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 *

239 related articles for article (PubMed ID: 32179743)

  • 21. Understanding ligand-based modulation of the Hsp90 molecular chaperone dynamics at atomic resolution.
    Colombo G; Morra G; Meli M; Verkhivker G
    Proc Natl Acad Sci U S A; 2008 Jun; 105(23):7976-81. PubMed ID: 18511558
    [TBL] [Abstract][Full Text] [Related]  

  • 22. Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis.
    Koulov AV; LaPointe P; Lu B; Razvi A; Coppinger J; Dong MQ; Matteson J; Laister R; Arrowsmith C; Yates JR; Balch WE
    Mol Biol Cell; 2010 Mar; 21(6):871-84. PubMed ID: 20089831
    [TBL] [Abstract][Full Text] [Related]  

  • 23. 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]  

  • 24. The Hsp70-Hsp90 Chaperone Cascade in Protein Folding.
    Morán Luengo T; Mayer MP; Rüdiger SGD
    Trends Cell Biol; 2019 Feb; 29(2):164-177. PubMed ID: 30502916
    [TBL] [Abstract][Full Text] [Related]  

  • 25. Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate.
    Sung N; Lee J; Kim JH; Chang C; Joachimiak A; Lee S; Tsai FT
    Proc Natl Acad Sci U S A; 2016 Mar; 113(11):2952-7. PubMed ID: 26929380
    [TBL] [Abstract][Full Text] [Related]  

  • 26. 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]  

  • 27. Intrinsic inhibition of the Hsp90 ATPase activity.
    Richter K; Moser S; Hagn F; Friedrich R; Hainzl O; Heller M; Schlee S; Kessler H; Reinstein J; Buchner J
    J Biol Chem; 2006 Apr; 281(16):11301-11. PubMed ID: 16461354
    [TBL] [Abstract][Full Text] [Related]  

  • 28. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions.
    Meyer P; Prodromou C; Hu B; Vaughan C; Roe SM; Panaretou B; Piper PW; Pearl LH
    Mol Cell; 2003 Mar; 11(3):647-58. PubMed ID: 12667448
    [TBL] [Abstract][Full Text] [Related]  

  • 29. The Hsp90 Chaperone:
    Lee BL; Rashid S; Wajda B; Wolmarans A; LaPointe P; Spyracopoulos L
    Biochemistry; 2019 Apr; 58(14):1869-1877. PubMed ID: 30869872
    [TBL] [Abstract][Full Text] [Related]  

  • 30. Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries.
    Dahiya V; Agam G; Lawatscheck J; Rutz DA; Lamb DC; Buchner J
    Mol Cell; 2019 May; 74(4):816-830.e7. PubMed ID: 31027879
    [TBL] [Abstract][Full Text] [Related]  

  • 31. The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis.
    Cunningham CN; Southworth DR; Krukenberg KA; Agard DA
    Protein Sci; 2012 Aug; 21(8):1162-71. PubMed ID: 22653663
    [TBL] [Abstract][Full Text] [Related]  

  • 32. Structural studies on the co-chaperone Hop and its complexes with Hsp90.
    Onuoha SC; Coulstock ET; Grossmann JG; Jackson SE
    J Mol Biol; 2008 Jun; 379(4):732-44. PubMed ID: 18485364
    [TBL] [Abstract][Full Text] [Related]  

  • 33. Extended conformational states dominate the Hsp90 chaperone dynamics.
    Jussupow A; Lopez A; Baumgart M; Mader SL; Sattler M; Kaila VRI
    J Biol Chem; 2022 Jul; 298(7):102101. PubMed ID: 35667441
    [TBL] [Abstract][Full Text] [Related]  

  • 34. A methylated lysine is a switch point for conformational communication in the chaperone Hsp90.
    Rehn A; Lawatscheck J; Jokisch ML; Mader SL; Luo Q; Tippel F; Blank B; Richter K; Lang K; Kaila VRI; Buchner J
    Nat Commun; 2020 Mar; 11(1):1219. PubMed ID: 32139682
    [TBL] [Abstract][Full Text] [Related]  

  • 35. 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]  

  • 36. Stimulation of heat shock protein 90 chaperone function through binding of a novobiocin analog KU-32.
    Chatterjee BK; Jayaraj A; Kumar V; Blagg B; Davis RE; Jayaram B; Deep S; Chaudhuri TK
    J Biol Chem; 2019 Apr; 294(16):6450-6467. PubMed ID: 30792306
    [TBL] [Abstract][Full Text] [Related]  

  • 37. 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]  

  • 38. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.
    Grenert JP; Sullivan WP; Fadden P; Haystead TA; Clark J; Mimnaugh E; Krutzsch H; Ochel HJ; Schulte TW; Sausville E; Neckers LM; Toft DO
    J Biol Chem; 1997 Sep; 272(38):23843-50. PubMed ID: 9295332
    [TBL] [Abstract][Full Text] [Related]  

  • 39. A switch point in the molecular chaperone Hsp90 responding to client interaction.
    Rutz DA; Luo Q; Freiburger L; Madl T; Kaila VRI; Sattler M; Buchner J
    Nat Commun; 2018 Apr; 9(1):1472. PubMed ID: 29662162
    [TBL] [Abstract][Full Text] [Related]  

  • 40. Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.
    Southworth DR; Agard DA
    Mol Cell; 2011 Jun; 42(6):771-81. PubMed ID: 21700222
    [TBL] [Abstract][Full Text] [Related]  

    [Previous]   [Next]    [New Search]
    of 12.