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Volumn , Issue 17, 2008, Pages

Screening for amyloid aggregation by semi-denaturing detergent-agarose gel electrophoresis

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EID: 80055112289     PISSN: 1940087X     EISSN: None     Source Type: Journal    
DOI: 10.3791/838     Document Type: Article
Times cited : (163)

References (10)
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    • Kryndushkin, D.S., Alexandrov, I.M., Ter-Avanesyan, M.D. & Kushnirov, V.V. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J. Biol. Chem. 278, 49636-49643 (2003).
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  • 2
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    • Appearance and Propagation of Polyglutamine-based Amyloids in Yeast: TYROSINE RESIDUES ENABLE POLYMER FRAGMENTATION
    • Alexandrov, I.M., Vishnevskaya, A.B., Ter-Avanesyan, M.D. & Kushnirov, V.V. Appearance and Propagation of Polyglutamine-based Amyloids in Yeast: TYROSINE RESIDUES ENABLE POLYMER FRAGMENTATION. J. Biol. Chem. 283, 15185-15192 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 15185-15192
    • Alexandrov, I.M.1    Vishnevskaya, A.B.2    Ter-Avanesyan, M.D.3    Kushnirov, V.V.4
  • 3
    • 17444417025 scopus 로고    scopus 로고
    • Hsp70 chaperones as modulators of prion life cycle: Novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]
    • Allen, K.D. et al. Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics 169, 1227-1242 (2005).
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    • Allen, K.D.1
  • 4
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    • J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation
    • Aron, R., Higurashi, T., Sahi, C. & Craig, E.A. J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. The EMBO journal 26, 3794-3803 (2007).
    • (2007) The EMBO Journal , vol.26 , pp. 3794-3803
    • Aron, R.1    Higurashi, T.2    Sahi, C.3    Craig, E.A.4
  • 5
  • 7
    • 15744371668 scopus 로고    scopus 로고
    • Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids
    • Salnikova, A.B., Kryndushkin, D.S., Smirnov, V.N., Kushnirov, V.V. & Ter-Avanesyan, M.D. Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J. Biol. Chem. 280, 8808-8812 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 8808-8812
    • Salnikova, A.B.1    Kryndushkin, D.S.2    Smirnov, V.N.3    Kushnirov, V.V.4    Ter-Avanesyan, M.D.5
  • 8
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    • Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability
    • Tank, E.M., Harris, D.A., Desai, A.A. & True, H.L. Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability. Mol. Cell. Biol. 27, 5445-5455 (2007).
    • (2007) Mol. Cell. Biol. 27 , pp. 5445-5455
    • Tank, E.M.1    Harris, D.A.2    Desai, A.A.3    True, H.L.4
  • 9
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    • Chaperone-dependent amyloid assembly protects cells from prion toxicity
    • Douglas, P.M. et al. Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proc. Natl. Acad. Sci. USA 105, 7206-7211 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7206-7211
    • Douglas, P.M.1
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    • Downward blotting of proteins in a model based on apolipoprotein(a) phenotyping
    • Nagy, B., Costello, R., and Csako, G. Downward blotting of proteins in a model based on apolipoprotein(a) phenotyping. Analytical Biochemistry. 231, 40-45 (1995).
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.