These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

150 related articles for article (PubMed ID: 15178690)

  • 1. Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation.
    Tkach JM; Glover JR
    J Biol Chem; 2004 Aug; 279(34):35692-701. PubMed ID: 15178690
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance.
    Jung G; Jones G; Masison DC
    Proc Natl Acad Sci U S A; 2002 Jul; 99(15):9936-41. PubMed ID: 12105276
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.
    Lum R; Tkach JM; Vierling E; Glover JR
    J Biol Chem; 2004 Jul; 279(28):29139-46. PubMed ID: 15128736
    [TBL] [Abstract][Full Text] [Related]  

  • 4. 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; 173(2):611-20. PubMed ID: 16582428
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation.
    Miot M; Reidy M; Doyle SM; Hoskins JR; Johnston DM; Genest O; Vitery MC; Masison DC; Wickner S
    Proc Natl Acad Sci U S A; 2011 Apr; 108(17):6915-20. PubMed ID: 21474779
    [TBL] [Abstract][Full Text] [Related]  

  • 7. The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.
    Sénéchal P; Arseneault G; Leroux A; Lindquist S; Rokeach LA
    PLoS One; 2009 Sep; 4(9):e6939. PubMed ID: 19759825
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.
    Hattendorf DA; Lindquist SL
    EMBO J; 2002 Jan; 21(1-2):12-21. PubMed ID: 11782421
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.
    Sweeny EA; Shorter J
    J Mol Biol; 2016 May; 428(9 Pt B):1870-85. PubMed ID: 26608812
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase.
    Lee J; Sung N; Yeo L; Chang C; Lee S; Tsai FTF
    Biosci Rep; 2017 Dec; 37(6):. PubMed ID: 29175998
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.
    Hattendorf DA; Lindquist SL
    Proc Natl Acad Sci U S A; 2002 Mar; 99(5):2732-7. PubMed ID: 11867765
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregation.
    Kłosowska A; Chamera T; Liberek K
    Elife; 2016 May; 5():. PubMed ID: 27223323
    [TBL] [Abstract][Full Text] [Related]  

  • 13. The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation.
    Aslam K; Tsai CJ; Hazbun TR
    Prion; 2016 Nov; 10(6):444-465. PubMed ID: 27690738
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Processing of proteins by the molecular chaperone Hsp104.
    Schaupp A; Marcinowski M; Grimminger V; Bösl B; Walter S
    J Mol Biol; 2007 Jul; 370(4):674-86. PubMed ID: 17543332
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Functional analysis of proposed substrate-binding residues of Hsp104.
    Howard MK; Sohn BS; von Borcke J; Xu A; Jackrel ME
    PLoS One; 2020; 15(3):e0230198. PubMed ID: 32155221
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Remodeling of protein aggregates by Hsp104.
    Glover JR; Lum R
    Protein Pept Lett; 2009; 16(6):587-97. PubMed ID: 19519516
    [TBL] [Abstract][Full Text] [Related]  

  • 17. The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner.
    Sielaff B; Tsai FT
    J Mol Biol; 2010 Sep; 402(1):30-7. PubMed ID: 20654624
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.
    Glover JR; Lindquist S
    Cell; 1998 Jul; 94(1):73-82. PubMed ID: 9674429
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation.
    Kurahashi H; Nakamura Y
    Mol Microbiol; 2007 Mar; 63(6):1669-83. PubMed ID: 17367387
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Protein disaggregation mediated by heat-shock protein Hsp104.
    Parsell DA; Kowal AS; Singer MA; Lindquist S
    Nature; 1994 Dec; 372(6505):475-8. PubMed ID: 7984243
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 8.