ArticleACS infectious diseases2019
Ligand-Efficient Inhibitors of Trichomonas vaginalis Adenosine/Guanosine Preferring Nucleoside Ribohydrolase.
Article in ACS infectious diseases, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- Direct Measurement of Nucleoside Ribohydrolase Enzyme Activities inAnalytical chemistry · 2023Article
- Structure-Guided Insight into the Specificity and Mechanism of a Parasitic Nucleoside Hydrolase.Biochemistry · 2022Article
- Structure, Oligomerization and Activity Modulation in N-Ribohydrolases.International journal of molecular sciences · 2022Review
- Clinical Effect of Metronidazole Vaginal Effervescent Tablet Combined with Flavescentis Sophora Suppository in the Treatment of Trichomonas Vaginitis.Contrast media & molecular imaging · 2022Article
- Fluorine NMR functional screening: from purified enzymes to human intact living cells.Journal of biomolecular NMR · 2020Article
- Discovery of Ligand-Efficient Scaffolds for the Design of NovelACS omega · 2019Article
- NMR-Based Activity Assays for Determining Compound Inhibition, IC50 Values, Artifactual Activity, and Whole-Cell Activity of Nucleoside Ribohydrolases.Journal of visualized experiments : JoVE · 2019Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Trichomoniasis is caused by the parasitic protozoan Trichomonas vaginalis and is the most prevalent, nonviral sexually transmitted disease. The parasite has shown increasing resistance to the current 5-nitroimidazole therapies indicating the need for new therapies with different mechanisms. T. vaginalis is an obligate parasite that scavenges nucleosides from host cells and then uses salvage pathway enzymes to obtain the nucleobases. The adenosine/guanosine preferring nucleoside ribohydrolase was screened against a 2000-compound diversity fragment library using a
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Registered trials
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