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Volumn 400, Issue 6744, 1999, Pages 573-576

Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast

Author keywords

[No Author keywords available]

Indexed keywords

CONGO RED; FUNGAL PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; OLIGOPEPTIDE; PRION PROTEIN;

EID: 0033527045     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/23048     Document Type: Article
Times cited : (182)

References (29)
  • 1
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner, R. B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264, 566-569 (1994).
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 2
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino, M. M., Liu, L. J., Glover, J. R. & Lindquist, S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273, 622-626 (1996).
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, L.J.2    Glover, J.R.3    Lindquist, S.4
  • 3
    • 0029888121 scopus 로고    scopus 로고
    • -] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor
    • -] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J. 15, 3127-3134 (1996).
    • (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
  • 4
    • 0030728226 scopus 로고    scopus 로고
    • Mad cows meet psi-chotic yeast: The expansion of the prion hypothesis
    • Lindquist, S. Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis. Cell 89, 495-498 (1997).
    • (1997) Cell , vol.89 , pp. 495-498
    • Lindquist, S.1
  • 5
    • 0022477981 scopus 로고
    • Molecular cloning ofa human prion protein cDNA
    • Kretzschmar, H. A. et al. Molecular cloning ofa human prion protein cDNA. DNA 5, 315-324 (1986).
    • (1986) DNA , vol.5 , pp. 315-324
    • Kretzschmar, H.A.1
  • 6
    • 0023950107 scopus 로고
    • Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces cerevisiae
    • Kushnirov, V. V. et al. Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces cerevisiae. Gene 66, 45-54 (1988).
    • (1988) Gene , vol.66 , pp. 45-54
    • Kushnirov, V.V.1
  • 8
    • 0032427904 scopus 로고    scopus 로고
    • Neurological illness in transgenic mice expressing a prion protein with an insertional mutation
    • Chiesa, R., Piccardo, P., Ghetti, B. & Harris, D. A. Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21, 1339-1351 (1998).
    • (1998) Neuron , vol.21 , pp. 1339-1351
    • Chiesa, R.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 9
    • 0029145925 scopus 로고
    • Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3
    • Zhouravleva, G. et al. Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J. 14, 4065-4072 (1995).
    • (1995) EMBO J. , vol.14 , pp. 4065-4072
    • Zhouravleva, G.1
  • 10
    • 0029165882 scopus 로고
    • The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae
    • Stansfield, I. et al. The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J. 14, 4365-4373 (1995).
    • (1995) EMBO J. , vol.14 , pp. 4365-4373
    • Stansfield, I.1
  • 11
    • 0027513128 scopus 로고
    • Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein
    • Ter-Avanesyan, M. D. et al. Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol. Microbiol. 7, 683-692 (1993).
    • (1993) Mol. Microbiol. , vol.7 , pp. 683-692
    • Ter-Avanesyan, M.D.1
  • 13
    • 0030712145 scopus 로고    scopus 로고
    • +], a heritable prion-like factor of S. cerevisiae
    • +], a heritable prion-like factor of S. cerevisiae. Cell 89, 811-819 (1997).
    • (1997) Cell , vol.89 , pp. 811-819
    • Glover, J.R.1
  • 14
    • 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. & Weissman, J. S. A critical role for amino-terminal glutamine/ asparagine repeats in the formation and propagation of a yeast prion. Cell 93, 1241-1252 (1998).
    • (1998) Cell , vol.93 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 17
    • 0027483882 scopus 로고
    • Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae
    • Chernoff, Y. O., Derkach, I. L. & Inge-Vechtomov, S. G. Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr. Genet. 24, 268-270 (1993).
    • (1993) Curr. Genet. , vol.24 , pp. 268-270
    • Chernoff, Y.O.1    Derkach, I.L.2    Inge-Vechtomov, S.G.3
  • 18
    • 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. & Ter-Avanesyan, M. D. In vitro propagation of the prion-like state of yeast Sup35 protein. Science 277, 381-383 (1997).
    • (1997) Science , vol.277 , pp. 381-383
    • Paushkin, S.V.1    Kushnirov, V.V.2    Smirnov, V.N.3    Ter-Avanesyan, M.D.4
  • 19
    • 0032437926 scopus 로고    scopus 로고
    • The shortest known prion protein gene allele occurs in goats, has only three octapeptide repeats and is non-pathogenic
    • Goldmann, W., Chong, A., Foster, J., Hope, J. & Hunter, N. The shortest known prion protein gene allele occurs in goats, has only three octapeptide repeats and is non-pathogenic. J. Gen. Virol. 79, 3173-3176 (1998).
    • (1998) J. Gen. Virol. , vol.79 , pp. 3173-3176
    • Goldmann, W.1    Chong, A.2    Foster, J.3    Hope, J.4    Hunter, N.5
  • 20
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease
    • McCutchen, S. L., Lai, Z., Miroy, G. J., Kelly, J. W. & Colon, W. Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry 34, 13527-13536 (1995).
    • (1995) Biochemistry , vol.34 , pp. 13527-13536
    • McCutchen, S.L.1    Lai, Z.2    Miroy, G.J.3    Kelly, J.W.4    Colon, W.5
  • 21
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth, D. R. et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385, 787-793 (1997).
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1
  • 22
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki, W., Petersen, R. B., Gambetti, P. & Surewicz, W. K. Familial mutations and the thermodynamic stability of the recombinant human prion protein. J. Biol. Chem. 273, 31048-31052 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3    Surewicz, W.K.4
  • 23
    • 0033574161 scopus 로고    scopus 로고
    • Influence of amino acid substitutions related to inherited human prion diseases of the thermodynamical stability of the cellular prion protein
    • Liemann, S. & Glockshuber, R. Influence of amino acid substitutions related to inherited human prion diseases of the thermodynamical stability of the cellular prion protein. Biochemistry 38, 3258-3267 (1999).
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 24
    • 0024044018 scopus 로고
    • ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene
    • Thiele, D. J. ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene. Mol. Cell. Biol. 8, 2745-2752 (1988).
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2745-2752
    • Thiele, D.J.1
  • 25
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S. & Hieter, P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27 (1989).
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 29
    • 0024363054 scopus 로고
    • Two simple methods for quantifying low-affinity dye-substrating binding
    • Klunk, W. E., Pettegrew, J. W. & Abraham, D. I. Two simple methods for quantifying low-affinity dye-substrating binding. J. Histochem. Cytochem. 37, 1293-1297 (1989).
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1293-1297
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.