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Journal Abstract Search


850 related items for PubMed ID: 11146632

  • 1. 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
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  • 2. 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]

  • 3. 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 16; 3(1):100-5. PubMed ID: 11146634
    [Abstract] [Full Text] [Related]

  • 4. 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]

  • 5. CHIP: a link between the chaperone and proteasome systems.
    McDonough H, Patterson C.
    Cell Stress Chaperones; 2003 Aug 27; 8(4):303-8. PubMed ID: 15115282
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  • 6. Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation.
    Galigniana MD, Harrell JM, Housley PR, Patterson C, Fisher SK, Pratt WB.
    Brain Res Mol Brain Res; 2004 Apr 07; 123(1-2):27-36. PubMed ID: 15046863
    [Abstract] [Full Text] [Related]

  • 7. CHIP: a quality-control E3 ligase collaborating with molecular chaperones.
    Murata S, Chiba T, Tanaka K.
    Int J Biochem Cell Biol; 2003 May 07; 35(5):572-8. PubMed ID: 12672450
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  • 8. 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]

  • 9. Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery.
    Kanelakis KC, Morishima Y, Dittmar KD, Galigniana MD, Takayama S, Reed JC, Pratt WB.
    J Biol Chem; 1999 Nov 26; 274(48):34134-40. PubMed ID: 10567384
    [Abstract] [Full Text] [Related]

  • 10. 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 26; 19(6):4535-45. PubMed ID: 10330192
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  • 12. CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates.
    Stankiewicz M, Nikolay R, Rybin V, Mayer MP.
    FEBS J; 2010 Aug 26; 277(16):3353-67. PubMed ID: 20618441
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  • 14. 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]

  • 15. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold.
    Cyr DM, Höhfeld J, Patterson C.
    Trends Biochem Sci; 2002 Jul 05; 27(7):368-75. PubMed ID: 12114026
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  • 19. CHIP: a co-chaperone for degradation by the proteasome.
    Edkins AL.
    Subcell Biochem; 2015 Jul 05; 78():219-42. PubMed ID: 25487024
    [Abstract] [Full Text] [Related]

  • 20. CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-alpha.
    Fan M, Park A, Nephew KP.
    Mol Endocrinol; 2005 Dec 05; 19(12):2901-14. PubMed ID: 16037132
    [Abstract] [Full Text] [Related]


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