BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

497 related articles for article (PubMed ID: 19439666)

  • 1. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.
    Bertelsen EB; Chang L; Gestwicki JE; Zuiderweg ER
    Proc Natl Acad Sci U S A; 2009 May; 106(21):8471-6. PubMed ID: 19439666
    [TBL] [Abstract][Full Text] [Related]  

  • 2. New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE.
    Rossi MA; Pozhidaeva AK; Clerico EM; Petridis C; Gierasch LM
    J Biol Chem; 2024 Jan; 300(1):105574. PubMed ID: 38110031
    [TBL] [Abstract][Full Text] [Related]  

  • 3. An atomistic view of Hsp70 allosteric crosstalk: from the nucleotide to the substrate binding domain and back.
    Chiappori F; Merelli I; Milanesi L; Colombo G; Morra G
    Sci Rep; 2016 Mar; 6():23474. PubMed ID: 27025773
    [TBL] [Abstract][Full Text] [Related]  

  • 4. An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones.
    Zhuravleva A; Clerico EM; Gierasch LM
    Cell; 2012 Dec; 151(6):1296-307. PubMed ID: 23217711
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE.
    Melero R; Moro F; Pérez-Calvo MÁ; Perales-Calvo J; Quintana-Gallardo L; Llorca O; Muga A; Valpuesta JM
    J Biol Chem; 2015 Apr; 290(16):10083-92. PubMed ID: 25739641
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Monitoring conformational heterogeneity of the lid of DnaK substrate-binding domain during its chaperone cycle.
    Banerjee R; Jayaraj GG; Peter JJ; Kumar V; Mapa K
    FEBS J; 2016 Aug; 283(15):2853-68. PubMed ID: 27248857
    [TBL] [Abstract][Full Text] [Related]  

  • 7. The heat-sensitive Escherichia coli grpE280 phenotype: impaired interaction of GrpE(G122D) with DnaK.
    Grimshaw JP; Siegenthaler RK; Züger S; Schönfeld HJ; Z'graggen BR; Christen P
    J Mol Biol; 2005 Nov; 353(4):888-96. PubMed ID: 16198374
    [TBL] [Abstract][Full Text] [Related]  

  • 8. The Hsp70 interdomain linker is a dynamic switch that enables allosteric communication between two structured domains.
    English CA; Sherman W; Meng W; Gierasch LM
    J Biol Chem; 2017 Sep; 292(36):14765-14774. PubMed ID: 28754691
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Substrate-binding domain conformational dynamics mediate Hsp70 allostery.
    Zhuravleva A; Gierasch LM
    Proc Natl Acad Sci U S A; 2015 Jun; 112(22):E2865-73. PubMed ID: 26038563
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP.
    Qi R; Sarbeng EB; Liu Q; Le KQ; Xu X; Xu H; Yang J; Wong JL; Vorvis C; Hendrickson WA; Zhou L; Liu Q
    Nat Struct Mol Biol; 2013 Jul; 20(7):900-7. PubMed ID: 23708608
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Allostery in Hsp70 chaperones is transduced by subdomain rotations.
    Bhattacharya A; Kurochkin AV; Yip GN; Zhang Y; Bertelsen EB; Zuiderweg ER
    J Mol Biol; 2009 May; 388(3):475-90. PubMed ID: 19361428
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones.
    Zhuravleva A; Gierasch LM
    Proc Natl Acad Sci U S A; 2011 Apr; 108(17):6987-92. PubMed ID: 21482798
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC.
    Cupp-Vickery JR; Peterson JC; Ta DT; Vickery LE
    J Mol Biol; 2004 Sep; 342(4):1265-78. PubMed ID: 15351650
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Substrate Binding Switches the Conformation at the Lynchpin Site in the Substrate-Binding Domain of Human Hsp70 to Enable Allosteric Interdomain Communication.
    Umehara K; Hoshikawa M; Tochio N; Tate SI
    Molecules; 2018 Feb; 23(3):. PubMed ID: 29495458
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones.
    Kityk R; Kopp J; Sinning I; Mayer MP
    Mol Cell; 2012 Dec; 48(6):863-74. PubMed ID: 23123194
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Tracking the interplay between bound peptide and the lid domain of DnaK, using molecular dynamics.
    Azoulay I; Kucherenko N; Nachliel E; Gutman M; Azem A; Tsfadia Y
    Int J Mol Sci; 2013 Jun; 14(6):12675-95. PubMed ID: 23774839
    [TBL] [Abstract][Full Text] [Related]  

  • 17. NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.
    Revington M; Holder TM; Zuiderweg ER
    J Biol Chem; 2004 Aug; 279(32):33958-67. PubMed ID: 15175340
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Structural basis of J cochaperone binding and regulation of Hsp70.
    Jiang J; Maes EG; Taylor AB; Wang L; Hinck AP; Lafer EM; Sousa R
    Mol Cell; 2007 Nov; 28(3):422-33. PubMed ID: 17996706
    [TBL] [Abstract][Full Text] [Related]  

  • 19. An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activity.
    Li H; Zhu H; Sarbeng EB; Liu Q; Tian X; Yang Y; Lyons C; Zhou L; Liu Q
    J Biol Chem; 2020 Jan; 295(2):584-596. PubMed ID: 31806707
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Defining the structure of the substrate-free state of the DnaK molecular chaperone.
    Swain JF; Sivendran R; Gierasch LM
    Biochem Soc Symp; 2001; (68):69-82. PubMed ID: 11573348
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 25.