ArticleProceedings of the National Academy of Sciences of the United States of America2002
Directed evolution of novel polymerase activities: mutation of a DNA polymerase into an efficient RNA polymerase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 151 citations in OpenAlex.
- Rapid evolution of a highly efficient RNA polymerase by homologous recombination.Nature chemical biology · 2026Article
- Live culture-based qPCR screening of Taq DNA polymerase variants for resistance to PCR inhibitors.Frontiers in bioengineering and biotechnology · 2025Article
- Application of Deep Sequencing in Phage Display.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Modified Nucleotides for Chemical and Enzymatic Synthesis of Therapeutic RNA.Current medicinal chemistry · 2023Article
- From polymerase engineering to semi-synthetic life: artificial expansion of the central dogma.RSC chemical biology · 2022Review
- Structural Analysis of Monomeric RNA-Dependent Polymerases Revisited.Journal of molecular evolution · 2022Article
- Temperature effect on polymerase fidelity.The Journal of biological chemistry · 2021Article
- "NAD-display": Ultrahigh-Throughput in Vitro Screening of NAD(H) Dehydrogenases Using Bead Display and Flow Cytometry.Angewandte Chemie (International ed. in English) · 2021Article
- New Trends in Bioremediation Technologies Toward Environment-Friendly Society: A Mini-Review.Frontiers in bioengineering and biotechnology · 2021Review
- Modified nucleoside triphosphates in bacterial research forRSC chemical biology · 2020Article
- Review
- DNA Polymerase Activity Assay Using Near-infrared Fluorescent Labeled DNA Visualized by Acrylamide Gel Electrophoresis.Journal of visualized experiments : JoVE · 2017Article
- Engineering human PrimPol into an efficient RNA-dependent-DNA primase/polymerase.Nucleic acids research · 2017Article
- Selection platforms for directed evolution in synthetic biology.Biochemical Society transactions · 2016Review
- Evolution of thermophilic DNA polymerases for the recognition and amplification of C2'-modified DNA.Nature chemistry · 2016Article
- Modified Nucleoside Triphosphates for In-vitro Selection Techniques.Frontiers in chemistry · 2016Review
- Directed polymerase evolution.FEBS letters · 2014Review
- DNA polymerases engineered by directed evolution to incorporate non-standard nucleotides.Frontiers in microbiology · 2014Review
- Phage display--a powerful technique for immunotherapy: 2. Vaccine delivery.Human vaccines & immunotherapeutics · 2012Review
- Critical amino acids in Escherichia coli UmuC responsible for sugar discrimination and base-substitution fidelity.Nucleic acids research · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The creation of novel enzymatic function is of great interest, but remains a challenge because of the large sequence space of proteins. We have developed an activity-based selection method to evolve DNA polymerases with RNA polymerase activity. The Stoffel fragment (SF) of Thermus aquaticus DNA polymerase I is displayed on a filamentous phage by fusing it to a pIII coat protein, and the substrate DNA template/primer duplexes are attached to other adjacent pIII coat proteins. Phage particles displaying SF polymerases, which are able to extend the attached oligonucleotide primer by incorporating ribonucleoside triphosphates and biotinylated UTP, are immobilized to streptavidin-coated magnetic beads and subsequently recovered. After four rounds of screening an SF library, three SF mutants were isolated and shown to incorporate ribonucleoside triphosphates virtually as efficiently as the wild-type enzyme incorporates dNTP substrates.
Indexed as
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.