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477 related items for PubMed ID: 24715731

  • 1. Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA.
    Gessmann D, Chung YH, Danoff EJ, Plummer AM, Sandlin CW, Zaccai NR, Fleming KG.
    Proc Natl Acad Sci U S A; 2014 Apr 22; 111(16):5878-83. PubMed ID: 24715731
    [Abstract] [Full Text] [Related]

  • 2. Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding.
    Schiffrin B, Calabrese AN, Higgins AJ, Humes JR, Ashcroft AE, Kalli AC, Brockwell DJ, Radford SE.
    J Mol Biol; 2017 Nov 24; 429(23):3776-3792. PubMed ID: 28919234
    [Abstract] [Full Text] [Related]

  • 3. Conformational Changes That Coordinate the Activity of BamA and BamD Allowing β-Barrel Assembly.
    McCabe AL, Ricci D, Adetunji M, Silhavy TJ.
    J Bacteriol; 2017 Oct 15; 199(20):. PubMed ID: 28760846
    [Abstract] [Full Text] [Related]

  • 4. BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism.
    Plummer AM, Fleming KG.
    Biochemistry; 2015 Oct 06; 54(39):6009-11. PubMed ID: 26394056
    [Abstract] [Full Text] [Related]

  • 5. Interplay of protein primary sequence, lipid membrane, and chaperone in β-barrel assembly.
    Tiwari PB, Mahalakshmi R.
    Protein Sci; 2021 Mar 06; 30(3):624-637. PubMed ID: 33410567
    [Abstract] [Full Text] [Related]

  • 6. Functions of the BamBCDE Lipoproteins Revealed by Bypass Mutations in BamA.
    Hart EM, Silhavy TJ.
    J Bacteriol; 2020 Oct 08; 202(21):. PubMed ID: 32817097
    [Abstract] [Full Text] [Related]

  • 7. BamA β16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly.
    Gu Y, Zeng Y, Wang Z, Dong C.
    Biochem J; 2017 Nov 21; 474(23):3951-3961. PubMed ID: 28974626
    [Abstract] [Full Text] [Related]

  • 8. Extreme Dynamics in the BamA β-Barrel Seam.
    Doerner PA, Sousa MC.
    Biochemistry; 2017 Jun 20; 56(24):3142-3149. PubMed ID: 28569500
    [Abstract] [Full Text] [Related]

  • 9. Substitutions in the BamA β-barrel domain overcome the conditional lethal phenotype of a ΔbamB ΔbamE strain of Escherichia coli.
    Tellez R, Misra R.
    J Bacteriol; 2012 Jan 20; 194(2):317-24. PubMed ID: 22037403
    [Abstract] [Full Text] [Related]

  • 10. The β-Barrel Assembly Machinery Complex.
    Leyton DL, Belousoff MJ, Lithgow T.
    Methods Mol Biol; 2015 Jan 20; 1329():1-16. PubMed ID: 26427672
    [Abstract] [Full Text] [Related]

  • 11. In vivo roles of BamA, BamB and BamD in the biogenesis of BamA, a core protein of the β-barrel assembly machine of Escherichia coli.
    Misra R, Stikeleather R, Gabriele R.
    J Mol Biol; 2015 Mar 13; 427(5):1061-74. PubMed ID: 24792419
    [Abstract] [Full Text] [Related]

  • 12. Conserved residues of the putative L6 loop of Escherichia coli BamA play a critical role in the assembly of β-barrel outer membrane proteins, including that of BamA itself.
    Leonard-Rivera M, Misra R.
    J Bacteriol; 2012 Sep 13; 194(17):4662-8. PubMed ID: 22753067
    [Abstract] [Full Text] [Related]

  • 13. A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria.
    Wang Y, Wang R, Jin F, Liu Y, Yu J, Fu X, Chang Z.
    J Biol Chem; 2016 Aug 05; 291(32):16720-9. PubMed ID: 27298319
    [Abstract] [Full Text] [Related]

  • 14. Structural basis of BAM-mediated outer membrane β-barrel protein assembly.
    Shen C, Chang S, Luo Q, Chan KC, Zhang Z, Luo B, Xie T, Lu G, Zhu X, Wei X, Dong C, Zhou R, Zhang X, Tang X, Dong H.
    Nature; 2023 May 05; 617(7959):185-193. PubMed ID: 37100902
    [Abstract] [Full Text] [Related]

  • 15. 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]

  • 16. Crystal structure of BamB bound to a periplasmic domain fragment of BamA, the central component of the β-barrel assembly machine.
    Jansen KB, Baker SL, Sousa MC.
    J Biol Chem; 2015 Jan 23; 290(4):2126-36. PubMed ID: 25468906
    [Abstract] [Full Text] [Related]

  • 17. POTRA Domains, Extracellular Lid, and Membrane Composition Modulate the Conformational Stability of the β Barrel Assembly Factor BamA.
    Thoma J, Sun Y, Ritzmann N, Müller DJ.
    Structure; 2018 Jul 03; 26(7):987-996.e3. PubMed ID: 29861346
    [Abstract] [Full Text] [Related]

  • 18. Flexibility in the Periplasmic Domain of BamA Is Important for Function.
    Warner LR, Gatzeva-Topalova PZ, Doerner PA, Pardi A, Sousa MC.
    Structure; 2017 Jan 03; 25(1):94-106. PubMed ID: 27989620
    [Abstract] [Full Text] [Related]

  • 19. From Chaperones to the Membrane with a BAM!
    Plummer AM, Fleming KG.
    Trends Biochem Sci; 2016 Oct 03; 41(10):872-882. PubMed ID: 27450425
    [Abstract] [Full Text] [Related]

  • 20. The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition.
    Hussain S, Bernstein HD.
    J Biol Chem; 2018 Feb 23; 293(8):2959-2973. PubMed ID: 29311257
    [Abstract] [Full Text] [Related]

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