These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

276 related articles for article (PubMed ID: 31824256)

  • 1. Therapeutic Potential of the Hsp90/Cdc37 Interaction in Neurodegenerative Diseases.
    Gracia L; Lora G; Blair LJ; Jinwal UK
    Front Neurosci; 2019; 13():1263. PubMed ID: 31824256
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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; (181):. PubMed ID: 35435890
    [TBL] [Abstract][Full Text] [Related]  

  • 3. The Therapeutic Potential of Targeting Hsp90-Cdc37 Interactions in Several Diseases.
    Zhang X; Li S; Li Z; Cheng L; Liu Z; Wang C
    Curr Drug Targets; 2022; 23(10):1023-1038. PubMed ID: 35400341
    [TBL] [Abstract][Full Text] [Related]  

  • 4. 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; 11(1):59. PubMed ID: 29699578
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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; 292(7):2830-2841. PubMed ID: 28073914
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Hsp90 modulates human sperm capacitation via the Erk1/2 and p38 MAPK signaling pathways.
    Sun P; Wang Y; Gao T; Li K; Zheng D; Liu A; Ni Y
    Reprod Biol Endocrinol; 2021 Mar; 19(1):39. PubMed ID: 33663544
    [TBL] [Abstract][Full Text] [Related]  

  • 7. 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
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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; 288(22):16032-42. PubMed ID: 23569206
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Withaferin A Regulates LRRK2 Levels by Interfering with the Hsp90- Cdc37 Chaperone Complex.
    Narayan M; Zhang J; Braswell K; Gibson C; Zitnyar A; Lee DC; Varghese-Gupta S; Jinwal UK
    Curr Aging Sci; 2015; 8(3):259-65. PubMed ID: 25989799
    [TBL] [Abstract][Full Text] [Related]  

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

  • 11. 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; 58(2):405-421. PubMed ID: 29432007
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Rational design, synthesis and structural characterization of peptides and peptidomimetics to target Hsp90/Cdc37 interaction for treating hepatocellular carcinoma.
    Sukumaran S; Tan M; Ben-Uliel SF; Zhang H; De Zotti M; Chua MS; So SK; Qvit N
    Comput Struct Biotechnol J; 2023; 21():3159-3172. PubMed ID: 37304004
    [TBL] [Abstract][Full Text] [Related]  

  • 13. 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; 34(1):15-26. PubMed ID: 24292678
    [TBL] [Abstract][Full Text] [Related]  

  • 14. 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; 290(52):30843-54. PubMed ID: 26511315
    [TBL] [Abstract][Full Text] [Related]  

  • 15. The Hsp90 kinase co-chaperone Cdc37 regulates tau stability and phosphorylation dynamics.
    Jinwal UK; Trotter JH; Abisambra JF; Koren J; Lawson LY; Vestal GD; O'Leary JC; Johnson AG; Jin Y; Jones JR; Li Q; Weeber EJ; Dickey CA
    J Biol Chem; 2011 May; 286(19):16976-83. PubMed ID: 21367866
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Design, synthesis and bioevaluation of inhibitors targeting HSP90-CDC37 protein-protein interaction based on a hydrophobic core.
    Zhang Q; Wu X; Zhou J; Zhang L; Xu X; Zhang L; You Q; Wang L
    Eur J Med Chem; 2021 Jan; 210():112959. PubMed ID: 33109397
    [TBL] [Abstract][Full Text] [Related]  

  • 17. The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery.
    Xu Y; Liu F; Liu J; Wang D; Yan Y; Ji S; Zan J; Zhou J
    Sci Rep; 2016 Jun; 6():27123. PubMed ID: 27251758
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Targeting Hsp90-Cdc37: A Promising Therapeutic Strategy by Inhibiting Hsp90 Chaperone Function.
    Wang L; Li L; Gu K; Xu XL; Sun Y; You QD
    Curr Drug Targets; 2017; 18(13):1572-1585. PubMed ID: 27231111
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Cdc37 is a molecular chaperone with specific functions in signal transduction.
    Kimura Y; Rutherford SL; Miyata Y; Yahara I; Freeman BC; Yue L; Morimoto RI; Lindquist S
    Genes Dev; 1997 Jul; 11(14):1775-85. PubMed ID: 9242486
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Targeting Cdc37 inhibits multiple signaling pathways and induces growth arrest in prostate cancer cells.
    Gray PJ; Stevenson MA; Calderwood SK
    Cancer Res; 2007 Dec; 67(24):11942-50. PubMed ID: 18089825
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 14.