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Volumn 9, Issue 3, 2000, Pages 440-451

The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein

Author keywords

Amyloid; Prion; Ure2p; Yeast

Indexed keywords

AMYLOID; HYBRID PROTEIN;

EID: 0034067785     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.3.440     Document Type: Article
Times cited : (57)

References (40)
  • 1
    • 0030786717 scopus 로고    scopus 로고
    • Prion research: The next frontiers
    • Aguzzi A, Weissmann C. 1997. Prion research: The next frontiers. Nature 389:795-798.
    • (1997) Nature , vol.389 , pp. 795-798
    • Aguzzi, A.1    Weissmann, C.2
  • 2
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler DM, Susi H. 1986. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25:469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 4
    • 0000844417 scopus 로고
    • Electron microscopy of amyloid
    • Harris JR, ed. New York: Academic Press
    • Cohen AS, Shirahama T, Skinner M. 1982. Electron microscopy of amyloid. In: Harris JR, ed. Electron microscopy of proteins, vol. 3. New York: Academic Press, pp 165-206.
    • (1982) Electron Microscopy of Proteins , vol.3 , pp. 165-206
    • Cohen, A.S.1    Shirahama, T.2    Skinner, M.3
  • 5
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen FE, Prusiner SB. 1998. Pathologic conformations of prion proteins. Annu Rev Biochem 67:793-819.
    • (1998) Annu Rev Biochem , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 6
    • 0025959235 scopus 로고
    • The URE2 gene product of Saccharomyces 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 Saccharomyces 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
  • 7
    • 0031135380 scopus 로고    scopus 로고
    • Fusion of glutathione S-transferase with the N-terminus of yeast Sup35p protein inhibits its prion-like properties
    • Dagkesamanskaia AR, Kushnirov VV, Paushkin SV, Ter-Avanesian MD. 1997. Fusion of glutathione S-transferase with the N-terminus of yeast Sup35p protein inhibits its prion-like properties. Genetika 33:610-615.
    • (1997) Genetika , vol.33 , pp. 610-615
    • Dagkesamanskaia, A.R.1    Kushnirov, V.V.2    Paushkin, S.V.3    Ter-Avanesian, M.D.4
  • 8
    • 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
  • 9
    • 0033574042 scopus 로고    scopus 로고
    • The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments
    • Edskes HK, Gray VT, Wickner RB. 1999. The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc Natl Acad Sci USA 96:1498-1503.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1498-1503
    • Edskes, H.K.1    Gray, V.T.2    Wickner, R.B.3
  • 10
    • 0024211952 scopus 로고
    • Transmissible and non-transmissible amyloidoses: Autocatalytic post-translational conversion of host precursor proteins β-pleated sheet configurations
    • Gajdusek DC. 1988. Transmissible and non-transmissible amyloidoses: Autocatalytic post-translational conversion of host precursor proteins β-pleated sheet configurations. J Neuroimmunol 20:95-110.
    • (1988) J Neuroimmunol , vol.20 , pp. 95-110
    • Gajdusek, D.C.1
  • 12
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT Jr. 1993. Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury P.T., Jr.2
  • 13
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King C-Y, Tittman P, Gross H, Gebert R, Aebi M, Wüthrich K. 1997. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc Natl Acad Sci USA 94:6618-6622.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6618-6622
    • King, C.-Y.1    Tittman, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5    Wüthrich, K.6
  • 14
    • 0032503963 scopus 로고    scopus 로고
    • Structure and replication of yeast prions
    • Kushnirov VV, Ter-Avanesyan MD. 1998. Structure and replication of yeast prions. Cell 94:13-16.
    • (1998) Cell , vol.94 , pp. 13-16
    • Kushnirov, V.V.1    Ter-Avanesyan, M.D.2
  • 15
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H. 1993. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci 2:404-410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • LeVine, H.1
  • 17
    • 0030728226 scopus 로고    scopus 로고
    • Mad cow meet psi-chotic yeast: The expansion of the prion hypothesis
    • Lindquist S. 1997. Mad cow meet psi-chotic yeast: The expansion of the prion hypothesis. Cell 89:495-498.
    • (1997) Cell , vol.89 , pp. 495-498
    • Lindquist, S.1
  • 18
    • 0030780097 scopus 로고    scopus 로고
    • The prion model for [URE3] of yeast: Spontaneous generation and requirements for propagation
    • Masison DC, Maddelein M-L, Wickner RB. 1997. The prion model for [URE3] of yeast: Spontaneous generation and requirements for propagation. Proc Natl Acad Sci USA 94:12503-12508.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12503-12508
    • Masison, D.C.1    Maddelein, M.-L.2    Wickner, R.B.3
  • 19
    • 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
  • 20
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • McKinley MP, Meyer RK, Kenaga L, Rahbar F, Cotter R, Serban A, Prusiner SB. 1991. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J Virol 65:1340-1351.
    • (1991) J Virol , vol.65 , pp. 1340-1351
    • McKinley, M.P.1    Meyer, R.K.2    Kenaga, L.3    Rahbar, F.4    Cotter, R.5    Serban, A.6    Prusiner, S.B.7
  • 21
    • 0028931691 scopus 로고
    • Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug Praziquantel
    • McTigue MA, Williams DR, Tainer JA. 1995. Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug Praziquantel. J Bol Biol 246:21-27.
    • (1995) J Bol Biol , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 22
    • 0032951475 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
    • Newnam GP, Wegrzyn RD, Lindquist SL, Chernoff YO. 1999. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol Cell Biol 19:1325-1333.
    • (1999) Mol Cell Biol , vol.19 , pp. 1325-1333
    • Newnam, G.P.1    Wegrzyn, R.D.2    Lindquist, S.L.3    Chernoff, Y.O.4
  • 23
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino MM, Liu J-J, Glover JR, Lindquist S. 1996. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273:622-626.
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.-J.2    Glover, J.R.3    Lindquist, S.4
  • 24
  • 26
    • 0033516515 scopus 로고    scopus 로고
    • Equilibrium folding properties of the yeast prion protein determinant Ure2
    • Perrett S, Freeman SJ, Butler PJG, 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.G.3    Fersht, A.R.4
  • 27
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216:136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 32
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama N, Woody RW. 1993. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 209: 32-44.
    • (1993) Anal Biochem , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 33
    • 0031825554 scopus 로고    scopus 로고
    • From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation
    • Sunde M, Blake CCF. 1998. From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation. Q Rev Biophys 31:1-39.
    • (1998) Q Rev Biophys , vol.31 , pp. 1-39
    • Sunde, M.1    Blake, C.C.F.2
  • 34
    • 0029832863 scopus 로고    scopus 로고
    • Chemical chaperones interfere with the formation of scrapie prion protein
    • Tatzelt J, Prusiner SB, Welch WJ. 1996. Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J 15:6363-6373.
    • (1996) EMBO J , vol.15 , pp. 6363-6373
    • Tatzelt, J.1    Prusiner, S.B.2    Welch, W.J.3
  • 35
    • 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
  • 38
    • 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
  • 39
    • 0029655338 scopus 로고    scopus 로고
    • Evidence for two prions in yeast: [URE3] and [PSI]
    • Wickner RB, Masison DC. 1996. Evidence for two prions in yeast: [URE3] and [PSI]. Curr Top Microbiol Immunol 207:147-160.
    • (1996) Curr Top Microbiol Immunol , vol.207 , pp. 147-160
    • Wickner, R.B.1    Masison, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.