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Journal Abstract Search

192 related items for PubMed ID: 6583698

  • 1. 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
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  • 2. Energetics of subunit assembly and ligand binding in human hemoglobin.
    Ackers GK.
    Biophys J; 1980 Oct; 32(1):331-46. PubMed ID: 7248452
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  • 7. Structure-specific model of hemoglobin cooperativity.
    Lee AW, Karplus M.
    Proc Natl Acad Sci U S A; 1983 Dec; 80(23):7055-9. PubMed ID: 6580628
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  • 10. Oxygenation-linked subunit interactions in human hemoglobin: analysis of linkage functions for constituent energy terms.
    Johnson ML, Halvorson HR, Ackers GK.
    Biochemistry; 1976 Nov 30; 15(24):5363-71. PubMed ID: 999812
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  • 12. The pathway of allosteric control as revealed by hemoglobin intermediate states.
    Holt JM, Ackers GK.
    FASEB J; 1995 Feb 30; 9(2):210-8. PubMed ID: 7781923
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  • 13. Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin.
    Viggiano G, Ho C.
    Proc Natl Acad Sci U S A; 1979 Aug 30; 76(8):3673-7. PubMed ID: 291032
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  • 14. Description of the molecular mechanism of cooperativity in human hemoglobin cannot be limited to a first-order free energy coupling concept.
    Johnson ML.
    Biochemistry; 1988 Jan 26; 27(2):833-7. PubMed ID: 3349067
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  • 17. Three-state combinatorial switch models as applied to the binding of oxygen by human hemoglobin.
    Straume M, Johnson ML.
    Biochemistry; 1988 Feb 23; 27(4):1302-10. PubMed ID: 3365388
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  • 18. Analysis of proton release in oxygen binding by hemoglobin: implications for the cooperative mechanism.
    Lee AW, Karplus M, Poyart C, Bursaux E.
    Biochemistry; 1988 Feb 23; 27(4):1285-301. PubMed ID: 2835088
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  • 19. 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
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