ArticleThe European physical journal. E, Soft matter2011
Molecular level dynamics of genetic oscillator--the effect of protein-protein interaction.
Article in The European physical journal. E, Soft matter, 2011. 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
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
1 citing paper in PubMed.
- Species-specific roles of the Notch ligands, receptors, and targets orchestrating the signaling landscape of the segmentation clock.Frontiers in cell and developmental biology · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Uncovering how interactions of a set of molecular components influence the system's dynamic behavior is important for understanding intracellular processes and elucidating design principles, but unfortunately, there are limited efforts for studying this issue. Here, we study the effect of distinct post-translational dynamics controlled by protein dimerization on oscillations in the repressilator. For this, we propose three biologically motivated model scenarios of the repressilator with monomer or dimer being the active form of repressor, and with protein-protein interactions. It is found that the dimer dissociation constant can tune oscillatory regions, frequency and amplitude. Introducing a modified linear noise approximation to evaluate fluctuations of amplitude and period in the oscillatory systems, we show that different dimerization leads to a different effect on period and amplitude in reducing noise. The manipulation of the circuit's biochemical properties provides a practical strategy for designing a robust and tunable oscillator.
Indexed as
Identifiers
21822815What 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.