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Journal Abstract Search

361 related items for PubMed ID: 20969647

  • 1. Cross-linking FtsZ polymers into coherent Z rings.
    Dajkovic A, Pichoff S, Lutkenhaus J, Wirtz D.
    Mol Microbiol; 2010 Nov; 78(3):651-68. PubMed ID: 20969647
    [Abstract] [Full Text] [Related]

  • 2. Tetramerization of ZapA is required for FtsZ bundling.
    Pacheco-Gómez R, Cheng X, Hicks MR, Smith CJ, Roper DI, Addinall S, Rodger A, Dafforn TR.
    Biochem J; 2013 Feb 01; 449(3):795-802. PubMed ID: 23098212
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  • 3. Mapping the Contact Sites of the Escherichia coli Division-Initiating Proteins FtsZ and ZapA by BAMG Cross-Linking and Site-Directed Mutagenesis.
    Roseboom W, Nazir MG, Meiresonne NY, Mohammadi T, Verheul J, Buncherd H, Bonvin AMJJ, de Koning LJ, de Koster CG, de Jong L, den Blaauwen T.
    Int J Mol Sci; 2018 Sep 26; 19(10):. PubMed ID: 30261644
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  • 4. A conserved coiled-coil protein pair focuses the cytokinetic Z-ring in Caulobacter crescentus.
    Woldemeskel SA, McQuillen R, Hessel AM, Xiao J, Goley ED.
    Mol Microbiol; 2017 Sep 26; 105(5):721-740. PubMed ID: 28613431
    [Abstract] [Full Text] [Related]

  • 5. ZapA and ZapB form an FtsZ-independent structure at midcell.
    Buss JA, Peters NT, Xiao J, Bernhardt TG.
    Mol Microbiol; 2017 May 26; 104(4):652-663. PubMed ID: 28249098
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  • 7. Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring.
    Galli E, Gerdes K.
    Mol Microbiol; 2010 Jun 26; 76(6):1514-26. PubMed ID: 20487275
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  • 10. Structure and Mutational Analyses of Escherichia coli ZapD Reveal Charged Residues Involved in FtsZ Filament Bundling.
    Roach EJ, Wroblewski C, Seidel L, Berezuk AM, Brewer D, Kimber MS, Khursigara CM.
    J Bacteriol; 2016 Jun 01; 198(11):1683-1693. PubMed ID: 27021560
    [Abstract] [Full Text] [Related]

  • 11. Modeling FtsZ ring formation in the bacterial cell-anisotropic aggregation via mutual interactions of polymer rods.
    Fischer-Friedrich E, Gov N.
    Phys Biol; 2011 Apr 01; 8(2):026007. PubMed ID: 21335646
    [Abstract] [Full Text] [Related]

  • 12. Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria.
    Monahan LG, Robinson A, Harry EJ.
    Mol Microbiol; 2009 Nov 01; 74(4):1004-17. PubMed ID: 19843223
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  • 14. Examination of the interaction between FtsZ and MinCN in E. coli suggests how MinC disrupts Z rings.
    Shen B, Lutkenhaus J.
    Mol Microbiol; 2010 Mar 01; 75(5):1285-98. PubMed ID: 20132438
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  • 15. Characterization of the FtsZ C-Terminal Variable (CTV) Region in Z-Ring Assembly and Interaction with the Z-Ring Stabilizer ZapD in E. coli Cytokinesis.
    Huang KH, Mychack A, Tchorzewski L, Janakiraman A.
    PLoS One; 2016 Mar 01; 11(4):e0153337. PubMed ID: 27088231
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  • 16. Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking.
    Schumacher MA, Huang KH, Zeng W, Janakiraman A.
    J Biol Chem; 2017 Mar 03; 292(9):3740-3750. PubMed ID: 28100778
    [Abstract] [Full Text] [Related]

  • 17. A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis.
    Peters PC, Migocki MD, Thoni C, Harry EJ.
    Mol Microbiol; 2007 Apr 03; 64(2):487-99. PubMed ID: 17493130
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  • 18. Strong FtsZ is with the force: mechanisms to constrict bacteria.
    Mingorance J, Rivas G, Vélez M, Gómez-Puertas P, Vicente M.
    Trends Microbiol; 2010 Aug 03; 18(8):348-56. PubMed ID: 20598544
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  • 19. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.
    Anderson DE, Gueiros-Filho FJ, Erickson HP.
    J Bacteriol; 2004 Sep 03; 186(17):5775-81. PubMed ID: 15317782
    [Abstract] [Full Text] [Related]

  • 20. Crystal structure and site-directed mutational analysis reveals key residues involved in Escherichia coli ZapA function.
    Roach EJ, Kimber MS, Khursigara CM.
    J Biol Chem; 2014 Aug 22; 289(34):23276-86. PubMed ID: 25002581
    [Abstract] [Full Text] [Related]

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