메뉴 건너뛰기




Volumn 140, Issue 2, 2017, Pages 266-278

Like prions: The propagation of aggregated tau and α-synuclein in neurodegeneration

Author keywords

Alpha synuclein; Alzheimer's disease; Parkinson's disease; Prion like; Tau

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; CELL PROTEIN; PROTEIN AGGREGATE; TAU PROTEIN; PRION PROTEIN;

EID: 85014750154     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/aww230     Document Type: Review
Times cited : (235)

References (124)
  • 2
    • 84899944338 scopus 로고    scopus 로고
    • A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: The pattern of spread is determined by connectivity, not proximity
    • Ahmed Z, Cooper J, Murray TK, Garn K, McNaughton E, Clarke H, et al. A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: the pattern of spread is determined by connectivity, not proximity. Acta Neuropathol 2014; 127: 667-83.
    • (2014) Acta Neuropathol , vol.127 , pp. 667-683
    • Ahmed, Z.1    Cooper, J.2    Murray, T.K.3    Garn, K.4    McNaughton, E.5    Clarke, H.6
  • 4
    • 84945474523 scopus 로고    scopus 로고
    • Depletion of microglia and inhibition of exosome synthesis halt tau propagation
    • Asai H, Ikezu S, Tsunoda S, Medalla M, Luebke J, Haydar T, et al. Depletion of microglia and inhibition of exosome synthesis halt tau propagation. Nat Neurosci 2015; 18: 1584-93.
    • (2015) Nat Neurosci , vol.18 , pp. 1584-1593
    • Asai, H.1    Ikezu, S.2    Tsunoda, S.3    Medalla, M.4    Luebke, J.5    Haydar, T.6
  • 5
    • 84866679781 scopus 로고    scopus 로고
    • Antibody-aided clearance of extracellular α-synuclein prevents cell-to-cell aggregate transmission
    • Bae EJ, Lee HJ, Rockenstein E, Hwo DH, Park EB, Yang NY, et al. Antibody-aided clearance of extracellular α-synuclein prevents cell-to-cell aggregate transmission. J Neurosci 2012; 32, 13454-69.
    • (2012) J Neurosci , vol.32 , pp. 13454-13469
    • Bae, E.J.1    Lee, H.J.2    Rockenstein, E.3    Hwo, D.H.4    Park, E.B.5    Yang, N.Y.6
  • 7
    • 84964853990 scopus 로고    scopus 로고
    • Prion-like propagation of human brain-derived alpha-synuclein in transgenic mice expressing human wild-type alpha-synuclein
    • Bernis ME, Babila JT, Breid S, Wüsten KA, Wüllner U, Tamgüney G. Prion-like propagation of human brain-derived alpha-synuclein in transgenic mice expressing human wild-type alpha-synuclein. Acta Neuropathol Commun 2015; 3: 75.
    • (2015) Acta Neuropathol Commun , vol.3 , pp. 75
    • Bernis, M.E.1    Babila, J.T.2    Breid, S.3    Wüsten, K.A.4    Wüllner, U.5    Tamgüney, G.6
  • 8
    • 84929709813 scopus 로고    scopus 로고
    • Differential induction and spread of tau pathology in young PS19 tau transgenic mice following intracerebral injections of pathological tau from Alzheimer's disease or corticobasal degeneration brains
    • Boluda S, Iba M, Zhang B, Raible KM, Lee VMY, Trojanowski JQ, et al. Differential induction and spread of tau pathology in young PS19 tau transgenic mice following intracerebral injections of pathological tau from Alzheimer's disease or corticobasal degeneration brains. Acta Neuropathol 2015; 129: 221-37.
    • (2015) Acta Neuropathol , vol.129 , pp. 221-237
    • Boluda, S.1    Iba, M.2    Zhang, B.3    Raible, K.M.4    Lee, V.M.Y.5    Trojanowski, J.Q.6
  • 10
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 1991; 82: 239-59.
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 14
    • 33751118534 scopus 로고    scopus 로고
    • Age-associated increases of α-synuclein in monkeys and humans are associated with nigrostriatal dopamine depletion: Is this the target for Parkinson's disease?
    • Chu Y, Kordower JH. Age-associated increases of α-synuclein in monkeys and humans are associated with nigrostriatal dopamine depletion: is this the target for Parkinson's disease? Neurobiol Dis 2007; 25: 134-49.
    • (2007) Neurobiol Dis , vol.25 , pp. 134-149
    • Chu, Y.1    Kordower, J.H.2
  • 15
    • 77949906891 scopus 로고    scopus 로고
    • Lewy body pathology in fetal grafts
    • Chu Y, Kordower JH. Lewy body pathology in fetal grafts. Ann NY Acad Sci 2010; 1184: 55-67.
    • (2010) Ann NY Acad Sci , vol.1184 , pp. 55-67
    • Chu, Y.1    Kordower, J.H.2
  • 20
    • 84896697812 scopus 로고    scopus 로고
    • Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice
    • Clavaguera F, Hench J, Lavenir I, Schweighauser G, Frank S, Goedert M, et al. Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice. Acta Neuropathol 2014; 127: 299-301.
    • (2014) Acta Neuropathol , vol.127 , pp. 299-301
    • Clavaguera, F.1    Hench, J.2    Lavenir, I.3    Schweighauser, G.4    Frank, S.5    Goedert, M.6
  • 21
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of α-synuclein
    • Cremades N, Cohen SIA, Deas E, Abramov AY, Chen AY, Orte A, et al. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 2012; 149: 1048-59.
