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Journal Abstract Search

312 related items for PubMed ID: 17825319

  • 1. The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues.
    Xu X, Wang S, Hu YX, McKay DB.
    J Mol Biol; 2007 Oct 19; 373(2):367-81. PubMed ID: 17825319
    [Abstract] [Full Text] [Related]

  • 2. The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins.
    Bitto E, McKay DB.
    J Biol Chem; 2003 Dec 05; 278(49):49316-22. PubMed ID: 14506253
    [Abstract] [Full Text] [Related]

  • 3. Conformational Dynamics of the Periplasmic Chaperone SurA.
    Jia M, Wu B, Yang Z, Chen C, Zhao M, Hou X, Niu X, Jin C, Hu Y.
    Biochemistry; 2020 Sep 08; 59(35):3235-3246. PubMed ID: 32786408
    [Abstract] [Full Text] [Related]

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  • 5. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins.
    Bitto E, McKay DB.
    Structure; 2002 Nov 08; 10(11):1489-98. PubMed ID: 12429090
    [Abstract] [Full Text] [Related]

  • 6. Conserved substrate binding by chaperones in the bacterial periplasm and the mitochondrial intermembrane space.
    Alcock FH, Grossmann JG, Gentle IE, Likić VA, Lithgow T, Tokatlidis K.
    Biochem J; 2008 Jan 15; 409(2):377-87. PubMed ID: 17894549
    [Abstract] [Full Text] [Related]

  • 7. Generation of a highly active folding enzyme by combining a parvulin-type prolyl isomerase from SurA with an unrelated chaperone domain.
    Geitner AJ, Varga E, Wehmer M, Schmid FX.
    J Mol Biol; 2013 Nov 15; 425(22):4089-98. PubMed ID: 23871892
    [Abstract] [Full Text] [Related]

  • 8. Components of SurA required for outer membrane biogenesis in uropathogenic Escherichia coli.
    Watts KM, Hunstad DA.
    PLoS One; 2008 Oct 06; 3(10):e3359. PubMed ID: 18836534
    [Abstract] [Full Text] [Related]

  • 9. The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT.
    Humes JR, Schiffrin B, Calabrese AN, Higgins AJ, Westhead DR, Brockwell DJ, Radford SE.
    J Mol Biol; 2019 Mar 15; 431(6):1267-1283. PubMed ID: 30716334
    [Abstract] [Full Text] [Related]

  • 10. The Periplasmic Chaperones Skp and SurA.
    Mas G, Thoma J, Hiller S.
    Subcell Biochem; 2019 Mar 15; 92():169-186. PubMed ID: 31214987
    [Abstract] [Full Text] [Related]

  • 11. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.
    Behrens S, Maier R, de Cock H, Schmid FX, Gross CA.
    EMBO J; 2001 Jan 15; 20(1-2):285-94. PubMed ID: 11226178
    [Abstract] [Full Text] [Related]

  • 12. The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain.
    Soltes GR, Schwalm J, Ricci DP, Silhavy TJ.
    J Bacteriol; 2016 Jan 04; 198(6):921-9. PubMed ID: 26728192
    [Abstract] [Full Text] [Related]

  • 13. The periplasmic peptidyl prolyl cis-trans isomerases PpiD and SurA have partially overlapping substrate specificities.
    Stymest KH, Klappa P.
    FEBS J; 2008 Jul 04; 275(13):3470-9. PubMed ID: 18498364
    [Abstract] [Full Text] [Related]

  • 14. Insights into the function and structural flexibility of the periplasmic molecular chaperone SurA.
    Zhong M, Ferrell B, Lu W, Chai Q, Wei Y.
    J Bacteriol; 2013 Mar 04; 195(5):1061-7. PubMed ID: 23275244
    [Abstract] [Full Text] [Related]

  • 15. 1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli.
    Jia M, Hu Y, Jin C.
    Biomol NMR Assign; 2019 Apr 04; 13(1):183-186. PubMed ID: 30684235
    [Abstract] [Full Text] [Related]

  • 16. Diverse sequences are functional at the C-terminus of the E. coli periplasmic chaperone SurA.
    Chai Q, Ferrell B, Zhong M, Zhang X, Ye C, Wei Y.
    Protein Eng Des Sel; 2014 Apr 04; 27(4):111-6. PubMed ID: 24586054
    [Abstract] [Full Text] [Related]

  • 17. The virulence factor PEB4 (Cj0596) and the periplasmic protein Cj1289 are two structurally related SurA-like chaperones in the human pathogen Campylobacter jejuni.
    Kale A, Phansopa C, Suwannachart C, Craven CJ, Rafferty JB, Kelly DJ.
    J Biol Chem; 2011 Jun 17; 286(24):21254-65. PubMed ID: 21524997
    [Abstract] [Full Text] [Related]

  • 18. Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id essential and sufficient for peptide binding.
    Webb HM, Ruddock LW, Marchant RJ, Jonas K, Klappa P.
    J Biol Chem; 2001 Dec 07; 276(49):45622-7. PubMed ID: 11546789
    [Abstract] [Full Text] [Related]

  • 19. Periplasmic chaperones--new structural and functional insights.
    Behrens S.
    Structure; 2002 Nov 07; 10(11):1469-71. PubMed ID: 12429086
    [Abstract] [Full Text] [Related]

  • 20. Dual client binding sites in the ATP-independent chaperone SurA.
    Schiffrin B, Crossley JA, Walko M, Machin JM, Nasir Khan G, Manfield IW, Wilson AJ, Brockwell DJ, Fessl T, Calabrese AN, Radford SE, Zhuravleva A.
    Nat Commun; 2024 Sep 14; 15(1):8071. PubMed ID: 39277579
    [Abstract] [Full Text] [Related]

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