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158 related items for PubMed ID: 11352903

  • 1. Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants.
    Buczynski G, Slepenkov SV, Sehorn MG, Witt SN.
    J Biol Chem; 2001 Jul 20; 276(29):27231-6. PubMed ID: 11352903
    [Abstract] [Full Text] [Related]

  • 2. Importance of the D and E helices of the molecular chaperone DnaK for ATP binding and substrate release.
    Slepenkov SV, Patchen B, Peterson KM, Witt SN.
    Biochemistry; 2003 May 20; 42(19):5867-76. PubMed ID: 12741845
    [Abstract] [Full Text] [Related]

  • 3. Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state.
    Slepenkov SV, Witt SN.
    Biochemistry; 2002 Oct 08; 41(40):12224-35. PubMed ID: 12356325
    [Abstract] [Full Text] [Related]

  • 4. Interdomain communication in the molecular chaperone DnaK.
    Han W, Christen P.
    Biochem J; 2003 Feb 01; 369(Pt 3):627-34. PubMed ID: 12383055
    [Abstract] [Full Text] [Related]

  • 5. Deletion of DnaK's lid strengthens binding to the nucleotide exchange factor, GrpE: a kinetic and thermodynamic analysis.
    Chesnokova LS, Slepenkov SV, Protasevich II, Sehorn MG, Brouillette CG, Witt SN.
    Biochemistry; 2003 Aug 05; 42(30):9028-40. PubMed ID: 12885236
    [Abstract] [Full Text] [Related]

  • 6. Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone.
    Russell R, Jordan R, McMacken R.
    Biochemistry; 1998 Jan 13; 37(2):596-607. PubMed ID: 9425082
    [Abstract] [Full Text] [Related]

  • 7. The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG.
    Stevens SY, Cai S, Pellecchia M, Zuiderweg ER.
    Protein Sci; 2003 Nov 13; 12(11):2588-96. PubMed ID: 14573869
    [Abstract] [Full Text] [Related]

  • 8. Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ.
    Suh WC, Lu CZ, Gross CA.
    J Biol Chem; 1999 Oct 22; 274(43):30534-9. PubMed ID: 10521435
    [Abstract] [Full Text] [Related]

  • 9. Structural dynamics of the DnaK-peptide complex.
    Popp S, Packschies L, Radzwill N, Vogel KP, Steinhoff HJ, Reinstein J.
    J Mol Biol; 2005 Apr 15; 347(5):1039-52. PubMed ID: 15784262
    [Abstract] [Full Text] [Related]

  • 10. Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling.
    Montgomery DL, Morimoto RI, Gierasch LM.
    J Mol Biol; 1999 Feb 26; 286(3):915-32. PubMed ID: 10024459
    [Abstract] [Full Text] [Related]

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  • 12. The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system.
    Pierpaoli EV, Sandmeier E, Baici A, Schönfeld HJ, Gisler S, Christen P.
    J Mol Biol; 1997 Jun 27; 269(5):757-68. PubMed ID: 9223639
    [Abstract] [Full Text] [Related]

  • 13. Detection of a concerted conformational change in the ATPase domain of DnaK triggered by peptide binding.
    Slepenkov SV, Witt SN.
    FEBS Lett; 2003 Mar 27; 539(1-3):100-4. PubMed ID: 12650934
    [Abstract] [Full Text] [Related]

  • 14. Multistep mechanism of substrate binding determines chaperone activity of Hsp70.
    Mayer MP, Schröder H, Rüdiger S, Paal K, Laufen T, Bukau B.
    Nat Struct Biol; 2000 Jul 27; 7(7):586-93. PubMed ID: 10876246
    [Abstract] [Full Text] [Related]

  • 15. The insect antimicrobial peptide, L-pyrrhocoricin, binds to and stimulates the ATPase activity of both wild-type and lidless DnaK.
    Chesnokova LS, Slepenkov SV, Witt SN.
    FEBS Lett; 2004 May 07; 565(1-3):65-9. PubMed ID: 15135054
    [Abstract] [Full Text] [Related]

  • 16. Kinetics of the reactions of the Escherichia coli molecular chaperone DnaK with ATP: evidence that a three-step reaction precedes ATP hydrolysis.
    Slepenkov SV, Witt SN.
    Biochemistry; 1998 Jan 27; 37(4):1015-24. PubMed ID: 9454592
    [Abstract] [Full Text] [Related]

  • 17. Defining the structure of the substrate-free state of the DnaK molecular chaperone.
    Swain JF, Sivendran R, Gierasch LM.
    Biochem Soc Symp; 2001 Jan 27; (68):69-82. PubMed ID: 11573348
    [Abstract] [Full Text] [Related]

  • 18. The allosteric transition in DnaK probed by infrared difference spectroscopy. Concerted ATP-induced rearrangement of the substrate binding domain.
    Moro F, Fernández-Sáiz V, Muga A.
    Protein Sci; 2006 Feb 27; 15(2):223-33. PubMed ID: 16384998
    [Abstract] [Full Text] [Related]

  • 19. Conformational properties of bacterial DnaK and yeast mitochondrial Hsp70. Role of the divergent C-terminal alpha-helical subdomain.
    Moro F, Fernández-Sáiz V, Slutsky O, Azem A, Muga A.
    FEBS J; 2005 Jun 27; 272(12):3184-96. PubMed ID: 15955075
    [Abstract] [Full Text] [Related]

  • 20. Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication.
    Buchberger A, Gässler CS, Büttner M, McMacken R, Bukau B.
    J Biol Chem; 1999 Dec 31; 274(53):38017-26. PubMed ID: 10608870
    [Abstract] [Full Text] [Related]

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