The total quasi-steady-state approximation is valid for reversible enzyme kinetics
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Publication:2187480
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Cites work
- Enzyme kinetics at high enzyme concentration
- Extending the quasi-steady state approximation by changing variables
- scientific article; zbMATH DE number 3222145 (Why is no real title available?)
- scientific article; zbMATH DE number 3285097 (Why is no real title available?)
- Michaelis-Menten kinetics at high enzyme concentrations
- On the Lambert \(w\) function
- On the validity of the steady state assumption of enzyme kinetics
- Simplification and Scaling
- The Quasi-Steady-State Assumption: A Case Study in Perturbation
Cited in
(38)- The total quasi-steady-state approximation for complex enzyme reactions
- An alternative approach to Michaelis-Menten kinetics that is based on the renormalization group
- Operating regimes of covalent modification cycles at high enzyme concentrations
- Antagonism and bistability in protein interaction networks
- The total quasi-steady-state for multiple alternative substrate reactions
- Heineken, Tsuchiya and Aris: ``On the mathematical status of the pseudo-steady state hypothesis. A classic from Volume 1 of \textit{Mathematical Biosciences}
- Analysis of compartmental models of ligand-induced endocytosis
- Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant
- Competitive effects in bacterial mRNA decay
- Long-term behaviours of autocatalytic sets
- Reduced models of networks of coupled enzymatic reactions
- A study case for the analysis of asymptotic expansions beyond the tQSSA for inhibitory mechanisms in enzyme kinetics.
- A population dynamics model of mosquito-borne disease transmission, focusing on mosquitoes' biased distribution and mosquito repellent use
- Efficacy of quasi-steady-state approximation in Michaelis-Menten kinetics: a stochastic signature
- Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics
- Determining ``small parameters for quasi-steady state
- The total quasi-steady-state approximation for fully competitive enzyme reactions
- A transformed time-dependent Michaelis-Menten enzymatic reaction model and its asymptotic stability
- Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond
- New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper
- Zero-order ultrasensitivity: a study of criticality and fluctuations under the total quasi-steady state approximation in the linear noise regime
- Reciprocal enzyme regulation as a source of bistability in covalent modification cycles
- scientific article; zbMATH DE number 4097169 (Why is no real title available?)
- Quasi-steady-state laws in reversible model of enzyme kinetics
- A new piecewise spectral homotopy analysisof the Michaelis-Menten enzymatic reactions model
- Mathematical modelling of metapopulation dynamics: revisiting its meaning
- Solution method for the transformed time-dependent Michaelis-Menten enzymatic reaction model
- Singular perturbation techniques and asymptotic expansions for some complex enzyme reactions
- Uniform asymptotic expansions beyond the tQSSA for the Goldbeter-Koshland switch
- Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution
- An approximate solution for the transient kinetic behavior of enzyme- catalyzed reactions: The irreversible Michaelis-Menten kinetics
- Algorithmic criteria for the validity of quasi-steady state and partial equilibrium models: the Michaelis-Menten reaction mechanism
- The unreasonable effectiveness of the total quasi-steady state approximation, and its limitations
- Asymptotic analysis of the total quasi-steady state approximation for the Michaelis-Menten enzyme kinetic reactions
- On the validity of the quasi-steady state approximation of bimolecular reactions in solution
- Extension and justification of quasi-steady-state approximation for reversible bimolecular binding
- Deterministic and stochastic models of enzymatic networks-applications to pharmaceutical research
- Approximations and their consequences for dynamic modelling of signal transduction pathways
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