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1    Cohen, S.I.A.2    Deas, E.3    Abramov, A.Y.4    Chen, A.Y.5    Orte, A.6
  • 23
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by α-synuclein oligomers provides evidence for spreading of α-synuclein pathology
    • Danzer KM, Krebs SK, Wolff M, Birk G, Hengerer B. Seeding induced by α-synuclein oligomers provides evidence for spreading of α-synuclein pathology. J Neurochem 2009; 111: 192-203.
    • (2009) J Neurochem , vol.111 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3    Birk, G.4    Hengerer, B.5
  • 26
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
    • Desplats P, Lee HJ, Bae E, Patrick C, Rockenstein E, Crews L et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein. Proc Natl Acad Sci USA 2009; 106: 13010-15.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13010-13015
    • Desplats, P.1    Lee, H.J.2    Bae, E.3    Patrick, C.4    Rockenstein, E.5    Crews, L.6
  • 27
    • 84973895577 scopus 로고    scopus 로고
    • α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson's disease
    • Di Maio R, Barrett PJ, Hoffman EK, Barrett CW, Zharikov A, Borah A, et al. α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson's disease. Sci Transl Med 2016; 8: 342ra78.
    • (2016) Sci Transl Med , vol.8 , pp. 342ra78
    • Di Maio, R.1    Barrett, P.J.2    Hoffman, E.K.3    Barrett, C.W.4    Zharikov, A.5    Borah, A.6
  • 28
    • 84954168300 scopus 로고    scopus 로고
    • Alpha-synuclein expression in the oligodendrocyte lineage: An in vitro and in vivo study using rodent and human models
    • Djelloul M, Holmqvist S, Boza-Serrano A, Azevedo C, Yeung MS, Goldwurm S, et al. Alpha-synuclein expression in the oligodendrocyte lineage: an in vitro and in vivo study using rodent and human models. Stem Cell Rep 2015; 5: 174-84.
    • (2015) Stem Cell Rep , vol.5 , pp. 174-184
    • Djelloul, M.1    Holmqvist, S.2    Boza-Serrano, A.3    Azevedo, C.4    Yeung, M.S.5    Goldwurm, S.6
  • 29
    • 84878892468 scopus 로고    scopus 로고
    • Calcium entry and α-synuclein inclusions elevate dendritic mitochondrial oxidant stress in dopaminergic neurons
    • Dryanovski DI, Guzman JN, Xie Z, Galteri DJ, Volpicelli-Daley LA, Lee VMY, et al. Calcium entry and α-synuclein inclusions elevate dendritic mitochondrial oxidant stress in dopaminergic neurons. J Neurosci 2013; 33: 10154-64.
    • (2013) J Neurosci , vol.33 , pp. 10154-10164
    • Dryanovski, D.I.1    Guzman, J.N.2    Xie, Z.3    Galteri, D.J.4    Volpicelli-Daley, L.A.5    Lee, V.M.Y.6
  • 30
    • 84903541550 scopus 로고    scopus 로고
    • Neuron-to-neuron wild-type Tau protein transfer through a trans-synaptic mechanism: Relevance to sporadic tauopathies
    • Dujardin Sl, Lecolle K, Caillierez R, Begard S, Zommer N, Lachaud C, et al. Neuron-to-neuron wild-type Tau protein transfer through a trans-synaptic mechanism: relevance to sporadic tauopathies. Acta Neuropathol Commun 2014; 2: 14.
    • (2014) Acta Neuropathol Commun , vol.2 , pp. 14
    • Dujardin, S.L.1    Lecolle, K.2    Caillierez, R.3    Begard, S.4    Zommer, N.5    Lachaud, C.6
  • 31
    • 0030902162 scopus 로고    scopus 로고
    • Dissociation of Alzheimer type pathology in a disconnected piece of cortex
    • Duyckaerts C, Uchihara T, Seilhean D, He Y, Hauw JJ. Dissociation of Alzheimer type pathology in a disconnected piece of cortex. Acta Neuropathol 1997; 93: 501-7.
    • (1997) Acta Neuropathol , vol.93 , pp. 501-507
    • Duyckaerts, C.1    Uchihara, T.2    Seilhean, D.3    He, Y.4    Hauw, J.J.5
  • 33
    • 77952648551 scopus 로고    scopus 로고
    • Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival
    • Emmanouilidou E, Melachroinou K, Roumeliotis T, Garbis SD, Ntzouni M, Margaritis LH, et al. Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival. J Neurosci 2010; 30: 6838-51.
    • (2010) J Neurosci , vol.30 , pp. 6838-6851
    • Emmanouilidou, E.1    Melachroinou, K.2    Roumeliotis, T.3    Garbis, S.D.4    Ntzouni, M.5    Margaritis, L.H.6
  • 34
    • 84920901644 scopus 로고    scopus 로고
    • Conformation determines the seeding potencies of native and recombinant tau aggregates
    • Falcon B, Cavallini A, Angers R, Glover S, Murray TK, Barnham L, et al. Conformation determines the seeding potencies of native and recombinant tau aggregates. J Biol Chem 2015; 290: 1049-65.
    • (2015) J Biol Chem , vol.290 , pp. 1049-1065
    • Falcon, B.1    Cavallini, A.2    Angers, R.3    Glover, S.4    Murray, T.K.5    Barnham, L.6
  • 35
    • 84973304473 scopus 로고    scopus 로고
    • DnaJ/Hsc70 chaperone complexes control the extracellular release of neurodegenerative-associated proteins
    • Fontaine SN, Zheng D, Sabbagh JJ, et al. DnaJ/Hsc70 chaperone complexes control the extracellular release of neurodegenerative-associated proteins. EMBO J 2016; 35: 1537-49.
