These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

114 related items for PubMed ID: 24280305

  • 1. The N-terminal domain of DnaT, a primosomal DNA replication protein, is crucial for PriB binding and self-trimerization.
    Huang YH, Huang CY.
    Biochem Biophys Res Commun; 2013 Dec 13; 442(3-4):147-52. PubMed ID: 24280305
    [Abstract] [Full Text] [Related]

  • 2. DnaT is a single-stranded DNA binding protein.
    Huang YH, Lin MJ, Huang CY.
    Genes Cells; 2013 Nov 13; 18(11):1007-19. PubMed ID: 24118681
    [Abstract] [Full Text] [Related]

  • 3. Structure and mechanism of the primosome protein DnaT-functional structures for homotrimerization, dissociation of ssDNA from the PriB·ssDNA complex, and formation of the DnaT·ssDNA complex.
    Fujiyama S, Abe Y, Tani J, Urabe M, Sato K, Aramaki T, Katayama T, Ueda T.
    FEBS J; 2014 Dec 13; 281(23):5356-70. PubMed ID: 25265331
    [Abstract] [Full Text] [Related]

  • 4. Insight into the interaction between PriB and DnaT on bacterial DNA replication restart: Significance of the residues on PriB dimer interface and highly acidic region on DnaT.
    Fujiyama S, Abe Y, Shiroishi M, Ikeda Y, Ueda T.
    Biochim Biophys Acta Proteins Proteom; 2019 Apr 13; 1867(4):367-375. PubMed ID: 30659961
    [Abstract] [Full Text] [Related]

  • 5. DnaT is a PriC-binding protein.
    Huang CC, Huang CY.
    Biochem Biophys Res Commun; 2016 Sep 02; 477(4):988-992. PubMed ID: 27387236
    [Abstract] [Full Text] [Related]

  • 6.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 7.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 8. A structural model of the PriB-DnaT complex in Escherichia coli replication restart.
    Abe Y, Ikeda Y, Fujiyama S, Kini RM, Ueda T.
    FEBS Lett; 2021 Feb 02; 595(3):341-350. PubMed ID: 33275781
    [Abstract] [Full Text] [Related]

  • 9.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 10.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 11.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 12.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 13.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 14. Yeast two-hybrid analysis of PriB-interacting proteins in replication restart primosome: a proposed PriB-SSB interaction model.
    Huang YH, Lin MJ, Huang CY.
    Protein J; 2013 Aug 02; 32(6):477-83. PubMed ID: 23963891
    [Abstract] [Full Text] [Related]

  • 15. A single residue determines the cooperative binding property of a primosomal DNA replication protein, PriB, to single-stranded DNA.
    Huang YH, Lin HH, Huang CY.
    Biosci Biotechnol Biochem; 2012 Aug 02; 76(6):1110-5. PubMed ID: 22790931
    [Abstract] [Full Text] [Related]

  • 16. Crystal structure of PriB, a component of the Escherichia coli replication restart primosome.
    Lopper M, Holton JM, Keck JL.
    Structure; 2004 Nov 02; 12(11):1967-75. PubMed ID: 15530361
    [Abstract] [Full Text] [Related]

  • 17.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 18.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 19.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 20. Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site.
    Shioi S, Ose T, Maenaka K, Shiroishi M, Abe Y, Kohda D, Katayama T, Ueda T.
    Biochem Biophys Res Commun; 2005 Jan 28; 326(4):766-76. PubMed ID: 15607735
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 6.