ArticleMethods in enzymology2022
Use of an unnatural amino acid to map helicase/DNA interfaces via photoactivated crosslinking.
Article in Methods in enzymology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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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Who cites it
3 citing papers in PubMed, 1 citations in OpenAlex.
- Visualization of the complete preprimosome reveals the structural mechanisms governing DNA replication restart.Nature communications · 2026Article
- Visualization of the complete primosome reveals the structural mechanisms governing DNA replication restart.bioRxiv : the preprint server for biology · 2026Article
- Replication fork binding triggers structural changes in the PriA helicase that govern DNA replication restart in E. coli.Nature communications · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Formation of protein/nucleic acid complexes is essential for life. From DNA replication and repair to transcription and translation, myriad different proteins bind nucleic acids to execute their essential cellular functions. Our understanding of the mechanisms underlying recognition and processing of nucleic acids can be greatly informed by mapping protein domains and residues that form interfaces with their DNA or RNA targets. Here we describe a crosslinking protocol in which the unnatural amino acid p-benzoyl-l-phenylalanine (Bpa) integrated at selected sites within the PriA DNA helicase is used to map surfaces of the protein that interact with specific positions in a synthetic DNA replication fork in vitro.
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