메뉴 건너뛰기




Volumn 2, Issue 10, 2004, Pages

Mechanism of prion propagation: Amyloid growth occurs by monomer addition

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; MONOMER; FUNGAL PROTEIN; PEPTIDE; POLYMER; SACCHAROMYCES CEREVISIAE PROTEIN; SUP35 PROTEIN, S CEREVISIAE; THIAZOLE DERIVATIVE; THIOFLAVINE;

EID: 8844247180     PISSN: 15449173     EISSN: None     Source Type: Journal    
DOI: 10.1371/journal.pbio.0020321     Document Type: Article
Times cited : (438)

References (40)
  • 1
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways
    • Bitan G, Kirkitadze MD, Lomakin A, Vollers SS, Benedek GB, et al. (2003) Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci U S A 100: 330-335.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 330-335
    • Bitan, G.1    Kirkitadze, M.D.2    Lomakin, A.3    Vollers, S.S.4    Benedek, G.B.5
  • 2
    • 1642524541 scopus 로고    scopus 로고
    • The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions
    • Bradley ME, Liebman SW (2004) The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions. Mol Microbiol 51: 1649-1659.
    • (2004) Mol Microbiol , vol.51 , pp. 1649-1659
    • Bradley, M.E.1    Liebman, S.W.2
  • 4
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26: 267-298.
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 5
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen S, Ferrone FA, Wetzel R (2002) Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc Natl Acad Sci U S A 99: 11884-11889.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 6
    • 0141455115 scopus 로고    scopus 로고
    • Analysis of the generation and segregation of propagons: Entities that propagate the [PSI+] prion in yeast
    • Cox B, Ness F, Tuite M (2003) Analysis of the generation and segregation of propagons: Entities that propagate the [PSI+] prion in yeast. Genetics 165: 23-33.
    • (2003) Genetics , vol.165 , pp. 23-33
    • Cox, B.1    Ness, F.2    Tuite, M.3
  • 7
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice
    • Cummings CJ, Reinstein E, Sun Y, Antalffy B, Jiang Y, et al. (1999) Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron 24: 879-892.
    • (1999) Neuron , vol.24 , pp. 879-892
    • Cummings, C.J.1    Reinstein, E.2    Sun, Y.3    Antalffy, B.4    Jiang, Y.5
  • 8
    • 0036233931 scopus 로고    scopus 로고
    • Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
    • DePace AH, Weissman JS (2002) Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nat Struct Biol 9: 389-396.
    • (2002) Nat Struct Biol , vol.9 , pp. 389-396
    • DePace, A.H.1    Weissman, J.S.2
  • 9
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • DePace AH, Santoso A, Hillner P, Weissman JS (1998) A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93: 1241-1252.
    • (1998) Cell , vol.93 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 10
    • 0035237310 scopus 로고    scopus 로고
    • Protein folding and its links with human disease
    • Dobson CM (2001) Protein folding and its links with human disease. Biochem Soc Symp 2001: 1-26.
    • (2001) Biochem Soc Symp , vol.2001 , pp. 1-26
    • Dobson, C.M.1
  • 11
    • 0034733023 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism
    • Esler WP, Stimson ER, Jennings JM, Vinters HV, Ghilardi JR, et al. (2000) Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism. Biochemistry 39: 6288-6295.
    • (2000) Biochemistry , vol.39 , pp. 6288-6295
    • Esler, W.P.1    Stimson, E.R.2    Jennings, J.M.3    Vinters, H.V.4    Ghilardi, J.R.5
  • 12
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F (1999) Analysis of protein aggregation kinetics. Methods Enzymol 309: 256-274.
    • (1999) Methods Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 13
    • 0030712145 scopus 로고    scopus 로고
    • Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
    • Glover JR, Kowal AS, Schirmer EC, Patino MM, Liu JJ, et al. (1997) Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 89: 811-819.
    • (1997) Cell , vol.89 , pp. 811-819
    • Glover, J.R.1    Kowal, A.S.2    Schirmer, E.C.3    Patino, M.M.4    Liu, J.J.5
  • 14
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg MS, Lansbury PT (2000) Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat Cell Biol 2: E115-E119.
    • (2000) Nat Cell Biol , vol.2
    • Goldberg, M.S.1    Lansbury, P.T.2
  • 15
    • 0020857088 scopus 로고
    • Length dependence of rate constants for end-to-end association and dissociation of equilibrium linear aggregates
    • Hill TL (1983) Length dependence of rate constants for end-to-end association and dissociation of equilibrium linear aggregates. Biophys J 44: 285-288.
    • (1983) Biophys J , vol.44 , pp. 285-288
    • Hill, T.L.1
  • 16
    • 0035929584 scopus 로고    scopus 로고
    • Strong growth polarity of yeast prion fiber revealed by single fiber imaging
    • Inoue Y, Kishimoto A, Hirao J, Yoshida M, Taguchi H (2001) Strong growth polarity of yeast prion fiber revealed by single fiber imaging. J Biol Chem 276: 35227-35230.
    • (2001) J Biol Chem , vol.276 , pp. 35227-35230
    • Inoue, Y.1    Kishimoto, A.2    Hirao, J.3    Yoshida, M.4    Taguchi, H.5
  • 17
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly JW (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 8: 101-106.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 18
    • 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: 319-323.
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 19
