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

DOI10.1007/s10910-007-9248-4zbMath1217.92052MaRDI QIDQ551897

Alberto Maria Bersani, Morten Gram Pedersen, 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 kinetics; double phosphorylation; enzyme signaling networks; MAPK cascade; quasi steady-state assumption

Mathematics Subject Classification ID

92C45: Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.)

92C42: Systems biology, networks

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Cites Work

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