ReviewComputational and structural biotechnology journal2025
Structure, function and evolution of the bacterial DinG-like proteins.
Review in Computational and structural biotechnology journal, 2025. 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.
- Structural and biochemical characterization of a novel DinG containing an endonuclease domain.Cellular and molecular life sciences : CMLS · 2026Article
- Phage-encoded factor stimulates DNA degradation by the Hna anti-phage defense system.Nature communications · 2026Article
- Article
- Article
- AlphaFold in protein structure and function prediction.Computational and structural biotechnology journal · 2025Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The damage-inducible G (DinG)-like proteins represent a widespread superfamily 2 (SF2) of DNA helicases, exhibiting remarkable diversity in domain architecture, substrate specificity, regulatory mechanisms, biological functions, interaction partners, and taxonomic distribution. Many characterized DinG-like proteins play critical roles in bacterial stress responses and immunity, including the SOS response, DNA repair, and phage interference. This review aims to provide a summary of bacterial DinG-like proteins, categorizing them into subgroups such as DinG, YoaA, CasDinG, CasDinG-HNH, ExoDinG, pExoDinG, EndoDinG, RadC-like DinG, sDinG, and others. This classification provides an analysis of sequence-structure-function relationships within this superfamily. Further sequence clustering revealed inter-cluster relationships and subgroup heterogeneity, suggesting potential functional divergence. Integrating sequence analysis, domain architecture, structural data, and genomic context enabled functional predictions for these DinG-like protein subgroups, shedding light on their evolutionary and biological significance.
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