Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
1 to 5 of 5  Show
  1. 1
    Category: Sequences.
    Strain: VF5.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1552 other entries.

  2. 2
    "The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation."
    Erzberger J.P., Pirruccello M.M., Berger J.M.
    EMBO J. 21:4763-4773(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 76-399.
    Category: Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  3. 3
    "Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling."
    Erzberger J.P., Mott M.L., Berger J.M.
    Nat. Struct. Mol. Biol. 13:676-683(2006) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:2HCB.
  4. 4
    "Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators."
    Mott M.L., Erzberger J.P., Coons M.M., Berger J.M.
    Cell 135:623-634(2008) [PubMed] [Europe PMC] [Abstract]
    Category: Family & Domains.
    Annotation: DnaC is a molecular adaptor that uses ATP-activated DnaA as a docking site for regulating the recruitment and correct spatial deposition of the DnaB helicase onto originsImported.
    Source: GeneRIF:1192893.

    This publication is mapped to 1 other entry.

  5. 5
    "DNA stretching by bacterial initiators promotes replication origin opening."
    Duderstadt K.E., Chuang K., Berger J.M.
    Nature 478:209-213(2011) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:3R8F.
1 to 5 of 5  Show
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again