A retrospective on statistical mechanical models for hemoglobin allostery
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[1] W. Eaton. Impact of Conformational Substates and Energy Landscapes on Understanding Hemoglobin Kinetics and Function , 2021, Journal of Biological Physics.
[2] W. Eaton. Impact of hemoglobin biophysical studies on molecular pathogenesis and drug therapy for sickle cell disease. , 2021, Molecular aspects of medicine.
[3] A. Gupta. [Hemoglobin]. , 2018, Nihon Ketsueki Gakkai zasshi : journal of Japan Haematological Society.
[4] M. Martí,et al. Tertiary and quaternary structural basis of oxygen affinity in human hemoglobin as revealed by multiscale simulations , 2017, Scientific Reports.
[5] E. Henry,et al. Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models. , 2015, Biophysical journal.
[6] M. Brunori. Half a Century of Hemoglobin's Allostery. , 2015, Biophysical journal.
[7] C. Ho,et al. New look at hemoglobin allostery. , 2015, Chemical reviews.
[8] E. Henry,et al. Experimental basis for a new allosteric model for multisubunit proteins , 2014, Proceedings of the National Academy of Sciences.
[9] E. M. Jones,et al. Differential Control of Heme Reactivity in Alpha and Beta Subunits of Hemoglobin: A Combined Raman Spectroscopic and Computational Study , 2014, Journal of the American Chemical Society.
[10] M. Brunori. Variations on the theme: allosteric control in hemoglobin , 2014, The FEBS journal.
[11] S. Edelstein. Allosteric interactions after 50 years. , 2013, Journal of molecular biology.
[12] Sarah Marzen,et al. Statistical mechanics of Monod-Wyman-Changeux (MWC) models. , 2013, Journal of molecular biology.
[13] M. Brunori. Allostery turns 50: Is the vintage yet attractive? , 2011, Protein science : a publication of the Protein Society.
[14] M. Karplus,et al. Allostery and cooperativity revisited , 2008, Protein science : a publication of the Protein Society.
[15] W. Eaton,et al. New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[16] E. Henry,et al. A tertiary two-state allosteric model for hemoglobin. , 2002, Biophysical chemistry.
[17] A. Mozzarelli,et al. Correlation of protein functional properties in the crystal and in solution: The case study of T‐state hemoglobin , 2002, Protein science : a publication of the Protein Society.
[18] R. Shulman. Spectroscopic Contributions to the Understanding of Hemoglobin Function: Implications for Structural Biology , 2001, IUBMB life.
[19] J. Changeux,et al. Allosteric mechanisms in normal and pathological nicotinic acetylcholine receptors , 2001, Current Opinion in Neurobiology.
[20] Andrea Mozzarelli,et al. Is cooperative oxygen binding by hemoglobin really understood? , 1999, Nature Structural Biology.
[21] A. Mozzarelli,et al. T State Hemoglobin Binds Oxygen Noncooperatively with Allosteric Effects of Protons, Inositol Hexaphosphate, and Chloride* , 1997, The Journal of Biological Chemistry.
[22] C. M. Jones,et al. Can a two-state MWC allosteric model explain hemoglobin kinetics? , 1997, Biochemistry.
[23] N. Shibayama,et al. Fixation of the quaternary structures of human adult haemoglobin by encapsulation in transparent porous silica gels. , 1995, Journal of molecular biology.
[24] D. Koshland. The Key–Lock Theory and the Induced Fit Theory , 1995 .
[25] E. Henry,et al. Oxygen binding by single crystals of hemoglobin. , 1993, Biochemistry.
[26] C. M. Jones,et al. Speed of intersubunit communication in proteins. , 1992, Biochemistry.
[27] M. Doyle,et al. Molecular code for cooperativity in hemoglobin. , 1992, Science.
[28] E. Henry,et al. Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect , 1991, Nature.
[29] M. Karplus,et al. Analysis of proton release in oxygen binding by hemoglobin: implications for the cooperative mechanism. , 1988, Biochemistry.
[30] M. Brunori,et al. Cooperative free energies for nested allosteric models as applied to human hemoglobin. , 1986, Biophysical Journal.
