207 related articles for article (PubMed ID: 17126800)
1. Steady-state kinetic behaviour of two- or n-enzyme systems made of free sequential enzymes involved in a metabolic pathway.
Legent G; Thellier M; Norris V; Ripoll C
C R Biol; 2006 Dec; 329(12):963-6. PubMed ID: 17126800
[TBL] [Abstract][Full Text] [Related]
2. Sigmoidal substrate saturation curves in Michaelis-Menten mechanism as an artefact.
Fischer E; Keleti T
Acta Biochim Biophys Acad Sci Hung; 1975; 10(3):221-7. PubMed ID: 1211106
[TBL] [Abstract][Full Text] [Related]
3. Steady-state kinetic behaviour of functioning-dependent structures.
Thellier M; Legent G; Amar P; Norris V; Ripoll C
FEBS J; 2006 Sep; 273(18):4287-99. PubMed ID: 16939622
[TBL] [Abstract][Full Text] [Related]
4. Role of conformational dynamics in kinetics of an enzymatic cycle in a nonequilibrium steady state.
Min W; Xie XS; Bagchi B
J Chem Phys; 2009 Aug; 131(6):065104. PubMed ID: 19691414
[TBL] [Abstract][Full Text] [Related]
5. Modeling networks of coupled enzymatic reactions using the total quasi-steady state approximation.
Ciliberto A; Capuani F; Tyson JJ
PLoS Comput Biol; 2007 Mar; 3(3):e45. PubMed ID: 17367203
[TBL] [Abstract][Full Text] [Related]
6. Sequential activation of metabolic pathways: a dynamic optimization approach.
Oyarzún DA; Ingalls BP; Middleton RH; Kalamatianos D
Bull Math Biol; 2009 Nov; 71(8):1851-72. PubMed ID: 19412635
[TBL] [Abstract][Full Text] [Related]
7. Concentration profiles near an activated enzyme.
Park S; Agmon N
J Phys Chem B; 2008 Sep; 112(38):12104-14. PubMed ID: 18759406
[TBL] [Abstract][Full Text] [Related]
8. Chemical mechanism of a cysteine protease, cathepsin C, as revealed by integration of both steady-state and pre-steady-state solvent kinetic isotope effects.
Schneck JL; Villa JP; McDevitt P; McQueney MS; Thrall SH; Meek TD
Biochemistry; 2008 Aug; 47(33):8697-710. PubMed ID: 18656960
[TBL] [Abstract][Full Text] [Related]
9. Michaelis-Menten kinetics at high enzyme concentrations.
Tzafriri AR
Bull Math Biol; 2003 Nov; 65(6):1111-29. PubMed ID: 14607291
[TBL] [Abstract][Full Text] [Related]
10. Kinetic analysis of the transient phase and steady state of open multicyclic enzyme cascades.
Varón R; Havsteen BH; Valero E; Molina-Alarcón M; García-Cánovas F; García-Moreno M
Acta Biochim Pol; 2005; 52(4):765-80. PubMed ID: 16086076
[TBL] [Abstract][Full Text] [Related]
11. Quasi-steady-state laws in enzyme kinetics.
Li B; Shen Y; Li B
J Phys Chem A; 2008 Mar; 112(11):2311-21. PubMed ID: 18303867
[TBL] [Abstract][Full Text] [Related]
12. Ultrasensitivity in (supra)molecularly organized and crowded environments.
Aon MA; Gomez-Casati DF; Iglesias AA; Cortassa S
Cell Biol Int; 2001; 25(11):1091-9. PubMed ID: 11913953
[TBL] [Abstract][Full Text] [Related]
13. [Kinetics of poly-enzyme system reactions. II. Nonsteady-state kinetics. Presteady-state and relation modes in a bi-enzyme system and linear sequences].
Varfolomeev SD
Mol Biol (Mosk); 1977; 11(4):790-800. PubMed ID: 618322
[TBL] [Abstract][Full Text] [Related]
14. Accelerated stochastic simulation of the stiff enzyme-substrate reaction.
Cao Y; Gillespie DT; Petzold LR
J Chem Phys; 2005 Oct; 123(14):144917. PubMed ID: 16238434
[TBL] [Abstract][Full Text] [Related]
15. Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant.
Rami Tzafriri A; Edelman ER
J Theor Biol; 2007 Apr; 245(4):737-48. PubMed ID: 17234216
[TBL] [Abstract][Full Text] [Related]
16. Enzymes are open systems.
Zahradník FJ
IUBMB Life; 2000 Apr; 49(4):255-7. PubMed ID: 10995025
[TBL] [Abstract][Full Text] [Related]
17. Control analysis of unbranched enzymatic chains in states of maximal activity.
Heinrich R; Klipp E
J Theor Biol; 1996 Oct; 182(3):243-52. PubMed ID: 8944155
[TBL] [Abstract][Full Text] [Related]
18. [Can parameters of amperometric single-enzyme sensors be assessed using the concentration dependence of their response?].
Sorochinskiĭ VV; Kurganov BI
Prikl Biokhim Mikrobiol; 1995; 31(1):27-35. PubMed ID: 7740024
[TBL] [Abstract][Full Text] [Related]
19. The total quasi-steady-state approximation for fully competitive enzyme reactions.
Pedersena MG; Bersani AM; Bersani E
Bull Math Biol; 2007 Jan; 69(1):433-57. PubMed ID: 16850351
[TBL] [Abstract][Full Text] [Related]
20. A novel method for determining kinetic parameters of dissociating enzyme systems.
Wang ZX
Anal Biochem; 1998 Nov; 264(1):8-21. PubMed ID: 9784182
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]