    • (2016) EMBO J , vol.35 , pp. 1537-1549
    • Fontaine, S.N.1    Zheng, D.2    Sabbagh, J.J.3
  • 36
    • 84969659293 scopus 로고    scopus 로고
    • Amyloid-α pathology and cerebral amyloid angiopathy are frequent in iatrogenic Creutzfeldt-Jakob disease after dural grafting
    • Frontzek K, Lutz MI, Aguzzi A, Kovacs GG, Budka H. Amyloid-α pathology and cerebral amyloid angiopathy are frequent in iatrogenic Creutzfeldt-Jakob disease after dural grafting. Swiss Med Wkly 2016; 146: w14287.
    • (2016) Swiss Med Wkly , vol.146 , pp. w14287
    • Frontzek, K.1    Lutz, M.I.2    Aguzzi, A.3    Kovacs, G.G.4    Budka, H.5
  • 37
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 2009; 284: 123845-52.
    • (2009) J Biol Chem , vol.284 , pp. 123845-123852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 38
    • 84940897433 scopus 로고    scopus 로고
    • Human HSP70 disaggregase reverses Parkinson's-linked α-synuclein amyloid fibrils
    • Gao X, Carroni M, Nussbaum-Krammer C, Mogk A, Nillegoda N, et al. Human HSP70 disaggregase reverses Parkinson's-linked α-synuclein amyloid fibrils. Mol Cell 2015; 59: 781-93.
    • (2015) Mol Cell , vol.59 , pp. 781-793
    • Gao, X.1    Carroni, M.2    Nussbaum-Krammer, C.3    Mogk, A.4    Nillegoda, N.5
  • 39
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 1989; 3: 519-26.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 41
    • 84939506533 scopus 로고    scopus 로고
    • Alzheimer's and Parkinson's diseases: The prion concept in relation to assembled Aβ, tau, and α-synuclein
    • Goedert M. Alzheimer's and Parkinson's diseases: the prion concept in relation to assembled Aβ, tau, and α-synuclein. Science 2015; 349: 1255555.
    • (2015) Science , vol.349 , pp. 1255555
    • Goedert, M.1
  • 42
    • 84879895467 scopus 로고    scopus 로고
    • Distinct α-synuclein strains differentially promote tau inclusions in neurons
    • Guo JL, Covell DJ, Daniels JP, Iba M, Stieber A, Zhang B, et al. Distinct α-synuclein strains differentially promote tau inclusions in neurons. Cell 2013; 154: 103-17.
    • (2013) Cell , vol.154 , pp. 103-117
    • Guo, J.L.1    Covell, D.J.2    Daniels, J.P.3    Iba, M.4    Stieber, A.5    Zhang, B.6
  • 43
    • 84893642253 scopus 로고    scopus 로고
    • Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
    • Guo JL, Lee VMY. Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat Med 2014; 20: 130-8.
    • (2014) Nat Med , vol.20 , pp. 130-138
    • Guo, J.L.1    Lee, V.M.Y.2
  • 44
    • 79551519276 scopus 로고    scopus 로고
    • α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells
    • Hansen C, Angot E, Bergström AL, Steiner JA, Pieri L, Paul G, et al. α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells. J Clin Invest 2011; 121: 715-25.
    • (2011) J Clin Invest , vol.121 , pp. 715-725
    • Hansen, C.1    Angot, E.2    Bergström, A.L.3    Steiner, J.A.4    Pieri, L.5    Paul, G.6
  • 45
    • 84866681445 scopus 로고    scopus 로고
    • Human P301L-mutant tau expression in mouse entorhinal-hippocampal network causes tau aggregation and presynaptic pathology but no cognitive defects
    • Harris JA, Koyama A, Maeda S, Ho K, Devidze N, Dubal DB, et al. Human P301L-mutant tau expression in mouse entorhinal-hippocampal network causes tau aggregation and presynaptic pathology but no cognitive defects. PLoS One 2012; 9: e45881.
    • (2012) PLoS One , vol.9
    • Harris, J.A.1    Koyama, A.2    Maeda, S.3    Ho, K.4    Devidze, N.5    Dubal, D.B.6
  • 46
    • 84882306577 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans mediate internalization and propagation of specific proteopathic seeds
    • Holmes BB, De Vos SL, Kfoury N, Li M, Jacks R, Yanamandra K, et al. Heparan sulphate proteoglycans mediate internalization and propagation of specific proteopathic seeds. Proc Natl Acad Sci USA 2013; 110: E3138-47.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E3138-E3147
    • Holmes, B.B.1    De Vos, S.L.2    Kfoury, N.3    Li, M.4    Jacks, R.5    Yanamandra, K.6
  • 47
    • 44349094812 scopus 로고    scopus 로고
    • Growth hormone, IGF-1 and insulin and their abuse in sport
    • Holt RIG, Sönksen PH. Growth hormone, IGF-1 and insulin and their abuse in sport. Br J Pharmacol 2008; 154: 542-56.
    • (2008) Br J Pharmacol , vol.154 , pp. 542-556
    • Holt, R.I.G.1    Sönksen, P.H.2
  • 48
    • 84872346089 scopus 로고    scopus 로고
    • Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's disease-like tauopathy
    • Iba M, Guo JL, McBride JD, Zhang B, Trojanowski JQ, Lee VMY. Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's disease-like tauopathy. J Neurosci 2013; 33: 1024-37.
