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Journal Abstract Search

279 related items for PubMed ID: 9020108

  • 1. The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase.
    Stancato LF, Silverstein AM, Owens-Grillo JK, Chow YH, Jove R, Pratt WB.
    J Biol Chem; 1997 Feb 14; 272(7):4013-20. PubMed ID: 9020108
    [Abstract] [Full Text] [Related]

  • 2. Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway.
    Schulte TW, Blagosklonny MV, Romanova L, Mushinski JF, Monia BP, Johnston JF, Nguyen P, Trepel J, Neckers LM.
    Mol Cell Biol; 1996 Oct 14; 16(10):5839-45. PubMed ID: 8816498
    [Abstract] [Full Text] [Related]

  • 3. p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function.
    Grammatikakis N, Lin JH, Grammatikakis A, Tsichlis PN, Cochran BH.
    Mol Cell Biol; 1999 Mar 14; 19(3):1661-72. PubMed ID: 10022854
    [Abstract] [Full Text] [Related]

  • 4. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association.
    Schulte TW, Blagosklonny MV, Ingui C, Neckers L.
    J Biol Chem; 1995 Oct 13; 270(41):24585-8. PubMed ID: 7592678
    [Abstract] [Full Text] [Related]

  • 5. Differential effects of Hsp90 inhibition on protein kinases regulating signal transduction pathways required for myoblast differentiation.
    Yun BG, Matts RL.
    Exp Cell Res; 2005 Jul 01; 307(1):212-23. PubMed ID: 15922741
    [Abstract] [Full Text] [Related]

  • 6. Requirement for a hsp90 chaperone-dependent MEK1/2-ERK pathway for B cell antigen receptor-induced cyclin D2 expression in mature B lymphocytes.
    Piatelli MJ, Doughty C, Chiles TC.
    J Biol Chem; 2002 Apr 05; 277(14):12144-50. PubMed ID: 11823472
    [Abstract] [Full Text] [Related]

  • 7. The Hsp90-specific inhibitor geldanamycin selectively disrupts kinase-mediated signaling events of T-lymphocyte activation.
    Schnaider T, Somogyi J, Csermely P, Szamel M.
    Cell Stress Chaperones; 2000 Jan 05; 5(1):52-61. PubMed ID: 10701840
    [Abstract] [Full Text] [Related]

  • 8. Epidermal growth factor receptors harboring kinase domain mutations associate with the heat shock protein 90 chaperone and are destabilized following exposure to geldanamycins.
    Shimamura T, Lowell AM, Engelman JA, Shapiro GI.
    Cancer Res; 2005 Jul 15; 65(14):6401-8. PubMed ID: 16024644
    [Abstract] [Full Text] [Related]

  • 9. The heat shock protein 90-binding geldanamycin inhibits cancer cell proliferation, down-regulates oncoproteins, and inhibits epidermal growth factor-induced invasion in thyroid cancer cell lines.
    Park JW, Yeh MW, Wong MG, Lobo M, Hyun WC, Duh QY, Clark OH.
    J Clin Endocrinol Metab; 2003 Jul 15; 88(7):3346-53. PubMed ID: 12843186
    [Abstract] [Full Text] [Related]

  • 10. Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization.
    Stewart S, Sundaram M, Zhang Y, Lee J, Han M, Guan KL.
    Mol Cell Biol; 1999 Aug 15; 19(8):5523-34. PubMed ID: 10409742
    [Abstract] [Full Text] [Related]

  • 11. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin.
    Schulte TW, Neckers LM.
    Cancer Chemother Pharmacol; 1998 Aug 15; 42(4):273-9. PubMed ID: 9744771
    [Abstract] [Full Text] [Related]

  • 12. Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants.
    Owens-Grillo JK, Stancato LF, Hoffmann K, Pratt WB, Krishna P.
    Biochemistry; 1996 Dec 03; 35(48):15249-55. PubMed ID: 8952474
    [Abstract] [Full Text] [Related]

  • 13. Immunosuppressive effects of the heat shock protein 90-binding antibiotic geldanamycin.
    Sugita T, Tanaka S, Murakami T, Miyoshi H, Ohnuki T.
    Biochem Mol Biol Int; 1999 Apr 03; 47(4):587-95. PubMed ID: 10319410
    [Abstract] [Full Text] [Related]

  • 14. 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 03; 11(7):355-60. PubMed ID: 10939589
    [Abstract] [Full Text] [Related]

  • 15. 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]

  • 16. KF25706, a novel oxime derivative of radicicol, exhibits in vivo antitumor activity via selective depletion of Hsp90 binding signaling molecules.
    Soga S, Neckers LM, Schulte TW, Shiotsu Y, Akasaka K, Narumi H, Agatsuma T, Ikuina Y, Murakata C, Tamaoki T, Akinaga S.
    Cancer Res; 1999 Jun 15; 59(12):2931-8. PubMed ID: 10383157
    [Abstract] [Full Text] [Related]

  • 17. Heat shock protein 90 indirectly regulates ERK activity by affecting Raf protein metabolism.
    Dou F, Yuan LD, Zhu JJ.
    Acta Biochim Biophys Sin (Shanghai); 2005 Jul 15; 37(7):501-5. PubMed ID: 15999212
    [Abstract] [Full Text] [Related]

  • 18. Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity.
    Neckers L, Schulte TW, Mimnaugh E.
    Invest New Drugs; 1999 Jul 15; 17(4):361-73. PubMed ID: 10759403
    [Abstract] [Full Text] [Related]

  • 19. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin.
    Schulte TW, Akinaga S, Soga S, Sullivan W, Stensgard B, Toft D, Neckers LM.
    Cell Stress Chaperones; 1998 Jun 15; 3(2):100-8. PubMed ID: 9672245
    [Abstract] [Full Text] [Related]

  • 20. The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin.
    Segnitz B, Gehring U.
    J Biol Chem; 1997 Jul 25; 272(30):18694-701. PubMed ID: 9228040
    [Abstract] [Full Text] [Related]

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