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Volumn 100, Issue 2, 2000, Pages 277-288

Molecular basis of a yeast prion species barrier

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; PRION PROTEIN;

EID: 0034695569     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81565-2     Document Type: Article
Times cited : (240)

References (37)
  • 3
    • 0032832981 scopus 로고    scopus 로고
    • Genetic study of interactions between the cytoskeletal assembly protein Sla1 and prion-forming domain of the release factor Sup35 (eRF3) in saccharomyces cerevisiae
    • Bailleul, P.A., Newnam, G.P., Steenbergen, J.N., and Chernoff, Y.O. (1999). Genetic study of interactions between the cytoskeletal assembly protein Sla1 and prion-forming domain of the release factor Sup35 (eRF3) in saccharomyces cerevisiae. Genetics 153, 81-94.
    • (1999) Genetics , vol.153 , pp. 81-94
    • Bailleul, P.A.1    Newnam, G.P.2    Steenbergen, J.N.3    Chernoff, Y.O.4
  • 6
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
    • Chernoff, Y.O., Lindquist, S.L., Ono, B., Inge-Vechtomov, S.G., and Liebman, S.W. (1995). Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268, 880-884.
    • (1995) Science , vol.268 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 7
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases: Importance of seeding
    • Come, J.H., Fraser, P.E., and Lansbury, P.T. (1993). A kinetic model for amyloid formation in the prion diseases: Importance of seeding. Proc. Natl. Acad. Sci. USA 90, 5959-5963.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury, P.T.3
  • 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, A.H., Santoso, A., Hillner, P., and Weissman, J.S. (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
    • 0028174948 scopus 로고
    • The dominant PNM2- mutation which eliminates the psi factor of saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene
    • Doel, S.M., McCready, S.J., Nierras, C.R., and Cox, B.S. (1994). The dominant PNM2- mutation which eliminates the psi factor of saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 137, 659-670.
    • (1994) Genetics , vol.137 , pp. 659-670
    • Doel, S.M.1    McCready, S.J.2    Nierras, C.R.3    Cox, B.S.4
  • 11
    • 0033118934 scopus 로고    scopus 로고
    • Translation termination efficiency can be regulated in saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism
    • Eaglestone, S.S., Cox, B.S., and Tuite, M.F. (1999). Translation termination efficiency can be regulated in saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J. 18, 1974-1981.
    • (1999) EMBO J. , vol.18 , pp. 1974-1981
    • Eaglestone, S.S.1    Cox, B.S.2    Tuite, M.F.3
  • 12
    • 0033574042 scopus 로고    scopus 로고
    • The (URE3) prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments
    • Edskes, H., Gray, V.T., and Wickner, R.B. (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.1    Gray, V.T.2    Wickner, R.B.3
  • 13
    • 0027248268 scopus 로고
    • Rapid amplification of complementary DNA ends for generation of full-length complementary DNAs: Thermal RACE
    • Frohman, M.A. (1993). Rapid amplification of complementary DNA ends for generation of full-length complementary DNAs: Thermal RACE. Meth. Enzymol. 218, 340-356.
    • (1993) Meth. Enzymol. , vol.218 , pp. 340-356
    • Frohman, M.A.1
  • 14
    • 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, J.R., Kowal, A.S., Schirmer, E.C., Patino, M.M., Liu, J.J., and Lindquist, S. (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    Lindquist, S.6
  • 15
    • 0029257497 scopus 로고
    • The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: Is NAC a common trigger or target in neurodegenerative disease?
    • Han, H., Weinreb, P.H., and Lansbury, P.T., Jr. (1995). The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: Is NAC a common trigger or target in neurodegenerative disease? Chem. Biol. 2, 163-169.
    • (1995) Chem. Biol. , vol.2 , pp. 163-169
    • Han, H.1    Weinreb, P.H.2    Lansbury P.T., Jr.3
  • 16
    • 0029976603 scopus 로고    scopus 로고
    • Using CLUSTAL for multiple sequence alignments
    • Higgins, D.G., Thompson, J.D., and Gibson, T.J. (1996). Using clustal for multiple sequence alignments. Meth. Enzymol. 266, 383-402.
    • (1996) Meth. Enzymol. , vol.266 , pp. 383-402
    • Higgins, D.G.1    Thompson, J.D.2    Gibson, T.J.3
  • 17
    • 0033564204 scopus 로고    scopus 로고
    • Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state
    • Horiuchi, M., and Caughey, B. (1999). Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state. EMBO J. 18, 3193-3203.
