메뉴 건너뛰기




Volumn 5, Issue 9, 2010, Pages 1-12

Amyloid-like aggregates of the yeast prion protein ure2 enter vertebrate cells by specific endocytotic pathways and induce apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; CLATHRIN; PRION PROTEIN; UNCLASSIFIED DRUG; URE2 PROTEIN; CALCIUM; GLUTATHIONE PEROXIDASE; SACCHAROMYCES CEREVISIAE PROTEIN; URE2 PROTEIN, S CEREVISIAE;

EID: 77958616350     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0012529     Document Type: Article
Times cited : (23)

References (65)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, et al. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416: 507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5
  • 5
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, et al. (1998) Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A 95: 6448-6453.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5
  • 6
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, et al. (1999) Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 19: 8876-8884.
    • (1999) J Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5
  • 7
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg MS, Lansbury PT Jr. (2000) Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat Cell Biol 2: E115-119.
    • (2000) Nat Cell Biol , vol.2
    • Goldberg, M.S.1    Lansbury, P.T.2
  • 8
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway KA, Lee SJ, Rochet JC, Ding TT, Williamson RE, et al. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both alpha synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc Natl Acad Sci U S A 97: 571-576.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5
  • 9
    • 0035180285 scopus 로고    scopus 로고
    • Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: Evidence for toxicity of nonfibrillar aggregates
    • Sousa MM, Cardoso I, Fernandes R, Guimaraes A, Saraiva MJ (2001) Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. Am J Pathol 159: 1993-2000.
    • (2001) Am J Pathol , vol.159 , pp. 1993-2000
    • Sousa, M.M.1    Cardoso, I.2    Fernandes, R.3    Guimaraes, A.4    Saraiva, M.J.5
  • 10
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, et al. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416: 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5
  • 11
    • 3843148352 scopus 로고    scopus 로고
    • Prefibrillar amyloid protein aggregates share common features of cytotoxicity
    • Bucciantini M, Calloni G, Chiti F, Formigli L, Nosi D, et al. (2004) Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J Biol Chem 279: 31374-31382.
    • (2004) J Biol Chem , vol.279 , pp. 31374-31382
    • Bucciantini, M.1    Calloni, G.2    Chiti, F.3    Formigli, L.4    Nosi, D.5
  • 12
    • 0032191105 scopus 로고    scopus 로고
    • Filamentous nerve cell inclusions in neurodegenerative diseases
    • Goedert M, Spillantini MG, Davies SW (1998) Filamentous nerve cell inclusions in neurodegenerative diseases. Curr Opin Neurobiol 8: 619-632.
    • (1998) Curr Opin Neurobiol , vol.8 , pp. 619-632
    • Goedert, M.1    Spillantini, M.G.2    Davies, S.W.3
  • 13
    • 33344463679 scopus 로고    scopus 로고
    • Common mechanisms of amyloid oligomer pathogenesis in degenerative disease
    • Glabe CG (2006) Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol Aging 27: 570-575.
    • (2006) Neurobiol Aging , vol.27 , pp. 570-575
    • Glabe, C.G.1
  • 14
    • 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: 566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 15
    • 0028859540 scopus 로고
    • Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells
    • Masison DC, Wickner RB (1995) Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270: 93-95.
    • (1995) Science , vol.270 , pp. 93-95
    • Masison, D.C.1    Wickner, R.B.2
  • 16
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • Taylor KL, Cheng N, Williams RW, Steven AC, Wickner RB (1999) Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 283: 1339-1343.
    • (1999) Science , vol.283 , pp. 1339-1343
    • Taylor, K.L.1    Cheng, N.2    Williams, R.W.3    Steven, A.C.4    Wickner, R.B.5
  • 17
    • 0033532192 scopus 로고    scopus 로고
    • Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2
    • Thual C, Komar AA, Bousset L, Fernandez-Bellot E, Cullin C, et al. (1999) Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2. J Biol Chem 274: 13666-13674.
    • (1999) J Biol Chem , vol.274 , pp. 13666-13674
    • Thual, C.1    Komar, A.A.2    Bousset, L.3    Fernandez-Bellot, E.4    Cullin, C.5
  • 18
    • 0034067785 scopus 로고    scopus 로고
    • The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein
    • Schlumpberger M, Wille H, Baldwin MA, Butler DA, Herskowitz I, et al. (2000) The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein. Protein Sci 9: 440-451.
