ArticleBiomolecular NMR assignments2012
¹H, ¹³C, and ¹⁵N NMR assignments for the helicase interaction domain of Staphylococcus aureus DnaG primase.
Article in Biomolecular NMR assignments, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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2 citing papers in PubMed, 2 citations in OpenAlex.
- DnaG Primase-A Target for the Development of Novel Antibacterial Agents.Antibiotics (Basel, Switzerland) · 2018Review
- Identification of a Ligand-Binding Site on the Staphylococcus aureus DnaG Primase C-Terminal Domain.Biochemistry · 2017Article
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3 authors at 1 institution in 1 country.
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Abstract
The interaction between DnaG primase and DnaB helicase is essential for stimulating primer synthesis during bacterial DNA replication. The interaction occurs between the N-terminal domain of helicase and the C-terminal domain of primase. Here we present the (1)H, (13)C, and (15)N backbone and side-chain resonance assignments for the C-terminal helicase interaction domain of Staphylococcus aureus primase.
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