ArticleThe Journal of biological chemistry2017
Structural analyses of the bacterial primosomal protein DnaB reveal that it is a tetramer and forms a complex with a primosomal re-initiation protein.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Bacillus subtilis DnaB forms multiple protein-protein interactions essential for DNA replication initiation.Nucleic acids research · 2026Article
- Quantifying the concentration dependence of sedimentation coefficients for globular macromolecules: a continuing age-old problem.Biophysical reviews · 2021Review
- Bacillus subtilis RarA modulates replication restart.Nucleic acids research · 2018Article
- Allowance for radial dilution in evaluating the concentration dependence of sedimentation coefficients for globular proteins.European biophysics journal : EBJ · 2018Article
- Mechanisms of bacterial DNA replication restart.Nucleic acids research · 2018Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DnaB primosomal protein from Gram-positive bacteria plays a key role in DNA replication and restart as a loader protein for the recruitment of replisome cascade proteins. Previous investigations have established that DnaB is composed of an N-terminal domain, a middle domain, and a C-terminal domain. However, structural evidence for how DnaB functions at the atomic level is lacking. Here, we report the crystal structure of DnaB, encompassing the N-terminal and middle domains (residues 1-300), from
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