    • (2000) Protein Sci , vol.9 , pp. 440-451
    • Schlumpberger, M.1    Wille, H.2    Baldwin, M.A.3    Butler, D.A.4    Herskowitz, I.5
  • 19
    • 0037453298 scopus 로고    scopus 로고
    • Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: A quantitative analysis of the effects of pH and buffer system
    • Zhu L, Zhang XJ, Wang LY, Zhou JM, Perrett S (2003) Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: a quantitative analysis of the effects of pH and buffer system. J Mol Biol 328: 235-254.
    • (2003) J Mol Biol , vol.328 , pp. 235-254
    • Zhu, L.1    Zhang, X.J.2    Wang, L.Y.3    Zhou, J.M.4    Perrett, S.5
  • 20
    • 9644287905 scopus 로고    scopus 로고
    • The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms
    • Bai M, Zhou JM, Perrett S (2004) The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms. J Biol Chem 279: 50025-50030.
    • (2004) J Biol Chem , vol.279 , pp. 50025-50030
    • Bai, M.1    Zhou, J.M.2    Perrett, S.3
  • 21
    • 55149089058 scopus 로고    scopus 로고
    • ''Restoration''of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2
    • Zhang ZR, Bai M, Wang XY, Zhou JM, Perrett S (2008) ''Restoration''of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2. J Mol Biol 384: 641-651.
    • (2008) J Mol Biol , vol.384 , pp. 641-651
    • Zhang, Z.R.1    Bai, M.2    Wang, X.Y.3    Zhou, J.M.4    Perrett, S.5
  • 22
    • 67649815210 scopus 로고    scopus 로고
    • Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils
    • Zhang ZR, Perrett S (2009) Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils. J Biol Chem 284: 14058-14067.
    • (2009) J Biol Chem , vol.284 , pp. 14058-14067
    • Zhang, Z.R.1    Perrett, S.2
  • 23
    • 0033516515 scopus 로고    scopus 로고
    • Equilibrium folding properties of the yeast prion protein determinant Ure2
    • Perrett S, Freeman SJ, Butler PJ, Fersht AR (1999) Equilibrium folding properties of the yeast prion protein determinant Ure2. J Mol Biol 290: 331-345.
    • (1999) J Mol Biol , vol.290 , pp. 331-345
    • Perrett, S.1    Freeman, S.J.2    Butler, P.J.3    Fersht, A.R.4
  • 24
    • 0035156642 scopus 로고    scopus 로고
    • Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae
    • Bousset L, Belrhali H, Janin J, Melki R, Morera S (2001) Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 9: 39-46.
    • (2001) Structure , vol.9 , pp. 39-46
    • Bousset, L.1    Belrhali, H.2    Janin, J.3    Melki, R.4    Morera, S.5
  • 25
    • 0035852745 scopus 로고    scopus 로고
    • The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p
    • Umland TC, Taylor KL, Rhee S, Wickner RB, Davies DR (2001) The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. Proc Natl Acad Sci U S A 98: 1459-1464.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1459-1464
    • Umland, T.C.1    Taylor, K.L.2    Rhee, S.3    Wickner, R.B.4    Davies, D.R.5
  • 26
    • 0035852824 scopus 로고    scopus 로고
    • Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p
    • Thual C, Bousset L, Komar AA, Walter S, Buchner J, et al. (2001) Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p. Biochemistry 40: 1764-1773.
    • (2001) Biochemistry , vol.40 , pp. 1764-1773
    • Thual, C.1    Bousset, L.2    Komar, A.A.3    Walter, S.4    Buchner, J.5
  • 27
    • 0942298128 scopus 로고    scopus 로고
    • Amyloid nucleation and hierarchical assembly of Ure2p fibrils. Role of asparagine/glutamine repeat and nonrepeat regions of the prion domains
    • Jiang Y, Li H, Zhu L, Zhou JM, Perrett S (2004) Amyloid nucleation and hierarchical assembly of Ure2p fibrils. Role of asparagine/glutamine repeat and nonrepeat regions of the prion domains. J Biol Chem 279: 3361-3369.
    • (2004) J Biol Chem , vol.279 , pp. 3361-3369
    • Jiang, Y.1    Li, H.2    Zhu, L.3    Zhou, J.M.4    Perrett, S.5
  • 28
    • 0035856522 scopus 로고    scopus 로고
    • Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds
    • Bousset L, Belrhali H, Melki R, Morera S (2001) Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds. Biochemistry 40: 13564-13573.
    • (2001) Biochemistry , vol.40 , pp. 13564-13573
    • Bousset, L.1    Belrhali, H.2    Melki, R.3    Morera, S.4
  • 29
    • 0025959235 scopus 로고
    • The URE2 gene product of Saccharo-myces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases
    • Coschigano PW, Magasanik B (1991) The URE2 gene product of Saccharo-myces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases. Mol Cell Biol 11: 822-832.
