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Journal Abstract Search

279 related items for PubMed ID: 24285298

  • 1. Bacillus subtilis RecA and its accessory factors, RecF, RecO, RecR and RecX, are required for spore resistance to DNA double-strand break.
    Vlašić I, Mertens R, Seco EM, Carrasco B, Ayora S, Reitz G, Commichau FM, Alonso JC, Moeller R.
    Nucleic Acids Res; 2014 Feb; 42(4):2295-307. PubMed ID: 24285298
    [Abstract] [Full Text] [Related]

  • 2. Bacillus subtilis RecO and SsbA are crucial for RecA-mediated recombinational DNA repair.
    Carrasco B, Yadav T, Serrano E, Alonso JC.
    Nucleic Acids Res; 2015 Jul 13; 43(12):5984-97. PubMed ID: 26001966
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  • 6. Genetic recombination in Bacillus subtilis: a division of labor between two single-strand DNA-binding proteins.
    Yadav T, Carrasco B, Myers AR, George NP, Keck JL, Alonso JC.
    Nucleic Acids Res; 2012 Jul 13; 40(12):5546-59. PubMed ID: 22373918
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  • 8. Roles of Bacillus subtilis DprA and SsbA in RecA-mediated genetic recombination.
    Yadav T, Carrasco B, Serrano E, Alonso JC.
    J Biol Chem; 2014 Oct 03; 289(40):27640-52. PubMed ID: 25138221
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  • 9. Bacillus subtilis RadA/Sms-Mediated Nascent Lagging-Strand Unwinding at Stalled or Reversed Forks Is a Two-Step Process: RadA/Sms Assists RecA Nucleation, and RecA Loads RadA/Sms.
    Torres R, Carrasco B, Alonso JC.
    Int J Mol Sci; 2023 Feb 25; 24(5):. PubMed ID: 36901969
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  • 10. Replication Restart after Replication-Transcription Conflicts Requires RecA in Bacillus subtilis.
    Million-Weaver S, Samadpour AN, Merrikh H.
    J Bacteriol; 2015 Jul 25; 197(14):2374-82. PubMed ID: 25939832
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  • 11. Bacillus subtilis DprA recruits RecA onto single-stranded DNA and mediates annealing of complementary strands coated by SsbB and SsbA.
    Yadav T, Carrasco B, Hejna J, Suzuki Y, Takeyasu K, Alonso JC.
    J Biol Chem; 2013 Aug 02; 288(31):22437-50. PubMed ID: 23779106
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  • 12. Bacillus subtilis SsbA and dATP regulate RecA nucleation onto single-stranded DNA.
    Carrasco B, Manfredi C, Ayora S, Alonso JC.
    DNA Repair (Amst); 2008 Jun 01; 7(6):990-6. PubMed ID: 18472308
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  • 13. Visualization of DNA double-strand break repair in live bacteria reveals dynamic recruitment of Bacillus subtilis RecF, RecO and RecN proteins to distinct sites on the nucleoids.
    Kidane D, Sanchez H, Alonso JC, Graumann PL.
    Mol Microbiol; 2004 Jun 01; 52(6):1627-39. PubMed ID: 15186413
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  • 14. Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein.
    Umezu K, Kolodner RD.
    J Biol Chem; 1994 Nov 25; 269(47):30005-13. PubMed ID: 7962001
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  • 15. Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein.
    Umezu K, Chi NW, Kolodner RD.
    Proc Natl Acad Sci U S A; 1993 May 01; 90(9):3875-9. PubMed ID: 8483906
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  • 16. The process of displacing the single-stranded DNA-binding protein from single-stranded DNA by RecO and RecR proteins.
    Inoue J, Honda M, Ikawa S, Shibata T, Mikawa T.
    Nucleic Acids Res; 2008 Jan 01; 36(1):94-109. PubMed ID: 18000001
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  • 17. RecFOR proteins target RecA protein to a DNA gap with either DNA or RNA at the 5' terminus: implication for repair of stalled replication forks.
    Morimatsu K, Wu Y, Kowalczykowski SC.
    J Biol Chem; 2012 Oct 12; 287(42):35621-35630. PubMed ID: 22902627
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  • 18. Replication restart in UV-irradiated Escherichia coli involving pols II, III, V, PriA, RecA and RecFOR proteins.
    Rangarajan S, Woodgate R, Goodman MF.
    Mol Microbiol; 2002 Feb 12; 43(3):617-28. PubMed ID: 11929519
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  • 19. RecO-mediated DNA homology search and annealing is facilitated by SsbA.
    Manfredi C, Suzuki Y, Yadav T, Takeyasu K, Alonso JC.
    Nucleic Acids Res; 2010 Nov 12; 38(20):6920-9. PubMed ID: 20581116
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  • 20. RecA Is Required for the Assembly of RecN into DNA Repair Complexes on the Nucleoid.
    McLean EK, Lenhart JS, Simmons LA.
    J Bacteriol; 2021 Sep 23; 203(20):e0024021. PubMed ID: 34339298
    [Abstract] [Full Text] [Related]

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