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Journal Abstract Search

213 related items for PubMed ID: 19387550

  • 21. Targeting the HSP90-CDC37-kinase chaperone cycle: A promising therapeutic strategy for cancer.
    Wang L, Zhang Q, You Q.
    Med Res Rev; 2022 Jan; 42(1):156-182. PubMed ID: 33846988
    [Abstract] [Full Text] [Related]

  • 22. 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]

  • 23. Cdc37 goes beyond Hsp90 and kinases.
    MacLean M, Picard D.
    Cell Stress Chaperones; 2003 Jan 17; 8(2):114-9. PubMed ID: 14627196
    [Abstract] [Full Text] [Related]

  • 24. HSP-90/kinase complexes are stabilized by the large PPIase FKB-6.
    Sima S, Barkovits K, Marcus K, Schmauder L, Hacker SM, Hellwig N, Morgner N, Richter K.
    Sci Rep; 2021 Jun 11; 11(1):12347. PubMed ID: 34117308
    [Abstract] [Full Text] [Related]

  • 25. Cdc37 as a Co-chaperone to Hsp90.
    Prince TL, Lang BJ, Okusha Y, Eguchi T, Calderwood SK.
    Subcell Biochem; 2023 Jun 11; 101():141-158. PubMed ID: 36520306
    [Abstract] [Full Text] [Related]

  • 26. p17-Modulated Hsp90/Cdc37 Complex Governs Oncolytic Avian Reovirus Replication by Chaperoning p17, Which Promotes Viral Protein Synthesis and Accumulation of Viral Proteins σC and σA in Viral Factories.
    Huang WR, Li JY, Wu YY, Liao TL, Nielsen BL, Liu HJ.
    J Virol; 2022 Mar 23; 96(6):e0007422. PubMed ID: 35107368
    [Abstract] [Full Text] [Related]

  • 27. 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]

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  • 29. The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37.
    Kowallik S, Kritikos A, Kästle M, Thurm C, Schraven B, Simeoni L.
    Int J Mol Sci; 2020 Dec 24; 22(1):. PubMed ID: 33374422
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  • 31. Protein quality control of DYRK family protein kinases by the Hsp90-Cdc37 molecular chaperone.
    Miyata Y, Nishida E.
    Biochim Biophys Acta Mol Cell Res; 2021 Sep 24; 1868(10):119081. PubMed ID: 34147560
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  • 34. Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.
    Bunney TD, Inglis AJ, Sanfelice D, Farrell B, Kerr CJ, Thompson GS, Masson GR, Thiyagarajan N, Svergun DI, Williams RL, Breeze AL, Katan M.
    Structure; 2018 Mar 06; 26(3):446-458.e8. PubMed ID: 29478821
    [Abstract] [Full Text] [Related]

  • 35. Coordinated targeting of CK2 and KIT in gastrointestinal stromal tumours.
    Huang M, Yang W, Zhu J, Mariño-Enríquez A, Zhu C, Chen J, Wu Y, Quan Y, Qiu H, Li X, Chai L, Fletcher JA, Ou WB.
    Br J Cancer; 2020 Feb 06; 122(3):372-381. PubMed ID: 31776458
    [Abstract] [Full Text] [Related]

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  • 37. Phosphorylated and unphosphorylated serine 13 of CDC37 stabilize distinct interactions between its client and HSP90 binding domains.
    Liu W, Landgraf R.
    Biochemistry; 2015 Feb 24; 54(7):1493-504. PubMed ID: 25619116
    [Abstract] [Full Text] [Related]

  • 38. Evaluating CK2 activity with the antibody specific for the CK2-phosphorylated form of a kinase-targeting cochaperone Cdc37.
    Miyata Y, Nishida E.
    Mol Cell Biochem; 2008 Sep 24; 316(1-2):127-34. PubMed ID: 18566753
    [Abstract] [Full Text] [Related]

  • 39. 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
    [Abstract] [Full Text] [Related]

  • 40. Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.
    Eckl JM, Rutz DA, Haslbeck V, Zierer BK, Reinstein J, Richter K.
    J Biol Chem; 2013 May 31; 288(22):16032-42. PubMed ID: 23569206
    [Abstract] [Full Text] [Related]

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