Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution

DOI10.1007/S10910-007-9248-4MaRDI QIDQ551897zbMATH OpenOpenAlexFDO

Authors Morten Gram Pedersen, Alberto Bersani, Enrico Bersani

Publication date 21 July 2011

Published in Journal of Mathematical Chemistry (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1007/s10910-007-9248-4

zbMATH Keywords

Michaelis-Menten kineticsdouble phosphorylationenzyme signaling networksMAPK cascadequasi steady-state assumption

Mathematics Subject Classification ID

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

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• The total quasi-steady-state approximation for complex enzyme reactions
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• The total quasi-steady-state approximation is valid for reversible enzyme kinetics

Cites work

• Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios
• Extending the quasi-steady state approximation by changing variables
• Michaelis-Menten kinetics at high enzyme concentrations
• The Quasi-Steady-State Assumption: A Case Study in Perturbation
• Time-dependent closed form solutions for fully competitive enzyme reactions

Cited in

(24)

• Deterministic and stochastic models of enzymatic networks-applications to pharmaceutical research
• Long-term behaviours of autocatalytic sets
• A study case for the analysis of asymptotic expansions beyond the tQSSA for inhibitory mechanisms in enzyme kinetics.
• A new Michaelis-Menten equation valid everywhere multi-scale dynamics prevails
• The total quasi-steady-state approximation for complex enzyme reactions
• Modeling the action of drugs on cellular enzymes by means of optimal control techniques
• Quasi steady state and partial equilibrium approximations: their relation and their validity
• On the qualitative behaviour of oscillating biochemical systems: the stochastic approach
• Uniform asymptotic expansions beyond the tQSSA for the Goldbeter-Koshland switch
• The total quasi-steady-state approximation for fully competitive enzyme reactions
• Reduced models of networks of coupled enzymatic reactions
• Is there anything left to say on enzyme kinetic constants and quasi-steady state approximation?
• Approximation of enzyme kinetics for high enzyme concentration by a first order perturbation approach
• Singular perturbation techniques and asymptotic expansions for some complex enzyme reactions
• Balanced truncation for model reduction of biological oscillators
• Partial equilibrium approximations in apoptosis. I: The intracellular-signaling subsystem
• Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity
• A perturbation solution of Michaelis-Menten kinetics in a ``total framework
• New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper
• Approximations and their consequences for dynamic modelling of signal transduction pathways
• Effects of quasi-steady-state reduction on biophysical models with oscillations
• Asymptotic analysis of a target-mediated drug disposition model: algorithmic and traditional approaches
• Algorithmic criteria for the validity of quasi-steady state and partial equilibrium models: the Michaelis-Menten reaction mechanism
• No-oscillation theorem for the transient dynamics of the linear signal transduction pathway and beyond

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