Pages that link to "Item:Q2164666"
From MaRDI portal
The following pages link to On the anti-quasi-steady-state conditions of enzyme kinetics (Q2164666):
Displaying 13 items.
- A general solution for the steady-state kinetics of immobilized enzyme systems (Q790738) (← links)
- On the relationship between the Hill coefficients for steady-state and transient kinetic data: a criterion for concerted transitions in allosteric proteins (Q886767) (← links)
- On the quasi-steady-state approximation in an open Michaelis-Menten reaction mechanism (Q2130743) (← links)
- The quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kinetics (Q2197737) (← links)
- Two new regulatory properties arising from the transient phase kinetics of monocyclic enzyme cascades (Q2503686) (← links)
- (Q3789394) (← links)
- Natural parameter conditions for singular perturbations of chemical and biochemical reaction networks (Q6044243) (← links)
- The potential roles of transacylation in intracellular lipolysis and related Qssa approximations (Q6049010) (← links)
- The unreasonable effectiveness of the total quasi-steady state approximation, and its limitations (Q6130760) (← links)
- The Michaelis-Menten reaction at low substrate concentrations: pseudo-first-order kinetics and conditions for timescale separation (Q6540667) (← links)
- Rigorous estimates for the quasi-steady state approximation of the Michaelis-Menten reaction mechanism at low enzyme concentrations (Q6553019) (← links)
- In memory of Edmund John Crampin: multi-scale and multi-physics phenomena in biology (Q6632658) (← links)
- Enlightening the blind spot of the Michaelis-Menten rate law: the role of relaxation dynamics in molecular complex formation (Q6671214) (← links)