ArticleBiomolecules2019
The Role of a Key Amino Acid Position in Species-Specific Proteinaceous dUTPase Inhibition.
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
The trial behind it
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Full-length inhibitor protein is the most effective to perturb human dUTPase activity.Scientific reports · 2025Article
- The homodimerization domain of the Stl repressor is crucial for efficient inhibition of mycobacterial dUTPase.Scientific reports · 2024Article
- Practical courses on advanced methods in macromolecular crystallization: 20 years of history and future perspectives.Journal of applied crystallography · 2024Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein inhibitors of key DNA repair enzymes play an important role in deciphering physiological pathways responsible for genome integrity, and may also be exploited in biomedical research. The staphylococcal repressor StlSaPIbov1 protein was described to be an efficient inhibitor of dUTPase homologues showing a certain degree of species-specificity. In order to provide insight into the inhibition mechanism, in the present study we investigated the interaction of StlSaPIbov1 and
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Registered trials
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