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PUBMED FOR HANDHELDS

Journal Abstract Search

167 related items for PubMed ID: 19517531

  • 1. Integrity of N- and C-termini is important for E. coli Hsp31 chaperone activity.
    Sastry MS, Zhou W, Baneyx F.
    Protein Sci; 2009 Jul; 18(7):1439-47. PubMed ID: 19517531
    [Abstract] [Full Text] [Related]

  • 2. The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures.
    Sastry MS, Quigley PM, Hol WG, Baneyx F.
    Proc Natl Acad Sci U S A; 2004 Jun 08; 101(23):8587-92. PubMed ID: 15173574
    [Abstract] [Full Text] [Related]

  • 3. A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function.
    Quigley PM, Korotkov K, Baneyx F, Hol WG.
    Protein Sci; 2004 Jan 08; 13(1):269-77. PubMed ID: 14691241
    [Abstract] [Full Text] [Related]

  • 4. Zinc-mediated Reversible Multimerization of Hsp31 Enhances the Activity of Holding Chaperone.
    Kim J, Choi D, Cha SY, Oh YM, Hwang E, Park C, Ryu KS.
    J Mol Biol; 2018 Jun 08; 430(12):1760-1772. PubMed ID: 29709570
    [Abstract] [Full Text] [Related]

  • 5. Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions.
    Mujacic M, Bader MW, Baneyx F.
    Mol Microbiol; 2004 Feb 08; 51(3):849-59. PubMed ID: 14731284
    [Abstract] [Full Text] [Related]

  • 6. Peptidase activity of the Escherichia coli Hsp31 chaperone.
    Malki A, Caldas T, Abdallah J, Kern R, Eckey V, Kim SJ, Cha SS, Mori H, Richarme G.
    J Biol Chem; 2005 Apr 15; 280(15):14420-6. PubMed ID: 15550391
    [Abstract] [Full Text] [Related]

  • 7. The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli.
    Jiao W, Qian M, Li P, Zhao L, Chang Z.
    J Mol Biol; 2005 Apr 08; 347(4):871-84. PubMed ID: 15769476
    [Abstract] [Full Text] [Related]

  • 8. Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli.
    Mujacic M, Baneyx F.
    Appl Environ Microbiol; 2007 Feb 08; 73(3):1014-8. PubMed ID: 17158627
    [Abstract] [Full Text] [Related]

  • 9. Structural alteration of Escherichia coli Hsp31 by thermal unfolding increases chaperone activity.
    Choi D, Ryu KS, Park C.
    Biochim Biophys Acta; 2013 Feb 08; 1834(2):621-8. PubMed ID: 23202248
    [Abstract] [Full Text] [Related]

  • 10. The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites.
    Zhao Y, Liu D, Kaluarachchi WD, Bellamy HD, White MA, Fox RO.
    Protein Sci; 2003 Oct 08; 12(10):2303-11. PubMed ID: 14500888
    [Abstract] [Full Text] [Related]

  • 11. The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad.
    Quigley PM, Korotkov K, Baneyx F, Hol WG.
    Proc Natl Acad Sci U S A; 2003 Mar 18; 100(6):3137-42. PubMed ID: 12621151
    [Abstract] [Full Text] [Related]

  • 12. Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31.
    Mujacic M, Baneyx F.
    Mol Microbiol; 2006 Jun 18; 60(6):1576-89. PubMed ID: 16796689
    [Abstract] [Full Text] [Related]

  • 13. Combination of the human prolyl isomerase FKBP12 with unrelated chaperone domains leads to chimeric folding enzymes with high activity.
    Geitner AJ, Schmid FX.
    J Mol Biol; 2012 Jul 20; 420(4-5):335-49. PubMed ID: 22542528
    [Abstract] [Full Text] [Related]

  • 14. Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain.
    Lee SJ, Kim SJ, Kim IK, Ko J, Jeong CS, Kim GH, Park C, Kang SO, Suh PG, Lee HS, Cha SS.
    J Biol Chem; 2003 Nov 07; 278(45):44552-9. PubMed ID: 12939276
    [Abstract] [Full Text] [Related]

  • 15. Backbone resonance assignments of the Escherichia coli 62 kDa protein, Hsp31.
    Kim J, Choi D, Park C, Ryu KS.
    Biomol NMR Assign; 2017 Oct 07; 11(2):159-163. PubMed ID: 28258548
    [Abstract] [Full Text] [Related]

  • 16. The N-terminal domain of Escherichia coli ClpB enhances chaperone function.
    Chow IT, Barnett ME, Zolkiewski M, Baneyx F.
    FEBS Lett; 2005 Aug 15; 579(20):4242-8. PubMed ID: 16051221
    [Abstract] [Full Text] [Related]

  • 17. Hsp31 of Escherichia coli K-12 is glyoxalase III.
    Subedi KP, Choi D, Kim I, Min B, Park C.
    Mol Microbiol; 2011 Aug 15; 81(4):926-36. PubMed ID: 21696459
    [Abstract] [Full Text] [Related]

  • 18. Genetic selection designed to stabilize proteins uncovers a chaperone called Spy.
    Quan S, Koldewey P, Tapley T, Kirsch N, Ruane KM, Pfizenmaier J, Shi R, Hofmann S, Foit L, Ren G, Jakob U, Xu Z, Cygler M, Bardwell JC.
    Nat Struct Mol Biol; 2011 Mar 15; 18(3):262-9. PubMed ID: 21317898
    [Abstract] [Full Text] [Related]

  • 19. Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity.
    Chi SW, Jeong DG, Woo JR, Lee HS, Park BC, Kim BY, Erikson RL, Ryu SE, Kim SJ.
    FEBS Lett; 2011 Feb 18; 585(4):664-70. PubMed ID: 21266175
    [Abstract] [Full Text] [Related]

  • 20. 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]

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