[31] F. Ferrone. Allosteric interpretation of the measurement of cooperative free energy in cyanomethemoglobin. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[32] M Karplus,et al. Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism. , 1983, Journal of molecular biology.
[33] M. Karplus,et al. Structure-specific model of hemoglobin cooperativity. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[34] C. Ho,et al. Role of the beta 146 histidyl residue in the alkaline Bohr effect of hemoglobin. , 1980, Biochemistry.
[35] A. Szabó,et al. Ligand binding to macromolecules: Allosteric and sequential models of cooperativity , 1979 .
[36] M Karplus,et al. Mechanism of tertiary structural change in hemoglobin. , 1977, Proceedings of the National Academy of Sciences of the United States of America.
[37] M. Karplus,et al. Analysis of the interaction of organic phosphates with hemoglobin. , 1976, Biochemistry.
[38] Q H Gibson,et al. Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin. , 1976, The Journal of biological chemistry.
[39] R. Noble,et al. Conditions restricting allosteric transitions in carp hemoglobin. , 1973, The Journal of biological chemistry.
[40] M Karplus,et al. A mathematical model for structure-function relations in hemoglobin. , 1972, Journal of molecular biology.
[41] M. McDonald,et al. The effect of pH on the rates of ligand replacement reactions of human adult and fetal hemoglobins and their subunits. , 1972, The Journal of biological chemistry.
[42] J. Hopfield,et al. An allosteric model of hemoglobin. I. Kinetics. , 1971, Journal of molecular biology.
[43] S. Edelstein. Extensions of the Allosteric Model for Haemoglobin , 1971, Nature.
[44] J. Changeux,et al. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.
[45] J. Wyman,et al. THE BINDING POTENTIAL, A NEGLECTED LINKAGE CONCEPT. , 1965, Journal of molecular biology.
[46] J. Wyman,et al. Studies on carboxypeptidase digests of human hemoglobin. , 1961, The Journal of biological chemistry.
[47] D. Koshland. Application of a Theory of Enzyme Specificity to Protein Synthesis. , 1958, Proceedings of the National Academy of Sciences of the United States of America.
[48] J. Wyman,et al. The problem of the heme interactions in hemoglobin and the basis of the bohr effect , 1951 .
[49] C. D. Coryell,et al. The Magnetic Properties and Structure of Hemoglobin, Oxyhemoglobin and Carbonmonoxyhemoglobin , 1936, Proceedings of the National Academy of Sciences.
[50] L. Pauling,et al. The Oxygen Equilibrium of Hemoglobin and Its Structural Interpretation. , 1935, Proceedings of the National Academy of Sciences of the United States of America.
[51] G. Adair. THE HEMOGLOBIN SYSTEM VI. THE OXYGEN DISSOCIATION CURVE OF HEMOGLOBIN , 1925 .
[52] E. Henry,et al. Evolution of allosteric models for hemoglobin , 2007, IUBMB life.
[53] N. Shibayama,et al. The contribution of the asymmetric alpha 1beta 1 half-oxygenated intermediate to human hemoglobin cooperativity. , 2002, The Journal of biological chemistry.
[54] M Paoli,et al. The stereochemical mechanism of the cooperative effects in hemoglobin revisited. , 1998, Annual review of biophysics and biomolecular structure.
[55] S. Edelstein,et al. Cooperative interactions of hemoglobin. , 1975, Annual review of biochemistry.
[56] H. Mcconnell,et al. The binding of a spin-labeled triphosphate to hemoglobin. , 1972, Cold Spring Harbor symposia on quantitative biology.
[57] M. Perutz. Stereochemistry of cooperative effects in haemoglobin. , 1970, Nature.
[58] J. Richards. The structure and action of proteins , 1969 .
[59] D. Koshland,et al. Comparison of experimental binding data and theoretical models in proteins containing subunits. , 1966, Biochemistry.
[60] H. Watson,et al. STRUCTURE OF HAEMOGLOBIN. AN X-RAY EXAMINATION OF REDUCED HORSE HAEMOGLOBIN. , 1964, Nature.
[61] J. Wyman. Allosteric Effects in Hemoglobin , 1963 .
[62] J. Changeux. Allosteric Interactions on Biosynthetic L-threonine Deaminase from E. coli K12 , 1963 .