    • (2013) J Neurosci , vol.33 , pp. 1024-1037
    • Iba, M.1    Guo, J.L.2    McBride, J.D.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.Y.6
  • 49
    • 84939569230 scopus 로고    scopus 로고
    • Tau pathology spread in PS19 tau transgenic mice following locus coeruleus (LC) injections of synthetic tau fibrils is determined by LC's afferent and efferent connections
    • Iba M, McBride JD, Guo JL, Zhang B, Trojanowski JQ, Lee VMY, Tau pathology spread in PS19 tau transgenic mice following locus coeruleus (LC) injections of synthetic tau fibrils is determined by LC's afferent and efferent connections. Acta Neuropathol 2015; 130: 249-62.
    • (2015) Acta Neuropathol , vol.130 , pp. 249-262
    • Iba, M.1    McBride, J.D.2    Guo, J.L.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.Y.6
  • 51
    • 84955101086 scopus 로고    scopus 로고
    • Short fibrils constitute the major species of seed-competent tau in the brains of mice transgenic for human P301S tau
    • Jackson SJ, Kerridge C, Cooper J, Cavallini A, Falcon B, Cella CV, et al. Short fibrils constitute the major species of seed-competent tau in the brains of mice transgenic for human P301S tau. J Neurosci 2016; 36: 762-72.
    • (2016) J Neurosci , vol.36 , pp. 762-772
    • Jackson, S.J.1    Kerridge, C.2    Cooper, J.3    Cavallini, A.4    Falcon, B.5    Cella, C.V.6
  • 53
    • 84885461450 scopus 로고    scopus 로고
    • α-Synucleinopathy associated with G51D SNCA mutation: A link between Parkinson's disease and multiple system atrophy?
    • Kiely AP, Asi Y, Kara E, Lumousin P, Ling H, Lewis P, et al. α-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson's disease and multiple system atrophy? Acta Neuropathol 2013; 125: 753-69.
    • (2013) Acta Neuropathol , vol.125 , pp. 753-769
    • Kiely, A.P.1    Asi, Y.2    Kara, E.3    Lumousin, P.4    Ling, H.5    Lewis, P.6
  • 54
    • 84861758226 scopus 로고    scopus 로고
    • Transcellular propagation of tau aggregation by fibrillar species
    • Kfoury N, Holmes BB, Jiang H, Holtzman DM, Diamond M. Transcellular propagation of tau aggregation by fibrillar species. J Biol Chem 2012; 287: 19440-51.
    • (2012) J Biol Chem , vol.287 , pp. 19440-19451
    • Kfoury, N.1    Holmes, B.B.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.5
  • 56
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic neural transplants in Parkinson's disease
    • Kordower JH, Chu Y, Hauser RA, Freeman TB, Olanow CW. Lewy body-like pathology in long-term embryonic neural transplants in Parkinson's disease. Nat Med 2008; 14: 504-6.
    • (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
  • 58
    • 54449096081 scopus 로고    scopus 로고
    • White matter tauopathy with globular glial inclusions: A distinct sporadic frontotemporal lobar degeneration
    • Kovacs GG, Majtenyi K, Spina S, Murrell JR, Gelpi E, Hoftberger R, et al. White matter tauopathy with globular glial inclusions: a distinct sporadic frontotemporal lobar degeneration. J Neuropathol Exp Neurol 2008; 67: 963-75.
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 963-975
    • Kovacs, G.G.1    Majtenyi, K.2    Spina, S.3    Murrell, J.R.4    Gelpi, E.5    Hoftberger, R.6
  • 59
    • 84956969211 scopus 로고    scopus 로고
    • Stabilization of α-synuclein fibril clusters prevents fragmentation and reduces seeding activity and toxicity
    • Lam HT, Graber MC, Gentry KA, Bieschke J. Stabilization of α-synuclein fibril clusters prevents fragmentation and reduces seeding activity and toxicity. Biochemistry 2016; 55: 675-85.
    • (2016) Biochemistry , vol.55 , pp. 675-685
    • Lam, H.T.1    Graber, M.C.2    Gentry, K.A.3    Bieschke, J.4
  • 60
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of alpha-synuclein and its aggregates
    • Lee HJ, Patel S,Lee SJ. Intravesicular localization and exocytosis of alpha-synuclein and its aggregates. J Neurosci 2005; 25: 6016-24.
    • (2005) J Neurosci , vol.25 , pp. 6016-6024
    • Lee, H.J.1    Patel, S.2    Lee, S.J.3
  • 62
    • 84976515858 scopus 로고    scopus 로고
    • Unconventional secretion of misfolded proteins promotes adaptation to proteasome dysfunction in mammalian cells
    • Lee JG, Takahama S, Zhang G, Tomarev SI, Ye Y. Unconventional secretion of misfolded proteins promotes adaptation to proteasome dysfunction in mammalian cells. Nat Cell Biol 2016; 18: 765-76. DOI: 10.1038/ncb3372.
    • (2016) Nat Cell Biol , vol.18 , pp. 765-776
    • Lee, J.G.1    Takahama, S.2    Zhang, G.3    Tomarev, S.I.4    Ye, Y.5
  • 63
    • 43249110200 scopus 로고    scopus 로고
    • Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation
    • Li J, Englund E, Holton JL, Soulet D, Hagell P, Lees AJ, et al. Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation. Nat Med 2008; 14: 501-3.
    • (2008) Nat Med , vol.14 , pp. 501-503
    • Li, J.1    Englund, E.2    Holton, J.L.3    Soulet, D.4    Hagell, P.5    Lees, A.J.6
  • 64
    • 84973324671 scopus 로고    scopus 로고
    • Extensive graft-derived dopaminergic innervation is maintained 24 years after transplantation in the degenerating parkinsonian brain
    • Li W, Englund E, Widner H, Mattson B, van Westen D, Lätt J, et al. Extensive graft-derived dopaminergic innervation is maintained 24 years after transplantation in the degenerating parkinsonian brain. Proc Natl Acad Sci USA 2016; 113: 6544-9.
