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Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

200 related items for PubMed ID: 9637927

  • 1. Formation of RuvABC-Holliday junction complexes in vitro.
    Davies AA, West SC.
    Curr Biol; 1998 Jun 04; 8(12):725-7. PubMed ID: 9637927
    [Abstract] [Full Text] [Related]

  • 2. Coordinated actions of RuvABC in Holliday junction processing.
    Zerbib D, Mézard C, George H, West SC.
    J Mol Biol; 1998 Aug 28; 281(4):621-30. PubMed ID: 9710535
    [Abstract] [Full Text] [Related]

  • 3. Functional interactions of Mycobacterium leprae RuvA with Escherichia coli RuvB and RuvC on holliday junctions.
    Arenas-Licea J, van Gool AJ, Keeley AJ, Davies A, West SC, Tsaneva IR.
    J Mol Biol; 2000 Aug 25; 301(4):839-50. PubMed ID: 10966790
    [Abstract] [Full Text] [Related]

  • 4. Functional interactions between the holliday junction resolvase and the branch migration motor of Escherichia coli.
    van Gool AJ, Shah R, Mézard C, West SC.
    EMBO J; 1998 Mar 16; 17(6):1838-45. PubMed ID: 9501105
    [Abstract] [Full Text] [Related]

  • 5. Interactions between RuvA and RuvC at Holliday junctions: inhibition of junction cleavage and formation of a RuvA-RuvC-DNA complex.
    Whitby MC, Bolt EL, Chan SN, Lloyd RG.
    J Mol Biol; 1996 Dec 20; 264(5):878-90. PubMed ID: 9000618
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  • 9. Processing of recombination intermediates by the RuvABC proteins.
    West SC.
    Annu Rev Genet; 1997 Dec 20; 31():213-44. PubMed ID: 9442895
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  • 10. The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome.
    Ingleston SM, Sharples GJ, Lloyd RG.
    EMBO J; 2000 Nov 15; 19(22):6266-74. PubMed ID: 11080172
    [Abstract] [Full Text] [Related]

  • 11. Processing of Holliday junctions by the Escherichia coli RuvA, RuvB, RuvC and RecG proteins.
    Müller B, West SC.
    Experientia; 1994 Mar 15; 50(3):216-22. PubMed ID: 8143795
    [Abstract] [Full Text] [Related]

  • 12. Characterisation of RuvAB-Holliday junction complexes by glycerol gradient sedimentation.
    Hiom K, West SC.
    Nucleic Acids Res; 1995 Sep 25; 23(18):3621-6. PubMed ID: 7478987
    [Abstract] [Full Text] [Related]

  • 13. The role of RuvA octamerization for RuvAB function in vitro and in vivo.
    Privezentzev CV, Keeley A, Sigala B, Tsaneva IR.
    J Biol Chem; 2005 Feb 04; 280(5):3365-75. PubMed ID: 15556943
    [Abstract] [Full Text] [Related]

  • 14. Resolution of Holliday intermediates in recombination and DNA repair: indirect suppression of ruvA, ruvB, and ruvC mutations.
    Mandal TN, Mahdi AA, Sharples GJ, Lloyd RG.
    J Bacteriol; 1993 Jul 04; 175(14):4325-34. PubMed ID: 8331065
    [Abstract] [Full Text] [Related]

  • 15. Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions.
    Parsons CA, Tsaneva I, Lloyd RG, West SC.
    Proc Natl Acad Sci U S A; 1992 Jun 15; 89(12):5452-6. PubMed ID: 1608954
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  • 16. Formation of a RuvAB-Holliday junction complex in vitro.
    Parsons CA, West SC.
    J Mol Biol; 1993 Jul 20; 232(2):397-405. PubMed ID: 8393934
    [Abstract] [Full Text] [Related]

  • 17. Recognition and manipulation of branched DNA by the RusA Holliday junction resolvase of Escherichia coli.
    Chan SN, Vincent SD, Lloyd RG.
    Nucleic Acids Res; 1998 Apr 01; 26(7):1560-6. PubMed ID: 9512524
    [Abstract] [Full Text] [Related]

  • 18. Branch migration and Holliday junction resolution catalyzed by activities from mammalian cells.
    Constantinou A, Davies AA, West SC.
    Cell; 2001 Jan 26; 104(2):259-68. PubMed ID: 11207366
    [Abstract] [Full Text] [Related]

  • 19. Molecular analysis of the Pseudomonas aeruginosa genes, ruvA, ruvB and ruvC, involved in processing of homologous recombination intermediates.
    Hishida T, Iwasaki H, Ishioka K, Shinagawa H.
    Gene; 1996 Dec 05; 182(1-2):63-70. PubMed ID: 8982068
    [Abstract] [Full Text] [Related]

  • 20. In vitro reconstitution of the late steps of genetic recombination in E. coli.
    Eggleston AK, Mitchell AH, West SC.
    Cell; 1997 May 16; 89(4):607-17. PubMed ID: 9160752
    [Abstract] [Full Text] [Related]

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