720 scopus 로고    scopus 로고
    • Prions hijack tunnelling nanotubes for intercellular spread
    • Gousset, K. et al. Prions hijack tunnelling nanotubes for intercellular spread. Nat. Cell Biol. 11, 328-336 (2009).
    • (2009) Nat. Cell. Biol. , vol.11 , pp. 328-336
    • Gousset, K.1
  • 29
    • 34447639732 scopus 로고    scopus 로고
    • Continuum of prion protein structures enciphers a multitude of prion isolatespecified phenotypes
    • Legname, G. et al. Continuum of prion protein structures enciphers a multitude of prion isolatespecified phenotypes. Proc. Natl Acad. Sci. USA 103, 19105-19110 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 19105-19110
    • Legname, G.1
  • 30
    • 29144487182 scopus 로고    scopus 로고
    • Synaptic activity regulates interstitial fluid amyloid-β levels in vivo
    • Cirrito, J. R. et al. Synaptic activity regulates interstitial fluid amyloid-β levels in vivo. Neuron 48, 913-922 (2005).
    • (2005) Neuron , vol.48 , pp. 913-922
    • Cirrito, J.R.1
  • 31
    • 28044461467 scopus 로고    scopus 로고
    • Neural activity controls the synaptic accumulation of α-synuclein
    • Fortin, D. L. et al. Neural activity controls the synaptic accumulation of α-synuclein. J. Neurosci. 25, 10913-10921 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 10913-10921
    • Fortin, D.L.1
  • 32
    • 3442889359 scopus 로고    scopus 로고
    • Synthetic mammalian prions
    • Legname, G. et al. Synthetic mammalian prions. Science 305, 673-676 (2004).
    • (2004) Science , vol.305 , pp. 673-676
    • Legname, G.1
  • 33
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey, B. & Baron, G. S. Prions and their partners in crime. Nature 443, 803-810 (2006).
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 34
    • 69149098707 scopus 로고    scopus 로고
    • Induction of cerebral β-amyloidosis: Intracerebral versus systemic Aβ inoculation
    • Eisele, Y. S. et al. Induction of cerebral β-amyloidosis: intracerebral versus systemic Aβ inoculation. Proc. Natl Acad. Sci. USA 106, 12926-12931 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 12926-12931
    • Eisele, Y.S.1
  • 35
    • 67650077008 scopus 로고    scopus 로고
    • Transmission and spreading of tauopathy in transgenic mouse brain
    • Clavaguera, F. et al. Transmission and spreading of tauopathy in transgenic mouse brain. Nat. Cell Biol. 11, 909-913 (2009).
    • (2009) Nat. Cell. Biol. , vol.11 , pp. 909-913
    • Clavaguera, F.1
  • 36
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
    • Desplats, P. et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein. Proc. Natl Acad. Sci. USA 106, 13010-13015 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13010-13015
    • Desplats, P.1
  • 37
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • Kordower, J. H., Chu, Y., Hauser, R. A., Freeman, T. B. & Olanow, C. W. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat. Med. 14, 504-506 (2008).
    • (2008) Nat. Med. , vol.14 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 38
    • 43249110200 scopus 로고    scopus 로고
    • Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation
    • Li, J. Y. et al. Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation. Nat. Med. 14, 501-503 (2008).
    • (2008) Nat. Med. , vol.14 , pp. 501-503
    • Li, J.Y.1
  • 39
    • 43249085326 scopus 로고    scopus 로고
    • Dopamine neurons implanted into people with Parkinson's disease survive without pathology for 14 years
    • Mendez, I. et al. Dopamine neurons implanted into people with Parkinson's disease survive without pathology for 14 years. Nat. Med. 14, 507-509 (2008).
    • (2008) Nat. Med. , vol.14 , pp. 507-509
    • Mendez, I.1
  • 40
    • 47949132196 scopus 로고    scopus 로고
    • Active and passive immunotherapy for neurodegenerative disorders
    • Brody, D. L. & Holtzman, D. M. Active and passive immunotherapy for neurodegenerative disorders. Annu. Rev. Neurosci. 31, 175-193 (2008).
    • (2008) Annu. Rev. Neurosci. , vol.31 , pp. 175-193
    • Brody, D.L.1    Holtzman, D.M.2
  • 41
    • 0037394788 scopus 로고    scopus 로고
    • Adult mouse astrocytes degrade amyloid-β in vitro and in situ
    • Wyss-Coray, T. et al. Adult mouse astrocytes degrade amyloid-β in vitro and in situ. Nat. Med. 9, 453-457 (2003).
    • (2003) Nat. Med. , vol.9 , pp. 453-457
    • Wyss-Coray, T.1
  • 42
    • 33847652900 scopus 로고    scopus 로고
    • Autophagy and neurodegeneration: When the cleaning crew goes on strike
    • Martinez-Vicente, M. & Cuervo, A. M. Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol. 6, 352-361 (2007).
    • (2007) Lancet Neurol. , vol.6 , pp. 352-361
    • Martinez-Vicente, M.1    Cuervo, A.M.2
  • 43
    • 0036830228 scopus 로고    scopus 로고
    • The neuropathogenic contributions of lysosomal dysfunction
    • Bahr, B. A. & Bendiske, J. The neuropathogenic contributions of lysosomal dysfunction. J. Neurochem. 83, 481-489 (2002).
    • (2002) J. Neurochem. , vol.83 , pp. 481-489
    • Bahr, B.A.1    Bendiske, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.