(en) Jean Lamy, Josette Lamy, Joseph Bonaventura et Celia Bonaventura, « Structure, function, and assembly in the hemocyanin system of the scorpion Androctonus australis », Biochemistry, vol. 19, no 13, , p. 3033-3039 (PMID7397116, DOI10.1021/bi00554a031, lire en ligne)
(en) Heinz Decker et Felix Tuczek, « Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism », Trends in Biochemical Sciences, vol. 25, no 8, , p. 392-397 (PMID10916160, DOI10.1016/S0968-0004(00)01602-9, lire en ligne)
doi.org
dx.doi.org
(en) Christopher J. Coates et Jacqueline Nairn, « Diverse immune functions of hemocyanins », Developmental & Comparative Immunology, vol. 45, no 1, , p. 43-55 (PMID24486681, DOI10.1016/j.dci.2014.01.021, lire en ligne)
(en) N. S. Rannulu et M. T. Rodgers, « Solvation of copper ions by imidazole: Structures and sequential binding energies of Cu+(imidazole)x, x = 1–4. Competition between ion solvation and hydrogen bonding », Physical Chemistry Chemical Physics, vol. 7, no 5, , p. 1014-1025 (PMID19791394, DOI10.1039/B418141G, Bibcode2005PCCP....7.1014R, lire en ligne)
(en) Anneli Strobel, Marian Y. A. Hu, Magalena A. Gutowska, Bernhard Lieb, Magnus Lucassen, Frank Melzner, Hans O. Pörtner et Felix C. Mark, « Influence of Temperature, Hypercapnia, and Development on the Relative Expression of Different Hemocyanin Isoforms in the Common Cuttlefish Sepia officinalis », Journal of Experimental Zoology. Part A, Ecological Genetics and Physiology, vol. 317, no 8, décembre, p. 2012 (PMID22791630, DOI10.1002/jez.1743, lire en ligne)
(en) Jean Lamy, Josette Lamy, Joseph Bonaventura et Celia Bonaventura, « Structure, function, and assembly in the hemocyanin system of the scorpion Androctonus australis », Biochemistry, vol. 19, no 13, , p. 3033-3039 (PMID7397116, DOI10.1021/bi00554a031, lire en ligne)
(en) Felix de Haas et Ernst F.J. van Bruggen, « The Interhexameric Contacts in the Four-hexameric Hemocyanin from the Tarantula Eurypelma californicum: A Tentative Mechanism for Cooperative Behavior », Journal of Molecular Biology, vol. 237, no 4, , p. 464-478 (PMID8151706, DOI10.1006/jmbi.1994.1248, lire en ligne)
(en) Frank G. Perton, Jaap J. Beintema et Heinz Decker, « Influence of antibody binding on oxygen binding behavior of Panulirus interruptus hemocyanin », FEBS Letters, vol. 408, no 2, , p. 124-126 (PMID9187351, DOI10.1016/S0014-5793(97)00269-X, lire en ligne)
(en) Heinz Decker et Felix Tuczek, « Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism », Trends in Biochemical Sciences, vol. 25, no 8, , p. 392-397 (PMID10916160, DOI10.1016/S0968-0004(00)01602-9, lire en ligne)
(en) Heinz Decker, Thorsten Schweikardt, Dorothea Nillius, Uwe Salzbrunn, Elmar Jaenicke et Felix Tuczek, « Similar enzyme activation and catalysis in hemocyanins and tyrosinases », Gene, vol. 398, nos 1-2, , p. 183-191 (PMID17566671, DOI10.1016/j.gene.2007.02.051, lire en ligne)
(en) David W. McFadden, Dale R. Riggs, Barbara J. Jackson et Linda Vona-Davis, « Keyhole limpet hemocyanin, a novel immune stimulant with promising anticancer activity in Barrett's esophageal adenocarcinoma », The American Journal of Surgery, vol. 186, no 5, , p. 552-555 (PMID14599624, DOI10.1016/j.amjsurg.2003.08.002, lire en ligne)