    • (1991) Mol Cell Biol , vol.11 , pp. 822-832
    • Coschigano, P.W.1    Magasanik, B.2
  • 30
    • 0036024577 scopus 로고    scopus 로고
    • Transmitting the signal of excess nitrogen in Saccharomyces cerevisiae from the Tor proteins to the GATA factors: Connecting the dots
    • Cooper TG (2002) Transmitting the signal of excess nitrogen in Saccharomyces cerevisiae from the Tor proteins to the GATA factors: connecting the dots. FEMS Microbiol Rev 26: 223-238.
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 223-238
    • Cooper, T.G.1
  • 31
    • 33744961740 scopus 로고    scopus 로고
    • The yeast prion Ure2p native-like assemblies are toxic to mammalian cells regardless of their aggregation state
    • Pieri L, Bucciantini M, Nosi D, Formigli L, Savistchenko J, et al. (2006) The yeast prion Ure2p native-like assemblies are toxic to mammalian cells regardless of their aggregation state. J Biol Chem 281: 15337-15344.
    • (2006) J Biol Chem , vol.281 , pp. 15337-15344
    • Pieri, L.1    Bucciantini, M.2    Nosi, D.3    Formigli, L.4    Savistchenko, J.5
  • 32
    • 67649403750 scopus 로고    scopus 로고
    • Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: Insights on vesicle permeabilization and charge selectivity
    • Pieri L, Bucciantini M, Guasti P, Savistchenko J, Melki R, et al. (2009) Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: insights on vesicle permeabilization and charge selectivity. Biophys J 96: 3319-3330.
    • (2009) Biophys J , vol.96 , pp. 3319-3330
    • Pieri, L.1    Bucciantini, M.2    Guasti, P.3    Savistchenko, J.4    Melki, R.5
  • 33
    • 0037200068 scopus 로고    scopus 로고
    • Controlled elimination of clathrin heavy-chain expression in DT40 lymphocytes
    • Wettey FR, Hawkins SF, Stewart A, Luzio JP, Howard JC, et al. (2002) Controlled elimination of clathrin heavy-chain expression in DT40 lymphocytes. Science 297: 1521-1525.
    • (2002) Science , vol.297 , pp. 1521-1525
    • Wettey, F.R.1    Hawkins, S.F.2    Stewart, A.3    Luzio, J.P.4    Howard, J.C.5
  • 34
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed R, Sokolov Y, Edmonds B, McIntire TM, Milton SC, et al. (2004) Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 279: 46363-46366.
    • (2004) J Biol Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5
  • 35
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A, Mina E, Kayed R, Milton SC, Parker I, et al. (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280: 17294-17300.
    • (2005) J Biol Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5
  • 36
    • 48049110050 scopus 로고    scopus 로고
    • p75(NTR) activation of NF-kappaB is involved in PrP106-126-induced apoptosis in mouse neuroblastoma cells
    • Bai Y, Li Q, Yang J, Zhou X, Yin X, et al. (2008) p75(NTR) activation of NF-kappaB is involved in PrP106-126-induced apoptosis in mouse neuroblastoma cells. Neurosci Res 62: 9-14.
    • (2008) Neurosci Res , vol.62 , pp. 9-14
    • Bai, Y.1    Li, Q.2    Yang, J.3    Zhou, X.4    Yin, X.5
  • 37
    • 52049108464 scopus 로고    scopus 로고
    • The involvement of cellular prion protein in the autophagy pathway in neuronal cells
    • Oh JM, Shin HY, Park SJ, Kim BH, Choi JK, et al. (2008) The involvement of cellular prion protein in the autophagy pathway in neuronal cells. Mol Cell Neurosci 39: 238-247.
    • (2008) Mol Cell Neurosci , vol.39 , pp. 238-247
    • Oh, J.M.1    Shin, H.Y.2    Park, S.J.3    Kim, B.H.4    Choi, J.K.5
  • 38
    • 53549128078 scopus 로고    scopus 로고
    • Species-specific anti-apoptotic activity of cellular prion protein in a mouse PrP-deficient neuronal cell line transfected with mouse, hamster, and bovine Prnp
    • Wu G, Nakajima K, Takeyama N, Yukawa M, Taniuchi Y, et al. (2008) Species-specific anti-apoptotic activity of cellular prion protein in a mouse PrP-deficient neuronal cell line transfected with mouse, hamster, and bovine Prnp. Neurosci Lett 446: 11-15.