    • (2016) Proc Natl Acad Sci USA , vol.113 , pp. 6544-6549
    • Li, W.1    Englund, E.2    Widner, H.3    Mattson, B.4    Van Westen, D.5    Lätt, J.6
  • 66
    • 72149119358 scopus 로고    scopus 로고
    • Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells
    • Luk KC, Song C, O'Brien P, Stieber A, Branch JR, Brunden KR, et al. Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Proc Natl Acad Sci USA 2009; 106: 20051-6.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20051-20056
    • Luk, K.C.1    Song, C.2    O'Brien, P.3    Stieber, A.4    Branch, J.R.5    Brunden, K.R.6
  • 67
    • 84862609075 scopus 로고    scopus 로고
    • Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice
    • Luk KC, Kehm VM, Zhang B, O'Brien P, Trojanowski JQ, Lee VMY. Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice. J Exp Med 2012a; 209: 975-86.
    • (2012) J Exp Med , vol.209 , pp. 975-986
    • Luk, K.C.1    Kehm, V.M.2    Zhang, B.3    O'Brien, P.4    Trojanowski, J.Q.5    Lee, V.M.Y.6
  • 68
    • 84869109864 scopus 로고    scopus 로고
    • Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk KC, Kehm V, Carroll J, Zhang B, O'Brien P, Trojanowski JQ, et al. Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 2012b; 338: 949-53.
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6
  • 73
    • 84885455505 scopus 로고    scopus 로고
    • Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein
    • Morozova OA, March ZM, Robinson AS, Colby DW. Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein. Biochemistry 2013; 52: 6960-7.
    • (2013) Biochemistry , vol.52 , pp. 6960-6967
    • Morozova, O.A.1    March, Z.M.2    Robinson, A.S.3    Colby, D.W.4
  • 75
    • 85018218251 scopus 로고    scopus 로고
    • Filamentous aggregations of phosphorylated alpha-synuclein in Schwann cells (Schwann cell cytoplasmic inclusions) in multiple system atrophy
    • Nakamura K, Mori F, Kon T, Tanji K, Miki Y, Tomiyama M, et al. Filamentous aggregations of phosphorylated alpha-synuclein in Schwann cells (Schwann cell cytoplasmic inclusions) in multiple system atrophy. Acta Neuropathol Commun 2015; 3: 29.
    • (2015) Acta Neuropathol Commun , vol.3 , pp. 29
    • Nakamura, K.1    Mori, F.2    Kon, T.3    Tanji, K.4    Miki, Y.5    Tomiyama, M.6
  • 77
    • 78049376559 scopus 로고    scopus 로고
    • Seeded aggregation and toxicity of α-synuclein and tau
    • Nonaka T, Watanabe ST, Iwatsubo T, Hasegawa M. Seeded aggregation and toxicity of α-synuclein and tau. J Biol Chem 2010; 285: 34885-98.
    • (2010) J Biol Chem , vol.285 , pp. 34885-34898
    • Nonaka, T.1    Watanabe, S.T.2    Iwatsubo, T.3    Hasegawa, M.4
  • 78
    • 84924554924 scopus 로고    scopus 로고
    • Progressive aggregation of alpha-synuclein and selective degeneration of Lewy inclusion-bearing neurons in a mouse model of parkinsonism
    • Osterberg VR, Spinelli KJ, Weston LJ, Luk KC, Woltjer RL, Unni VK. Progressive aggregation of alpha-synuclein and selective degeneration of Lewy inclusion-bearing neurons in a mouse model of parkinsonism. Cell Rep 2015; 10: 1252-60.
    • (2015) Cell Rep , vol.10 , pp. 1252-1260
    • Osterberg, V.R.1    Spinelli, K.J.2    Weston, L.J.3    Luk, K.C.4    Woltjer, R.L.5    Unni, V.K.6
  • 79
    • 84902118984 scopus 로고    scopus 로고
    • A novel α-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson's disease-type pathology
    • Pasanen P, Myllykangeas L, Siitonen M, Raunio A, Kaakkola S, Lyytinen J, et al. A novel α-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson's disease-type pathology. Neurobiol Aging 2014; 35: 2180.e1-e5.
    • (2014) Neurobiol Aging , vol.35 , pp. 2180.e1-2180.e5
    • Pasanen, P.1    Myllykangeas, L.2    Siitonen, M.3    Raunio, A.4    Kaakkola, S.5    Lyytinen, J.6
  • 80
    • 84934955012 scopus 로고    scopus 로고
    • Intrastriatal injection of pre-formed mouse α-synuclein fibrils into rats triggers α-synuclein pathology and bilateral nigrostriatal degeneration
    • Paumier KL, Luk KC, Manfredsson FP, Kanaan NM, Lipton JW, Collier TJ, et al. Intrastriatal injection of pre-formed mouse α-synuclein fibrils into rats triggers α-synuclein pathology and bilateral nigrostriatal degeneration. Neurobiol Dis 2015; 82: 185-99.
    • (2015) Neurobiol Dis , vol.82 , pp. 185-199
    • Paumier, K.L.1    Luk, K.C.2    Manfredsson, F.P.3    Kanaan, N.M.4    Lipton, J.W.5    Collier, T.J.6
  • 81
    • 84905023942 scopus 로고    scopus 로고
    • Transneuronal propagation of mutant huntingtin contributes to non-cell autonomous pathology in neurons
    • Pecho-Vrieseling E, Rieker C, Fuchs S, Bleckmann D, Esposito MS, Botta P, et al. Transneuronal propagation of mutant huntingtin contributes to non-cell autonomous pathology in neurons. Nat Neurosci 2014; 17: 1064-72.
    • (2014) Nat Neurosci , vol.17 , pp. 1064-1072
    • Pecho-Vrieseling, E.1    Rieker, C.2    Fuchs, S.3    Bleckmann, D.4    Esposito, M.S.5    Botta, P.6
  • 82
    • 84934983329 scopus 로고    scopus 로고
    • α-Synuclein strains cause distinct synucleinopathies after local and systemic administration
    • Peelaerts W, Bousset L, Van der Perren A, Moskalyuk A, Pulizzi R, Giugliano M, et al. α-Synuclein strains cause distinct synucleinopathies after local and systemic administration. Nature 2015; 522: 340-4.
    • (2015) Nature , vol.522 , pp. 340-344
    • Peelaerts, W.1    Bousset, L.2    Van Der Perren, A.3    Moskalyuk, A.4    Pulizzi, R.5    Giugliano, M.6
  • 83
    • 84974530686 scopus 로고    scopus 로고
    • Extracellular vesicles isolated from the brains of rTg4510 mice seed tau protein aggregation in a threshold-dependent manner
    • Polanco JC, Scicluna J, Hill AF, Götz J. Extracellular vesicles isolated from the brains of rTg4510 mice seed tau protein aggregation in a threshold-dependent manner. J Biol Chem 2016; 291: 12445-66.
    • (2016) J Biol Chem , vol.291 , pp. 12445-12466
    • Polanco, J.C.1    Scicluna, J.2    Hill, A.F.3    Götz, J.4
  • 85
    • 33644527269 scopus 로고    scopus 로고
    • Alzheimer-type neuropathology in a 28 year old patient with iatrogenic Creutzfeldt-Jakob disease after dural grafting
    • Preusser M, Ströbel T, Gelpi E, Eiler M, Broessner G, Schmutzhard E, et al. Alzheimer-type neuropathology in a 28 year old patient with iatrogenic Creutzfeldt-Jakob disease after dural grafting. J Neurol Neurosurg Psychiatry 2006; 77: 413-16.
    • (2006) J Neurol Neurosurg Psychiatry , vol.77 , pp. 413-416
    • Preusser, M.1    Ströbel, T.2    Gelpi, E.3    Eiler, M.4    Broessner, G.5    Schmutzhard, E.6
  • 86
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216: 136-44.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 87
    • 84888594143 scopus 로고    scopus 로고
    • Biology and genetics of prions causing neurodegeneration
    • Prusiner SB. Biology and genetics of prions causing neurodegeneration. Annu Rev Genet 2013; 47: 601-23.
    • (2013) Annu Rev Genet , vol.47 , pp. 601-623
    • Prusiner, S.B.1
  • 89
    • 84897977607 scopus 로고    scopus 로고
    • Lewy body extracts from Parkinson disease brains trigger α-synuclein pathology and neurodegeneration in mice and monkeys
    • Recasens A, Dehay B, Bové J, Carballo-Carbajal I, Dovero S, Pérez-Villalba A, et al. Lewy body extracts from Parkinson disease brains trigger α-synuclein pathology and neurodegeneration in mice and monkeys. Ann Neurol 2014; 75: 351-62.
    • (2014) Ann Neurol , vol.75 , pp. 351-362
    • Recasens, A.1    Dehay, B.2    Bové, J.3    Carballo-Carbajal, I.4    Dovero, S.5    Pérez-Villalba, A.6
  • 92
    • 33747878233 scopus 로고    scopus 로고
    • Very long term studies of the seeding of β-amyloidosis in primates
    • Ridley RM, Baker HF, Windle CP, Cummings RM. Very long term studies of the seeding of β-amyloidosis in primates. J Neural Transm 2006; 113: 1243-51.
    • (2006) J Neural Transm , vol.113 , pp. 1243-1251
    • Ridley, R.M.1    Baker, H.F.2    Windle, C.P.3    Cummings, R.M.4
  • 94
    • 84904636970 scopus 로고    scopus 로고
    • Intramuscular injection of α-synuclein induces CNS α-synuclein pathology and a rapid-onset motor phenotype in transgenic mice
    • Sacino AN, Brooks M, Thomas MA, McKinney AB, Lee S, Regenhardt RW, et al. Intramuscular injection of α-synuclein induces CNS α-synuclein pathology and a rapid-onset motor phenotype in transgenic mice. Proc Natl Acad Sci USA 2014; 111: 10732-7.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 10732-10737
    • Sacino, A.N.1    Brooks, M.2    Thomas, M.A.3    McKinney, A.B.4    Lee, S.5    Regenhardt, R.W.6
  • 96
    • 84856707794 scopus 로고    scopus 로고
    • Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease
    • Saman S, Kim WH, Raya M, Visnick Y, Miro S, Saman S, et al. Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J Biol Chem 2012; 287: 3842-9.
    • (2012) J Biol Chem , vol.287 , pp. 3842-3849
    • Saman, S.1    Kim, W.H.2    Raya, M.3    Visnick, Y.4    Miro, S.5    Saman, S.6
  • 97
    • 79952167224 scopus 로고    scopus 로고
    • Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
    • Sandberg MK, Al-Doujaily H, Sharps B, Clarke AR, Collinge J. Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature 2011; 470: 540-2.
    • (2011) Nature , vol.470 , pp. 540-542
    • Sandberg, M.K.1    Al-Doujaily, H.2    Sharps, B.3    Clarke, A.R.4    Collinge, J.5
  • 98
    • 84902486430 scopus 로고    scopus 로고
    • Distinct tau prion strains propagate in cells and mice and define different tauopathies
    • Sanders SW, Kaufman SK, De Vos SL, Sharma AM, Mirhaba H, Li A, et al. Distinct tau prion strains propagate in cells and mice and define different tauopathies. Neuron 2014; 82: 1271-88.
