Is cooperative oxygen binding by hemoglobin really understood?
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Andrea Mozzarelli | William A. Eaton | E. Henry | J. Hofrichter | W. Eaton | A. Mozzarelli | James Hofrichter | Eric. R. Henry
[1] C. Bohr. Ueber den respiratorischen Stoffwechsel beim Embryo kaltblütiger Thiere1 , 1904 .
[2] M Paoli,et al. The stereochemical mechanism of the cooperative effects in hemoglobin revisited. , 1998, Annual review of biophysics and biomolecular structure.
[3] D. P. Sun,et al. Contribution of surface histidyl residues in the alpha-chain to the Bohr effect of human normal adult hemoglobin: roles of global electrostatic effects. , 1997, Biochemistry.
[4] J. Edsall. Hemoglobin and the origins of the concept of allosterism. , 1980, Federation proceedings.
[5] E. Henry,et al. Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[6] J. Changeux,et al. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.
[7] 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.
[8] N. Shibayama,et al. Asymmetric cyanomet valency hybrid hemoglobin, (alpha+CN-beta+CN-)(alpha beta): the issue of valency exchange. , 1998, Biochemistry.
[9] M. Lim,et al. Complex nonexponential relaxation in myoglobin after photodissociation of MbCO: measurement and analysis from 2 ps to 56 υs , 1994 .
[10] M. Brunori,et al. Enzyme Proteins. (Book Reviews: Hemoglobin and Myoglobin in Their Reactions with Ligands) , 1971 .
[11] H Frauenfelder,et al. Dynamics of ligand binding to myoglobin. , 1975, Biochemistry.
[12] Max F. Perutz,et al. Mechanisms of Cooperativity and Allosteric Regulation in Proteins , 1990 .
[13] K. Imai. The Monod-Wyman-Changeux allosteric model describes haemoglobin oxygenation with only one adjustable parameter. , 1983, Journal of molecular biology.
[14] Marshall A. Lichtman,et al. Commentary on and reprint of Pauling L, Itano HA, Singer SJ, Wells IC, Sickle cell anemia, a molecular disease, in Science (1949) 110:543–548 , 2000 .
[15] J. Hopfield,et al. CO binding to heme proteins: A model for barrier height distributions and slow conformational changes , 1983 .
[16] Q H Gibson,et al. Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin. , 1976, The Journal of biological chemistry.
[17] 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.
[18] J. Hopfield,et al. An allosteric model of hemoglobin. I. Kinetics. , 1971, Journal of molecular biology.
[19] G. Adair. A Critical Study of the Direct Method of Measuring the Osmotic Pressure of Haemoglobin , 1925 .
[20] E. Henry,et al. Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[21] Edsall Jt. Hemoglobin and the origins of the concept of allosterism. , 1980 .
[22] J. Hofrichter,et al. Sickle cell hemoglobin polymerization. , 1990, Advances in protein chemistry.
[23] M. Brunori,et al. Cooperative free energies for nested allosteric models as applied to human hemoglobin. , 1986, Biophysical Journal.
[24] E. Henry,et al. Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals , 1997, Protein science : a publication of the Protein Society.
[25] M. Doyle,et al. Effects of NaCl on the linkages between O2 binding and subunit assembly in human hemoglobin: titration of the quaternary enhancement effect. , 1997, Biophysical chemistry.
[26] S. W. Jones. A Plausible Model , 1999 .
[27] S. Edelstein. Extensions of the Allosteric Model for Haemoglobin , 1971, Nature.
[28] P. Wolynes,et al. The energy landscapes and motions of proteins. , 1991, Science.
[29] D. Koshland,et al. Comparison of experimental binding data and theoretical models in proteins containing subunits. , 1966, Biochemistry.
[30] G. K. Ackers,et al. Experimental resolution of cooperative free energies for the ten ligation states of human hemoglobin. , 1985, Proceedings of the National Academy of Sciences of the United States of America.
[31] S. Edelstein,et al. Pairings and polarities of the 14 strands in sickle cell hemoglobin fibers. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[32] A. Colosimo,et al. What the intermediate compounds in ligand binding to hemoglobin tell about the mechanism of cooperativity. , 1990, Biophysical chemistry.
[33] L. Pauling,et al. Molecular disease. , 1959, The American journal of orthopsychiatry.
[34] Christian Bohr,et al. Ueber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensäurespannung des Blutes auf dessen Sauerstoffbindung übt1 , 1904 .
[35] E. Henry,et al. Oxygen binding by single crystals of hemoglobin. , 1993, Biochemistry.
[36] R G Shulman,et al. Allosteric interpretation of haemoglobin properties , 1975, Quarterly Reviews of Biophysics.
[37] S. W. Jones,et al. Commentary: a plausible model. , 1999, The Journal of general physiology.
[38] M Karplus,et al. A mathematical model for structure-function relations in hemoglobin. , 1972, Journal of molecular biology.
[39] Q. Gibson. The photochemical formation of a quickly reacting form of haemoglobin. , 1959, The Biochemical journal.
[40] M. Perutz. Stereochemistry of cooperative effects in haemoglobin. , 1970, Nature.
[41] G. K. Ackers. The energetics of ligand-linked subunit assembly in hemoglobin require a third allosteric structure. , 1990, Biophysical chemistry.
[42] Richard Earl Dickerson,et al. Hemoglobin : structure, function, evolution, and pathology , 1983 .
[43] J. Hofrichter,et al. Protein reaction kinetics in a room-temperature glass , 1995, Science.
[44] 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.
[45] M. Perutz,et al. Allosteric mechanism of haemoglobin: rupture of salt-bridges raises the oxygen affinity of the T-structure. , 1998, Journal of molecular biology.
[46] Zygmunt Derewenda,et al. Structure of the liganded T state of haemoglobin identifies the origin of cooperative oxygen binding , 1988, Nature.
[47] G. K. Ackers,et al. Deciphering the molecular code of hemoglobin allostery. , 1998, Advances in protein chemistry.
[48] C. M. Jones,et al. Can a two-state MWC allosteric model explain hemoglobin kinetics? , 1997, Biochemistry.
[49] M. Doyle,et al. The oxygen-binding intermediates of human hemoglobin: evaluation of their contributions to cooperativity using zinc-containing hybrids. , 1996, Biophysical journal.
[50] L. Pauling,et al. Sickle cell anemia a molecular disease. , 1949, Science.
[51] H. Watson,et al. STRUCTURE OF HAEMOGLOBIN. AN X-RAY EXAMINATION OF REDUCED HORSE HAEMOGLOBIN. , 1964, Nature.