50th anniversary of the word ???allosteric???, Protein Science, vol.2, issue.7, pp.1119-1124, 2011. ,
DOI : 10.1002/pro.658
The Origins of Allostery: From Personal Memories to Material for the Future, Journal of Molecular Biology, vol.425, issue.9, pp.1396-1406, 2013. ,
DOI : 10.1016/j.jmb.2013.02.033
Allosteric proteins and cellular control systems, Journal of Molecular Biology, vol.6, issue.4, pp.306-329, 1963. ,
DOI : 10.1016/S0022-2836(63)80091-1
On the nature of allosteric transitions: A plausible model, Journal of Molecular Biology, vol.12, issue.1, pp.88-118, 1965. ,
DOI : 10.1016/S0022-2836(65)80285-6
Interactions between Jacques Monod and Jeffries Wyman (or the burdens of co-authorship), Rendiconti Lincei, vol.29, issue.1-2, 2006. ,
DOI : 10.1007/BF02904500
Structure of H??moglobin: A Three-Dimensional Fourier Synthesis at 5.5-???. Resolution, Obtained by X-Ray Analysis, Nature, vol.254, issue.4711, pp.416-422, 1960. ,
DOI : 10.1085/jgp.36.1.1
Stereochemistry of Cooperative Effects in Hemoglobin, Cold Spring Harbor Symposia on Quantitative Biology, vol.36, issue.0, pp.726-739, 1970. ,
DOI : 10.1101/SQB.1972.036.01.040
Hemoglobin and Myoglobin, Adv Protein Chem, vol.19, pp.73-222, 1964. ,
DOI : 10.1016/S0065-3233(08)60189-8
Linked Functions and Reciprocal Effects in Hemoglobin: A Second Look, Adv Protein Chem, vol.19, pp.223-286, 1964. ,
DOI : 10.1016/S0065-3233(08)60190-4
The Hemoglobins, Adv Protein Chem, vol.19, pp.1-73, 1964. ,
DOI : 10.1016/S0065-3233(08)60188-6
Hemoglobin and Myoglobin in their Reactions with Ligands, 1971. ,
Structure and function of haemoglobin, Progress in Biophysics and Molecular Biology, vol.29, pp.225-320, 1975. ,
DOI : 10.1016/0079-6107(76)90024-9
The problem of the heme interactions in hemoglobin and the basis of the bohr effect, Journal of Polymer Science, vol.7, issue.5, pp.499-518, 1951. ,
DOI : 10.1002/pol.1951.120070506
Understanding allosteric and cooperative interactions in enzymes, FEBS Journal, vol.20, issue.2, pp.10-1111, 2013. ,
DOI : 10.1111/febs.12469
URL : https://hal.archives-ouvertes.fr/hal-01494607
Variations on a theme: A comparative study of fish hemoglobins, Comparative Biochemistry and Physiology Part A: Physiology, vol.62, issue.1, pp.9-12, 1979. ,
DOI : 10.1016/0300-9629(79)90737-0
Allosteric interpretation of haemoglobin properties, Quarterly Reviews of Biophysics, vol.247, issue.03, pp.325-420, 1975. ,
DOI : 10.1073/pnas.58.1.19
Is cooperative oxygen binding by hemoglobin really understood?, Rendiconti Lincei, vol.37, issue.1-2, pp.351-358, 1999. ,
DOI : 10.1007/BF02904506
Allosteric Effects in Hemoglobin, 1982. ,
Allosteric Linkage, Journal of the American Chemical Society, vol.89, issue.9, pp.2202-2218, 1967. ,
DOI : 10.1021/ja00985a037
Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect, Nature, vol.351, issue.6325, pp.416-419, 1991. ,
DOI : 10.1038/351416a0
Evolution of allosteric models for hemoglobin, IUBMB Life, vol.59, issue.8, pp.586-599, 2007. ,
DOI : 10.1080/15216540701272380
Studies on the functional properties of fish hemoglobins, Archives of Biochemistry and Biophysics, vol.142, issue.1, pp.274-280, 1971. ,
DOI : 10.1016/0003-9861(71)90284-0
Molecular Adaptation to Physiological Requirements: The Hemoglobin System of Trout, Curr Top Cell Regul, vol.9, pp.1-39, 1975. ,