    • (2014) Neuron , vol.82 , pp. 1271-1288
    • Sanders, S.W.1    Kaufman, S.K.2    De Vos, S.L.3    Sharma, A.M.4    Mirhaba, H.5    Li, A.6
  • 99
    • 84928720424 scopus 로고    scopus 로고
    • Passive immunization with phospho-tau antibodies reduces tau pathology and functional deficits in two distinct mouse tauopathy models
    • Sankaranarayanan S, Barten DM, Vana L, Devidze N, Yang L, Cadelina G, et al. Passive immunization with phospho-tau antibodies reduces tau pathology and functional deficits in two distinct mouse tauopathy models. PLoS One 2015; 10: e0125614.
    • (2015) PLoS One , vol.10
    • Sankaranarayanan, S.1    Barten, D.M.2    Vana, L.3    Devidze, N.4    Yang, L.5    Cadelina, G.6
  • 100
    • 84862003756 scopus 로고    scopus 로고
    • Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes
    • Santa-Maria I, Varghese M, Ksiezak-Reding H, Dzhun A, Wang J, Pasinetti GM. Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes. J Biol Chem 2012; 287: 20522-33.
    • (2012) J Biol Chem , vol.287 , pp. 20522-20533
    • Santa-Maria, I.1    Varghese, M.2    Ksiezak-Reding, H.3    Dzhun, A.4    Wang, J.5    Pasinetti, G.M.6
  • 101
    • 0023473468 scopus 로고
    • Axonal and transneuronal transport in the transmission of neurological disease: Potential role in system degenerations, including Alzheimer's disease
    • Saper CB, Wainer BH, German DC. Axonal and transneuronal transport in the transmission of neurological disease: potential role in system degenerations, including Alzheimer's disease. Neuroscience 1987; 23: 389-98.
    • (1987) Neuroscience , vol.23 , pp. 389-398
    • Saper, C.B.1    Wainer, B.H.2    German, D.C.3
  • 102
    • 84863210676 scopus 로고    scopus 로고
    • Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
    • Schaeffer V, Lavenir I, Ozcelik S, Tolnay M, Winkler DT, Goedert M. Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy. Brain 2012; 135: 2169-77.
    • (2012) Brain , vol.135 , pp. 2169-2177
    • Schaeffer, V.1    Lavenir, I.2    Ozcelik, S.3    Tolnay, M.4    Winkler, D.T.5    Goedert, M.6
  • 103
    • 0017225223 scopus 로고
    • Electron microscopic evidence for a trans-synaptic migration of tetanus toxin in spinal cord motoneurons: An autoradiographic and morphometric study
    • Schwab ME, Thoenen H. Electron microscopic evidence for a trans-synaptic migration of tetanus toxin in spinal cord motoneurons: an autoradiographic and morphometric study. Brain Res 1976; 105: 213-27.
    • (1976) Brain Res , vol.105 , pp. 213-227
    • Schwab, M.E.1    Thoenen, H.2
  • 104
    • 84891637212 scopus 로고    scopus 로고
    • A rapid gene delivery-based mouse model for early-stage Alzheimer's disease-type tauopathy
    • Siman R, Lin YG, Malthankar-Phatak G, Dong Y. A rapid gene delivery-based mouse model for early-stage Alzheimer's disease-type tauopathy. J Neuropathol Exp Neurol 2013; 72: 1062-71.
    • (2013) J Neuropathol Exp Neurol , vol.72 , pp. 1062-1071
    • Siman, R.1    Lin, Y.G.2    Malthankar-Phatak, G.3    Dong, Y.4
  • 105
    • 84977123370 scopus 로고    scopus 로고
    • Induction of α-synuclein aggregate formation by CSF exosomes from patients with Parkinson's disease and dementia with Lewy bodies
    • Steundel A, Kunadt M, Kruse N, et al. Induction of α-synuclein aggregate formation by CSF exosomes from patients with Parkinson's disease and dementia with Lewy bodies. Brain 2016; 139: 481-94.
    • (2016) Brain , vol.139 , pp. 481-494
    • Steundel, A.1    Kunadt, M.2    Kruse, N.3
  • 107
    • 84963819506 scopus 로고    scopus 로고
    • Pathological alpha-synuclein in gastrointestinal tissues from prodromal Parkinson's disease patients
    • Stokholm MS, Danielsen EH, Hamilton-Dutoit SJ, Borghammer P. Pathological alpha-synuclein in gastrointestinal tissues from prodromal Parkinson's disease patients. Ann Neurol 2016; 79: 940-9.
    • (2016) Ann Neurol , vol.79 , pp. 940-949
    • Stokholm, M.S.1    Danielsen, E.H.2    Hamilton-Dutoit, S.J.3    Borghammer, P.4
  • 110
    • 84903441419 scopus 로고    scopus 로고
    • α-Synuclein immunotherapy blocks uptake and template propagation of misfolded α-synuclein and neurodegeneration
    • Tran HT, Chung CHY, Iba M, Zhang B, Trojanowski JQ, et al. α-Synuclein immunotherapy blocks uptake and template propagation of misfolded α-synuclein and neurodegeneration. Cell Rep 2014; 7: 2054-65.