harvard.edu
ui.adsabs.harvard.edu
(en) N. S. Rannulu et M. T. Rodgers, « Solvation of copper ions by imidazole: Structures and sequential binding energies of Cu+(imidazole)x, x = 1–4. Competition between ion solvation and hydrogen bonding », Physical Chemistry Chemical Physics, vol. 7, no 5, , p. 1014-1025 (PMID19791394, DOI10.1039/B418141G, Bibcode2005PCCP....7.1014R, lire en ligne)
jbc.org
(en) L. Waxman, « The structure of arthropod and mollusc hemocyanins », Journal of Biological Chemistry, vol. 250, no 10, , p. 3796-3806 (PMID1126935, lire en ligne)
nih.gov
ncbi.nlm.nih.gov
(en) Christopher J. Coates et Jacqueline Nairn, « Diverse immune functions of hemocyanins », Developmental & Comparative Immunology, vol. 45, no 1, , p. 43-55 (PMID24486681, DOI10.1016/j.dci.2014.01.021, lire en ligne)
(en) N. S. Rannulu et M. T. Rodgers, « Solvation of copper ions by imidazole: Structures and sequential binding energies of Cu+(imidazole)x, x = 1–4. Competition between ion solvation and hydrogen bonding », Physical Chemistry Chemical Physics, vol. 7, no 5, , p. 1014-1025 (PMID19791394, DOI10.1039/B418141G, Bibcode2005PCCP....7.1014R, lire en ligne)
(en) Anneli Strobel, Marian Y. A. Hu, Magalena A. Gutowska, Bernhard Lieb, Magnus Lucassen, Frank Melzner, Hans O. Pörtner et Felix C. Mark, « Influence of Temperature, Hypercapnia, and Development on the Relative Expression of Different Hemocyanin Isoforms in the Common Cuttlefish Sepia officinalis », Journal of Experimental Zoology. Part A, Ecological Genetics and Physiology, vol. 317, no 8, décembre, p. 2012 (PMID22791630, DOI10.1002/jez.1743, lire en ligne)
(en) L. Waxman, « The structure of arthropod and mollusc hemocyanins », Journal of Biological Chemistry, vol. 250, no 10, , p. 3796-3806 (PMID1126935, lire en ligne)
(en) Nobuo Makino, « Hemocyanin from Tachypleus gigas. I. Oxygen-Binding Properties », Journal of Biochemistry, vol. 106, no 3, , p. 418-422 (PMID2606894, lire en ligne)
(en) Nobuo Makino, « Hemocyanin from Tachypleus gigas. II. Cooperative Interactions of the Subunits », Journal of Biochemistry, vol. 106, no 3, , p. 423-429 (PMID2606895, lire en ligne)
(en) Jean Lamy, Josette Lamy, Joseph Bonaventura et Celia Bonaventura, « Structure, function, and assembly in the hemocyanin system of the scorpion Androctonus australis », Biochemistry, vol. 19, no 13, , p. 3033-3039 (PMID7397116, DOI10.1021/bi00554a031, lire en ligne)
(en) Felix de Haas et Ernst F.J. van Bruggen, « The Interhexameric Contacts in the Four-hexameric Hemocyanin from the Tarantula Eurypelma californicum: A Tentative Mechanism for Cooperative Behavior », Journal of Molecular Biology, vol. 237, no 4, , p. 464-478 (PMID8151706, DOI10.1006/jmbi.1994.1248, lire en ligne)
(en) Frank G. Perton, Jaap J. Beintema et Heinz Decker, « Influence of antibody binding on oxygen binding behavior of Panulirus interruptus hemocyanin », FEBS Letters, vol. 408, no 2, , p. 124-126 (PMID9187351, DOI10.1016/S0014-5793(97)00269-X, lire en ligne)
(en) Heinz Decker et Felix Tuczek, « Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism », Trends in Biochemical Sciences, vol. 25, no 8, , p. 392-397 (PMID10916160, DOI10.1016/S0968-0004(00)01602-9, lire en ligne)
