Allosteric interpretation of haemoglobin properties
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R G Shulman | J J Hopfield | J. Hopfield | S. Ogawa | R. Shulman | S Ogawa
[1] A. Riggs,et al. Kinetic and equilibrium properties of hemoglobin Kansas. , 1973, The Journal of biological chemistry.
[2] J. Greer. Three-dimensional structure of abnormal human haemoglobins Kansas and Richmond. , 1971, Journal of molecular biology.
[3] A. Hayashi,et al. The oxygen equilibrium of hemoglobin MSaskatoon. , 1966, Biochimica et biophysica acta.
[4] R. Nagel,et al. Relation between structure and function in Hemoglobin Chesapeake. , 1967, Biochemistry.
[5] G. Guidotti. Studies on the chemistry of hemoglobin. II. The effect of salts on the dissociation of hemoglobin into subunits. , 1967, The Journal of biological chemistry.
[6] R. S. Eliot,et al. The effects of 2,3-diphosphoglycerate on the kinetics of deoxygenation of human hemoglobin. , 1970, Biochemical and biophysical research communications.
[7] Y. Henry,et al. Reciprocal effects of change of subunit structure on ligand equilibria of haemoglobin valency hybrids. Attempted correlation with electron paramagnetic resonance spectra. , 1973, Journal of molecular biology.
[8] M. Raftery,et al. Characterization of intermediate states in the ligation of hemoglobin. , 1973, Biochemistry.
[9] J J Hopfield,et al. Relation between structure, co-operativity and spectra in a model of hemoglobin action. , 1973, Journal of molecular biology.
[10] S. Edelstein,et al. Observation of the dissociation of unliganded hemoglobin. , 1972, The Journal of biological chemistry.
[11] M. Brunori,et al. On the rate of a conformation change associated with ligand binding in hemoglobin. , 1969, The Journal of biological chemistry.
[12] C. Ho,et al. Nuclear magnetic resonance studies of hemoglobins. 8. Evidence for preferential ligand binding to chains within deoxyhemoglobins. , 1971, Biochemical and biophysical research communications.
[13] A. Riggs,et al. Studies of the interaction of 2,3-diphosphoglycerate and carbon dioxide with hemoglobins from mouse, man, and elephant. , 1971, The Journal of biological chemistry.
[14] A. Minton,et al. The three-state model: a minimal allosteric description of homotropic and heterotropic effects in the binding of ligands to hemoglobin. , 1974, Proceedings of the National Academy of Sciences of the United States of America.
[15] S. Ogawa,et al. Spin-label study of hemoglobin conformations in solution. , 1967, Proceedings of the National Academy of Sciences of the United States of America.
[16] S. Ogawa,et al. Observation of allosteric transition in hemoglobin. , 1971, Biochemical and biophysical research communications.
[17] K. Imai,et al. Analysis of oxygen equilibrium of hemoglobin and control mechanism of organic phosphates. , 1973, Biochemistry.
[18] Q. Gibson,et al. The kinetics of ligand binding to hemoglobin valency hybrids and the effect of anions. , 1972, The Journal of biological chemistry.
[19] K. Reissmann,et al. A human hemoglobin with lowered oxygen affinity and impaired heme-heme interactions. , 1961, The Journal of clinical investigation.
[20] J. Greer. Three-dimensional structure of abnormal human haemoglobins M Hyde Park and M Iwate. , 1971, Journal of molecular biology.
[21] Q. Gibson,et al. Ligand binding kinetics of des arginine haemoglobin. , 1973, Journal of molecular biology.
[22] H. Morimoto,et al. Properties of hemoglobin M, Milwaukee-I variant and its unique characteristic. , 1969, Biochimica et biophysica acta.
[23] M. Brunori,et al. Enzyme Proteins. (Book Reviews: Hemoglobin and Myoglobin in Their Reactions with Ligands) , 1971 .
[24] H. Mcconnell,et al. The binding of a spin-labeled triphosphate to hemoglobin. , 1972, Cold Spring Harbor symposia on quantitative biology.
[25] J. Haber,et al. The effect of 2,3-diphosphoglyceric acid on the changes in - interactions in hemoglobin during oxygenation. , 1971, The Journal of biological chemistry.
[26] K. Imai,et al. Effects of 2,3-diphosphoglycerate on the oxygen equilibria of the half-cyanmet hybrid hemoglobins. , 1972, Biochemistry.
[27] J. Hopfield,et al. An allosteric model of hemoglobin. I. Kinetics. , 1971, Journal of molecular biology.
