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Journal Abstract Search

569 related items for PubMed ID: 22580344

  • 1. Chaperone networks in protein disaggregation and prion propagation.
    Winkler J, Tyedmers J, Bukau B, Mogk A.
    J Struct Biol; 2012 Aug; 179(2):152-60. PubMed ID: 22580344
    [Abstract] [Full Text] [Related]

  • 2. Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation.
    Haslberger T, Bukau B, Mogk A.
    Biochem Cell Biol; 2010 Feb; 88(1):63-75. PubMed ID: 20130680
    [Abstract] [Full Text] [Related]

  • 3. Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation.
    Tessarz P, Mogk A, Bukau B.
    Mol Microbiol; 2008 Apr; 68(1):87-97. PubMed ID: 18312264
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  • 4. Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions.
    Reidy M, Miot M, Masison DC.
    Genetics; 2012 Sep; 192(1):185-93. PubMed ID: 22732191
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  • 11. Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation.
    Winkler J, Tyedmers J, Bukau B, Mogk A.
    J Cell Biol; 2012 Aug 06; 198(3):387-404. PubMed ID: 22869599
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  • 12. Chaperone functional specificity promotes yeast prion diversity.
    Killian AN, Hines JK.
    PLoS Pathog; 2018 Jan 06; 14(1):e1006695. PubMed ID: 29300791
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  • 13. N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression.
    Hung GC, Masison DC.
    Genetics; 2006 Jun 06; 173(2):611-20. PubMed ID: 16582428
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  • 14. The middle domain of Hsp104 can ensure substrates are functional after processing.
    Buchholz HE, Dorweiler JE, Guereca S, Wisniewski BT, Shorter J, Manogaran AL.
    PLoS Genet; 2024 Oct 06; 20(10):e1011424. PubMed ID: 39361717
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  • 15. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.
    Shorter J, Lindquist S.
    EMBO J; 2008 Oct 22; 27(20):2712-24. PubMed ID: 18833196
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  • 16. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.
    Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, Zentgraf H, Weber-Ban EU, Dougan DA, Tsai FT, Mogk A, Bukau B.
    Cell; 2004 Nov 24; 119(5):653-65. PubMed ID: 15550247
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  • 17. Novel insights into the mechanism of chaperone-assisted protein disaggregation.
    Weibezahn J, Schlieker C, Tessarz P, Mogk A, Bukau B.
    Biol Chem; 2005 Aug 24; 386(8):739-44. PubMed ID: 16201868
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  • 18. In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104.
    Tipton KA, Verges KJ, Weissman JS.
    Mol Cell; 2008 Nov 21; 32(4):584-91. PubMed ID: 19026788
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  • 19. DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface.
    Acebrón SP, Martín I, del Castillo U, Moro F, Muga A.
    FEBS Lett; 2009 Sep 17; 583(18):2991-6. PubMed ID: 19698713
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  • 20. The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions.
    Kimura Y, Koitabashi S, Kakizuka A, Fujita T.
    Genes Cells; 2004 Aug 17; 9(8):685-96. PubMed ID: 15298677
    [Abstract] [Full Text] [Related]

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