Pages that link to "Item:Q2517609"

The following pages link to Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond (Q2517609):

Displaying 27 items.

• Applying structural transition theory to describe enzyme kinetics in heterogeneous systems (Q460904) (← links)
• Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution (Q551897) (← links)
• Enzyme kinetics with a twist (Q652718) (← links)
• Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios (Q751534) (← links)
• A general solution for the steady-state kinetics of immobilized enzyme systems (Q790738) (← links)
• The kinetic effect of the inactivation of the enzyme--substrate complex in an enzymatic reaction with slow-binding inhibition (Q814739) (← links)
• Effects of periodic input on the quasi-steady state assumptions for enzyme-catalysed reactions (Q814942) (← 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)
• The total quasi-steady-state approximation for complex enzyme reactions (Q1010015) (← links)
• On the validity of the steady state assumption of enzyme kinetics (Q1108228) (← links)
• Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations (Q1609384) (← links)
• Michaelis-Menten equation for degradation of insoluble substrate (Q1698530) (← links)
• Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions (Q1708501) (← links)
• Mechanism equivalence in enzyme-substrate reactions: Distributed differential delay in enzyme kinetics (Q1878862) (← links)
• Quasi-steady state assumptions for non-isolated enzyme-catalysed reactions (Q1879029) (← links)
• Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation (Q1936971) (← links)
• Stochastic enzyme kinetics and the quasi-steady-state reductions: application of the slow scale linear noise approximation à la Fenichel (Q2153739) (← links)
• The total quasi-steady-state approximation is valid for reversible enzyme kinetics (Q2187480) (← links)
• The quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kinetics (Q2197737) (← links)
• Efficacy of quasi-steady-state approximation in Michaelis-Menten kinetics: a stochastic signature (Q2322238) (← links)
• Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics (Q2328227) (← links)
• Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity (Q2340012) (← links)
• Quasi-steady-state approximations derived from the stochastic model of enzyme kinetics (Q2417511) (← links)
• Seven competing ways to recover the Michaelis-Menten equation reveal the alternative approaches to steady state modeling (Q2443867) (← links)
• Why substrate depletion has apparent first-order kinetics in enzymatic digestion (Q2500381) (← links)
• Optimizing enzymatic catalysts for rapid turnover of substrates with low enzyme sequestration (Q2659627) (← links)
• (Q5156423) (← links)