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226 related items for PubMed ID: 15046863

  • 1. 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]

  • 2. Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton.
    Galigniana MD, Scruggs JL, Herrington J, Welsh MJ, Carter-Su C, Housley PR, Pratt WB.
    Mol Endocrinol; 1998 Dec 07; 12(12):1903-13. PubMed ID: 9849964
    [Abstract] [Full Text] [Related]

  • 3. Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus.
    Czar MJ, Galigniana MD, Silverstein AM, Pratt WB.
    Biochemistry; 1997 Jun 24; 36(25):7776-85. PubMed ID: 9201920
    [Abstract] [Full Text] [Related]

  • 4. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells.
    Whitesell L, Cook P.
    Mol Endocrinol; 1996 Jun 24; 10(6):705-12. PubMed ID: 8776730
    [Abstract] [Full Text] [Related]

  • 5. Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus.
    Galigniana MD, Radanyi C, Renoir JM, Housley PR, Pratt WB.
    J Biol Chem; 2001 May 04; 276(18):14884-9. PubMed ID: 11278753
    [Abstract] [Full Text] [Related]

  • 6. 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 04; 19(12):2901-14. PubMed ID: 16037132
    [Abstract] [Full Text] [Related]

  • 7. Development and validation of a high-content screening assay to identify inhibitors of cytoplasmic dynein-mediated transport of glucocorticoid receptor to the nucleus.
    Johnston PA, Shinde SN, Hua Y, Shun TY, Lazo JS, Day BW.
    Assay Drug Dev Technol; 2012 Oct 04; 10(5):432-56. PubMed ID: 22830992
    [Abstract] [Full Text] [Related]

  • 8. Regulation of nuclear retention of glucocorticoid receptor by nuclear Hsp90.
    Tago K, Tsukahara F, Naruse M, Yoshioka T, Takano K.
    Mol Cell Endocrinol; 2004 Jan 15; 213(2):131-8. PubMed ID: 15062560
    [Abstract] [Full Text] [Related]

  • 9. 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 15; 3(1):93-6. PubMed ID: 11146632
    [Abstract] [Full Text] [Related]

  • 10. Inhibition of mineralocorticoid and glucocorticoid receptor function by the heat shock protein 90-binding agent geldanamycin.
    Bamberger CM, Wald M, Bamberger AM, Schulte HM.
    Mol Cell Endocrinol; 1997 Aug 08; 131(2):233-40. PubMed ID: 9296382
    [Abstract] [Full Text] [Related]

  • 11. Alteration of the glucocorticoid receptor subcellular localization by non steroidal compounds.
    Prima V, Depoix C, Masselot B, Formstecher P, Lefebvre P.
    J Steroid Biochem Mol Biol; 2000 Aug 08; 72(1-2):1-12. PubMed ID: 10731632
    [Abstract] [Full Text] [Related]

  • 12. CYP2E1 degradation by in vitro reconstituted systems: role of the molecular chaperone hsp90.
    Goasduff T, Cederbaum AI.
    Arch Biochem Biophys; 2000 Jul 15; 379(2):321-30. PubMed ID: 10898951
    [Abstract] [Full Text] [Related]

  • 13. 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 15; 11(7):355-60. PubMed ID: 10939589
    [Abstract] [Full Text] [Related]

  • 14. Dynamic changes in subcellular localization of mineralocorticoid receptor in living cells: in comparison with glucocorticoid receptor using dual-color labeling with green fluorescent protein spectral variants.
    Nishi M, Ogawa H, Ito T, Matsuda KI, Kawata M.
    Mol Endocrinol; 2001 Jul 15; 15(7):1077-92. PubMed ID: 11435609
    [Abstract] [Full Text] [Related]

  • 15. Hsp90 rescues PTK6 from proteasomal degradation in breast cancer cells.
    Kang SA, Cho HS, Yoon JB, Chung IK, Lee ST.
    Biochem J; 2012 Oct 15; 447(2):313-20. PubMed ID: 22849407
    [Abstract] [Full Text] [Related]

  • 16. 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]

  • 17. Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes.
    Stavreva DA, Müller WG, Hager GL, Smith CL, McNally JG.
    Mol Cell Biol; 2004 Apr 01; 24(7):2682-97. PubMed ID: 15024059
    [Abstract] [Full Text] [Related]

  • 18. Geldanamycin, an inhibitor of Hsp90, blocks cytoplasmic retention of progesterone receptors and glucocorticoid receptors via their respective ligand binding domains.
    Kakar M, Kanwal C, Davis JR, Li H, Lim CS.
    AAPS J; 2006 Nov 22; 8(4):E718-28. PubMed ID: 17233535
    [Abstract] [Full Text] [Related]

  • 19. Ubiquitination and proteasomal degradation of nucleophosmin-anaplastic lymphoma kinase induced by 17-allylamino-demethoxygeldanamycin: role of the co-chaperone carboxyl heat shock protein 70-interacting protein.
    Bonvini P, Dalla Rosa H, Vignes N, Rosolen A.
    Cancer Res; 2004 May 01; 64(9):3256-64. PubMed ID: 15126367
    [Abstract] [Full Text] [Related]

  • 20. Glucocorticoid receptors in hippocampal neurons that do not engage proteasomes escape from hormone-dependent down-regulation but maintain transactivation activity.
    Wang X, Pongrac JL, DeFranco DB.
    Mol Endocrinol; 2002 Sep 01; 16(9):1987-98. PubMed ID: 12198236
    [Abstract] [Full Text] [Related]

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