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Journal Abstract Search

278 related items for PubMed ID: 32966159

  • 1. 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]

  • 2. 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 Nov 15; 8(1):e52099. PubMed ID: 23341891
    [Abstract] [Full Text] [Related]

  • 3. 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]

  • 4. Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation.
    Stolz A, Besser S, Hottmann H, Wolf DH.
    Proc Natl Acad Sci U S A; 2013 Sep 17; 110(38):15271-6. PubMed ID: 23988329
    [Abstract] [Full Text] [Related]

  • 5. 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]

  • 6. 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]

  • 7. A protein quality control pathway at the mitochondrial outer membrane.
    Metzger MB, Scales JL, Dunklebarger MF, Loncarek J, Weissman AM.
    Elife; 2020 Mar 02; 9():. PubMed ID: 32118579
    [Abstract] [Full Text] [Related]

  • 8. 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]

  • 9. N-Myristoylation of the Rpt2 subunit of the yeast 26S proteasome is implicated in the subcellular compartment-specific protein quality control system.
    Kimura A, Kurata Y, Nakabayashi J, Kagawa H, Hirano H.
    J Proteomics; 2016 Jan 01; 130():33-41. PubMed ID: 26344132
    [Abstract] [Full Text] [Related]

  • 10. Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1.
    Heck JW, Cheung SK, Hampton RY.
    Proc Natl Acad Sci U S A; 2010 Jan 19; 107(3):1106-11. PubMed ID: 20080635
    [Abstract] [Full Text] [Related]

  • 11. 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]

  • 12. 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]

  • 13. Molecular mass as a determinant for nuclear San1-dependent targeting of misfolded cytosolic proteins to proteasomal degradation.
    Amm I, Wolf DH.
    FEBS Lett; 2016 Jun 21; 590(12):1765-75. PubMed ID: 27173001
    [Abstract] [Full Text] [Related]

  • 14. CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates.
    Stankiewicz M, Nikolay R, Rybin V, Mayer MP.
    FEBS J; 2010 Aug 21; 277(16):3353-67. PubMed ID: 20618441
    [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. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein.
    Nakatsukasa K, Huyer G, Michaelis S, Brodsky JL.
    Cell; 2008 Jan 11; 132(1):101-12. PubMed ID: 18191224
    [Abstract] [Full Text] [Related]

  • 17. CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome.
    Chakraborty A, Edkins AL.
    Subcell Biochem; 2023 Jan 11; 101():351-387. PubMed ID: 36520313
    [Abstract] [Full Text] [Related]

  • 18. Structural insights into Ubr1-mediated N-degron polyubiquitination.
    Pan M, Zheng Q, Wang T, Liang L, Mao J, Zuo C, Ding R, Ai H, Xie Y, Si D, Yu Y, Liu L, Zhao M.
    Nature; 2021 Dec 11; 600(7888):334-338. PubMed ID: 34789879
    [Abstract] [Full Text] [Related]

  • 19. 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 11; 24(13):2076-87. PubMed ID: 23637465
    [Abstract] [Full Text] [Related]

  • 20. Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1.
    Eisele F, Wolf DH.
    FEBS Lett; 2008 Dec 24; 582(30):4143-6. PubMed ID: 19041308
    [Abstract] [Full Text] [Related]

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