Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution
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Publication:551897
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
Michaelis-Menten kinetics; double phosphorylation; enzyme signaling networks; MAPK cascade; quasi steady-state assumption
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