[28] M. Perutz,et al. Structure of hemoglobin M Boston, a variant with a five-coordinated ferric heme. , 1973, Proceedings of the National Academy of Sciences of the United States of America.
[29] J. Clegg,et al. Polycythemia associated with a hemoglobinopathy. , 1966, The Journal of clinical investigation.
[30] L. Janssen,et al. The interaction of 2,3-diphosphoglycerate on human deoxy and oxyhemoglobin. , 1973, Biochemical and biophysical research communications.
[31] M. Raftery,et al. A study of cooperative interactions in hemoglobin using fluorine nuclear magnetic resonance. , 1972, Biochemistry.
[32] C. Cantor,et al. Measurement of ligand-induced conformational changes in hemoglobin by circular dichroism. , 1969, Proceedings of the National Academy of Sciences of the United States of America.
[33] H. Morimoto,et al. Some observations on the physicochemical properties of hemoglobin M-Hyde Park. , 1968, Archives of biochemistry and biophysics.
[34] K. Imai,et al. Studies on the function of abnormal hemoglobins. I. An improved method for automatic measurement of the oxygen equilibrium curve of hemoglobin. , 1970, Biochimica et biophysica acta.
[35] W. Gratzer,et al. Cofactor binding and oxygen equilibria in haemoglobin. , 1971, Nature: New biology.
[36] C. Ho,et al. Effects of ligands and organic phosphates on functional properties of human adult hemoglobin. , 1974, Biochemistry.
[37] C. Ho,et al. Functional nonequivalence of and hemes in human adult hemoglobin. , 1972, Proceedings of the National Academy of Sciences of the United States of America.
[38] S. Edelstein. Extensions of the Allosteric Model for Haemoglobin , 1971, Nature.
[39] R G Shulman,et al. High resolution nuclear magnetic resonance spectra of hemoglobin: III. The half-ligated state and allosteric interactions , 1972 .
[40] S. Ogawa,et al. Effects of phosphate upon CO binding kinetics and NMR spectra of hemoglobin valency hybrids. , 1971, Biochemical and biophysical research communications.
[41] K. Gersonde,et al. High-resolution proton nuclear magnetic resonance studies of the quaternary state of hemoglobin M Iwate. , 1973, Journal of molecular biology.
[42] C. Ho,et al. Nuclear magnetic resonance and spin-label studies of hemoglobin Kempsey. , 1973, Biochemistry.
[43] M. Brunori,et al. Preparation and kinetic properties of intermediates in the reaction of hemoglobin with ligands. , 1966, The Journal of biological chemistry.
[44] R. Gray. The kinetics of the alkaline Bohr effect of human hemoglobin. , 1970, Journal of Biological Chemistry.
[45] S. Edelstein,et al. Observation of the dissociation of unliganded hemoglobin. II. Effect of pH, salt, and dioxane. , 1973, The Journal of biological chemistry.
[46] M. Raftery,et al. Conformation and cooperativity in hemoglobin. , 1975, Biochemistry.
[47] T. Shiga,et al. Electron paramagnetic resonance studies of nitric oxide hemoglobin derivatives. I. Human hemoglobin subunits. , 1969, Biochemistry.
[48] J. Wyman,et al. LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK. , 1964, Advances in protein chemistry.
[49] Q. Gibson,et al. The effect of inositol hexaphosphate on the kinetics of CO and O 2 binding by human hemoglobin. , 1971, The Journal of biological chemistry.
[50] H. Bunn,et al. Some observations on the properties of hemoglobin M Milwaukee-1. , 1970, Journal of molecular biology.
[51] F. Roughton,et al. The kinetics of dissociation of the first ligand molecule from fully saturated carboxyhaemoglobin and nitric oxide haemoglobin in sheep blood solutions , 1957, Proceedings of the Royal Society of London. Series B - Biological Sciences.
[52] J. Haber,et al. Evidence for β-β interactions during the binding of oxygen to hemoglobin , 1969 .
[53] A. Riggs. Mechanism of the enhancement of the Bohr effect in mammalian hemoglobins by diphosphoglycerate. , 1971, Proceedings of the National Academy of Sciences of the United States of America.
[54] M. F. Perutz,et al. Nature of Haem–Haem Interaction , 1972, Nature.
[55] S. Ogawa,et al. High resolution nuclear magnetic resonance spectra of hemoglobin: II. Ligated tetramers , 1972 .
[56] C. Ho,et al. Nuclear magnetic resonance studies of haemoglobin M Milwaukee. , 1972, Nature: New biology.
[57] J. Changeux,et al. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.
[58] C. Ho,et al. Effects of anions and ligands on the tertiary structure around ligand binding site in human adult hemoglobin. , 1973, Biochemistry.
