ArticleScientific reports2017
Structural and functional characterization of deep-sea thermophilic bacteriophage GVE2 HNH endonuclease.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 60 citations in OpenAlex.
- A novel temperate phage fromMicrobiology spectrum · 2026Article
- Functional Evaluation of a Conserved HNH Endonuclease Gene in Lactococcal Skunavirus Genomes.Microbial biotechnology · 2026Article
- Novel Koutsourovirus phages disrupt clinical multidrug-resistant Enterobacter cloacae biofilms: genomic and functional characterization.Folia microbiologica · 2026Article
- Bacteriophage deploys a RecA-dependent nuclease to inhibit Staphylococcus aureus replication and promote phage propagation.Nucleic acids research · 2026Article
- Genomic landscape of completeFrontiers in microbiology · 2026Article
- Diversity and functional characterization of HNH endonucleases encoded by lactococcalMicrobial genomics · 2025Article
- Learning Universal Representations of Intermolecular Interactions with ATOMICA.bioRxiv : the preprint server for biology · 2025Article
- Genomic and Functional Characterization of Novel Phages Targeting Multidrug-ResistantInternational journal of molecular sciences · 2025Article
- Whole-Genome Shotgun Sequencing from Chicken Clinical Tracheal Samples for Bacterial and Novel Bacteriophage Identification.Veterinary sciences · 2025Article
- Structural basis for RNA-guided DNA degradation by Cas5-HNH/Cascade complex.Nature communications · 2025Article
- An Actively Homing Insertion Element in a Phage Methylase Contains a Hidden HNH Endonuclease.Genes · 2025Article
- Deciphering the Genetic Architecture ofViruses · 2024Article
- Structural basis for the type I-F Cas8-HNH system.The EMBO journal · 2024Article
- Isolation and Characterization of Two Novel Genera of Jumbo Bacteriophages InfectingAntibiotics (Basel, Switzerland) · 2024Article
- Biological Characterization and Genomic Analysis of Three NovelInternational journal of molecular sciences · 2024Article
- The Expanding Diversity of Viruses from Extreme Environments.International journal of molecular sciences · 2024Review
- Identification and genomic analysis of temperateMicrobiology spectrum · 2023Article
- Article
- Characteristics and Whole-Genome Analysis ofFoods (Basel, Switzerland) · 2023Article
- Enrichment Culture but Not Metagenomic Sequencing Identified a Highly Prevalent Phage InfectingMicrobiology spectrum · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HNH endonucleases in bacteriophages play a variety of roles in the phage lifecycle as key components of phage DNA packaging machines. The deep-sea thermophilic bacteriophage Geobacillus virus E2 (GVE2) encodes an HNH endonuclease (GVE2 HNHE). Here, the crystal structure of GVE2 HNHE is reported. This is the first structural study of a thermostable HNH endonuclease from a thermophilic bacteriophage. Structural comparison reveals that GVE2 HNHE possesses a typical ββα-metal fold and Zn-finger motif similar to those of HNH endonucleases from other bacteriophages, apart from containing an extra α-helix, suggesting conservation of these enzymes among bacteriophages. Biochemical analysis suggests that the alanine substitutions of the conserved residues (H93, N109 and H118) in the HNH motif of GVE2 HNHE abolished 94%, 60% and 83% of nicking activity, respectively. Compared to the wild type enzyme, the H93A mutant displayed almost the same conformation while the N108A and H118A mutants had different conformations. In addition, the wild type enzyme was more thermostable than the mutants. In the presence of Mn
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.