    • (1999) EMBO J. , vol.18 , pp. 3193-3203
    • Horiuchi, M.1    Caughey, B.2
  • 18
    • 0031857784 scopus 로고    scopus 로고
    • The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast
    • Ito, K., Ebihara, K., and Nakamura Y. (1998). The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast. RNA 4, 958-97
    • (1998) RNA , vol.4 , pp. 958-997
    • Ito, K.1    Ebihara, K.2    Nakamura, Y.3
  • 19
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King, C.Y., Tittmann, P., Gross, H., Gebert, R., Aebi, M., and 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    Tittmann, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5    Wüthrich, K.6
  • 20
    • 0029066886 scopus 로고
    • Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier
    • Kocisko, D.A., Priola, S.A., Raymond, G.J., Chesebro, B., Lansbury, P.T., Jr., and Caughey, B. (1995). Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier. Proc. Natl. Acad. Sci. USA 92, 3923- 3927.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3923-3927
    • Kocisko, D.A.1    Priola, S.A.2    Raymond, G.J.3    Chesebro, B.4    Lansbury P.T., Jr.5    Caughey, B.6
  • 21
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo, E.H., Lansbury, P.T., Jr., and Kelly, J.W. (1999). Amyloid diseases: Abnormal protein aggregation in neurodegeneration. Proc. Natl. Acad. Sci USA 96, 9989-9990.
    • (1999) Proc. Natl. Acad. Sci USA , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury P.T., Jr.2    Kelly, J.W.3
  • 22
    • 0028675509 scopus 로고
    • Molecular taxonomy of the yeasts
    • Kurtzman, C.P. (1994). Molecular taxonomy of the yeasts. Yeast 10, 1727-1740.
    • (1994) Yeast , vol.10 , pp. 1727-1740
    • Kurtzman, C.P.1
  • 24
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
    • Lansbury, P.T., Jr. (1999). Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl. Acad. Sci. USA 96, 3342-3344.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3342-3344
    • Lansbury P.T., Jr.1
  • 25
    • 0030728226 scopus 로고    scopus 로고
    • -chotic yeast: The expansion of the prion hypothesis
    • -chotic yeast: The expansion of the prion hypothesis. Cell 89, 495-498.
    • (1997) Cell , vol.89 , pp. 495-498
    • Lindquist, S.1
  • 26
    • 0033527045 scopus 로고    scopus 로고
    • Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast
    • Liu, J.J., and Lindquist, S. (1999). Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast. Nature 400, 573-576.
    • (1999) Nature , vol.400 , pp. 573-576
    • Liu, J.J.1    Lindquist, S.2
  • 27
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino, M.M., Liu, J.J., Glover, J.R., and 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
  • 28
    • 0029888121 scopus 로고    scopus 로고
    • Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor
    • Paushkin, S.V., Kushnirov, V.V., Smirnov, V.N., and Ter-Avanesyan, M.D. (1996). Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J. 15, 3127-3134.
    • (1996) EMBO J. , vol.15 , pp. 3127-3134
    • Paushkin, S.V.1    Kushnirov, V.V.2    Smirnov, V.N.3    Ter-Avanesyan, M.D.4
  • 29
    • 0030758280 scopus 로고    scopus 로고
    • In vitro propagation of the prion-like state of yeast Sup35 protein
    • Paushkin, S.V., Kushnirov, V.V., Smirnov, V.N., and Ter-Avanesyan, M.D. (1997). In vitro propagation of the prion-like state of yeast Sup35 protein. Science 277, 381-383.
    • (1997) Science , vol.277 , pp. 381-383
    • Paushkin, S.V.1    Kushnirov, V.V.2    Smirnov, V.N.3    Ter-Avanesyan, M.D.4
  • 31
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde, M., and Blake, C. (1997). The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50, 123-159.
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 32
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling, G.C., Scott, M., Mastrianni, J., Gabizon, R., Torchia, M., Cohen, F.E., Dearmond, S.J., and Prusiner, S.B. (1995). Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83, 79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    Dearmond, S.J.7    Prusiner, S.B.8
  • 35
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in saccharomyces cerevisiae
    • Wickner, R.B. (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
  • 36
    • 0029584303 scopus 로고
    • [PSI] and [URE3] as yeast prions
    • Wickner, R.B., Masison, D.C., and Edskes, H.K. (1995). [PSI] and [URE3] as yeast prions. Yeast 11, 1671-1685.
    • (1995) Yeast , vol.11 , pp. 1671-1685
    • Wickner, R.B.1    Masison, D.C.2    Edskes, H.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.