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Laberge, Monique; Yonetani, Takashi (2008) Molecular dynamics simulations of hemoglobin A in different states and bound to DPG: effector-linked perturbation of tertiary conformations and HbA concerted dynamics. Biophys J 94:2737-51
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Egawa, Tsuyoshi; Tsuneshige, Antonio; Suematsu, Makoto et al. (2007) Method for determination of association and dissociation rate constants of reversible bimolecular reactions by isothermal titration calorimeters. Anal Chem 79:2972-8
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Laberge, Monique; Kovesi, Istvan; Yonetani, Takashi et al. (2006) Normal mode analysis of the horseradish peroxidase collective motions: correlation with spectroscopically observed heme distortions. Biopolymers 82:425-9
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Schay, Gusztav; Smeller, Laszlo; Tsuneshige, Antonio et al. (2006) Allosteric effectors influence the tetramer stability of both R- and T-states of hemoglobin A. J Biol Chem 281:25972-83
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Suganuma, Kazuhiro; Tsukada, Kosuke; Kashiba, Misato et al. (2006) Erythrocytes with T-state-stabilized hemoglobin as a therapeutic tool for postischemic liver dysfunction. Antioxid Redox Signal 8:1847-55
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Kovesi, I; Schay, G; Yonetani, T et al. (2006) High pressure reveals that the stability of interdimeric contacts in the R- and T-state of HbA is influenced by allosteric effectors: Insights from computational simulations. Biochim Biophys Acta 1764:516-21
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Yokoyama, Takeshi; Neya, Saburo; Tsuneshige, Antonio et al. (2006) R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35. J Mol Biol 356:790-801
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Laberge, Monique; Kovesi, Istvan; Yonetani, Takashi et al. (2005) R-state hemoglobin bound to heterotropic effectors: models of the DPG, IHP and RSR13 binding sites. FEBS Lett 579:627-32
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Nagatomo, Shigenori; Nagai, Masako; Mizutani, Yasuhisa et al. (2005) Quaternary structures of intermediately ligated human hemoglobin a and influences from strong allosteric effectors: resonance Raman investigation. Biophys J 89:1203-13
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Tsuneshige, Antonio; Kanaori, Kenji; Samuni, Uri et al. (2004) Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers. J Biol Chem 279:48959-67
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