[59] K. Wüthrich,et al. The absence of "heme-heme" interactions in hemoglobin. , 1969, Science.
[60] L. Mazzarella,et al. Structure Of Hæemoglobin: A Preliminary X-Ray Analysis of Haemoglobin H , 1963, Nature.
[61] A. Hayashi,et al. Functional abnormality of hemoglobin M-Osaka. , 1965, Biochemical and biophysical research communications.
[62] K. Imai. Analyses of oxygen equilibria of native and chemically modified human adult hemoglobins on the basis of Adair's stepwise oxygenation theory and the allosteric model of Monod, Wyman, and Changeux. , 1973, Biochemistry.
[63] R. Benesch. The influence of oxygenation on the reactivity of the--SH groups of hemoglobin. , 1962, Biochemistry.
[64] J E Ladner,et al. Influence of globin structure on the state of the heme. 3. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme-heme interaction. , 1974, Biochemistry.
[65] C. Ho,et al. Nuclear magnetic resonance studies of hemoglobins. VII. Tertiary structure around ligand binding site in carbonmonoxyhemoglobin. , 1972, Biochemistry.
[66] M. Brunori,et al. Functional properties of carboxypeptidase-digested hemoglobins. , 1974, Journal of molecular biology.
[67] J. M. Salhany. The deoxygenation kinetics of hemoglobin Rainier (α2β2145 Tyr→Cys) , 1972 .
[68] J E Ladner,et al. Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin. , 1974, Biochemistry.
[69] J. Greer. Three-dimensional structure of abnormal human haemoglobins Chesapeake and J Capetown. , 1971, Journal of molecular biology.
[70] Q. Gibson,et al. Preparation and Properties of α- and β-Chains from Human Hemoglobin , 1969 .
[71] Q. Gibson,et al. The rate of reaction of carbon monoxide with hemoglobins M. , 1966, The Journal of biological chemistry.
[72] L. Stryer,et al. Kinetics of azide binding to normal and mutant ferrihemoglobins as evidence for subunit interaction. , 1968, Journal of molecular biology.
[73] R. Benesch,et al. Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. , 1968, Proceedings of the National Academy of Sciences of the United States of America.
[74] M. Brunori,et al. Artificial intermediates in the reaction of haemoglobin. Functional and conformational properties of the cyanmet intermediates. , 1970, Journal of molecular biology.
[75] A. Riggs. The binding of N-ethylmaleimide by human hemoglobin and its effect upon the oxygen equilibrium. , 1961, The Journal of biological chemistry.
[76] M. Perutz,et al. Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic Model , 1968, Nature.
[77] D. Koshland,et al. Comparison of experimental binding data and theoretical models in proteins containing subunits. , 1966, Biochemistry.
[78] M. Perutz,et al. Noncooperativity of the dimer in the reaction of hemoglobin with oxygen (human-dissociation-equilibrium-sulfhydryl-absorption-x-ray analysis). , 1972, Proceedings of the National Academy of Sciences of the United States of America.
[79] A. Fersht,et al. Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin. , 1974, Biochemistry.
[80] M. Perutz. Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery , 1970, Nature.
[81] Y. Henry,et al. Electron paramagnetic studies of nitric oxide haemoglobin derivatives: isolated subunits and nitric oxide hybrids. , 1973, Journal of molecular biology.
[82] L. Anderson. Structures of deoxy and carbonmonoxy haemoglobin Kansas in the deoxy quaternary conformation. , 1975, Journal of molecular biology.
[83] D. G. Davis,et al. Nuclear magnetic resonance studies of hemoglobiss. V. The heme proton spectra of human deoxyhemoglobins A, F, Zurich, and Chesapeake. , 1970, Biochemical and biophysical research communications.
[84] R. Nagel,et al. Oxygen equilibrium of hemoglobin M-Hyde Park. , 1968, Biochimica et biophysica acta.
[85] J. Kilmartin,et al. The effect of removal of C-terminal residues on cooperative interactions in hemoglobin. , 1972, Cold Spring Harbor symposia on quantitative biology.
[86] S. Ogawa,et al. The effects of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance. , 1971, The Journal of biological chemistry.
[87] M. Raftery,et al. 31 P-NMR studies of the release of diphospholygeric acid on carbon monoxide binding to hemoglobin. , 1972, Biochemical and biophysical research communications.
[88] F. Roughton,et al. The kinetics of dissociation of the first oxygen molecule from fully saturated oxyhaemoglobin in sheep blood solutions , 1955, Proceedings of the Royal Society of London. Series B - Biological Sciences.
