BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

597 related articles for article (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; 11(20):1569-77. PubMed ID: 11676916
    [TBL] [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; 275(7):4613-7. PubMed ID: 10671488
    [TBL] [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; 277(48):45920-7. PubMed ID: 12297498
    [TBL] [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; 35(5):572-8. PubMed ID: 12672450
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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; 3(1):93-6. PubMed ID: 11146632
    [TBL] [Abstract][Full Text] [Related]  

  • 6. CHIP: a link between the chaperone and proteasome systems.
    McDonough H; Patterson C
    Cell Stress Chaperones; 2003; 8(4):303-8. PubMed ID: 15115282
    [TBL] [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; 27(7):368-75. PubMed ID: 12114026
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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; 3(1):100-5. PubMed ID: 11146634
    [TBL] [Abstract][Full Text] [Related]  

  • 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; 276(46):42938-44. PubMed ID: 11557750
    [TBL] [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; 410(1):134-40. PubMed ID: 12559985
    [TBL] [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; 321(3):574-83. PubMed ID: 15358145
    [TBL] [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; 16(12):5891-900. PubMed ID: 16207813
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Protein turnover: a CHIP programmed for proteolysis.
    Wiederkehr T; Bukau B; Buchberger A
    Curr Biol; 2002 Jan; 12(1):R26-8. PubMed ID: 11790321
    [TBL] [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; 2(12):1133-8. PubMed ID: 11743028
    [TBL] [Abstract][Full Text] [Related]  

  • 15. CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome.
    Chakraborty A; Edkins AL
    Subcell Biochem; 2023; 101():351-387. PubMed ID: 36520313
    [TBL] [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; 8(3):225-31. PubMed ID: 14984055
    [TBL] [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; 2(10):885-90. PubMed ID: 11600451
    [TBL] [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; 15(9):4003-10. PubMed ID: 15215316
    [TBL] [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; 19(6):4535-45. PubMed ID: 10330192
    [TBL] [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; 280(46):38673-81. PubMed ID: 16169850
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 30.