ArticleOrganic & biomolecular chemistry2017
Structure-activity relationships of the ATP cofactor in ligase-catalysed oligonucleotide polymerisations.
Article in Organic & biomolecular chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
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.
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Who cites it
3 citing papers in PubMed, 13 citations in OpenAlex.
- Template-dependent DNA ligation for the synthesis of modified oligonucleotides.Nature communications · 2024Article
- Rapid genome-wide profiling of DNA methylation and genetic variation using guide positioning sequencing (GPS).Frontiers in cell and developmental biology · 2024Article
- Efficiency and fidelity of T3 DNA ligase in ligase-catalysed oligonucleotide polymerisations.Organic & biomolecular chemistry · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A T4 DNA ligase-catalysed oligonucleotide polymerisation process has been recently developed to enable the incorporation of multiple functional groups throughout a nucleic acid polymer. T4 DNA ligase requires ATP as a cofactor to catalyse phosphodiester bond formation during the polymerisation process. Herein, we describe the structure-activity relationship of ATP within the context of T4 DNA ligase-catalyzed oligonucleotide polymerisation. Using high-throughput sequencing, we study not only the influence of ATP modification on polymerisation efficiency, but also on the fidelity and sequence bias of the polymerisation process.
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Registered trials
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