ArticleProtein and peptide letters2024
Characterization of Heat-labile Uracil-DNA Glycosylase from
Article in Protein and peptide letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed, 1 citations in OpenAlex.
- Noncatalytic surface electrostatic networks tune thermolability in uracil-DNA glycosylase.The Journal of biological chemistry · 2026Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundHeat-labile uracil-DNA glycosylase (HL-UDG) is commonly employed to eliminate carry-over contamination in DNA amplifications. However, the prevailing HL-UDG is markedly inactivated at 50°C, rendering it unsuitable for specific one-step RT-qPCR protocols utilizing reverse transcriptase at an optimal temperature of 42°C.
objectiveThis study aimed to explore novel HL-UDG with lower inactivation temperature and for recombinant expression.
methodsThe gene encoding an HL-UDG was cloned from the cold-water fish rainbow trout
resultsThis recombinantly expressed truncated HL-UDG of rainbow trout (OmUDG) exhibited high amino acids similarity (84.1% identity) to recombinant Atlantic cod UDG (rcUDG) and was easily denatured at 40°C. The optimal pH of OmUDG was 8.0, and the optimal concentrations of both Na
conclusionWe successfully identified and recombinantly expressed a novel HL-UDG with an inactivation temperature of 40°C. It is suitable for eliminating carry-over contamination in one-step RT-qPCR.
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Registered trials
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