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Journal Abstract Search

395 related items for PubMed ID: 15115282

  • 1. CHIP: a link between the chaperone and proteasome systems.
    McDonough H, Patterson C.
    Cell Stress Chaperones; 2003; 8(4):303-8. PubMed ID: 15115282
    [Abstract] [Full Text] [Related]

  • 2. CHIP: a quality-control E3 ligase collaborating with molecular chaperones.
    Murata S, Chiba T, Tanaka K.
    Int J Biochem Cell Biol; 2003 May; 35(5):572-8. PubMed ID: 12672450
    [Abstract] [Full Text] [Related]

  • 3. Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling.
    Demand J, Alberti S, Patterson C, Höhfeld J.
    Curr Biol; 2001 Oct 16; 11(20):1569-77. PubMed ID: 11676916
    [Abstract] [Full Text] [Related]

  • 4. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins.
    Connell P, Ballinger CA, Jiang J, Wu Y, Thompson LJ, Höhfeld J, Patterson C.
    Nat Cell Biol; 2001 Jan 16; 3(1):93-6. PubMed ID: 11146632
    [Abstract] [Full Text] [Related]

  • 5. Co-chaperone CHIP associates with mutant Cu/Zn-superoxide dismutase proteins linked to familial amyotrophic lateral sclerosis and promotes their degradation by proteasomes.
    Choi JS, Cho S, Park SG, Park BC, Lee DH.
    Biochem Biophys Res Commun; 2004 Aug 27; 321(3):574-83. PubMed ID: 15358145
    [Abstract] [Full Text] [Related]

  • 6. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.
    Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C.
    Mol Cell Biol; 1999 Jun 27; 19(6):4535-45. PubMed ID: 10330192
    [Abstract] [Full Text] [Related]

  • 7. CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome.
    Chakraborty A, Edkins AL.
    Subcell Biochem; 2023 Jun 27; 101():351-387. PubMed ID: 36520313
    [Abstract] [Full Text] [Related]

  • 8. Protein-Protein Interactions Modulate the Docking-Dependent E3-Ubiquitin Ligase Activity of Carboxy-Terminus of Hsc70-Interacting Protein (CHIP).
    Narayan V, Landré V, Ning J, Hernychova L, Muller P, Verma C, Walkinshaw MD, Blackburn EA, Ball KL.
    Mol Cell Proteomics; 2015 Nov 27; 14(11):2973-87. PubMed ID: 26330542
    [Abstract] [Full Text] [Related]

  • 9. CHIP: a co-chaperone for degradation by the proteasome.
    Edkins AL.
    Subcell Biochem; 2015 Nov 27; 78():219-42. PubMed ID: 25487024
    [Abstract] [Full Text] [Related]

  • 10. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation.
    Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM.
    Nat Cell Biol; 2001 Jan 27; 3(1):100-5. PubMed ID: 11146634
    [Abstract] [Full Text] [Related]

  • 11. Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome.
    Alberti S, Demand J, Esser C, Emmerich N, Schild H, Hohfeld J.
    J Biol Chem; 2002 Nov 29; 277(48):45920-7. PubMed ID: 12297498
    [Abstract] [Full Text] [Related]

  • 12. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold.
    Cyr DM, Höhfeld J, Patterson C.
    Trends Biochem Sci; 2002 Jul 29; 27(7):368-75. PubMed ID: 12114026
    [Abstract] [Full Text] [Related]

  • 13. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome.
    Lüders J, Demand J, Höhfeld J.
    J Biol Chem; 2000 Feb 18; 275(7):4613-7. PubMed ID: 10671488
    [Abstract] [Full Text] [Related]

  • 14. C-terminal Hsp-interacting protein slows androgen receptor synthesis and reduces its rate of degradation.
    Cardozo CP, Michaud C, Ost MC, Fliss AE, Yang E, Patterson C, Hall SJ, Caplan AJ.
    Arch Biochem Biophys; 2003 Feb 01; 410(1):134-40. PubMed ID: 12559985
    [Abstract] [Full Text] [Related]

  • 15. Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubiquitin ligase CHIP.
    Jiang J, Cyr D, Babbitt RW, Sessa WC, Patterson C.
    J Biol Chem; 2003 Dec 05; 278(49):49332-41. PubMed ID: 14507928
    [Abstract] [Full Text] [Related]

  • 16. U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy.
    Hatakeyama S, Matsumoto M, Kamura T, Murayama M, Chui DH, Planel E, Takahashi R, Nakayama KI, Takashima A.
    J Neurochem; 2004 Oct 05; 91(2):299-307. PubMed ID: 15447663
    [Abstract] [Full Text] [Related]

  • 17. Chaperone-dependent E3 ligase CHIP ubiquitinates and mediates proteasomal degradation of soluble guanylyl cyclase.
    Xia T, Dimitropoulou C, Zeng J, Antonova GN, Snead C, Venema RC, Fulton D, Qian S, Patterson C, Papapetropoulos A, Catravas JD.
    Am J Physiol Heart Circ Physiol; 2007 Nov 05; 293(5):H3080-7. PubMed ID: 17873020
    [Abstract] [Full Text] [Related]

  • 18. Purification and assay of the chaperone-dependent ubiquitin ligase of the carboxyl terminus of Hsc70-interacting protein.
    Murata S, Minami M, Minami Y.
    Methods Enzymol; 2005 Nov 05; 398():271-9. PubMed ID: 16275335
    [Abstract] [Full Text] [Related]

  • 19. Ca2+/S100 proteins act as upstream regulators of the chaperone-associated ubiquitin ligase CHIP (C terminus of Hsc70-interacting protein).
    Shimamoto S, Kubota Y, Yamaguchi F, Tokumitsu H, Kobayashi R.
    J Biol Chem; 2013 Mar 08; 288(10):7158-68. PubMed ID: 23344957
    [Abstract] [Full Text] [Related]

  • 20. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein.
    Murata S, Minami Y, Minami M, Chiba T, Tanaka K.
    EMBO Rep; 2001 Dec 08; 2(12):1133-8. PubMed ID: 11743028
    [Abstract] [Full Text] [Related]

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