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PUBMED FOR HANDHELDS

Journal Abstract Search


276 related items for PubMed ID: 23502424

  • 1. ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system.
    Polier S, Samant RS, Clarke PA, Workman P, Prodromou C, Pearl LH.
    Nat Chem Biol; 2013 May; 9(5):307-12. PubMed ID: 23502424
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  • 2. 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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  • 3. Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins.
    Smith JR, de Billy E, Hobbs S, Powers M, Prodromou C, Pearl L, Clarke PA, Workman P.
    Oncogene; 2015 Jan 02; 34(1):15-26. PubMed ID: 24292678
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  • 5. Nucleotide-Free sB-Raf is Preferentially Bound by Hsp90 and Cdc37 In Vitro.
    Eckl JM, Daake M, Schwartz S, Richter K.
    J Mol Biol; 2016 Oct 09; 428(20):4185-4196. PubMed ID: 27620500
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  • 6. Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.
    Czemeres J, Buse K, Verkhivker GM.
    PLoS One; 2017 Oct 09; 12(12):e0190267. PubMed ID: 29267381
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  • 10. Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors.
    Smith JR, Clarke PA, de Billy E, Workman P.
    Oncogene; 2009 Jan 15; 28(2):157-69. PubMed ID: 18931700
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  • 11. How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.
    Verba KA, Agard DA.
    Trends Biochem Sci; 2017 Oct 15; 42(10):799-811. PubMed ID: 28784328
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  • 12. The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37).
    Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH.
    Cell; 2004 Jan 09; 116(1):87-98. PubMed ID: 14718169
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  • 14. Targeting the HSP90-CDC37-kinase chaperone cycle: A promising therapeutic strategy for cancer.
    Wang L, Zhang Q, You Q.
    Med Res Rev; 2022 Jan 09; 42(1):156-182. PubMed ID: 33846988
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  • 15. Simvastatin functions as a heat shock protein 90 inhibitor against triple-negative breast cancer.
    Kou X, Jiang X, Liu H, Wang X, Sun F, Han J, Fan J, Feng G, Lin Z, Jiang L, Yang Y.
    Cancer Sci; 2018 Oct 09; 109(10):3272-3284. PubMed ID: 30039622
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  • 17. 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
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  • 18. Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology.
    Lerner Y, Sukumaran S, Chua MS, So SK, Qvit N.
    J Vis Exp; 2022 Mar 31; (181):. PubMed ID: 35435890
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  • 19. Targeting CDC37: an alternative, kinase-directed strategy for disruption of oncogenic chaperoning.
    Smith JR, Workman P.
    Cell Cycle; 2009 Feb 01; 8(3):362-72. PubMed ID: 19177013
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  • 20. Characterization of celastrol to inhibit hsp90 and cdc37 interaction.
    Zhang T, Li Y, Yu Y, Zou P, Jiang Y, Sun D.
    J Biol Chem; 2009 Dec 18; 284(51):35381-9. PubMed ID: 19858214
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