ReviewRSC advances2018
Nucleobase deaminases: a potential enzyme system for new therapies.
Review in RSC advances, 2018. 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
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
5 citing papers in PubMed, 15 citations in OpenAlex.
- Applications of catalytic systems containing DNA nucleobases (adenine, cytosine, guanine, and thymine) in organic reactions.RSC advances · 2025Review
- Hydrolysis of Acetamide on Low-Index CeOACS catalysis · 2022Article
- Real-Time Monitoring of Human Guanine Deaminase Activity by an Emissive Guanine Analog.ACS chemical biology · 2021Article
- Discovery of Bacterial Deaminases That Convert 5-Fluoroisocytosine Into 5-Fluorouracil.Frontiers in microbiology · 2018Article
- Modern Approaches to the Genome Editing of Antibiotic Biosynthetic Clusters in Actinomycetes.Acta naturaeArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleobase deaminases are essential enzymes that are involved in the catabolic pathway and stringently regulate the concentration of the nucleobase derivative pool, which is paramount for nucleotide recycling. This review presents an overview of the structure, function and mechanism of CDA deaminases and their potential as enzyme systems for the development of new antimicrobial therapies. The evolutionary divergence of human nucleobase deaminases with respect to bacterial enzymes has been used as a central theme towards the development of strategies for potential drug targets. Especially, differences in their tertiary fold, active site architectures and mechanisms of regulation have been highlighted in this study. Overall, deaminases present a unique opportunity as drug targets because of their functional plasticity and fidelity.
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.