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Journal Abstract Search

208 related items for PubMed ID: 14580201

  • 1. High affinity binding of Hsp90 is triggered by multiple discrete segments of its kinase clients.
    Scroggins BT, Prince T, Shao J, Uma S, Huang W, Guo Y, Yun BG, Hedman K, Matts RL, Hartson SD.
    Biochemistry; 2003 Nov 04; 42(43):12550-61. PubMed ID: 14580201
    [Abstract] [Full Text] [Related]

  • 2. Functional dissection of cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding.
    Shao J, Irwin A, Hartson SD, Matts RL.
    Biochemistry; 2003 Nov 04; 42(43):12577-88. PubMed ID: 14580204
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  • 5. Exposure of protein kinase motifs that trigger binding of Hsp90 and Cdc37.
    Prince T, Matts RL.
    Biochem Biophys Res Commun; 2005 Dec 23; 338(3):1447-54. PubMed ID: 16269130
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  • 6. Evidence for chaperone heterocomplexes containing both Hsp90 and VCP.
    Prince T, Shao J, Matts RL, Hartson SD.
    Biochem Biophys Res Commun; 2005 Jun 17; 331(4):1331-7. PubMed ID: 15883021
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  • 7. p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules.
    Hartson SD, Irwin AD, Shao J, Scroggins BT, Volk L, Huang W, Matts RL.
    Biochemistry; 2000 Jun 27; 39(25):7631-44. PubMed ID: 10858314
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  • 9. Biochemical and structural studies of the interaction of Cdc37 with Hsp90.
    Zhang W, Hirshberg M, McLaughlin SH, Lazar GA, Grossmann JG, Nielsen PR, Sobott F, Robinson CV, Jackson SE, Laue ED.
    J Mol Biol; 2004 Jul 16; 340(4):891-907. PubMed ID: 15223329
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  • 10. Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37.
    Roiniotis J, Masendycz P, Ho S, Scholz GM.
    Biochemistry; 2005 May 03; 44(17):6662-9. PubMed ID: 15850399
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  • 12. A client-binding site of Cdc37.
    Terasawa K, Minami Y.
    FEBS J; 2005 Sep 03; 272(18):4684-90. PubMed ID: 16156789
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  • 13. Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90.
    Turnbull EL, Martin IV, Fantes PA.
    FEBS J; 2005 Aug 03; 272(16):4129-40. PubMed ID: 16098195
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  • 15. The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins.
    McLaughlin SH, Sobott F, Yao ZP, Zhang W, Nielsen PR, Grossmann JG, Laue ED, Robinson CV, Jackson SE.
    J Mol Biol; 2006 Feb 24; 356(3):746-58. PubMed ID: 16403413
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  • 16. Functional specificity of co-chaperone interactions with Hsp90 client proteins.
    Riggs DL, Cox MB, Cheung-Flynn J, Prapapanich V, Carrigan PE, Smith DF.
    Crit Rev Biochem Mol Biol; 2004 Feb 24; 39(5-6):279-95. PubMed ID: 15763706
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  • 18. Functional Role and Hierarchy of the Intermolecular Interactions in Binding of Protein Kinase Clients to the Hsp90-Cdc37 Chaperone: Structure-Based Network Modeling of Allosteric Regulation.
    Stetz G, Verkhivker GM.
    J Chem Inf Model; 2018 Feb 26; 58(2):405-421. PubMed ID: 29432007
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  • 19. Targeting Cdc37 inhibits multiple signaling pathways and induces growth arrest in prostate cancer cells.
    Gray PJ, Stevenson MA, Calderwood SK.
    Cancer Res; 2007 Dec 15; 67(24):11942-50. PubMed ID: 18089825
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  • 20. Analysis of Hsp90 cochaperone interactions reveals a novel mechanism for TPR protein recognition.
    Chadli A, Bruinsma ES, Stensgard B, Toft D.
    Biochemistry; 2008 Mar 04; 47(9):2850-7. PubMed ID: 18211007
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