메뉴 건너뛰기




Volumn 110, Issue 15, 2013, Pages 5951-5956

Cell-to-cell propagation of infectious cytosolic protein aggregates

Author keywords

[No Author keywords available]

Indexed keywords

TRANSLATION TERMINATION FACTOR; TRANSLATION TERMINATION FACTOR SUP35; UNCLASSIFIED DRUG;

EID: 84876049853     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1217321110     Document Type: Article
Times cited : (42)

References (49)
  • 2
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner RB (1994) [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae. Science 264(5158):566-569.
    • (1994) Science , vol.264 , Issue.5158 , pp. 566-569
    • Wickner, R.B.1
  • 4
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S, Halfmann R, King O, Kapila A, Lindquist S (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137(1):146-158.
    • (2009) Cell , vol.137 , Issue.1 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 5
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases: Importance of seeding
    • Come JH, Fraser PE, Lansbury PT, Jr. (1993) A kinetic model for amyloid formation in the prion diseases: Importance of seeding. Proc Natl Acad Sci USA 90(13):5959-5963.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.13 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury Jr., P.T.3
  • 6
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions
    • Michelitsch MD, Weissman JS (2000) A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions. Proc Natl Acad Sci USA 97(22):11910-11915.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.22 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 7
    • 79952578947 scopus 로고    scopus 로고
    • Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB)
    • Heinrich SU, Lindquist S (2011) Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB). Proc Natl Acad Sci USA 108(7):2999-3004.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.7 , pp. 2999-3004
    • Heinrich, S.U.1    Lindquist, S.2
  • 8
    • 0037076355 scopus 로고    scopus 로고
    • Transmissibility of systemic amyloidosis by a prion-like mechanism
    • Lundmark K, et al. (2002) Transmissibility of systemic amyloidosis by a prion-like mechanism. Proc Natl Acad Sci USA 99(10):6979-6984.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.10 , pp. 6979-6984
    • Lundmark, K.1
  • 9
    • 79958110883 scopus 로고    scopus 로고
    • Alzheimer's pathogenesis: Is there neuron-to-neuron propagation?
    • Braak H, Del Tredici K (2011) Alzheimer's pathogenesis: Is there neuron-to-neuron propagation? Acta Neuropathol 121(5):589-595.
    • (2011) Acta Neuropathol , vol.121 , Issue.5 , pp. 589-595
    • Braak, H.1    Del Tredici, K.2
  • 10
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • Goedert M, Clavaguera F, Tolnay M (2010) The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci 33(7):317-325.
    • (2010) Trends Neurosci , vol.33 , Issue.7 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 12
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, Diamond MI (2009) Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 284(19):12845-12852.
    • (2009) J Biol Chem , vol.284 , Issue.19 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 13
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by alphasynuclein oligomers provides evidence for spreading of alpha-synuclein pathology
    • Danzer KM, Krebs SK, Wolff M, Birk G, Hengerer B (2009) Seeding induced by alphasynuclein oligomers provides evidence for spreading of alpha-synuclein pathology. J Neurochem 111(1):192-203.
    • (2009) J Neurochem , vol.111 , Issue.1 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3    Birk, G.4    Hengerer, B.5
  • 14
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuronto-neuron transmission of alpha-synuclein
    • Desplats P, et al. (2009) Inclusion formation and neuronal cell death through neuronto-neuron transmission of alpha-synuclein. Proc Natl Acad Sci USA 106(31):13010-13015.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.31 , pp. 13010-13015
    • Desplats, P.1
  • 15
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren PH, et al. (2009) Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 11(2):219-225.
    • (2009) Nat Cell Biol , vol.11 , Issue.2 , pp. 219-225
    • Ren, P.H.1
  • 16
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles
    • Guo JL, Lee VM (2011) Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J Biol Chem 286(17):15317-15331.
    • (2011) J Biol Chem , vol.286 , Issue.17 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.2
  • 17
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • Münch C, O'Brien J, Bertolotti A (2011) Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc Natl Acad Sci USA 108(9):3548-3553.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.9 , pp. 3548-3553
    • Münch, C.1    O'Brien, J.2    Bertolotti, A.3
  • 18
    • 40449095371 scopus 로고    scopus 로고
    • Prion protein/protein interactions: Fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells
    • Krammer C, et al. (2008) Prion protein/protein interactions: Fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells. FASEB J 22(3):762-773.
    • (2008) FASEB J , vol.22 , Issue.3 , pp. 762-773
    • Krammer, C.1
  • 19
    • 58849091748 scopus 로고    scopus 로고
    • The yeast Sup35NM domain propagates as a prion in mammalian cells
    • Krammer C, et al. (2009) The yeast Sup35NM domain propagates as a prion in mammalian cells. Proc Natl Acad Sci USA 106(2):462-467.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.2 , pp. 462-467
    • Krammer, C.1
  • 20
    • 3142726518 scopus 로고    scopus 로고
    • Acute formation of protease-resistant prion protein does not always lead to persistent scrapie infection in vitro
    • Vorberg I, Raines A, Priola SA (2004) Acute formation of protease-resistant prion protein does not always lead to persistent scrapie infection in vitro. J Biol Chem 279(28):29218-29225.
    • (2004) J Biol Chem , vol.279 , Issue.28 , pp. 29218-29225
    • Vorberg, I.1    Raines, A.2    Priola, S.A.3
  • 21
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • Tanaka M, Collins SR, Toyama BH, Weissman JS (2006) The physical basis of how prion conformations determine strain phenotypes. Nature 442(7102):585-589.
    • (2006) Nature , vol.442 , Issue.7102 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 22
    • 1542782213 scopus 로고    scopus 로고
    • Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104
    • Kryndushkin DS, Alexandrov IM, Ter-Avanesyan MD, Kushnirov VV (2003) Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem 278(49):49636-49643.
    • (2003) J Biol Chem , vol.278 , Issue.49 , pp. 49636-49643
    • Kryndushkin, D.S.1    Alexandrov, I.M.2    Ter-Avanesyan, M.D.3    Kushnirov, V.V.4
  • 23
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani M, Dobson CM (2003) Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution. J Mol Med (Berl) 81(11):678-699.
    • (2003) J Mol Med (Berl) , vol.81 , Issue.11 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 24
    • 78650963274 scopus 로고    scopus 로고
    • Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
    • Olzscha H, et al. (2011) Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144(1):67-78.
    • (2011) Cell , vol.144 , Issue.1 , pp. 67-78
    • Olzscha, H.1
  • 25
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • Uptain SM, Lindquist S (2002) Prions as protein-based genetic elements. Annu Rev Microbiol 56:703-741.
    • (2002) Annu Rev Microbiol , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 26
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS (2004) Conformational variations in an infectious protein determine prion strain differences. Nature 428(6980):323-328.
    • (2004) Nature , vol.428 , Issue.6980 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 27
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King CY, Diaz-Avalos R (2004) Protein-only transmission of three yeast prion strains. Nature 428(6980):319-323.
    • (2004) Nature , vol.428 , Issue.6980 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 28
    • 67650747654 scopus 로고    scopus 로고
    • Getting a grip on prions: Oligomers, amyloids, and pathological membrane interactions
    • Caughey B, Baron GS, Chesebro B, Jeffrey M (2009) Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions. Annu Rev Biochem 78:177-204.
    • (2009) Annu Rev Biochem , vol.78 , pp. 177-204
    • Caughey, B.1    Baron, G.S.2    Chesebro, B.3    Jeffrey, M.4
  • 29
    • 77149123027 scopus 로고    scopus 로고
    • GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells
    • Speare JO, Offerdahl DK, Hasenkrug A, Carmody AB, Baron GS (2010) GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells. EMBO J 29(4):782-794.
    • (2010) EMBO J , vol.29 , Issue.4 , pp. 782-794
    • Speare, J.O.1    Offerdahl, D.K.2    Hasenkrug, A.3    Carmody, A.B.4    Baron, G.S.5
  • 30
    • 20344394154 scopus 로고    scopus 로고
    • Anchorless prion protein results in infectious amyloid disease without clinical scrapie
    • Chesebro B, et al. (2005) Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308(5727):1435-1439.
    • (2005) Science , vol.308 , Issue.5727 , pp. 1435-1439
    • Chesebro, B.1
  • 31
    • 78951477465 scopus 로고    scopus 로고
    • Crucial role for prion protein membrane anchoring in the neuroinvasion and neural spread of prion infection
    • Klingeborn M, et al. (2011) Crucial role for prion protein membrane anchoring in the neuroinvasion and neural spread of prion infection. J Virol 85(4):1484-1494.
    • (2011) J Virol , vol.85 , Issue.4 , pp. 1484-1494
    • Klingeborn, M.1
  • 32
    • 3042788972 scopus 로고    scopus 로고
    • Cells release prions in association with exosomes
    • Fevrier B, et al. (2004) Cells release prions in association with exosomes. Proc Natl Acad Sci USA 101(26):9683-9688.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.26 , pp. 9683-9688
    • Fevrier, B.1
  • 33
    • 0037006804 scopus 로고    scopus 로고
    • Transfer of scrapie prion infectivity by cell contact in culture