    • (2008) Neurosci Lett , vol.446 , pp. 11-15
    • Wu, G.1    Nakajima, K.2    Takeyama, N.3    Yukawa, M.4    Taniuchi, Y.5
  • 39
    • 0030820875 scopus 로고    scopus 로고
    • Caspase-3-generated fragment of gelsolin: Effector of morphological change in apoptosis
    • Kothakota S, Azuma T, Reinhard C, Klippel A, Tang J, et al. (1997) Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis. Science 278: 294-298.
    • (1997) Science , vol.278 , pp. 294-298
    • Kothakota, S.1    Azuma, T.2    Reinhard, C.3    Klippel, A.4    Tang, J.5
  • 40
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Abeta amyloid protofibrils by atomic force microscopy
    • Harper JD, Wong SS, Lieber CM, Lansbury PT (1997) Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem Biol 4: 119-125.
    • (1997) Chem Biol , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 41
    • 0033538015 scopus 로고    scopus 로고
    • Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro
    • Kayed R, Bernhagen J, Greenfield N, Sweimeh K, Brunner H, et al. (1999) Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro. J Mol Biol 287: 781-796.
    • (1999) J Mol Biol , vol.287 , pp. 781-796
    • Kayed, R.1    Bernhagen, J.2    Greenfield, N.3    Sweimeh, K.4    Brunner, H.5
  • 42
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • Conway KA, Harper JD, Lansbury PT Jr. (2000) Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 39: 2552-2563.
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 43
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5
  • 44
    • 24344467958 scopus 로고    scopus 로고
    • Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates
    • Cecchi C, Baglioni S, Fiorillo C, Pensalfini A, Liguri G, et al. (2005) Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates. J Cell Sci 118: 3459-3470.
    • (2005) J Cell Sci , vol.118 , pp. 3459-3470
    • Cecchi, C.1    Baglioni, S.2    Fiorillo, C.3    Pensalfini, A.4    Liguri, G.5
  • 45
    • 56349137590 scopus 로고    scopus 로고
    • Differentiation increases the resistance of neuronal cells to amyloid toxicity
    • Cecchi C, Pensalfini A, Liguri G, Baglioni S, Fiorillo C, et al. (2008) Differentiation increases the resistance of neuronal cells to amyloid toxicity. Neurochem Res 33: 2516-2531.
    • (2008) Neurochem Res , vol.33 , pp. 2516-2531
    • Cecchi, C.1    Pensalfini, A.2    Liguri, G.3    Baglioni, S.4    Fiorillo, C.5
  • 46
    • 19444374721 scopus 로고    scopus 로고
    • Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells
    • Magalhaes AC, Baron GS, Lee KS, Steele-Mortimer O, Dorward D, et al. (2005) Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells. J Neurosci 25: 5207-5216.
    • (2005) J Neurosci , vol.25 , pp. 5207-5216
    • Magalhaes, A.C.1    Baron, G.S.2    Lee, K.S.3    Steele-Mortimer, O.4    Dorward, D.5
  • 47
    • 53749088102 scopus 로고    scopus 로고
    • Pathologic prion protein infects cells by lipid-raft dependent macropinocytosis
    • e3314
    • Wadia JS, Schaller M, Williamson RA, Dowdy SF (2008) Pathologic prion protein infects cells by lipid-raft dependent macropinocytosis. PLoS One 3: e3314.
    • (2008) PLoS One , pp. 3
    • Wadia, J.S.1    Schaller, M.2    Williamson, R.A.3    Dowdy, S.F.4
  • 48
    • 0033527637 scopus 로고    scopus 로고
    • Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid beta-peptide by microglial cells
    • Chung H, Brazil MI, Soe TT, Maxfield FR (1999) Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid beta-peptide by microglial cells. J Biol Chem 274: 32301-32308.
    • (1999) J Biol Chem , vol.274 , pp. 32301-32308
    • Chung, H.1    Brazil, M.I.2    Soe, T.T.3    Maxfield, F.R.4
  • 49
    • 34547969807 scopus 로고    scopus 로고
    • Endocytosis: Clathrin-mediated membrane budding
    • Ungewickell EJ, Hinrichsen L (2007) Endocytosis: clathrin-mediated membrane budding. Curr Opin Cell Biol 19: 417-425.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 417-425
    • Ungewickell, E.J.1    Hinrichsen, L.2
  • 50
    • 45349091779 scopus 로고    scopus 로고
    • Focusing on clathrin-mediated endocytosis
    • Rappoport JZ (2008) Focusing on clathrin-mediated endocytosis. Biochem J 412: 415-423.
