Antagonism and bistability in protein interaction networks

DOI10.1016/J.JTBI.2007.09.001zbMath1397.92300OpenAlexW2010900077WikidataQ44933161 ScholiaQ44933161MaRDI QIDQ1788151

Mohsen Sabouri-Ghomi, Sandip Kar, Andrea Ciliberto, John J. Tyson, Bela Novak

Publication date: 8 October 2018

Published in: Journal of Theoretical Biology (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1016/j.jtbi.2007.09.001

zbMATH Keywords

stochastic simulationcell cycle controlMichaelis-Menten rate law

Mathematics Subject Classification ID

Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45) Systems biology, networks (92C42)

Related Items (10)

New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper ⋮ Network resilience ⋮ Test Models for Statistical Inference: Two-Dimensional Reaction Systems Displaying Limit Cycle Bifurcations and Bistability ⋮ Efficient modelling of yeast cell cycles based on multisite phosphorylation using coloured hybrid Petri nets with marking-dependent arc weights ⋮ Uniform Asymptotic Expansions beyond the tQSSA for the Goldbeter--Koshland Switch ⋮ Revisiting a skeleton model for the mammalian cell cycle: from bistability to Cdk oscillations and cellular heterogeneity ⋮ Modeling the dynamic behavior of biochemical regulatory networks ⋮ A study case for the analysis of asymptotic expansions beyond the tQSSA for inhibitory mechanisms in enzyme kinetics. ⋮ Stochastic Petri net extension of a yeast cell cycle model ⋮ Singular Perturbation Techniques and Asymptotic Expansions for Some Complex Enzyme Reactions

Cites Work

• Extending the quasi-steady state approximation by changing variables
• A model for restriction point control of the mammalian cell cycle
• The total quasi-steady-state approximation is valid for reversible enzyme kinetics
• The total quasi-steady-state approximation for fully competitive enzyme reactions
• Mathematical model of the cell division cycle of fission yeast
• Understanding bistability in complex enzyme-driven reaction networks

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