ArticleBiophysical chemistry2011
Kinetic mechanism of the ssDNA recognition by the polymerase X from African Swine Fever Virus. Dynamics and energetics of intermediate formations.
Article in Biophysical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- Engineering a Virus-Derived X Family DNA Polymerase FvPolX for de novo DNA Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Mechanisms of ligand binding.Biophysics reviews · 2020Review
- Identification of the viral RNA promoter stem loop A (SLA)-binding site on Zika virus polymerase NS5.Scientific reports · 2020Article
- Essential role of conformational selection in ligand binding.Biophysical chemistry · 2014Review
- How DNA polymerase X preferentially accommodates incoming dATP opposite 8-oxoguanine on the template.Biophysical journal · 2013Article
- Conformational selection is a dominant mechanism of ligand binding.Biochemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Kinetic mechanism of the ssDNA recognition by the polymerase X of African Swine Fever Virus (ASFV) and energetics of intermediate formations have been examined, using the fluorescence stopped-flow method. The association is a minimum three-step process PolX + ssDNA k(1) <-- --> k(-1) (P-ssDNA)(1) k(2) <-- --> k(-2) (P-ssDNA)(2) k(3) <-- --> k(-3) (P-ssDNA)(3). The nucleic acid makes the initial contact through the C-terminal domain, which generates most of the overall ΔG°. In the second step the nucleic acid engages the N-terminal domain, assuming the bent structure. In equilibrium, the complex exists in at least two different states. Apparent enthalpy and entropy changes, characterizing formations of intermediates, reflect association of the DNA with the C-terminal domain and gradual engagement of the catalytic domain by the nucleic acid. The intrinsic DNA-binding steps are entropy-driven processes accompanied by the net release of water molecules. The final conformational transition of the complex does not involve any large changes of the DNA topology, or the net release of the water molecules.
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.