ArticlePLoS computational biology2012
Protein scaffolds can enhance the bistability of multisite phosphorylation systems.
Article in PLoS computational biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 29 citations in OpenAlex.
- Understand the Functions of Scaffold Proteins in Cell Signaling by a Mesoscopic Simulation Method.Biophysical journal · 2020Article
- Exploring cyclic networks of multisite modification reveals origins of information processing characteristics.Scientific reports · 2020Article
- Exploring the intrinsic behaviour of multisite phosphorylation systems as part of signalling pathways.Journal of the Royal Society, Interface · 2018Article
- Enzyme sequestration by the substrate: An analysis in the deterministic and stochastic domains.PLoS computational biology · 2018Article
- Dynamics of Posttranslational Modification Systems: Recent Progress and Future Directions.Biophysical journal · 2018Review
- The effect of site-to-site variability in ultrasensitive dose responses.Journal of mathematical biology · 2017Article
- Core signalling motif displaying multistability through multi-state enzymes.Journal of the Royal Society, Interface · 2016Article
- A Hierarchical Mechanism of RIG-I Ubiquitination Provides Sensitivity, Robustness and Synergy in Antiviral Immune Responses.Scientific reports · 2016Article
- Lyapunov Functions, Stationary Distributions, and Non-equilibrium Potential for Reaction Networks.Bulletin of mathematical biology · 2015Article
- Clinical Significance of SASH1 Expression in Glioma.Disease markers · 2015Article
- Ultrasensitivity in independent multisite systems.Journal of mathematical biology · 2014Article
- Compact modeling of allosteric multisite proteins: application to a cell size checkpoint.PLoS computational biology · 2014Article
- Modeling CaMKII in cardiac physiology: from molecule to tissue.Frontiers in pharmacology · 2014Review
- Article
- Simplifying biochemical models with intermediate species.Journal of the Royal Society, Interface · 2013Article
- Building synthetic memory.Current biology : CB · 2013Review
- Ultrasensitivity in phosphorylation-dephosphorylation cycles with little substrate.PLoS computational biology · 2013Article
- Mass spectrometric analysis of mono- and multi-phosphopeptides by selective binding with NiZnFe₂O₄ magnetic nanoparticles.Nature communications · 2013Article
- How scaffolds shape MAPK signaling: what we know and opportunities for systems approaches.Frontiers in physiology · 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 3 institutions in 1 country.
Funding
Abstract
The phosphorylation of a substrate at multiple sites is a common protein modification that can give rise to important structural and electrostatic changes. Scaffold proteins can enhance protein phosphorylation by facilitating an interaction between a protein kinase enzyme and its target substrate. In this work we consider a simple mathematical model of a scaffold protein and show that under specific conditions, the presence of the scaffold can substantially raise the likelihood that the resulting system will exhibit bistable behavior. This phenomenon is especially pronounced when the enzymatic reactions have sufficiently large K(M), compared to the concentration of the target substrate. We also find for a closely related model that bistable systems tend to have a specific kinetic conformation. Using deficiency theory and other methods, we provide a number of necessary conditions for bistability, such as the presence of multiple phosphorylation sites and the dependence of the scaffold binding/unbinding rates on the number of phosphorylated sites.
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.