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 *

206 related articles for article (PubMed ID: 35177839)

  • 1. Amyloid conformation-dependent disaggregation in a reconstituted yeast prion system.
    Nakagawa Y; Shen HC; Komi Y; Sugiyama S; Kurinomaru T; Tomabechi Y; Krayukhina E; Okamoto K; Yokoyama T; Shirouzu M; Uchiyama S; Inaba M; Niwa T; Sako Y; Taguchi H; Tanaka M
    Nat Chem Biol; 2022 Mar; 18(3):321-331. PubMed ID: 35177839
    [TBL] [Abstract][Full Text] [Related]  

  • 2. ATP modulates self-perpetuating conformational conversion generating structurally distinct yeast prion amyloids that limit autocatalytic amplification.
    Mahapatra S; Sarbahi A; Punia N; Joshi A; Avni A; Walimbe A; Mukhopadhyay S
    J Biol Chem; 2023 May; 299(5):104654. PubMed ID: 36990219
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Hsp40/JDP Requirements for the Propagation of Synthetic Yeast Prions.
    Miller SC; Wegrzynowicz AK; Cole SJ; Hayward RE; Ganser SJ; Hines JK
    Viruses; 2022 Sep; 14(10):. PubMed ID: 36298715
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Substoichiometric Hsp104 regulates the genesis and persistence of self-replicable amyloid seeds of Sup35 prion domain.
    Mahapatra S; Sarbahi A; Madhu P; Swasthi HM; Sharma A; Singh P; Mukhopadhyay S
    J Biol Chem; 2022 Aug; 298(8):102143. PubMed ID: 35714774
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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; 198(3):387-404. PubMed ID: 22869599
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Amyloid Fragmentation and Disaggregation in Yeast and Animals.
    Kushnirov VV; Dergalev AA; Alexandrov AI
    Biomolecules; 2021 Dec; 11(12):. PubMed ID: 34944528
    [TBL] [Abstract][Full Text] [Related]  

  • 7. 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]  

  • 8. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.
    Shorter J; Lindquist S
    EMBO J; 2008 Oct; 27(20):2712-24. PubMed ID: 18833196
    [TBL] [Abstract][Full Text] [Related]  

  • 9. 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]  

  • 10. The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy.
    Ohta S; Kawai-Noma S; Kitamura A; Pack CG; Kinjo M; Taguchi H
    Biochem Biophys Res Commun; 2013 Dec; 442(1-2):28-32. PubMed ID: 24216111
    [TBL] [Abstract][Full Text] [Related]  

  • 11. 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; 32(4):584-91. PubMed ID: 19026788
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Over-expression of the molecular chaperone Hsp104 in Saccharomyces cerevisiae results in the malpartition of [PSI
    Ness F; Cox BS; Wongwigkarn J; Naeimi WR; Tuite MF
    Mol Microbiol; 2017 Apr; 104(1):125-143. PubMed ID: 28073182
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Prion and nonprion amyloids: a comparison inspired by the yeast Sup35 protein.
    Kushnirov VV; Vishnevskaya AB; Alexandrov IM; Ter-Avanesyan MD
    Prion; 2007; 1(3):179-84. PubMed ID: 19164899
    [TBL] [Abstract][Full Text] [Related]  

  • 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; 20(10):e1011424. PubMed ID: 39361717
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation.
    Dulle JE; Stein KC; True HL
    PLoS One; 2014; 9(1):e87521. PubMed ID: 24466354
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities.
    Shorter J; Lindquist S
    Mol Cell; 2006 Aug; 23(3):425-38. PubMed ID: 16885031
    [TBL] [Abstract][Full Text] [Related]  

  • 17. A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ].
    Helsen CW; Glover JR
    Prion; 2012 Jul; 6(3):234-9. PubMed ID: 22561166
    [TBL] [Abstract][Full Text] [Related]  

  • 18. 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]  

  • 19. Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability.
    Yang Z; Hong JY; Derkatch IL; Liebman SW
    PLoS Genet; 2013; 9(1):e1003236. PubMed ID: 23358669
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast.
    Killian AN; Miller SC; Hines JK
    Viruses; 2019 Apr; 11(4):. PubMed ID: 30995727
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 11.