ArticleAnalytical biochemistry2023
An enzyme-coupled microplate assay for activity and inhibition of hmdUMP hydrolysis by DNPH1.
Article in Analytical biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 5 citations in OpenAlex.
- DNPH1 exerts context-dependent tumor-promoting and -repressing functions during melanoma development.The Journal of investigative dermatology · 2026Article
- Promotion of breast cancer by the DNPH1 enzyme.iScience · 2026Article
- The energy landscape of N-ribosidic bond cleavage catalysed by 2'-deoxynucleoside 5'-phosphate N-hydrolase 1.The Biochemical journal · 2025Article
- Human 2'-Deoxynucleoside 5'-PhosphateBiochemistry · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
2'-Deoxynucleoside 5'-monophosphate N-glycosidase 1 (DNPH1) hydrolyzes the epigenetically modified nucleotide 5-hydroxymethyl 2'-deoxyuridine 5'-monophosphate (hmdUMP) derived from DNA metabolism. Published assays of DNPH1 activity are low throughput, use high concentrations of DNPH1, and have not incorporated or characterized reactivity with the natural substrate. We describe the enzymatic synthesis of hmdUMP from commercially available materials and define its steady-state kinetics with DNPH1 using a sensitive, two-pathway enzyme coupled assay. This continuous absorbance-based assay works in 96-well plate format using nearly 500-fold less DNPH1 than previous methods. With a Z prime value of 0.92, the assay is suitable for high-throughput assays, screening of DNPH1 inhibitors, or characterization of other deoxynucleotide monophosphate hydrolases.
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Registered trials
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