DOI : 10.1016/B978-0-12-152809-6.50008-1
Thermodynamics and Kinetics of the Reactions of Trout Hb I with O2 and CO, Hemoglobin and Oxygen Binding, 1982. ,
DOI : 10.1007/978-1-349-06488-5_59
The crystal structures of Trout Hb I in the deoxy and carbonmonoxy forms, J Mol Biol, vol.259, pp.749-760, 1996. ,
Hemoglobin Allostery: New Views on Old Players, Journal of Molecular Biology, vol.425, issue.9, pp.1515-1526, 2013. ,
DOI : 10.1016/j.jmb.2012.12.018
URL : https://hal.archives-ouvertes.fr/pasteur-01025328
A mathematical model for structure-function relations in hemoglobin, Journal of Molecular Biology, vol.72, issue.1, pp.163-197, 1972. ,
DOI : 10.1016/0022-2836(72)90077-0
Dynamics of the quaternary conformational change in trout hemoglobin, Biochemistry, vol.30, issue.26, pp.6583-6598, 1991. ,
DOI : 10.1021/bi00240a031
Membrane-covered thin-layer optical cell for gas-reaction studies of hemoglobin, Analytical Biochemistry, vol.87, issue.1, pp.127-134, 1978. ,
DOI : 10.1016/0003-2697(78)90576-6
Thermodynamic analysis of carbon monoxide binding by hemoglobin trout I, Biophysical Chemistry, vol.9, issue.3, pp.235-244, 1979. ,
DOI : 10.1016/0301-4622(79)85006-1
Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin, J Biol Chem, vol.251, pp.1533-1542, 1976. ,
Structure of binding sites for heterotropic effectors in fish haemoglobins, Nature, vol.284, issue.5833, pp.587-588, 1981. ,
DOI : 10.1038/293587a0
Temperature perturbation of the allosteric equilibrium in trout hemoglobin, J Biol Chem, vol.255, pp.3841-3843, 1980. ,
Hemoglobin Adaptation for Fast and Slow Water Habitats in Sympatric Catostomid Fishes, Science, vol.177, issue.4046, pp.360-362, 1972. ,
DOI : 10.1126/science.177.4046.360
THE RESPIRATORY FUNCTION OF THE BLOOD OF MARINE FISHES, The Biological Bulletin, vol.61, issue.3, pp.427-456, 1931. ,
DOI : 10.2307/1536959
Spectral changes and allosteric transition in trout haemoglobin, Nature, vol.13, issue.5520, pp.761-762, 1975. ,
DOI : 10.1038/256761a0
C NMR, FEBS Letters, vol.71, issue.2, pp.157-160, 1976. ,
DOI : 10.1016/0014-5793(76)80042-7
The buoyancy of fish and cephalophods, Prog Biophys Biophys Chem, vol.11, pp.177-234, 1961. ,
Rate of allosteric change in hemoglobin measured by modulated excitation using fluorescence detection, Biophysical Journal, vol.56, issue.4, pp.781-794, 1989. ,
DOI : 10.1016/S0006-3495(89)82725-0
[5] Optical measurements of quaternary structural changes in hemoglobin, Methods Enzymol, vol.232, pp.56-71, 1994. ,
DOI : 10.1016/0076-6879(94)32043-8
Novel Mechanisms of pH Sensitivity in Tuna Hemoglobin: A STRUCTURAL EXPLANATION OF THE ROOT EFFECT, Journal of Biological Chemistry, vol.279, issue.27, pp.28632-28640, 2004. ,
DOI : 10.1074/jbc.M401740200
Stereochemistry of cooperative effects in fish and amphibian haemoglobins, Nature, vol.237, issue.5882, pp.421-426, 1982. ,
DOI : 10.1038/299421a0
Haemoglobin of the Antarctic fish Pagothenia bernacchii, Journal of Molecular Biology, vol.224, issue.2, pp.449-460, 1992. ,
DOI : 10.1016/0022-2836(92)91007-C
Structural basis for the Root effect in haemoglobin, Nature Structural Biology, vol.102, issue.3, pp.275-283, 1996. ,
DOI : 10.1016/0263-7855(92)80022-6
Distal residues in the oxygen binding site of haemoglobin studied by protein engineering, Nature, vol.329, issue.6142, pp.858-860, 1987. ,
