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Journal Abstract Search

570 related items for PubMed ID: 9230303

  • 1. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.
    Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH.
    Cell; 1997 Jul 11; 90(1):65-75. PubMed ID: 9230303
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  • 4. The charged region of Hsp90 modulates the function of the N-terminal domain.
    Scheibel T, Siegmund HI, Jaenicke R, Ganz P, Lilie H, Buchner J.
    Proc Natl Acad Sci U S A; 1999 Feb 16; 96(4):1297-302. PubMed ID: 9990018
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  • 6. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.
    Grenert JP, Sullivan WP, Fadden P, Haystead TA, Clark J, Mimnaugh E, Krutzsch H, Ochel HJ, Schulte TW, Sausville E, Neckers LM, Toft DO.
    J Biol Chem; 1997 Sep 19; 272(38):23843-50. PubMed ID: 9295332
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  • 7. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent.
    Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP.
    Cell; 1997 Apr 18; 89(2):239-50. PubMed ID: 9108479
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  • 8. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.
    Panaretou B, Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH.
    EMBO J; 1998 Aug 17; 17(16):4829-36. PubMed ID: 9707442
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  • 9. 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 17; 3(2):100-8. PubMed ID: 9672245
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  • 10. A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90.
    Itoh H, Ogura M, Komatsuda A, Wakui H, Miura AB, Tashima Y.
    Biochem J; 1999 Nov 01; 343 Pt 3(Pt 3):697-703. PubMed ID: 10527951
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  • 11. Hsp90 & Co. - a holding for folding.
    Buchner J.
    Trends Biochem Sci; 1999 Apr 01; 24(4):136-41. PubMed ID: 10322418
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  • 12. Structure of the ATP-binding domain of Plasmodium falciparum Hsp90.
    Corbett KD, Berger JM.
    Proteins; 2010 Oct 01; 78(13):2738-44. PubMed ID: 20635416
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  • 13. A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket.
    Söti C, Rácz A, Csermely P.
    J Biol Chem; 2002 Mar 01; 277(9):7066-75. PubMed ID: 11751878
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  • 14. Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket.
    Donnelly A, Blagg BS.
    Curr Med Chem; 2008 Mar 01; 15(26):2702-17. PubMed ID: 18991631
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  • 15. [Molecular chaperone HSP90 as a novel target for cancer chemotherapy].
    Miyata Y.
    Nihon Yakurigaku Zasshi; 2003 Jan 01; 121(1):33-42. PubMed ID: 12617036
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  • 16. In vitro evidence that hsp90 contains two independent chaperone sites.
    Young JC, Schneider C, Hartl FU.
    FEBS Lett; 1997 Nov 24; 418(1-2):139-43. PubMed ID: 9414113
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  • 17. Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.
    Chu F, Maynard JC, Chiosis G, Nicchitta CV, Burlingame AL.
    Protein Sci; 2006 Jun 24; 15(6):1260-9. PubMed ID: 16731965
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  • 18. 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
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  • 19. Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins.
    Bohen SP.
    Mol Cell Biol; 1998 Jun 15; 18(6):3330-9. PubMed ID: 9584173
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  • 20. A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone.
    Prodromou C, Roe SM, Piper PW, Pearl LH.
    Nat Struct Biol; 1997 Jun 15; 4(6):477-82. PubMed ID: 9187656
    [Abstract] [Full Text] [Related]

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