BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

177 related articles for article (PubMed ID: 22853906)

  • 1. Molecular and thermodynamic insights into the conformational transitions of Hsp90.
    Simunovic M; Voth GA
    Biophys J; 2012 Jul; 103(2):284-92. PubMed ID: 22853906
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.
    Southworth DR; Agard DA
    Mol Cell; 2008 Dec; 32(5):631-40. PubMed ID: 19061638
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.
    Shiau AK; Harris SF; Southworth DR; Agard DA
    Cell; 2006 Oct; 127(2):329-40. PubMed ID: 17055434
    [TBL] [Abstract][Full Text] [Related]  

  • 4. 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]  

  • 5. Two closed ATP- and ADP-dependent conformations in yeast Hsp90 chaperone detected by Mn(II) EPR spectroscopic techniques.
    Giannoulis A; Feintuch A; Barak Y; Mazal H; Albeck S; Unger T; Yang F; Su XC; Goldfarb D
    Proc Natl Acad Sci U S A; 2020 Jan; 117(1):395-404. PubMed ID: 31862713
    [TBL] [Abstract][Full Text] [Related]  

  • 6. A dynamic view of ATP-coupled functioning cycle of Hsp90 N-terminal domain.
    Zhang H; Zhou C; Chen W; Xu Y; Shi Y; Wen Y; Zhang N
    Sci Rep; 2015 Apr; 5():9542. PubMed ID: 25867902
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: A comparative perspective.
    Minari K; de Azevedo ÉC; Kiraly VTR; Batista FAH; de Moraes FR; de Melo FA; Nascimento AS; Gava LM; Ramos CHI; Borges JC
    Int J Biol Macromol; 2019 Jun; 130():125-138. PubMed ID: 30797004
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Conformational Cycling within the Closed State of Grp94, an Hsp90-Family Chaperone.
    Huang B; Friedman LJ; Sun M; Gelles J; Street TO
    J Mol Biol; 2019 Aug; 431(17):3312-3323. PubMed ID: 31202885
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.
    Krukenberg KA; Förster F; Rice LM; Sali A; Agard DA
    Structure; 2008 May; 16(5):755-65. PubMed ID: 18462680
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Allosteric Modulation of Human Hsp90α Conformational Dynamics.
    Penkler DL; Atilgan C; Tastan Bishop Ö
    J Chem Inf Model; 2018 Feb; 58(2):383-404. PubMed ID: 29378140
    [TBL] [Abstract][Full Text] [Related]  

  • 11. The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones.
    Li J; Soroka J; Buchner J
    Biochim Biophys Acta; 2012 Mar; 1823(3):624-35. PubMed ID: 21951723
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Understanding the Hsp90
    Magwenyane AM; Mhlongo NN; Lawal MM; Amoako DG; Somboro AM; Sosibo SC; Shunmugam L; Khan RB; Kumalo HM
    Molecules; 2020 Apr; 25(8):. PubMed ID: 32295059
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer.
    Morra G; Verkhivker G; Colombo G
    PLoS Comput Biol; 2009 Mar; 5(3):e1000323. PubMed ID: 19300478
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Visualizing the Dynamics of a Protein Folding Machinery: The Mechanism of Asymmetric ATP Processing in Hsp90 and its Implications for Client Remodelling.
    D'Annessa I; Moroni E; Colombo G
    J Mol Biol; 2021 Jan; 433(2):166728. PubMed ID: 33275968
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.
    Graf C; Stankiewicz M; Kramer G; Mayer MP
    EMBO J; 2009 Mar; 28(5):602-13. PubMed ID: 19165152
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90.
    Mader SL; Lopez A; Lawatscheck J; Luo Q; Rutz DA; Gamiz-Hernandez AP; Sattler M; Buchner J; Kaila VRI
    Nat Commun; 2020 Mar; 11(1):1410. PubMed ID: 32179743
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding.
    Huai Q; Wang H; Liu Y; Kim HY; Toft D; Ke H
    Structure; 2005 Apr; 13(4):579-90. PubMed ID: 15837196
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform.
    McLaughlin SH; Ventouras LA; Lobbezoo B; Jackson SE
    J Mol Biol; 2004 Nov; 344(3):813-26. PubMed ID: 15533447
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide.
    Krukenberg KA; Böttcher UM; Southworth DR; Agard DA
    Protein Sci; 2009 Sep; 18(9):1815-27. PubMed ID: 19554567
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Molecular mechanism of bacterial Hsp90 pH-dependent ATPase activity.
    Jin Y; Hoxie RS; Street TO
    Protein Sci; 2017 Jun; 26(6):1206-1213. PubMed ID: 28383119
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 9.