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Journal Abstract Search

231 related items for PubMed ID: 8730870

  • 1. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins.
    Chen R, Henning U.
    Mol Microbiol; 1996 Mar; 19(6):1287-94. PubMed ID: 8730870
    [Abstract] [Full Text] [Related]

  • 2. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins.
    Schäfer U, Beck K, Müller M.
    J Biol Chem; 1999 Aug 27; 274(35):24567-74. PubMed ID: 10455120
    [Abstract] [Full Text] [Related]

  • 3. Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study.
    Qu J, Behrens-Kneip S, Holst O, Kleinschmidt JH.
    Biochemistry; 2009 Jun 09; 48(22):4926-36. PubMed ID: 19382746
    [Abstract] [Full Text] [Related]

  • 4. The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions.
    Qu J, Mayer C, Behrens S, Holst O, Kleinschmidt JH.
    J Mol Biol; 2007 Nov 16; 374(1):91-105. PubMed ID: 17928002
    [Abstract] [Full Text] [Related]

  • 5. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein.
    De Cock H, Schäfer U, Potgeter M, Demel R, Müller M, Tommassen J.
    Eur J Biochem; 1999 Jan 16; 259(1-2):96-103. PubMed ID: 9914480
    [Abstract] [Full Text] [Related]

  • 6. Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp.
    Jarchow S, Lück C, Görg A, Skerra A.
    Proteomics; 2008 Dec 16; 8(23-24):4987-94. PubMed ID: 19003857
    [Abstract] [Full Text] [Related]

  • 7. Role for Skp in LptD assembly in Escherichia coli.
    Schwalm J, Mahoney TF, Soltes GR, Silhavy TJ.
    J Bacteriol; 2013 Aug 16; 195(16):3734-42. PubMed ID: 23772069
    [Abstract] [Full Text] [Related]

  • 8. The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential.
    Patel GJ, Behrens-Kneip S, Holst O, Kleinschmidt JH.
    Biochemistry; 2009 Nov 03; 48(43):10235-45. PubMed ID: 19780589
    [Abstract] [Full Text] [Related]

  • 9. Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics.
    Denoncin K, Schwalm J, Vertommen D, Silhavy TJ, Collet JF.
    Proteomics; 2012 May 03; 12(9):1391-401. PubMed ID: 22589188
    [Abstract] [Full Text] [Related]

  • 10. Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
    Sklar JG, Wu T, Kahne D, Silhavy TJ.
    Genes Dev; 2007 Oct 01; 21(19):2473-84. PubMed ID: 17908933
    [Abstract] [Full Text] [Related]

  • 11. Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp.
    Lyu ZX, Shao Q, Gao YQ, Zhao XS.
    PLoS One; 2012 Oct 01; 7(9):e46068. PubMed ID: 23049938
    [Abstract] [Full Text] [Related]

  • 12. Biosynthesis of K88 fimbriae in Escherichia coli: interaction of tip-subunit FaeC with the periplasmic chaperone FaeE and the outer membrane usher FaeD.
    Mol O, Oudhuis WC, Oud RP, Sijbrandi R, Luirink J, Harms N, Oudega B.
    J Mol Microbiol Biotechnol; 2001 Jan 01; 3(1):135-42. PubMed ID: 11200226
    [Abstract] [Full Text] [Related]

  • 13. The CpxQ sRNA Negatively Regulates Skp To Prevent Mistargeting of β-Barrel Outer Membrane Proteins into the Cytoplasmic Membrane.
    Grabowicz M, Koren D, Silhavy TJ.
    mBio; 2016 Apr 05; 7(2):e00312-16. PubMed ID: 27048800
    [Abstract] [Full Text] [Related]

  • 14. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide.
    Bulieris PV, Behrens S, Holst O, Kleinschmidt JH.
    J Biol Chem; 2003 Mar 14; 278(11):9092-9. PubMed ID: 12509434
    [Abstract] [Full Text] [Related]

  • 15. The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane.
    Harms N, Koningstein G, Dontje W, Muller M, Oudega B, Luirink J, de Cock H.
    J Biol Chem; 2001 Jun 01; 276(22):18804-11. PubMed ID: 11278858
    [Abstract] [Full Text] [Related]

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  • 17. A novel chromosomal locus of enteropathogenic Escherichia coli (EPEC), which encodes a bfpT-regulated chaperone-like protein, TrcA, involved in microcolony formation by EPEC.
    Tobe T, Tatsuno I, Katayama E, Wu CY, Schoolnik GK, Sasakawa C.
    Mol Microbiol; 1999 Aug 01; 33(4):741-52. PubMed ID: 10447884
    [Abstract] [Full Text] [Related]

  • 18. Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation.
    Walton TA, Sousa MC.
    Mol Cell; 2004 Aug 13; 15(3):367-74. PubMed ID: 15304217
    [Abstract] [Full Text] [Related]

  • 19. The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains.
    Walton TA, Sandoval CM, Fowler CA, Pardi A, Sousa MC.
    Proc Natl Acad Sci U S A; 2009 Feb 10; 106(6):1772-7. PubMed ID: 19181847
    [Abstract] [Full Text] [Related]

  • 20. Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP.
    McMorran LM, Bartlett AI, Huysmans GH, Radford SE, Brockwell DJ.
    J Mol Biol; 2013 Sep 09; 425(17):3178-91. PubMed ID: 23796519
    [Abstract] [Full Text] [Related]

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