Bifunctional enzyme provides absolute concentration robustness in multisite covalent modification networks
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Publication:6149820
DOI10.1007/s00285-024-02060-5arXiv2304.02679OpenAlexW4392391661MaRDI QIDQ6149820
Publication date: 5 March 2024
Published in: Journal of Mathematical Biology (Search for Journal in Brave)
Full work available at URL: https://arxiv.org/abs/2304.02679
bifunctional enzymefutile cycleabsolute concentration robustnesscovalent modification networkparadoxical enzyme
Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45) Biochemistry, molecular biology (92C40) Systems biology, networks (92C42)
Cites Work
- On the number of steady states in a multiple futile cycle
- Foundations of chemical reaction network theory
- The rational parameterisation theorem for multisite post-translational modification systems
- Network translation and steady-state properties of chemical reaction systems
- Foundations of static and dynamic absolute concentration robustness
- A global convergence result for processive multisite phosphorylation systems
- Reciprocal enzyme regulation as a source of bistability in covalent modification cycles
- Prevalence of deficiency-zero reaction networks in an Erdös–Rényi framework
- Power-Engine-Load Form for Dynamic Absolute Concentration Robustness
- Reaction Network Motifs for Static and Dynamic Absolute Concentration Robustness
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