    • (2008) Biochem J , vol.412 , pp. 415-423
    • Rappoport, J.Z.1
  • 52
    • 33645290776 scopus 로고    scopus 로고
    • The prion protein and lipid rafts
    • Taylor DR, Hooper NM (2006) The prion protein and lipid rafts. Mol Membr Biol 23: 89-99.
    • (2006) Mol Membr Biol , vol.23 , pp. 89-99
    • Taylor, D.R.1    Hooper, N.M.2
  • 53
    • 67149137755 scopus 로고    scopus 로고
    • Lipid rafts and clathrin cooperate in the internalization of PrP in epithelial FRT cells
    • e5829
    • Sarnataro D, Caputo A, Casanova P, Puri C, Paladino S, et al. (2009) Lipid rafts and clathrin cooperate in the internalization of PrP in epithelial FRT cells. PLoS One 4: e5829.
    • (2009) PLoS One , vol.4
    • Sarnataro, D.1    Caputo, A.2    Casanova, P.3    Puri, C.4    Paladino, S.5
  • 54
    • 18244406506 scopus 로고    scopus 로고
    • Plasticity of B cell receptor internalization upon conditional depletion of clathrin
    • Stoddart A, Jackson AP, Brodsky FM (2005) Plasticity of B cell receptor internalization upon conditional depletion of clathrin. Mol Biol Cell 16: 2339-2348.
    • (2005) Mol Biol Cell , vol.16 , pp. 2339-2348
    • Stoddart, A.1    Jackson, A.P.2    Brodsky, F.M.3
  • 55
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • Arispe N, Rojas E, Pollard HB (1993) Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc Natl Acad Sci U S A 90: 567-571.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 56
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT Jr. (2002) Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418: 291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 57
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • Mirzabekov TA, Lin MC, Kagan BL (1996) Pore formation by the cytotoxic islet amyloid peptide amylin. J Biol Chem 271: 1988-1992.
    • (1996) J Biol Chem , vol.271 , pp. 1988-1992
    • Mirzabekov, T.A.1    Lin, M.C.2    Kagan, B.L.3
  • 58
    • 0033048453 scopus 로고    scopus 로고
    • The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles
    • Janson J, Ashley RH, Harrison D, McIntyre S, Butler PC (1999) The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes 48: 491-498.
    • (1999) Diabetes , vol.48 , pp. 491-498
    • Janson, J.1    Ashley, R.H.2    Harrison, D.3    McIntyre, S.4    Butler, P.C.5
  • 59
    • 0037167613 scopus 로고    scopus 로고
    • Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes
    • Anguiano M, Nowak RJ, Lansbury PT Jr. (2002) Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. Biochemistry 41: 11338-11343.
    • (2002) Biochemistry , vol.41 , pp. 11338-11343
    • Anguiano, M.1    Nowak, R.J.2    Lansbury, P.T.3
  • 60
    • 0034657229 scopus 로고    scopus 로고
    • Polyglutamine-induced ion channels: A possible mechanism for the neurotoxicity of Huntington and other CAG repeat diseases
    • Hirakura Y, Azimov R, Azimova R, Kagan BL (2000) Polyglutamine-induced ion channels: a possible mechanism for the neurotoxicity of Huntington and other CAG repeat diseases. J Neurosci Res 60: 490-494.
    • (2000) J Neurosci Res , vol.60 , pp. 490-494
    • Hirakura, Y.1    Azimov, R.2    Azimova, R.3    Kagan, B.L.4
  • 61
    • 0031024927 scopus 로고    scopus 로고
    • Channel formation by a neurotoxic prion protein fragment
    • Lin MC, Mirzabekov T, Kagan BL (1997) Channel formation by a neurotoxic prion protein fragment. J Biol Chem 272: 44-47.
    • (1997) J Biol Chem , vol.272 , pp. 44-47
    • Lin, M.C.1    Mirzabekov, T.2    Kagan, B.L.3
  • 63
    • 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: 782-794.
    • (2010) EMBO J , vol.29 , pp. 782-794
    • Speare, J.O.1    Offerdahl, D.K.2    Hasenkrug, A.3    Carmody, A.B.4    Baron, G.S.5
  • 64
    • 0036618178 scopus 로고    scopus 로고
    • Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells
    • Shaw G, Morse S, Ararat M, Graham FL (2002) Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells. FASEB J 16: 869-871.
    • (2002) FASEB J , vol.16 , pp. 869-871
    • Shaw, G.1    Morse, S.2    Ararat, M.3    Graham, F.L.4
  • 65
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65: 55-63.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.