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Journal Abstract Search

320 related items for PubMed ID: 28073914

  • 1. Serine/Threonine Kinase Unc-51-like Kinase-1 (Ulk1) Phosphorylates the Co-chaperone Cell Division Cycle Protein 37 (Cdc37) and Thereby Disrupts the Stability of Cdc37 Client Proteins.
    Li R, Yuan F, Fu W, Zhang L, Zhang N, Wang Y, Ma K, Li X, Wang L, Zhu WG, Zhao Y.
    J Biol Chem; 2017 Feb 17; 292(7):2830-2841. PubMed ID: 28073914
    [Abstract] [Full Text] [Related]

  • 2. Hsp90-Cdc37 chaperone complex regulates Ulk1- and Atg13-mediated mitophagy.
    Joo JH, Dorsey FC, Joshi A, Hennessy-Walters KM, Rose KL, McCastlain K, Zhang J, Iyengar R, Jung CH, Suen DF, Steeves MA, Yang CY, Prater SM, Kim DH, Thompson CB, Youle RJ, Ney PA, Cleveland JL, Kundu M.
    Mol Cell; 2011 Aug 19; 43(4):572-85. PubMed ID: 21855797
    [Abstract] [Full Text] [Related]

  • 3. 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 Aug 19; 12(12):e0190267. PubMed ID: 29267381
    [Abstract] [Full Text] [Related]

  • 4. 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
    [Abstract] [Full Text] [Related]

  • 5. 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
    [Abstract] [Full Text] [Related]

  • 6. 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
    [Abstract] [Full Text] [Related]

  • 7. Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine.
    Xu W, Mollapour M, Prodromou C, Wang S, Scroggins BT, Palchick Z, Beebe K, Siderius M, Lee MJ, Couvillon A, Trepel JB, Miyata Y, Matts R, Neckers L.
    Mol Cell; 2012 Aug 10; 47(3):434-43. PubMed ID: 22727666
    [Abstract] [Full Text] [Related]

  • 8. Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.
    Shao J, Prince T, Hartson SD, Matts RL.
    J Biol Chem; 2003 Oct 03; 278(40):38117-20. PubMed ID: 12930845
    [Abstract] [Full Text] [Related]

  • 9. Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery.
    Miyata Y.
    Cell Mol Life Sci; 2009 Jun 03; 66(11-12):1840-9. PubMed ID: 19387550
    [Abstract] [Full Text] [Related]

  • 10. 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
    [Abstract] [Full Text] [Related]

  • 11. Hsp90 interacts with Cdc37, is phosphorylated by PKA/PKC, and regulates Src phosphorylation in human sperm capacitation.
    Li K, Sun P, Wang Y, Gao T, Zheng D, Liu A, Ni Y.
    Andrology; 2021 Jan 22; 9(1):185-195. PubMed ID: 32656999
    [Abstract] [Full Text] [Related]

  • 12. 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
    [Abstract] [Full Text] [Related]

  • 13. 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 09; 9(5):307-12. PubMed ID: 23502424
    [Abstract] [Full Text] [Related]

  • 14. Specific regulation of noncanonical p38alpha activation by Hsp90-Cdc37 chaperone complex in cardiomyocyte.
    Ota A, Zhang J, Ping P, Han J, Wang Y.
    Circ Res; 2010 Apr 30; 106(8):1404-12. PubMed ID: 20299663
    [Abstract] [Full Text] [Related]

  • 15. Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery.
    Li T, Jiang HL, Tong YG, Lu JJ.
    J Hematol Oncol; 2018 Apr 27; 11(1):59. PubMed ID: 29699578
    [Abstract] [Full Text] [Related]

  • 16. Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation.
    Bachman AB, Keramisanou D, Xu W, Beebe K, Moses MA, Vasantha Kumar MV, Gray G, Noor RE, van der Vaart A, Neckers L, Gelis I.
    Nat Commun; 2018 Jan 17; 9(1):265. PubMed ID: 29343704
    [Abstract] [Full Text] [Related]

  • 17. Exploring Mechanisms of Communication Switching in the Hsp90-Cdc37 Regulatory Complexes with Client Kinases through Allosteric Coupling of Phosphorylation Sites: Perturbation-Based Modeling and Hierarchical Community Analysis of Residue Interaction Networks.
    Stetz G, Astl L, Verkhivker GM.
    J Chem Theory Comput; 2020 Jul 14; 16(7):4706-4725. PubMed ID: 32492340
    [Abstract] [Full Text] [Related]

  • 18. Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.
    Eckl JM, Scherr MJ, Freiburger L, Daake MA, Sattler M, Richter K.
    J Biol Chem; 2015 Dec 25; 290(52):30843-54. PubMed ID: 26511315
    [Abstract] [Full Text] [Related]

  • 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
    [Abstract] [Full Text] [Related]

  • 20. Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37.
    Keramisanou D, Aboalroub A, Zhang Z, Liu W, Marshall D, Diviney A, Larsen RW, Landgraf R, Gelis I.
    Mol Cell; 2016 Apr 21; 62(2):260-271. PubMed ID: 27105117
    [Abstract] [Full Text] [Related]

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