Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations

From MaRDI portal
Publication:1609384

DOI10.1016/S0895-7177(01)00156-XzbMath0994.92024OpenAlexW1980085157MaRDI QIDQ1609384

Santiago Schnell, Philip K. Maini

Publication date: 15 August 2002

Published in: Mathematical and Computer Modelling (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1016/s0895-7177(01)00156-x




Related Items (24)

New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paperOn the anti-quasi-steady-state conditions of enzyme kineticsExtension and justification of quasi-steady-state approximation for reversible bimolecular bindingSubstrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulationAlgorithmic criteria for the validity of quasi-steady state and partial equilibrium models: the Michaelis-Menten reaction mechanismThe unreasonable effectiveness of the total quasi-steady state approximation, and its limitationsUniform Asymptotic Expansions beyond the tQSSA for the Goldbeter--Koshland SwitchThe quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kineticsMichaelis-Menten equation for degradation of insoluble substrateTrend to equilibrium for a reaction-diffusion system modelling reversible enzyme reactionTheory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactionsPartial equilibrium approximations in apoptosis. I: The intracellular-signaling subsystemUnnamed ItemStochastic aspects of asymmetric autocatalysis and absolute asymmetric synthesisOn the appropriate use of asymptotic expansions in enzyme kineticsA reconstruction of object properties with significant uncertaintiesStochastic approaches for modelling in vivo reactionsA perturbation solution of Michaelis-Menten kinetics in a ``total frameworkA study case for the analysis of asymptotic expansions beyond the tQSSA for inhibitory mechanisms in enzyme kinetics.Maini's many contributions to mathematical enzyme kinetics: a reviewCharacteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kineticsA new Michaelis-Menten equation valid everywhere multi-scale dynamics prevailsSingular Perturbation Techniques and Asymptotic Expansions for Some Complex Enzyme ReactionsHunting $\varepsilon$: The Origin and Validity of Quasi-Steady-State Reductions in Enzyme Kinetics



Cites Work




This page was built for publication: Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations