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Journal Abstract Search


252 related items for PubMed ID: 23530227

  • 1. Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins.
    Gowda NK, Kandasamy G, Froehlich MS, Dohmen RJ, Andréasson C.
    Proc Natl Acad Sci U S A; 2013 Apr 09; 110(15):5975-80. PubMed ID: 23530227
    [Abstract] [Full Text] [Related]

  • 2. Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast.
    Gowda NK, Kaimal JM, Masser AE, Kang W, Friedländer MR, Andréasson C.
    Mol Biol Cell; 2016 Apr 15; 27(8):1210-9. PubMed ID: 26912797
    [Abstract] [Full Text] [Related]

  • 3. The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein.
    Summers DW, Wolfe KJ, Ren HY, Cyr DM.
    PLoS One; 2013 Apr 15; 8(1):e52099. PubMed ID: 23341891
    [Abstract] [Full Text] [Related]

  • 4. Hsp70-Hsp110 chaperones deliver ubiquitin-dependent and -independent substrates to the 26S proteasome for proteolysis in yeast.
    Kandasamy G, Andréasson C.
    J Cell Sci; 2018 Mar 20; 131(6):. PubMed ID: 29507114
    [Abstract] [Full Text] [Related]

  • 5. Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.
    Abrams JL, Verghese J, Gibney PA, Morano KA.
    J Biol Chem; 2014 May 09; 289(19):13155-67. PubMed ID: 24671421
    [Abstract] [Full Text] [Related]

  • 6. Deubiquitinase activity is required for the proteasomal degradation of misfolded cytosolic proteins upon heat-stress.
    Fang NN, Zhu M, Rose A, Wu KP, Mayor T.
    Nat Commun; 2016 Oct 04; 7():12907. PubMed ID: 27698423
    [Abstract] [Full Text] [Related]

  • 7. HSP70-binding motifs function as protein quality control degrons.
    Abildgaard AB, Voutsinos V, Petersen SD, Larsen FB, Kampmeyer C, Johansson KE, Stein A, Ravid T, Andréasson C, Jensen MK, Lindorff-Larsen K, Hartmann-Petersen R.
    Cell Mol Life Sci; 2023 Jan 07; 80(1):32. PubMed ID: 36609589
    [Abstract] [Full Text] [Related]

  • 8. The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate.
    Jones RD, Enam C, Ibarra R, Borror HR, Mostoller KE, Fredrickson EK, Lin J, Chuang E, March Z, Shorter J, Ravid T, Kleiger G, Gardner RG.
    Mol Biol Cell; 2020 Feb 01; 31(3):221-233. PubMed ID: 31825716
    [Abstract] [Full Text] [Related]

  • 9. Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.
    Shiber A, Breuer W, Brandeis M, Ravid T.
    Mol Biol Cell; 2013 Jul 01; 24(13):2076-87. PubMed ID: 23637465
    [Abstract] [Full Text] [Related]

  • 10. Direct involvement of Hsp70 ATP hydrolysis in Ubr1-dependent quality control.
    Singh A, Vashistha N, Heck J, Tang X, Wipf P, Brodsky JL, Hampton RY.
    Mol Biol Cell; 2020 Nov 15; 31(24):2669-2686. PubMed ID: 32966159
    [Abstract] [Full Text] [Related]

  • 11. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding.
    Yam AY, Albanèse V, Lin HT, Frydman J.
    J Biol Chem; 2005 Dec 16; 280(50):41252-61. PubMed ID: 16219770
    [Abstract] [Full Text] [Related]

  • 12. Degradation Signals for Ubiquitin-Proteasome Dependent Cytosolic Protein Quality Control (CytoQC) in Yeast.
    Maurer MJ, Spear ED, Yu AT, Lee EJ, Shahzad S, Michaelis S.
    G3 (Bethesda); 2016 Jul 07; 6(7):1853-66. PubMed ID: 27172186
    [Abstract] [Full Text] [Related]

  • 13. A nucleus-based quality control mechanism for cytosolic proteins.
    Prasad R, Kawaguchi S, Ng DT.
    Mol Biol Cell; 2010 Jul 01; 21(13):2117-27. PubMed ID: 20462951
    [Abstract] [Full Text] [Related]

  • 14. The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system.
    Park SH, Bolender N, Eisele F, Kostova Z, Takeuchi J, Coffino P, Wolf DH.
    Mol Biol Cell; 2007 Jan 01; 18(1):153-65. PubMed ID: 17065559
    [Abstract] [Full Text] [Related]

  • 15. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.
    Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU.
    EMBO J; 2006 Jun 07; 25(11):2519-28. PubMed ID: 16688212
    [Abstract] [Full Text] [Related]

  • 16. Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.
    Nillegoda NB, Theodoraki MA, Mandal AK, Mayo KJ, Ren HY, Sultana R, Wu K, Johnson J, Cyr DM, Caplan AJ.
    Mol Biol Cell; 2010 Jul 01; 21(13):2102-16. PubMed ID: 20462952
    [Abstract] [Full Text] [Related]

  • 17. Early steps of protein disaggregation by Hsp70 chaperone and class B J-domain proteins are shaped by Hsp110.
    Sztangierska W, Wyszkowski H, Pokornowska M, Kochanowicz K, Rychłowski M, Liberek K, Kłosowska A.
    Elife; 2024 Oct 15; 13():. PubMed ID: 39404743
    [Abstract] [Full Text] [Related]

  • 18. Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70.
    Gowda NKC, Kaimal JM, Kityk R, Daniel C, Liebau J, Öhman M, Mayer MP, Andréasson C.
    Nat Struct Mol Biol; 2018 Jan 15; 25(1):83-89. PubMed ID: 29323280
    [Abstract] [Full Text] [Related]

  • 19. Chaperone-Mediated Protein Disaggregation Triggers Proteolytic Clearance of Intra-nuclear Protein Inclusions.
    den Brave F, Cairo LV, Jagadeesan C, Ruger-Herreros C, Mogk A, Bukau B, Jentsch S.
    Cell Rep; 2020 Jun 02; 31(9):107680. PubMed ID: 32492414
    [Abstract] [Full Text] [Related]

  • 20. Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligase.
    Guerriero CJ, Weiberth KF, Brodsky JL.
    J Biol Chem; 2013 Jun 21; 288(25):18506-20. PubMed ID: 23653356
    [Abstract] [Full Text] [Related]


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