    • (2014) Cell Rep , vol.7 , pp. 2054-2065
    • Tran, H.T.1    Chung, C.H.Y.2    Iba, M.3    Zhang, B.4    Trojanowski, J.Q.5
  • 112
    • 84944916678 scopus 로고    scopus 로고
    • Internalized tau oligomers cause neurodegeneration by inducing accumulation of pathogenic tau in human neurons derived from induced pluripotent stem cells
    • Usenovic M, Niroomand S, Drolet RE, Yao L, Gaspar RC, Hatcher NG, et al. Internalized tau oligomers cause neurodegeneration by inducing accumulation of pathogenic tau in human neurons derived from induced pluripotent stem cells. J Neurosci 2015; 35: 14234-50.
    • (2015) J Neurosci , vol.35 , pp. 14234-14250
    • Usenovic, M.1    Niroomand, S.2    Drolet, R.E.3    Yao, L.4    Gaspar, R.C.5    Hatcher, N.G.6
  • 114
    • 84922606978 scopus 로고    scopus 로고
    • The role of protein clearance mechanisms in organismal ageing and age-related disease
    • Vilchez D, Saez I, Dillin A. The role of protein clearance mechanisms in organismal ageing and age-related disease. Nat Commun 2014; 5: 5539.
    • (2014) Nat Commun , vol.5 , pp. 5539
    • Vilchez, D.1    Saez, I.2    Dillin, A.3
  • 115
    • 80053613574 scopus 로고    scopus 로고
    • Exogenous alpha-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death
    • Volpicelli-Daley LA, Luk KC, Patel TP, Tanik SA, Riddle DM, Stieber A, et al. Exogenous alpha-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death. Neuron 2011; 72: 57-71.
    • (2011) Neuron , vol.72 , pp. 57-71
    • Volpicelli-Daley, L.A.1    Luk, K.C.2    Patel, T.P.3    Tanik, S.A.4    Riddle, D.M.5    Stieber, A.6
  • 116
    • 84937392013 scopus 로고    scopus 로고
    • Neurodegenerative diseases: Expanding the prion concept
    • Walker LC, Jucker M. Neurodegenerative diseases: expanding the prion concept. Annu Rev Neurosci 2015; 38: 87-103.
    • (2015) Annu Rev Neurosci , vol.38 , pp. 87-103
    • Walker, L.C.1    Jucker, M.2
  • 117
    • 84962081972 scopus 로고    scopus 로고
    • A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration
    • Walsh DM, Selkoe DJ. A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration. Nat Rev Neurosci 2016; 17: 251-60.
    • (2016) Nat Rev Neurosci , vol.17 , pp. 251-260
    • Walsh, D.M.1    Selkoe, D.J.2
  • 118
    • 84955184686 scopus 로고    scopus 로고
    • Removing endogenous tau does not prevent tau propagation yet reduces its neurotoxicity
    • Wegmann S, Maury EA, Kirk MJ, Saqran L, Roe A, De Vos SL, et al. Removing endogenous tau does not prevent tau propagation yet reduces its neurotoxicity. EMBO J 2015; 34: 3028-41.
    • (2015) EMBO J , vol.34 , pp. 3028-3041
    • Wegmann, S.1    Maury, E.A.2    Kirk, M.J.3    Saqran, L.4    Roe, A.5    De Vos, S.L.6
  • 120
    • 84872714502 scopus 로고    scopus 로고
    • Small misfolded tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons
    • Wu JW, Herman M, Liu L, Simoes S, Acker CM, Figueroa H, et al. Small misfolded tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons. J Biol Chem 2013; 288: 1856-70.
    • (2013) J Biol Chem , vol.288 , pp. 1856-1870
    • Wu, J.W.1    Herman, M.2    Liu, L.3    Simoes, S.4    Acker, C.M.5    Figueroa, H.6
  • 121
    • 84885783467 scopus 로고    scopus 로고
    • Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo
    • Yanamandra K, Kfoury N, Jiang H, Mahan TE, Ma S, Maloney SE, et al. Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo. Neuron 2014; 80: 402-14.
    • (2014) Neuron , vol.80 , pp. 402-414
    • Yanamandra, K.1    Kfoury, N.2    Jiang, H.3    Mahan, T.E.4    Ma, S.5    Maloney, S.E.6
  • 122
    • 65549150887 scopus 로고    scopus 로고
    • Conversion of wild-type alpha-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant
    • Yonetani M, Nonaka M, Masuda M, Inukai Y, Oikawa T, Hisanaga S, et al. Conversion of wild-type alpha-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant. J Biol Chem 2009; 284: 7940-50.
    • (2009) J Biol Chem , vol.284 , pp. 7940-7950
    • Yonetani, M.1    Nonaka, M.2    Masuda, M.3    Inukai, Y.4    Oikawa, T.5    Hisanaga, S.6
  • 123
    • 44449092737 scopus 로고    scopus 로고
    • Fecal transmission of AA amyloidosis in the cheetah contributes to high incidence of disease
    • Zhang B, Une Y, Fu X, Yan J, Ge FX, Yao J, et al. Fecal transmission of AA amyloidosis in the cheetah contributes to high incidence of disease. Proc Natl Acad Sci USA 2008; 105: 7263-8.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7263-7268
    • Zhang, B.1    Une, Y.2    Fu, X.3    Yan, J.4    Ge, F.X.5    Yao, J.6
  • 124
    • 84863337784 scopus 로고    scopus 로고
    • Predicting regional neurodegeneration from the healthy brain functional connectome
    • Zhou J, Gennatas ED, Kramer JH, Miller BL, Seeley WW. Predicting regional neurodegeneration from the healthy brain functional connectome. Neuron 2012; 73: 1216-27.
    • (2012) Neuron , vol.73 , pp. 1216-1227
    • Zhou, J.1    Gennatas, E.D.2    Kramer, J.H.3    Miller, B.L.4    Seeley, W.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.