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5. Letter: Kinetic negative co-operativity in the allosteric model of Monod, Wyman and Changeux. Goldbeter A J Mol Biol; 1974 Nov; 90(1):185-90. PubMed ID: 4453011 [No Abstract] [Full Text] [Related]
6. Apparent co-operativity for highly concentrated Michaelian and allosteric enzymes. Laurent M; Kellershohn N J Mol Biol; 1984 Apr; 174(3):543-55. PubMed ID: 6716486 [TBL] [Abstract][Full Text] [Related]
7. Kinetic co-operativity of monomeric mnemonical enzymes. The significance of the kinetic Hill coefficient. Ricard J; Noat G Eur J Biochem; 1985 Nov; 152(3):557-64. PubMed ID: 4054121 [TBL] [Abstract][Full Text] [Related]
8. Co-operativity and the methods of plotting binding and steady-state kinetic data. Whitehead EP Biochem J; 1978 May; 171(2):501-4. PubMed ID: 656060 [TBL] [Abstract][Full Text] [Related]
9. The determination of thermodynamic allosteric parameters of an enzyme undergoing steady-state turnover. Reinhart GD Arch Biochem Biophys; 1983 Jul; 224(1):389-401. PubMed ID: 6870263 [TBL] [Abstract][Full Text] [Related]
10. The determination of positive and negative co-operativity with allosteric enzymes and the interpretation of sigmoid curves and non-linear double reciprocal plots for the MWC and KNF models. Bardsley WG; Waight RD J Theor Biol; 1978 Jan; 70(2):135-56. PubMed ID: 633912 [No Abstract] [Full Text] [Related]
11. A steady-state kinetic method for the verification of the rapid-equilibrium assumption in allosteric enzymes. Symcox MM; Reinhart GD Anal Biochem; 1992 Nov; 206(2):394-9. PubMed ID: 1443611 [TBL] [Abstract][Full Text] [Related]
12. The graphical diagnosis of positive and negative co-operativity and the factorability of the allosteric-binding polynomial [proceedings]. Bardsley WG Biochem Soc Trans; 1977; 5(3):753-6. PubMed ID: 902907 [No Abstract] [Full Text] [Related]
13. Analysis of competition for substrate sites in an allosteric enzyme with co-operative kinetics. Effects of dAMP and dUMP on donkey spleen deoxycytidylate aminohydrolase. Mastrantonio S; Nucci R; Vaccaro C; Rossi M; Whitehead EP Eur J Biochem; 1983 Dec; 137(3):421-7. PubMed ID: 6662104 [TBL] [Abstract][Full Text] [Related]
14. A model for the allosteric regulation of pH-sensitive enzymes. Shindler JS; Tipton KF Biochem J; 1977 Nov; 167(2):479-82. PubMed ID: 23113 [TBL] [Abstract][Full Text] [Related]
15. [Deviations from hyperbolic kinetics in slowly dissociating allosteric enzyme systems]. Kuranov BI; Dorozhko AI; Kagan ZS; Iakovlev VA Biokhimiia; 1975; 40(4):793-801. PubMed ID: 1203389 [TBL] [Abstract][Full Text] [Related]
16. Simplifications of the derivations and forms of steady-state equations for non-equilibrium random substrate-modifier and allosteric enzyme mechanisms. Whitehead EP Biochem J; 1976 Dec; 159(3):449-56. PubMed ID: 1008809 [TBL] [Abstract][Full Text] [Related]
17. The steady-state rate equation for the general modifier mechanism of Botts and Morales when the quasi-equilibrium assumption for the binding of the modifier is made. Varón R; García-Moreno M; Garrido C; García-Cánovas F Biochem J; 1992 Dec; 288 ( Pt 3)(Pt 3):1072-3. PubMed ID: 1471980 [No Abstract] [Full Text] [Related]
18. Some equilibrium and non-equilibrium properties of the allosteric interactions in enzymes. III. Dynamics of the amino acid residues and ligand binding process. Chuknyiski P J Theor Biol; 1978 Oct; 74(3):389-95. PubMed ID: 723283 [No Abstract] [Full Text] [Related]
19. Emergence of dynamic cooperativity in the stochastic kinetics of fluctuating enzymes. Kumar A; Chatterjee S; Nandi M; Dua A J Chem Phys; 2016 Aug; 145(8):085103. PubMed ID: 27586952 [TBL] [Abstract][Full Text] [Related]
20. Isomerization of the free enzyme versus induced fit: effects of steps involving induced fit that bypass enzyme isomerization on flux ratios and countertransport. Britton HG Biochem J; 1997 Jan; 321 ( Pt 1)(Pt 1):187-99. PubMed ID: 9003418 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]