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King CY, Tittmann P, Gross H, Gebert R, Aebi M, et al. (1997) Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc Natl Acad Sci U S A 94: 6618-6622.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 6618-6622
    • King, C.Y.1    Tittmann, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5
  • 21
    • 0036310663 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast
    • Ness F, Ferreira P, Cox BS, Tuite MF (2002) Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol Cell Biol 22: 5593-5605.
    • (2002) Mol Cell Biol , vol.22 , pp. 5593-5605
    • Ness, F.1    Ferreira, P.2    Cox, B.S.3    Tuite, M.F.4
  • 23
    • 0037046151 scopus 로고    scopus 로고
    • Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis
    • Padrick SB, Miranker AD (2002) Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis. Biochemistry 41: 4694-4703.
    • (2002) Biochemistry , vol.41 , pp. 4694-4703
    • Padrick, S.B.1    Miranker, A.D.2
  • 24
    • 0031937871 scopus 로고    scopus 로고
    • Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA
    • Reid KL, Rodriguez HM, Hillier BJ, Gregoret LM (1998) Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA. Protein Sci 7: 470-479.
    • (1998) Protein Sci , vol.7 , pp. 470-479
    • Reid, K.L.1    Rodriguez, H.M.2    Hillier, B.J.3    Gregoret, L.M.4
  • 25
    • 0033960784 scopus 로고    scopus 로고
    • Aggregation of an amyloidogenic fragment of human islet amyloid polypeptide
    • Rhoades E, Agarwal J, Gafni A (2000) Aggregation of an amyloidogenic fragment of human islet amyloid polypeptide. Biochim Biophys Acta 1476: 230-238.
    • (2000) Biochim Biophys Acta , vol.1476 , pp. 230-238
    • Rhoades, E.1    Agarwal, J.2    Gafni, A.3
  • 27
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95: 55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 28
    • 1442330505 scopus 로고    scopus 로고
    • The elongation of yeast prion fibers involves separable steps of association and conversion
    • Scheibel T, Bloom J, Lindquist SL (2004) The elongation of yeast prion fibers involves separable steps of association and conversion. Proc Natl Acad Sci U S A 101: 2287-2292.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2287-2292
    • Scheibel, T.1    Bloom, J.2    Lindquist, S.L.3
  • 29
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck P (2003) On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. Anal Biochem 320: 104-124.
    • (2003) Anal Biochem , vol.320 , pp. 104-124
    • Schuck, P.1
  • 30
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck P, Perugini MA, Gonzales NR, Howlett GJ, Schubert D (2002) Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems. Biophys J 82: 1096-1111.
    • (2002) Biophys J , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 31
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, et al. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289: 1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5
  • 32
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter J, Lindquist S (2004) Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304: 1793-1797.
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 33
    • 0038047044 scopus 로고    scopus 로고
    • Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN
    • Souillac PO, Uversky VN, Fink AL (2003) Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN. Biochemistry 42: 8094-8104.
    • (2003) Biochemistry , vol.42 , pp. 8094-8104
    • Souillac, P.O.1    Uversky, V.N.2    Fink, A.L.3
  • 34
    • 0034725747 scopus 로고    scopus 로고
    • Evidence for the prion hypothesis: Induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein
    • Sparrer HE, Santoso A, Szoka FC, Weissman JS (2000) Evidence for the prion hypothesis: Induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein. Science 289: 595-599.
    • (2000) Science , vol.289 , pp. 595-599
    • Sparrer, H.E.1    Santoso, A.2    Szoka, F.C.3    Weissman, J.S.4
  • 35
    • 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: 323-328.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 36
    • 0037397705 scopus 로고    scopus 로고
    • Emerging ideas on the molecular basis of protein and peptide aggregation
    • Thirumalai D, Klimov DK, Dima RI (2003) Emerging ideas on the molecular basis of protein and peptide aggregation. Curr Opin Struct Biol 13: 146-159.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 146-159
    • Thirumalai, D.1    Klimov, D.K.2    Dima, R.I.3
  • 38
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • Uversky VN, Li J, Fink AL (2001) Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J Biol Chem 276: 10737-10744.
    • (2001) J Biol Chem , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 39
    • 0035958642 scopus 로고    scopus 로고
    • Tauopathy in Drosophila Neurodegeneration without neurofibrillary tangles
    • Wittmann CW, Wszolek MF, Shulman JM, Salvaterra PM, Lewis J, et al. (2001) Tauopathy in Drosophila Neurodegeneration without neurofibrillary tangles. Science 293: 711-714.
    • (2001) Science , vol.293 , pp. 711-714
    • Wittmann, C.W.1    Wszolek, M.F.2    Shulman, J.M.3    Salvaterra, P.M.4    Lewis, J.5
  • 40
    • 0036377156 scopus 로고    scopus 로고
    • Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease
    • Zerovnik E (2002) Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease. Eur J Biochem 269: 3362-3371.
    • (2002) Eur J Biochem , vol.269 , pp. 3362-3371
    • Zerovnik, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.