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PUBMED FOR HANDHELDS

Journal Abstract Search


291 related items for PubMed ID: 6718418

  • 1. Intermolecular ligand substitution reactions.
    Jenkins WT.
    Prog Clin Biol Res; 1984; 144B():89-96. PubMed ID: 6718418
    [Abstract] [Full Text] [Related]

  • 2. [Specific ligand induced dimerization of allosteric enzymes].
    Kurganov BI.
    Mol Biol (Mosk); 1982; 16(2):424-33. PubMed ID: 7073865
    [Abstract] [Full Text] [Related]

  • 3.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 4. A theoretical model for calculation of the rate constant of enzyme-substrate complex formation. 3. Effect of intermolecular forces and diffusion motion of the enzyme molecule on the rate constant.
    Somogyi B.
    Acta Biochim Biophys Acad Sci Hung; 1974; 9(3):185-96. PubMed ID: 4419764
    [No Abstract] [Full Text] [Related]

  • 5. Synergism of substrate binding with enzymes, as observed by equilibrium isotope exchange kinetics: model patterns.
    Wedler FC.
    Physiol Chem Phys; 1978; 10(2):97-106. PubMed ID: 724812
    [Abstract] [Full Text] [Related]

  • 6. Measurement of dissociation constants of inhibitors binding to Src SH2 domain protein by non-covalent electrospray ionization mass spectrometry.
    Bligh SW, Haley T, Lowe PN.
    J Mol Recognit; 2003; 16(3):139-48. PubMed ID: 12833569
    [Abstract] [Full Text] [Related]

  • 7. Cooperativity in two-substrate reactions.
    Gol'dshtein BN, Vol'kenshtein MV.
    Mol Biol; 1972 Jan; 5(4):441-9. PubMed ID: 4670414
    [No Abstract] [Full Text] [Related]

  • 8. A graphical method for determining the number of essential sites in enzymes with multiple binding sites for a ligand.
    Wang ZX, Srivastava DK.
    Anal Biochem; 1994 Jan; 216(1):15-26. PubMed ID: 8135345
    [Abstract] [Full Text] [Related]

  • 9. Kinetic analysis of enzyme inhibition by substrate depletion.
    Cortese JD, Vidal JC.
    Acta Physiol Lat Am; 1981 Jan; 31(3):161-71. PubMed ID: 7187587
    [Abstract] [Full Text] [Related]

  • 10. [Deviations from hyperbolic kinetics in slowly dissociating allosteric enzyme systems].
    Kuranov BI, Dorozhko AI, Kagan ZS, Iakovlev VA.
    Biokhimiia; 1975 Jan; 40(4):793-801. PubMed ID: 1203389
    [Abstract] [Full Text] [Related]

  • 11. A theoretical model for calculation of the rate constant of enzyme-substrate complex formation. I. Calculation of rate constant in the case of motionless enzyme molecule without nonspecific intermolecular forces.
    Somogyi B, Damjanovich S.
    Acta Biochim Biophys Acad Sci Hung; 1973 Jan; 8(3):153-60. PubMed ID: 4784598
    [No Abstract] [Full Text] [Related]

  • 12. A theoretical model for calculation of the rate constant of enzyme-substrate complex formation. II. Effect of intermolecular forces on the parameters describing the translational diffusion motion of a particle.
    Somogyi B.
    Acta Biochim Biophys Acad Sci Hung; 1974 Jan; 9(3):175-84. PubMed ID: 4419763
    [No Abstract] [Full Text] [Related]

  • 13. Mechanisms of stabilization of the insulin hexamer through allosteric ligand interactions.
    Rahuel-Clermont S, French CA, Kaarsholm NC, Dunn MF, Chou CI.
    Biochemistry; 1997 May 13; 36(19):5837-45. PubMed ID: 9153424
    [Abstract] [Full Text] [Related]

  • 14. Allosteric regulation of biosynthetic threonine deaminase from Escherichia coli: effects of isoleucine and valine on active-site ligand binding and catalysis.
    Eisenstein E.
    Arch Biochem Biophys; 1995 Jan 10; 316(1):311-8. PubMed ID: 7840631
    [Abstract] [Full Text] [Related]

  • 15. Kinetic analysis of the generalized Monod-Wyman-Changeux model.
    Kurganov BI.
    Mol Biol; 1974 Sep 10; 8(2):193-9. PubMed ID: 4431416
    [No Abstract] [Full Text] [Related]

  • 16. [Kinetic behavior of slowly equilibrating association-dissociation enzyme systems].
    Kurganov BI, Dorozhko AI, Kagan ZS, Iakovlev VA.
    Mol Biol (Mosk); 1975 Sep 10; 9(4):533-42. PubMed ID: 1214796
    [Abstract] [Full Text] [Related]

  • 17. [Enzyme inactivation in the reaction process. Regulatory role].
    Varfolomeev SD.
    Biokhimiia; 1984 May 10; 49(5):723-35. PubMed ID: 6743701
    [Abstract] [Full Text] [Related]

  • 18. Towards the mechanism of trimeric purine nucleoside phosphorylases: stopped-flow studies of binding of multisubstrate analogue inhibitor - 2-amino-9-[2-(phosphonomethoxy)ethyl]-6-sulfanylpurine.
    Wielgus-Kutrowska B, Antosiewicz JM, Długosz M, Holý A, Bzowska A.
    Biophys Chem; 2007 Feb 10; 125(2-3):260-8. PubMed ID: 16989940
    [Abstract] [Full Text] [Related]

  • 19. [Relationship between the apparent order of substrate binding to an enzyme and the nature of the reaction between their active centers].
    Iashina LN, Malygin EG, Zinov'ev VV.
    Mol Biol (Mosk); 1980 Feb 10; 14(6):1396-405. PubMed ID: 7442676
    [Abstract] [Full Text] [Related]

  • 20. Ligand dissociation constants from competition binding assays: errors associated with ligand depletion.
    Goldstein A, Barrett RW.
    Mol Pharmacol; 1987 Jun 10; 31(6):603-9. PubMed ID: 3600604
    [Abstract] [Full Text] [Related]


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