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 *

129 related articles for article (PubMed ID: 25244159)

  • 1. Artificial accelerators of the molecular chaperone Hsp90 facilitate rate-limiting conformational transitions.
    Zierer BK; Weiwad M; Rübbelke M; Freiburger L; Fischer G; Lorenz OR; Sattler M; Richter K; Buchner J
    Angew Chem Int Ed Engl; 2014 Nov; 53(45):12257-62. PubMed ID: 25244159
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Asymmetric activation of the hsp90 dimer by its cochaperone aha1.
    Retzlaff M; Hagn F; Mitschke L; Hessling M; Gugel F; Kessler H; Richter K; Buchner J
    Mol Cell; 2010 Feb; 37(3):344-54. PubMed ID: 20159554
    [TBL] [Abstract][Full Text] [Related]  

  • 3. A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.
    Stiegler SC; Rübbelke M; Korotkov VS; Weiwad M; John C; Fischer G; Sieber SA; Sattler M; Buchner J
    J Biol Chem; 2017 Oct; 292(41):17073-17083. PubMed ID: 28851842
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.
    Hessling M; Richter K; Buchner J
    Nat Struct Mol Biol; 2009 Mar; 16(3):287-93. PubMed ID: 19234467
    [TBL] [Abstract][Full Text] [Related]  

  • 5. The chaperone Hsp90: changing partners for demanding clients.
    Röhl A; Rohrberg J; Buchner J
    Trends Biochem Sci; 2013 May; 38(5):253-62. PubMed ID: 23507089
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.
    Li J; Richter K; Reinstein J; Buchner J
    Nat Struct Mol Biol; 2013 Mar; 20(3):326-31. PubMed ID: 23396352
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Conformational dynamics of the molecular chaperone Hsp90.
    Krukenberg KA; Street TO; Lavery LA; Agard DA
    Q Rev Biophys; 2011 May; 44(2):229-55. PubMed ID: 21414251
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Dynamic Aha1 co-chaperone binding to human Hsp90.
    Oroz J; Blair LJ; Zweckstetter M
    Protein Sci; 2019 Sep; 28(9):1545-1551. PubMed ID: 31299134
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Hsp90 structure and function studied by NMR spectroscopy.
    Didenko T; Duarte AM; Karagöz GE; Rüdiger SG
    Biochim Biophys Acta; 2012 Mar; 1823(3):636-47. PubMed ID: 22155720
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Structure, function and regulation of the hsp90 machinery.
    Li J; Buchner J
    Biomed J; 2013; 36(3):106-17. PubMed ID: 23806880
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation.
    Harst A; Lin H; Obermann WM
    Biochem J; 2005 May; 387(Pt 3):789-96. PubMed ID: 15584899
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.
    Street TO; Lavery LA; Agard DA
    Mol Cell; 2011 Apr; 42(1):96-105. PubMed ID: 21474071
    [TBL] [Abstract][Full Text] [Related]  

  • 13. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle.
    Richter K; Walter S; Buchner J
    J Mol Biol; 2004 Oct; 342(5):1403-13. PubMed ID: 15364569
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Cooperative Nucleotide Binding in Hsp90 and Its Regulation by Aha1.
    Wortmann P; Götz M; Hugel T
    Biophys J; 2017 Oct; 113(8):1711-1718. PubMed ID: 29045865
    [TBL] [Abstract][Full Text] [Related]  

  • 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; 356(3):746-58. PubMed ID: 16403413
    [TBL] [Abstract][Full Text] [Related]  

  • 16. The Hsp90 molecular chaperone: an open and shut case for treatment.
    Pearl LH; Prodromou C; Workman P
    Biochem J; 2008 Mar; 410(3):439-53. PubMed ID: 18290764
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Hsp90: Friends, clients and natural foes.
    Verma S; Goyal S; Jamal S; Singh A; Grover A
    Biochimie; 2016 Aug; 127():227-40. PubMed ID: 27295069
    [TBL] [Abstract][Full Text] [Related]  

  • 18. C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle.
    Weikl T; Muschler P; Richter K; Veit T; Reinstein J; Buchner J
    J Mol Biol; 2000 Nov; 303(4):583-92. PubMed ID: 11054293
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Conserved conformational changes in the ATPase cycle of human Hsp90.
    Richter K; Soroka J; Skalniak L; Leskovar A; Hessling M; Reinstein J; Buchner J
    J Biol Chem; 2008 Jun; 283(26):17757-65. PubMed ID: 18400751
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation.
    Soroka J; Wandinger SK; Mäusbacher N; Schreiber T; Richter K; Daub H; Buchner J
    Mol Cell; 2012 Feb; 45(4):517-28. PubMed ID: 22365831
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 7.