ArticleScience advances2022
Single-molecule Taq DNA polymerase dynamics.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Recombinant Thermostable DNA Polymerases: Current Approaches to Production, Molecular Engineering, and Applications in Biotechnology and Diagnostics.International journal of molecular sciences · 2026Review
- A novel engineered vector for TA cloning of PCR products.Journal of applied genetics · 2026Article
- Molecular adaptations and engineering of extremophiles for synthetic biology and biotechnological applications.Frontiers in microbiology · 2026Review
- Decoding information stored in DNAs through single-molecule electrical detection platforms.Innovation (Cambridge (Mass.)) · 2025Review
- Dynamics and thermal stability of the bypass polymerase, DinB homolog (Dbh).Frontiers in molecular biosciences · 2024Article
- Substrate-independent activation pathways of the CRISPR-Cas9 HNH nuclease.Biophysical journal · 2023Article
- Review
- Structural and Molecular Kinetic Features of Activities of DNA Polymerases.International journal of molecular sciences · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors.
Funding
Abstract
Taq DNA polymerase functions at elevated temperatures with fast conformational dynamics-regimes previously inaccessible to mechanistic, single-molecule studies. Here, single-walled carbon nanotube transistors recorded the motions of Taq molecules processing matched or mismatched template-deoxynucleotide triphosphate pairs from 22° to 85°C. By using four enzyme orientations, the whole-enzyme closures of nucleotide incorporations were distinguished from more rapid, 20-μs closures of Taq's fingers domain testing complementarity and orientation. On average, one transient closure was observed for every nucleotide binding event; even complementary substrate pairs averaged five transient closures between each catalytic incorporation at 72°C. The rate and duration of the transient closures and the catalytic events had almost no temperature dependence, leaving all of Taq's temperature sensitivity to its rate-determining open state.
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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.