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Journal Abstract Search

67 related items for PubMed ID: 19361397

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  • 4. Structure and function of the molecular chaperone Hsp104 from yeast.
    Grimminger-Marquardt V, Lashuel HA.
    Biopolymers; 2010 Mar; 93(3):252-76. PubMed ID: 19768774
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  • 8. Modeling of protein misfolding in disease.
    Małolepsza EB.
    Methods Mol Biol; 2008 Mar; 443():297-330. PubMed ID: 18446294
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  • 9. [Structure and functional similarity of yeast Sup35p and Ure2p proteins to mammalian prions].
    Kushnirov VV, Ter-Avanesian MD, Smirnov VN.
    Mol Biol (Mosk); 1995 Mar; 29(4):750-5. PubMed ID: 7476941
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  • 13. Molecular mechanism for low pH triggered misfolding of the human prion protein.
    DeMarco ML, Daggett V.
    Biochemistry; 2007 Mar 20; 46(11):3045-54. PubMed ID: 17315950
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  • 17. [Diseases associated with protein aggregation].
    Bak D, Milewski M.
    Postepy Biochem; 2005 Mar 20; 51(3):297-307. PubMed ID: 16381174
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  • 18. Role of the 37 kDa laminin receptor precursor in the life cycle of prions.
    Rieger R, Lasmézas CI, Weiss S.
    Transfus Clin Biol; 1999 Feb 20; 6(1):7-16. PubMed ID: 10188208
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  • 19. The unfolded state of the murine prion protein and properties of single-point mutants related to human prion diseases.
    Gerum C, Schlepckow K, Schwalbe H.
    J Mol Biol; 2010 Aug 06; 401(1):7-12. PubMed ID: 20541558
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