Pages that link to "Item:Q1609384"

The following pages link to Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations (Q1609384):

Displaying 50 items.

• Is there anything left to say on enzyme kinetic constants and quasi-steady state approximation? (Q431971) (← links)
• A note on the kinetics of suicide substrates (Q454298) (← links)
• On the appropriate use of asymptotic expansions in enzyme kinetics (Q500685) (← links)
• An approximate solution for the transient kinetic behavior of enzyme- catalyzed reactions: The irreversible Michaelis-Menten kinetics (Q580222) (← links)
• Enzyme kinetics with a twist (Q652718) (← links)
• A perturbation solution of Michaelis-Menten kinetics in a ``total'' framework (Q714677) (← links)
• Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios (Q751534) (← links)
• Reduction of intrinsic kinetic and thermodynamic barriers for enzyme-catalysed proton transfers from carbon acid substrates (Q781272) (← links)
• 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)
• Time-dependent closed form solutions for fully competitive enzyme reactions (Q886771) (← links)
• Enzyme kinetics at high enzyme concentration (Q886790) (← links)
• Extension and justification of quasi-steady-state approximation for reversible bimolecular binding (Q887141) (← links)
• The total quasi-steady-state approximation for complex enzyme reactions (Q1010015) (← links)
• Chemical chaos in enzyme kinetics (Q1041848) (← links)
• On the validity of the steady state assumption of enzyme kinetics (Q1108228) (← links)
• How to derive flux control coefficients from the rate equations of classical enzyme kinetics (Q1126367) (← 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)
• Determination of kinetic parameters of enzyme-catalyzed reactions with a minimum number of velocity measurements (Q1797422) (← links)
• Mechanism equivalence in enzyme-substrate reactions: Distributed differential delay in enzyme kinetics (Q1878862) (← 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)
• Stochastic enzyme kinetics and the quasi-steady-state reductions: application of the slow scale linear noise approximation à la Fenichel (Q2153739) (← links)
• On the anti-quasi-steady-state conditions of enzyme kinetics (Q2164666) (← links)
• The total quasi-steady-state approximation is valid for reversible enzyme kinetics (Q2187480) (← links)
• Using singular perturbation theory to determine kinetic parameters in a non-standard coupled enzyme assay (Q2192670) (← links)
• The quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kinetics (Q2197737) (← links)
• A probabilistic approach to compact steady-state kinetic equations for enzymic reactions (Q2201930) (← links)
• A study case for the analysis of asymptotic expansions beyond the tQSSA for inhibitory mechanisms in enzyme kinetics. (Q2274586) (← links)
• Maini's many contributions to mathematical enzyme kinetics: a review (Q2328226) (← links)
• Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics (Q2328227) (← links)
• General mathematical formula for near equilibrium relaxation kinetics of basic enzyme reactions and its applications to find conformational selection steps (Q2328428) (← links)
• A new Michaelis-Menten equation valid everywhere multi-scale dynamics prevails (Q2328450) (← links)
• Partial equilibrium approximations in apoptosis. I: The intracellular-signaling subsystem (Q2439162) (← links)
• Monte Carlo simulations of enzymatic reactions in crowded media. Effect of the enzyme-obstacle relative size (Q2453777) (← links)
• Stochastic approaches for modelling in vivo reactions (Q2490589) (← links)
• Why substrate depletion has apparent first-order kinetics in enzymatic digestion (Q2500381) (← links)
• Two new regulatory properties arising from the transient phase kinetics of monocyclic enzyme cascades (Q2503686) (← links)
• Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond (Q2517609) (← links)
• New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper (Q2629039) (← links)
• Approximation of enzyme kinetics for high enzyme concentration by a first order perturbation approach (Q2636422) (← links)
• (Q3789394) (← links)
• Singular Perturbation Techniques and Asymptotic Expansions for Some Complex Enzyme Reactions (Q5013644) (← links)
• Hunting $\varepsilon$: The Origin and Validity of Quasi-Steady-State Reductions in Enzyme Kinetics (Q5023529) (← links)
• Uniform Asymptotic Expansions beyond the tQSSA for the Goldbeter--Koshland Switch (Q5110574) (← links)
• A reconstruction of object properties with significant uncertainties (Q5153260) (← links)
• Enzyme kinetics of multiple alternative substrates (Q5928777) (← links)
• An algebraic mathematical model for non-competitive enzyme inhibitors with slow and fast subsystems (Q6106839) (← links)