Pages that link to "Item:Q1609384"
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The following pages link to Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations (Q1609384):
Displayed 11 items.
- On the appropriate use of asymptotic expansions in enzyme kinetics (Q500685) (← links)
- A perturbation solution of Michaelis-Menten kinetics in a ``total'' framework (Q714677) (← links)
- Extension and justification of quasi-steady-state approximation for reversible bimolecular binding (Q887141) (← links)
- Michaelis-Menten equation for degradation of insoluble substrate (Q1698530) (← links)
- Trend to equilibrium for a reaction-diffusion system modelling reversible enzyme reaction (Q1706280) (← links)
- Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions (Q1708501) (← links)
- Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation (Q1936971) (← links)
- Stochastic aspects of asymmetric autocatalysis and absolute asymmetric synthesis (Q1959313) (← links)
- Partial equilibrium approximations in apoptosis. I: The intracellular-signaling subsystem (Q2439162) (← links)
- Stochastic approaches for modelling in vivo reactions (Q2490589) (← links)
- New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper (Q2629039) (← links)