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Journal Abstract Search


189 related items for PubMed ID: 1390701

  • 1. Allosteric modifiers of hemoglobin: 2-[4-[[(3,5-disubstituted anilino)carbonyl]methyl]phenoxy]-2-methylpropionic acid derivatives that lower the oxygen affinity of hemoglobin in red cell suspensions, in whole blood, and in vivo in rats.
    Abraham DJ, Wireko FC, Randad RS, Poyart C, Kister J, Bohn B, Liard JF, Kunert MP.
    Biochemistry; 1992 Sep 29; 31(38):9141-9. PubMed ID: 1390701
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  • 2. Effect of an allosteric modifier of hemoglobin, RSR-4, on oxygen affinity and oxygen saturation of hemoglobin in rabbits.
    Uchida K, Reilly MP, Abraham DJ, Asakura T.
    Jpn J Physiol; 1998 Dec 29; 48(6):439-44. PubMed ID: 10021497
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  • 3. High-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effector.
    Safo MK, Moure CM, Burnett JC, Joshi GS, Abraham DJ.
    Protein Sci; 2001 May 29; 10(5):951-7. PubMed ID: 11316875
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  • 4. Synthesized allosteric effectors of the hemoglobin molecule: a possible mechanism for improved erythrocyte oxygen release capability in hemoglobinopathy H disease.
    Papassotiriou I, Kister J, Griffon N, Abraham DJ, Kanavakis E, Traeger-Synodinos J, Stamoulakatou A, Marden MC, Poyart C.
    Exp Hematol; 1998 Sep 29; 26(10):922-6. PubMed ID: 9728926
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  • 5. Allosteric modifiers of hemoglobin. 1. Design, synthesis, testing, and structure-allosteric activity relationship of novel hemoglobin oxygen affinity decreasing agents.
    Randad RS, Mahran MA, Mehanna AS, Abraham DJ.
    J Med Chem; 1991 Feb 29; 34(2):752-7. PubMed ID: 1995897
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  • 6. Allosteric modifiers of hemoglobin. 2. Crystallographically determined binding sites and hydrophobic binding/interaction analysis of novel hemoglobin oxygen effectors.
    Wireko FC, Kellogg GE, Abraham DJ.
    J Med Chem; 1991 Feb 29; 34(2):758-67. PubMed ID: 1995898
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  • 7. X-ray crystallographic analyses of symmetrical allosteric effectors of hemoglobin: compounds designed to link primary and secondary binding sites.
    Safo MK, Boyiri T, Burnett JC, Danso-Danquah R, Moure CM, Joshi GS, Abraham DJ.
    Acta Crystallogr D Biol Crystallogr; 2002 Apr 29; 58(Pt 4):634-44. PubMed ID: 11914488
    [Abstract] [Full Text] [Related]

  • 8. New effectors of human hemoglobin: structure and function.
    Lalezari I, Lalezari P, Poyart C, Marden M, Kister J, Bohn B, Fermi G, Perutz MF.
    Biochemistry; 1990 Feb 13; 29(6):1515-23. PubMed ID: 2334712
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  • 12. RSR-13, an allosteric effector of hemoglobin, increases systemic and iliac vascular resistance in rats.
    Kunert MP, Liard JF, Abraham DJ.
    Am J Physiol; 1996 Aug 13; 271(2 Pt 2):H602-13. PubMed ID: 8770102
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  • 13. Methyl acetyl phosphate as a covalent probe for anion-binding sites in human and bovine hemoglobins.
    Ueno H, Pospischil MA, Manning JM.
    J Biol Chem; 1989 Jul 25; 264(21):12344-51. PubMed ID: 2745446
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  • 15. Synthesis and structure-activity relationships of chiral allosteric modifiers of hemoglobin.
    Phelps Grella M, Danso-Danquah R, Safo MK, Joshi GS, Kister J, Marden M, Hoffman SJ, Abraham DJ.
    J Med Chem; 2000 Dec 14; 43(25):4726-37. PubMed ID: 11123981
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  • 16. Intrinsic activity at the molecular level: E. J. Ariëns' concept visualized.
    Abraham DJ, Kister J, Joshi GS, Marden MC, Poyart C.
    J Mol Biol; 1995 May 12; 248(4):845-55. PubMed ID: 7752245
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  • 18. How allosteric effectors can bind to the same protein residue and produce opposite shifts in the allosteric equilibrium.
    Abraham DJ, Safo MK, Boyiri T, Danso-Danquah RE, Kister J, Poyart C.
    Biochemistry; 1995 Nov 21; 34(46):15006-20. PubMed ID: 7578114
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  • 19. Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers.
    Tsuneshige A, Kanaori K, Samuni U, Danstker D, Friedman JM, Neya S, Giangiacomo L, Yonetani T.
    J Biol Chem; 2004 Nov 19; 279(47):48959-67. PubMed ID: 15361521
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  • 20. Bezafibrate derivatives as potent effectors of hemoglobin.
    Poyart C, Marden MC, Kister J.
    Methods Enzymol; 1994 Nov 19; 232():496-513. PubMed ID: 8057877
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