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Journal Abstract Search

489 related items for PubMed ID: 11676916

  • 1. 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]

  • 2. 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]

  • 3. 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]

  • 4. CHIP: a quality-control E3 ligase collaborating with molecular chaperones.
    Murata S, Chiba T, Tanaka K.
    Int J Biochem Cell Biol; 2003 May 29; 35(5):572-8. PubMed ID: 12672450
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  • 6. CHIP: a link between the chaperone and proteasome systems.
    McDonough H, Patterson C.
    Cell Stress Chaperones; 2003 May 29; 8(4):303-8. PubMed ID: 15115282
    [Abstract] [Full Text] [Related]

  • 7. 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
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  • 9. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation.
    Jiang J, Ballinger CA, Wu Y, Dai Q, Cyr DM, Höhfeld J, Patterson C.
    J Biol Chem; 2001 Nov 16; 276(46):42938-44. PubMed ID: 11557750
    [Abstract] [Full Text] [Related]

  • 10. 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]

  • 11. 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]

  • 12. BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP.
    Arndt V, Daniel C, Nastainczyk W, Alberti S, Höhfeld J.
    Mol Biol Cell; 2005 Dec 27; 16(12):5891-900. PubMed ID: 16207813
    [Abstract] [Full Text] [Related]

  • 13. Protein turnover: a CHIP programmed for proteolysis.
    Wiederkehr T, Bukau B, Buchberger A.
    Curr Biol; 2002 Jan 08; 12(1):R26-8. PubMed ID: 11790321
    [Abstract] [Full Text] [Related]

  • 14. 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]

  • 15. CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome.
    Chakraborty A, Edkins AL.
    Subcell Biochem; 2023 Dec 08; 101():351-387. PubMed ID: 36520313
    [Abstract] [Full Text] [Related]

  • 16. BAG-1--a nucleotide exchange factor of Hsc70 with multiple cellular functions.
    Alberti S, Esser C, Höhfeld J.
    Cell Stress Chaperones; 2003 Dec 08; 8(3):225-31. PubMed ID: 14984055
    [Abstract] [Full Text] [Related]

  • 17. From the cradle to the grave: molecular chaperones that may choose between folding and degradation.
    Höhfeld J, Cyr DM, Patterson C.
    EMBO Rep; 2001 Oct 08; 2(10):885-90. PubMed ID: 11600451
    [Abstract] [Full Text] [Related]

  • 18. The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.
    Alberti S, Böhse K, Arndt V, Schmitz A, Höhfeld J.
    Mol Biol Cell; 2004 Sep 08; 15(9):4003-10. PubMed ID: 15215316
    [Abstract] [Full Text] [Related]

  • 19. 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 08; 19(6):4535-45. PubMed ID: 10330192
    [Abstract] [Full Text] [Related]

  • 20. Regulation of the cytoplasmic quality control protein degradation pathway by BAG2.
    Dai Q, Qian SB, Li HH, McDonough H, Borchers C, Huang D, Takayama S, Younger JM, Ren HY, Cyr DM, Patterson C.
    J Biol Chem; 2005 Nov 18; 280(46):38673-81. PubMed ID: 16169850
    [Abstract] [Full Text] [Related]

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