DOI : 10.1038/329858a0
The role of the distal histidine in myoglobin and haemoglobin, Nature, vol.336, issue.6196, pp.265-266, 1988. ,
DOI : 10.1038/336265a0
Distal Histidine Stabilizes Bound O2 and Acts as a Gate for Ligand Entry in Both Subunits of Adult Human Hemoglobin, Journal of Biological Chemistry, vol.285, issue.12, pp.8840-8854, 2010. ,
DOI : 10.1074/jbc.M109.053934
Comparative physiology in high altitudes, Journal of Cellular and Comparative Physiology, vol.110, issue.3, pp.301-313, 1936. ,
DOI : 10.1002/jcp.1030080302
Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering., Proceedings of the National Academy of Sciences, vol.88, issue.15, pp.6519-6522, 1991. ,
DOI : 10.1073/pnas.88.15.6519
The crystal structure of bar-headed goose hemoglobin in deoxy form: the allosteric mechanism of a hemoglobin species with high oxygen affinity, Journal of Molecular Biology, vol.313, issue.1, pp.123-137, 2001. ,
DOI : 10.1006/jmbi.2001.5028
Avian haemoglobins and structural basis of high affinity for oxygen: structure of bar-headed goose aquomet haemoglobin, Acta Crystallographica Section D Biological Crystallography, vol.57, issue.6, pp.775-783, 2001. ,
DOI : 10.1107/S0907444901004243
The Crystal Structure of a High Oxygen Affinity Species of Haemoglobin (Bar-headed Goose Haemoglobin in the Oxy Form), Journal of Molecular Biology, vol.255, issue.3, pp.484-493, 1996. ,
DOI : 10.1006/jmbi.1996.0040
Phylogenetic and structural analysis of the HbA (alphaA/betaA) and HbD (alphaD/betaA) hemoglobin genes in two high-altitude waterfowl from the Himalayas and the Andes: bar-headed goose (Anser indicus) and Andean goose, 2010. ,
High-Altitude Respiration of Geese. The Primary Structures of the Major and Minor Hemoglobin-Components of Adult Andean Goose (Chloephaga melanoptera, Anatidae): the Mutation Leu ??? Ser in Position 55 of the ??-Chains, Biological Chemistry Hoppe-Seyler, vol.368, issue.2, pp.1559-1569, 1987. ,
DOI : 10.1515/bchm3.1987.368.2.1559
High-altitude adaptations in vertebrate hemoglobins, Respiratory Physiology & Neurobiology, vol.158, issue.2-3, pp.132-142, 2007. ,
DOI : 10.1016/j.resp.2007.05.001
Selective oxidation of methionine b(55)D6 at the a 1 b 1 interface in hemoglobin completely destabilizes the T-state, J Biol Chem, vol.264, pp.17745-17749, 1989. ,
ON THE COOPERATIVITY OF BIOLOGICAL MEMBRANES, Proceedings of the National Academy of Sciences, vol.57, issue.2, pp.335-341, 1967. ,
DOI : 10.1073/pnas.57.2.335
Allosteric Receptors after 30 Years, Neuron, vol.21, issue.5, pp.959-980, 1998. ,
DOI : 10.1016/S0896-6273(00)80616-9
URL : http://dx.doi.org/10.1016/s0896-6273(00)80616-9
A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family, Nature, vol.98, issue.7123, pp.116-119, 2007. ,
DOI : 10.1038/nature05371
URL : https://hal.archives-ouvertes.fr/hal-00122527
The role of dynamic conformational ensembles in biomolecular recognition, Nature Chemical Biology, vol.12, issue.11, pp.789-796, 2009. ,
DOI : 10.1002/prot.22223
Allostery and cooperativity revisited, Protein Science, vol.326, issue.8, pp.1295-1307, 2008. ,
DOI : 10.1110/ps.03259908
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2492820
Nothing in biology makes sense except in the light of evolution, Am Biol Teach, vol.35, pp.125-129, 1973. ,