    • Kanu N, et al. (2002) Transfer of scrapie prion infectivity by cell contact in culture. Curr Biol 12(7):523-530.
    • (2002) Curr Biol , vol.12 , Issue.7 , pp. 523-530
    • Kanu, N.1
  • 34
    • 61849178720 scopus 로고    scopus 로고
    • Prions hijack tunnelling nanotubes for intercellular spread
    • Gousset K, et al. (2009) Prions hijack tunnelling nanotubes for intercellular spread. Nat Cell Biol 11(3):328-336.
    • (2009) Nat Cell Biol , vol.11 , Issue.3 , pp. 328-336
    • Gousset, K.1
  • 35
    • 33847366661 scopus 로고    scopus 로고
    • Retroviruses can establish filopodial bridges for efficient cellto-cell transmission
    • Sherer NM, et al. (2007) Retroviruses can establish filopodial bridges for efficient cellto-cell transmission. Nat Cell Biol 9(3):310-315.
    • (2007) Nat Cell Biol , vol.9 , Issue.3 , pp. 310-315
    • Sherer, N.M.1
  • 36
    • 84864520202 scopus 로고    scopus 로고
    • Melanoregulin regulates a shedding mechanism that drives melanosome transfer from melanocytes to keratinocytes
    • Wu XS, et al. (2012) Melanoregulin regulates a shedding mechanism that drives melanosome transfer from melanocytes to keratinocytes. Proc Natl Acad Sci USA 109(31):E2101-E2109.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.31
    • Wu, X.S.1
  • 37
    • 0242515763 scopus 로고    scopus 로고
    • Spread of HTLV-I between lymphocytes by virus-induced polarization of the cytoskeleton
    • Igakura T, et al. (2003) Spread of HTLV-I between lymphocytes by virus-induced polarization of the cytoskeleton. Science 299(5613):1713-1716.
    • (2003) Science , vol.299 , Issue.5613 , pp. 1713-1716
    • Igakura, T.1
  • 38
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • Jucker M, Walker LC (2011) Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann Neurol 70(4):532-540.
    • (2011) Ann Neurol , vol.70 , Issue.4 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 39
    • 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. (1993) Detection of tau proteins in normal and Alzheimer's disease cerebrospinal fluid with a sensitive sandwich enzyme-linked immunosorbent assay. J Neurochem 61(5):1828-1834.
    • (1993) J Neurochem , vol.61 , Issue.5 , pp. 1828-1834
    • Vandermeeren, M.1
  • 40
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of alphasynuclein and its aggregates
    • Lee HJ, Patel S, Lee SJ (2005) Intravesicular localization and exocytosis of alphasynuclein and its aggregates. J Neurosci 25(25):6016-6024.
    • (2005) J Neurosci , vol.25 , Issue.25 , pp. 6016-6024
    • Lee, H.J.1    Patel, S.2    Lee, S.J.3
  • 41
    • 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, et al. (2012) Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J Biol Chem 287(6):3842-3849.
    • (2012) J Biol Chem , vol.287 , Issue.6 , pp. 3842-3849
    • Saman, S.1
  • 42
    • 36749073968 scopus 로고    scopus 로고
    • Cell division modulates prion accumulation in cultured cells
    • Ghaemmaghami S, et al. (2007) Cell division modulates prion accumulation in cultured cells. Proc Natl Acad Sci USA 104(46):17971-17976.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.46 , pp. 17971-17976
    • Ghaemmaghami, S.1
  • 43
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
    • Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW (1995) Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268(5212):880-884.
    • (1995) Science , vol.268 , Issue.5212 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 44
    • 33845491748 scopus 로고    scopus 로고
    • Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes
    • Rujano MA, et al. (2006) Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes. PLoS Biol 4(12):e417.
    • (2006) PLoS Biol , vol.4 , Issue.12
    • Rujano, M.A.1
  • 45
    • 84864240409 scopus 로고    scopus 로고
    • The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis
    • Li J, et al. (2012) The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell 150(2):339-350.
    • (2012) Cell , vol.150 , Issue.2 , pp. 339-350
    • Li, J.1
  • 46
    • 67650809307 scopus 로고    scopus 로고
    • Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
    • Maji SK, et al. (2009) Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938):328-332.
    • (2009) Science , vol.325 , Issue.5938 , pp. 328-332
    • Maji, S.K.1
  • 47
    • 31144460030 scopus 로고    scopus 로고
    • Functional amyloid formation within mammalian tissue
    • Fowler DM, et al. (2006) Functional amyloid formation within mammalian tissue. PLoS Biol 4(1):e6.
    • (2006) PLoS Biol , vol.4 , Issue.1
    • Fowler, D.M.1
  • 48
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou F, et al. (2011) MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 146(3):448-461.
    • (2011) Cell , vol.146 , Issue.3 , pp. 448-461
    • Hou, F.1
  • 49
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King OD, Gitler AD, Shorter J (2012) The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res 1462:61-80.
    • (2012) Brain Res , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.