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Journal Abstract Search


193 related items for PubMed ID: 7248452

  • 1. Energetics of subunit assembly and ligand binding in human hemoglobin.
    Ackers GK.
    Biophys J; 1980 Oct; 32(1):331-46. PubMed ID: 7248452
    [Abstract] [Full Text] [Related]

  • 2. A quantitative model for the cooperative mechanism of human hemoglobin.
    Johnson ML, Turner BW, Ackers GK.
    Proc Natl Acad Sci U S A; 1984 Feb; 81(4):1093-7. PubMed ID: 6583698
    [Abstract] [Full Text] [Related]

  • 3. Enthalpic and entropic components of cooperativity for the partially ligated intermediates of hemoglobin support a "symmetry rule" mechanism.
    Huang Y, Ackers GK.
    Biochemistry; 1995 May 16; 34(19):6316-27. PubMed ID: 7756259
    [Abstract] [Full Text] [Related]

  • 4. Tetramer-dimer dissociation in homoglobin and the Bohr effect.
    Atha DH, Riggs A.
    J Biol Chem; 1976 Sep 25; 251(18):5537-43. PubMed ID: 9390
    [Abstract] [Full Text] [Related]

  • 5. Mutagenic dissection of hemoglobin cooperativity: effects of amino acid alteration on subunit assembly of oxy and deoxy tetramers.
    Turner GJ, Galacteros F, Doyle ML, Hedlund B, Pettigrew DW, Turner BW, Smith FR, Moo-Penn W, Rucknagel DL, Ackers GK.
    Proteins; 1992 Nov 25; 14(3):333-50. PubMed ID: 1438173
    [Abstract] [Full Text] [Related]

  • 6. Resolvability of free energy changes for oxygen binding and subunit association by human hemoglobin.
    Straume M, Johnson ML.
    Biophys J; 1989 Jul 25; 56(1):15-25. PubMed ID: 2752084
    [Abstract] [Full Text] [Related]

  • 7. Single-site modifications of half-ligated hemoglobin reveal autonomous dimer cooperativity within a quaternary T tetramer.
    LiCata VJ, Dalessio PM, Ackers GK.
    Proteins; 1993 Nov 25; 17(3):279-96. PubMed ID: 8272426
    [Abstract] [Full Text] [Related]

  • 8. Bohr effects of the partially-ligated (CN-met) intermediates of hemoglobin as probed by quaternary assembly.
    Daugherty MA, Shea MA, Ackers GK.
    Biochemistry; 1994 Aug 30; 33(34):10345-57. PubMed ID: 8068671
    [Abstract] [Full Text] [Related]

  • 9. 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]

  • 10. Mutual effects of protons, NaCl, and oxygen on the dimer-tetramer assembly of human hemoglobin. The dimer Bohr effect.
    Chu AH, Ackers GK.
    J Biol Chem; 1981 Feb 10; 256(3):1199-205. PubMed ID: 7451499
    [Abstract] [Full Text] [Related]

  • 11. Thermodynamic studies on subunit assembly in human hemoglobin. Calorimetric measurements on the reconstitution of oxyhemoglobin from isolated chains.
    Valdes R, Ackers GK.
    J Biol Chem; 1977 Jan 10; 252(1):88-91. PubMed ID: 833133
    [Abstract] [Full Text] [Related]

  • 12. Structure-specific model of hemoglobin cooperativity.
    Lee AW, Karplus M.
    Proc Natl Acad Sci U S A; 1983 Dec 10; 80(23):7055-9. PubMed ID: 6580628
    [Abstract] [Full Text] [Related]

  • 13. Electrostatic contributions to the energetics of dimer-tetramer assembly in human hemoglobin: pH dependence and effect of specifically bound chloride ions.
    Flanagan MA, Ackers GK, Matthew JB, Hanania GI, Gurd FR.
    Biochemistry; 1981 Dec 22; 20(26):7439-49. PubMed ID: 7326236
    [Abstract] [Full Text] [Related]

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  • 17. Thermodynamic analysis of human hemoglobins in terms of the Perutz mechanism: extensions of the Szabo--Karplus model to include subunit assembly.
    Johnson ML, Ackers GK.
    Biochemistry; 1982 Jan 19; 21(2):201-11. PubMed ID: 7074009
    [Abstract] [Full Text] [Related]

  • 18. 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]

  • 19. Molecular code for cooperativity in hemoglobin.
    Ackers GK, Doyle ML, Myers D, Daugherty MA.
    Science; 1992 Jan 03; 255(5040):54-63. PubMed ID: 1553532
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