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Journal Abstract Search

208 related items for PubMed ID: 3779009

  • 1. Cooperative free energies for nested allosteric models as applied to human hemoglobin.
    Gill SJ, Robert CH, Coletta M, Di Cera E, Brunori M.
    Biophys J; 1986 Oct; 50(4):747-52. PubMed ID: 3779009
    [Abstract] [Full Text] [Related]

  • 2. Subunit hybridization studies of partially ligated cyanomethemoglobins using a cryogenic method. Evidence for three allosteric states.
    Perrella M, Benazzi L, Shea MA, Ackers GK.
    Biophys Chem; 1990 Jan; 35(1):97-103. PubMed ID: 2328279
    [Abstract] [Full Text] [Related]

  • 3. The energetics of ligand-linked subunit assembly in hemoglobin require a third allosteric structure.
    Ackers GK.
    Biophys Chem; 1990 Aug 31; 37(1-3):371-82. PubMed ID: 2285798
    [Abstract] [Full Text] [Related]

  • 4. Linkage between ligand binding and the dimer-tetramer equilibrium in the Monod-Wyman-Changeux model of hemoglobin.
    Edelstein SJ, Edsall JT.
    Proc Natl Acad Sci U S A; 1986 Jun 31; 83(11):3796-800. PubMed ID: 3459157
    [Abstract] [Full Text] [Related]

  • 5. Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin.
    Doyle ML, Ackers GK.
    Biochemistry; 1992 Nov 17; 31(45):11182-95. PubMed ID: 1445857
    [Abstract] [Full Text] [Related]

  • 6. Allosteric interpretation of the measurement of cooperative free energy in cyanomethemoglobin.
    Ferrone FA.
    Proc Natl Acad Sci U S A; 1986 Sep 17; 83(17):6412-4. PubMed ID: 3462703
    [Abstract] [Full Text] [Related]

  • 7. Allosteric kinetics and equilibria differ for carbon monoxide and oxygen binding to hemoglobin.
    Zhang NQ, Ferrone FA, Martino AJ.
    Biophys J; 1990 Aug 17; 58(2):333-40. PubMed ID: 2207241
    [Abstract] [Full Text] [Related]

  • 8. Oxygen binding and subunit interaction of hemoglobin in relation to the two-state model.
    Gibson QH, Edelstein SJ.
    J Biol Chem; 1987 Jan 15; 262(2):516-9. PubMed ID: 3804994
    [Abstract] [Full Text] [Related]

  • 9. The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 1. Microstate linear free energy relations.
    Goldbeck RA, Esquerra RM, Holt JM, Ackers GK, Kliger DS.
    Biochemistry; 2004 Sep 28; 43(38):12048-64. PubMed ID: 15379545
    [Abstract] [Full Text] [Related]

  • 10.
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  • 11. Experimental resolution of cooperative free energies for the ten ligation states of human hemoglobin.
    Smith FR, Ackers GK.
    Proc Natl Acad Sci U S A; 1985 Aug 28; 82(16):5347-51. PubMed ID: 3860865
    [Abstract] [Full Text] [Related]

  • 12. The Hill coefficient: inadequate resolution of cooperativity in human hemoglobin.
    Holt JM, Ackers GK.
    Methods Enzymol; 2009 Aug 28; 455():193-212. PubMed ID: 19289207
    [Abstract] [Full Text] [Related]

  • 13. An analytic solution to the Monod-Wyman-Changeux model and all parameters in this model.
    Zhou G, Ho PS, van Holde KE.
    Biophys J; 1989 Feb 28; 55(2):275-80. PubMed ID: 2713440
    [Abstract] [Full Text] [Related]

  • 14. Evolution of allosteric models for hemoglobin.
    Eaton WA, Henry ER, Hofrichter J, Bettati S, Viappiani C, Mozzarelli A.
    IUBMB Life; 2007 Feb 28; 59(8-9):586-99. PubMed ID: 17701554
    [Abstract] [Full Text] [Related]

  • 15. Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals.
    Mozzarelli A, Rivetti C, Rossi GL, Eaton WA, Henry ER.
    Protein Sci; 1997 Feb 28; 6(2):484-9. PubMed ID: 9041656
    [Abstract] [Full Text] [Related]

  • 16. Understanding allosteric and cooperative interactions in enzymes.
    Cornish-Bowden A.
    FEBS J; 2014 Jan 28; 281(2):621-32. PubMed ID: 23910900
    [Abstract] [Full Text] [Related]

  • 17. The Monod-Wyman-Changeux allosteric model describes haemoglobin oxygenation with only one adjustable parameter.
    Imai K.
    J Mol Biol; 1983 Jul 05; 167(3):741-9. PubMed ID: 6876164
    [Abstract] [Full Text] [Related]

  • 18. An extended Monod-Wyman-Changeaux-model expressed in terms of the Herzfeld-Stanley formalism applied to oxygen and carbonmonoxide binding curves of hemoglobin trout IV.
    Schweitzer-Stenner R, Dreybrodt W.
    Biophys J; 1989 Apr 05; 55(4):691-701. PubMed ID: 2720067
    [Abstract] [Full Text] [Related]

  • 19. A thermodynamic model of hemoglobin suitable for physiological applications.
    Yoshida T, Dembo M.
    Am J Physiol; 1990 Mar 05; 258(3 Pt 1):C563-77. PubMed ID: 2107752
    [Abstract] [Full Text] [Related]

  • 20. Resolving the fast kinetics of cooperative binding: Ca2+ buffering by calretinin.
    Faas GC, Schwaller B, Vergara JL, Mody I.
    PLoS Biol; 2007 Nov 05; 5(11):e311. PubMed ID: 18044987
    [Abstract] [Full Text] [Related]

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