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850 related items for PubMed ID: 11146632

  • 21. 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
    [Abstract] [Full Text] [Related]

  • 22. Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways.
    McClellan AJ, Scott MD, Frydman J.
    Cell; 2005 Jun 03; 121(5):739-48. PubMed ID: 15935760
    [Abstract] [Full Text] [Related]

  • 23. hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1.
    Kanelakis KC, Murphy PJ, Galigniana MD, Morishima Y, Takayama S, Reed JC, Toft DO, Pratt WB.
    Biochemistry; 2000 Nov 21; 39(46):14314-21. PubMed ID: 11087380
    [Abstract] [Full Text] [Related]

  • 24. Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.
    Brychzy A, Rein T, Winklhofer KF, Hartl FU, Young JC, Obermann WM.
    EMBO J; 2003 Jul 15; 22(14):3613-23. PubMed ID: 12853476
    [Abstract] [Full Text] [Related]

  • 25. Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.
    Dittmar KD, Demady DR, Stancato LF, Krishna P, Pratt WB.
    J Biol Chem; 1997 Aug 22; 272(34):21213-20. PubMed ID: 9261129
    [Abstract] [Full Text] [Related]

  • 26. 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]

  • 27. Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1.
    Shang Y, Xu X, Duan X, Guo J, Wang Y, Ren F, He D, Chang Z.
    Biochem Biophys Res Commun; 2014 Mar 28; 446(1):387-92. PubMed ID: 24613385
    [Abstract] [Full Text] [Related]

  • 28. 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]

  • 29. Molecular chaperone complexes with antagonizing activities regulate stability and activity of the tumor suppressor LKB1.
    Gaude H, Aznar N, Delay A, Bres A, Buchet-Poyau K, Caillat C, Vigouroux A, Rogon C, Woods A, Vanacker JM, Höhfeld J, Perret C, Meyer P, Billaud M, Forcet C.
    Oncogene; 2012 Mar 22; 31(12):1582-91. PubMed ID: 21860411
    [Abstract] [Full Text] [Related]

  • 30. Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity.
    Angeletti PC, Walker D, Panganiban AT.
    Cell Stress Chaperones; 2002 Jul 22; 7(3):258-68. PubMed ID: 12482202
    [Abstract] [Full Text] [Related]

  • 31. Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90.
    Stancato LF, Hutchison KA, Krishna P, Pratt WB.
    Biochemistry; 1996 Jan 16; 35(2):554-61. PubMed ID: 8555227
    [Abstract] [Full Text] [Related]

  • 32. Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome.
    Loo MA, Jensen TJ, Cui L, Hou Y, Chang XB, Riordan JR.
    EMBO J; 1998 Dec 01; 17(23):6879-87. PubMed ID: 9843494
    [Abstract] [Full Text] [Related]

  • 33. 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]

  • 34. Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes.
    Graf C, Stankiewicz M, Nikolay R, Mayer MP.
    Biochemistry; 2010 Mar 16; 49(10):2121-9. PubMed ID: 20146531
    [Abstract] [Full Text] [Related]

  • 35. 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]

  • 36. Regulation of glucocorticoid receptor steroid binding and trafficking by the hsp90/hsp70-based chaperone machinery: implications for clinical intervention.
    Murphy PJ.
    Leukemia; 2005 May 08; 19(5):710-2. PubMed ID: 15759036
    [No Abstract] [Full Text] [Related]

  • 37. Chaperone-mediated hierarchical control in targeting misfolded proteins to aggresomes.
    Zhang X, Qian SB.
    Mol Biol Cell; 2011 Sep 08; 22(18):3277-88. PubMed ID: 21775628
    [Abstract] [Full Text] [Related]

  • 38. Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system.
    Mandal AK, Gibney PA, Nillegoda NB, Theodoraki MA, Caplan AJ, Morano KA.
    Mol Biol Cell; 2010 May 01; 21(9):1439-48. PubMed ID: 20237159
    [Abstract] [Full Text] [Related]

  • 39. 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 01; 293(5):H3080-7. PubMed ID: 17873020
    [Abstract] [Full Text] [Related]

  • 40. The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome.
    An WG, Schulte TW, Neckers LM.
    Cell Growth Differ; 2000 Jul 01; 11(7):355-60. PubMed ID: 10939589
    [Abstract] [Full Text] [Related]

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