[89] S. Ogawa,et al. Correlation between quaternary structure and ligand dissociation kinetics for fully liganded hemoglobin. , 1975, Biochemistry.
[90] S. Ogawa,et al. Overlapping conformation changes in spin-labeled hemoglobin. , 1968, Proceedings of the National Academy of Sciences of the United States of America.
[91] R. Nagel,et al. The binding of 2,3-diphosphoglycerate as a conformational probe of human hemoglobins. , 1973, Journal of molecular biology.
[92] M. Perutz,et al. Structure and subunit interaction of haemoglobin M Milwaukee. , 1972, Nature: New biology.
[93] S. Ogawa,et al. Spectral-kinetic heterogeneity in reactions of nitrosyl hemoglobin. , 1974, Proceedings of the National Academy of Sciences of the United States of America.
[94] M. Perutz,et al. Molecular Pathology of Human Haemoglobin: Stereochemical Interpretation of Abnormal Oxygen Affinities , 1971, Nature.
[95] N. Hayashi,et al. Studies on relationships between structure and function of hemoglobin M-Iwate. , 1966, The Journal of biological chemistry.
[96] S. Ogawa,et al. High resolution proton magnetic resonance study of the two quaternary states in fully ligated hemoglobin Kansas. , 1972, Biochemical and biophysical research communications.
[97] M. Brunori,et al. Spectral differences between haemoglobin and isolated haemoglobin chains in the deoxygenated state , 1968 .
[98] J. Hopfield,et al. The rate of carbon monoxide binding to hemoglobin Kansas. , 1972, Biochemical and biophysical research communications.
[99] H. Bunn. Dissociation of Haemoglobin Chesapeake into Subunits , 1970, Nature.
[100] J P Changeux,et al. On the nature of allosteric transitions: implications of non-exclusive ligand binding. , 1966, Journal of molecular biology.
[101] J. Hopfield,et al. An allosteric model of hemoglobin. II. The assumption of independent binding. , 1972, Archives of biochemistry and biophysics.
[102] M. Brunori,et al. THE KINETICS OF THE BOHR EFFECT IN THE REACTION OF HUMAN HEMOGLOBIN WITH CARBON MONOXIDE. , 1965, The Journal of biological chemistry.
[103] H. Mcconnell,et al. Mechanism of Cooperative Oxygen Binding to Hemoglobin , 1972 .
[104] S. Ogawa,et al. HIGH‐RESOLUTION PROTON NMR STUDIES OF LOW AFFINITY HEMOGLOBINS , 1973, Annals of the New York Academy of Sciences.
[105] Proton magnetic resonance study of the switch between the two quaternary structures in high-affinity hemoglobins in the deoxy state. , 1974, Biochemistry.
[106] G. Kellett. Dissociation of hemoglobin into subunits. Ligand-linked dissociation at neutral pH. , 1971, Journal of molecular biology.
[107] Q. Gibson. The photochemical formation of a quickly reacting form of haemoglobin. , 1959, The Biochemical journal.
[108] M. Perutz. Stereochemistry of cooperative effects in haemoglobin. , 1970, Nature.
[109] G. Guidotti,et al. Stabilizing interactions in hemoglobin. , 1972, The Journal of biological chemistry.
[110] R. Benesch,et al. The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. , 1967, Biochemical and biophysical research communications.
[111] T. Maeda,et al. Kinetic evidence for propagation of conformational changes in the alpha subunit to the beta subunit of hemoglobin. , 1971, Biochemistry.
[112] J. Bonaventura,et al. Hemoglobin Kansas, a human hemoglobin with a neutral amino acid substitution and an abnormal oxygen equilibrium. , 1968, The Journal of biological chemistry.
[113] M. Perutz,et al. Molecular Pathology of Human Haemoglobin , 1968, Nature.
[114] R. Shulman,et al. Proton NMR studies of hemoglobin in H2O. , 1970, Biochemical and biophysical research communications.
[115] L Anderson,et al. Intermediate structure of normal human haemoglobin: methaemoglobin in the deoxy quaternary conformation. , 1973, Journal of molecular biology.
[116] C. Ho,et al. Nuclear magnetic resonance studies of hemoglobin Chesapeake: an alpha1beta2 mutant. , 1974, Biochemistry.
[117] M. Perutz,et al. Structure Of Hæemoglobin: A Three-Dimensional Fourier Synthesis of Reduced Human Haemoglobin at 5.5 Å Resolution , 1963, Nature.
[118] Q. Gibson. The Kinetics of Reactions Between Haemoglobin and Gases , 1959 .