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Journal Abstract Search

192 related items for PubMed ID: 23275244

  • 1. 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; 195(5):1061-7. PubMed ID: 23275244
    [Abstract] [Full Text] [Related]

  • 2. 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]

  • 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]

  • 4. 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]

  • 5. Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics.
    Denoncin K, Schwalm J, Vertommen D, Silhavy TJ, Collet JF.
    Proteomics; 2012 May 04; 12(9):1391-401. PubMed ID: 22589188
    [Abstract] [Full Text] [Related]

  • 6. Bacterial Outer Membrane Proteins Are Targeted to the Bam Complex by Two Parallel Mechanisms.
    Wang X, Peterson JH, Bernstein HD.
    mBio; 2021 May 04; 12(3):. PubMed ID: 33947759
    [Abstract] [Full Text] [Related]

  • 7. The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli.
    Palomino C, Marín E, Fernández LÁ.
    J Bacteriol; 2011 Oct 04; 193(19):5222-30. PubMed ID: 21784935
    [Abstract] [Full Text] [Related]

  • 8. 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]

  • 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
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  • 12. Molecular mechanism of networking among DegP, Skp and SurA in periplasm for biogenesis of outer membrane proteins.
    Yang C, Peng S, Chen C, Zhao XS.
    Biochem J; 2020 Aug 28; 477(16):2949-2965. PubMed ID: 32729902
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  • 13. The Periplasmic Chaperones Skp and SurA.
    Mas G, Thoma J, Hiller S.
    Subcell Biochem; 2019 Aug 28; 92():169-186. PubMed ID: 31214987
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  • 15. Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.
    Calabrese AN, Schiffrin B, Watson M, Karamanos TK, Walko M, Humes JR, Horne JE, White P, Wilson AJ, Kalli AC, Tuma R, Ashcroft AE, Brockwell DJ, Radford SE.
    Nat Commun; 2020 May 01; 11(1):2155. PubMed ID: 32358557
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  • 16. Outer membrane protein assembly mediated by BAM-SurA complexes.
    Fenn KL, Horne JE, Crossley JA, Böhringer N, Horne RJ, Schäberle TF, Calabrese AN, Radford SE, Ranson NA.
    Nat Commun; 2024 Sep 01; 15(1):7612. PubMed ID: 39218969
    [Abstract] [Full Text] [Related]

  • 17. Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding.
    Schiffrin B, Machin JM, Karamanos TK, Zhuravleva A, Brockwell DJ, Radford SE, Calabrese AN.
    Commun Biol; 2022 Jun 08; 5(1):560. PubMed ID: 35676411
    [Abstract] [Full Text] [Related]

  • 18. SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins.
    Marx DC, Plummer AM, Faustino AM, Devlin T, Roskopf MA, Leblanc MJ, Lessen HJ, Amann BT, Fleming PJ, Krueger S, Fried SD, Fleming KG.
    Proc Natl Acad Sci U S A; 2020 Nov 10; 117(45):28026-28035. PubMed ID: 33093201
    [Abstract] [Full Text] [Related]

  • 19. PpiD is a player in the network of periplasmic chaperones in Escherichia coli.
    Matern Y, Barion B, Behrens-Kneip S.
    BMC Microbiol; 2010 Sep 29; 10():251. PubMed ID: 20920237
    [Abstract] [Full Text] [Related]

  • 20. The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition.
    Hennecke G, Nolte J, Volkmer-Engert R, Schneider-Mergener J, Behrens S.
    J Biol Chem; 2005 Jun 24; 280(25):23540-8. PubMed ID: 15840585
    [Abstract] [Full Text] [Related]

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