(en) Heinz Decker, Thorsten Schweikardt, Dorothea Nillius, Uwe Salzbrunn, Elmar Jaenicke et Felix Tuczek, « Similar enzyme activation and catalysis in hemocyanins and tyrosinases », Gene, vol. 398, nos 1-2, , p. 183-191 (PMID17566671, DOI10.1016/j.gene.2007.02.051, lire en ligne)
(en) David W. McFadden, Dale R. Riggs, Barbara J. Jackson et Linda Vona-Davis, « Keyhole limpet hemocyanin, a novel immune stimulant with promising anticancer activity in Barrett's esophageal adenocarcinoma », The American Journal of Surgery, vol. 186, no 5, , p. 552-555 (PMID14599624, DOI10.1016/j.amjsurg.2003.08.002, lire en ligne)
oxfordjournals.org
jb.oxfordjournals.org
(en) Nobuo Makino, « Hemocyanin from Tachypleus gigas. I. Oxygen-Binding Properties », Journal of Biochemistry, vol. 106, no 3, , p. 418-422 (PMID2606894, lire en ligne)
(en) Nobuo Makino, « Hemocyanin from Tachypleus gigas. II. Cooperative Interactions of the Subunits », Journal of Biochemistry, vol. 106, no 3, , p. 423-429 (PMID2606895, lire en ligne)
(en) N. S. Rannulu et M. T. Rodgers, « Solvation of copper ions by imidazole: Structures and sequential binding energies of Cu+(imidazole)x, x = 1–4. Competition between ion solvation and hydrogen bonding », Physical Chemistry Chemical Physics, vol. 7, no 5, , p. 1014-1025 (PMID19791394, DOI10.1039/B418141G, Bibcode2005PCCP....7.1014R, lire en ligne)
sciencedirect.com
(en) Christopher J. Coates et Jacqueline Nairn, « Diverse immune functions of hemocyanins », Developmental & Comparative Immunology, vol. 45, no 1, , p. 43-55 (PMID24486681, DOI10.1016/j.dci.2014.01.021, lire en ligne)
(en) Felix de Haas et Ernst F.J. van Bruggen, « The Interhexameric Contacts in the Four-hexameric Hemocyanin from the Tarantula Eurypelma californicum: A Tentative Mechanism for Cooperative Behavior », Journal of Molecular Biology, vol. 237, no 4, , p. 464-478 (PMID8151706, DOI10.1006/jmbi.1994.1248, lire en ligne)
(en) Heinz Decker, Thorsten Schweikardt, Dorothea Nillius, Uwe Salzbrunn, Elmar Jaenicke et Felix Tuczek, « Similar enzyme activation and catalysis in hemocyanins and tyrosinases », Gene, vol. 398, nos 1-2, , p. 183-191 (PMID17566671, DOI10.1016/j.gene.2007.02.051, lire en ligne)
(en) David W. McFadden, Dale R. Riggs, Barbara J. Jackson et Linda Vona-Davis, « Keyhole limpet hemocyanin, a novel immune stimulant with promising anticancer activity in Barrett's esophageal adenocarcinoma », The American Journal of Surgery, vol. 186, no 5, , p. 552-555 (PMID14599624, DOI10.1016/j.amjsurg.2003.08.002, lire en ligne)
(en) Anneli Strobel, Marian Y. A. Hu, Magalena A. Gutowska, Bernhard Lieb, Magnus Lucassen, Frank Melzner, Hans O. Pörtner et Felix C. Mark, « Influence of Temperature, Hypercapnia, and Development on the Relative Expression of Different Hemocyanin Isoforms in the Common Cuttlefish Sepia officinalis », Journal of Experimental Zoology. Part A, Ecological Genetics and Physiology, vol. 317, no 8, décembre, p. 2012 (PMID22791630, DOI10.1002/jez.1743, lire en ligne)
(en) Frank G. Perton, Jaap J. Beintema et Heinz Decker, « Influence of antibody binding on oxygen binding behavior of Panulirus interruptus hemocyanin », FEBS Letters, vol. 408, no 2, , p. 124-126 (PMID9187351, DOI10.1016/S0014-5793(97)00269-X, lire en ligne)