(en) Martina Zederbauer, Paul G. Furtmüller, Silvia Brogioni, Christa Jakopitsch, Giulietta Smulevich et Christian Obinger, « Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties », Natural Product Reports, vol. 24, , p. 571-584 (PMID17534531, DOI10.1039/B604178G, lire en ligne)
(en) R. M. Ten, L. R. Pease, D. J. McKean, M. P. Bell et G. J. Gleich, « Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family », The Journal of Experimental Medicine, vol. 169, no 5, , p. 1757-1769 (PMID2541222, PMCID2189302, DOI10.1084/jem.169.5.1757, lire en ligne)
(en) Paul G. Furtmüller, Martina Zederbauer, Walter Jantschko, Jutta Helm, Martin Bogner, Christa Jakopitsch et Christian Obinger, « Active site structure and catalytic mechanisms of human peroxidases », Archives of Biochemistry and Biophysics, vol. 445, no 2, , p. 199-213 (PMID16288970, DOI10.1016/j.abb.2005.09.017, lire en ligne)
(en) De Gioia, Elena M. Ghibaudi, Enzo Laurenti, Mario Salmona et R. P. Ferrari, « A theoretical three-dimensional model for lactoperoxidase and eosinophil peroxidase, built on the scaffold of the myeloperoxidase X-ray structure », JBIC Journal of Biological Inorganic Chemistry, vol. 1, no 5, , p. 476-485 (DOI10.1007/s007750050081, lire en ligne)
(en) Christof Straub, Konrad Pazdrak, Travis W. Young, Susan J. Stafford, Zheng Wu, John E. Wiktorowicz, Anthony M. Haag, Robert D. English, Kizhake V. Soman et Alexander Kurosky, « Toward the proteome of the human peripheral blood eosinophil », Proteomics Clinical Applications, vol. 3, no 10, , p. 1151-1173 (PMID21048890, PMCID2967046, DOI10.1002/prca.200900043, lire en ligne)
(en) Martina Ulrich, Alina Petre, Nikolay Youhnovski, Franziska Prömm, Markus Schirle, Michael Schumm, Ralph S. Pero, Alfred Doyle, James Checkel, Hirohito Kita, Nethaji Thiyagarajan, K. Ravi Acharya, Peter Schmid-Grendelmeier, Hans-Uwe Simon, Heinz Schwarz, Masato Tsutsui, Hiroaki Shimokawa, Gabriel Bellon, James J. Lee, Michael Przybylski et Gerd Döring, « Post-translational Tyrosine Nitration of Eosinophil Granule Toxins Mediated by Eosinophil Peroxidase », Journal of Biological Chemistry, vol. 283, no 42, , p. 28629-28640 (PMID18694936, PMCID2661412, DOI10.1074/jbc.M801196200, lire en ligne)
jbc.org
(en) A. N. Mayeno, A. J. Curran, R. L. Roberts et C. S. Foote, « Eosinophils preferentially use bromide to generate halogenating agents », Journal of Biological Chemistry, vol. 264, no 10, , p. 5660-5668 (PMID2538427, lire en ligne)
(en) A. Slungaard et J. R. Mahoney, Jr, « Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity », Journal of Biological Chemistry, vol. 266, no 8, , p. 4903-4910 (PMID2002037, lire en ligne)
(en) Martina Ulrich, Alina Petre, Nikolay Youhnovski, Franziska Prömm, Markus Schirle, Michael Schumm, Ralph S. Pero, Alfred Doyle, James Checkel, Hirohito Kita, Nethaji Thiyagarajan, K. Ravi Acharya, Peter Schmid-Grendelmeier, Hans-Uwe Simon, Heinz Schwarz, Masato Tsutsui, Hiroaki Shimokawa, Gabriel Bellon, James J. Lee, Michael Przybylski et Gerd Döring, « Post-translational Tyrosine Nitration of Eosinophil Granule Toxins Mediated by Eosinophil Peroxidase », Journal of Biological Chemistry, vol. 283, no 42, , p. 28629-28640 (PMID18694936, PMCID2661412, DOI10.1074/jbc.M801196200, lire en ligne)
jimmunol.org
(en) M. G. Carlson, C. G. Peterson et P. Venge, « Human eosinophil peroxidase: purification and characterization », The Journal of Immunology, vol. 134, no 3, , p. 1875-1879 (PMID3918110, lire en ligne)
nih.gov
ncbi.nlm.nih.gov
(en) A. N. Mayeno, A. J. Curran, R. L. Roberts et C. S. Foote, « Eosinophils preferentially use bromide to generate halogenating agents », Journal of Biological Chemistry, vol. 264, no 10, , p. 5660-5668 (PMID2538427, lire en ligne)
(en) A. Slungaard et J. R. Mahoney, Jr, « Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity », Journal of Biological Chemistry, vol. 266, no 8, , p. 4903-4910 (PMID2002037, lire en ligne)
(en) Martina Zederbauer, Paul G. Furtmüller, Silvia Brogioni, Christa Jakopitsch, Giulietta Smulevich et Christian Obinger, « Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties », Natural Product Reports, vol. 24, , p. 571-584 (PMID17534531, DOI10.1039/B604178G, lire en ligne)
(en) R. M. Ten, L. R. Pease, D. J. McKean, M. P. Bell et G. J. Gleich, « Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family », The Journal of Experimental Medicine, vol. 169, no 5, , p. 1757-1769 (PMID2541222, PMCID2189302, DOI10.1084/jem.169.5.1757, lire en ligne)
(en) M. G. Carlson, C. G. Peterson et P. Venge, « Human eosinophil peroxidase: purification and characterization », The Journal of Immunology, vol. 134, no 3, , p. 1875-1879 (PMID3918110, lire en ligne)
(en) Paul G. Furtmüller, Martina Zederbauer, Walter Jantschko, Jutta Helm, Martin Bogner, Christa Jakopitsch et Christian Obinger, « Active site structure and catalytic mechanisms of human peroxidases », Archives of Biochemistry and Biophysics, vol. 445, no 2, , p. 199-213 (PMID16288970, DOI10.1016/j.abb.2005.09.017, lire en ligne)
(en) Christof Straub, Konrad Pazdrak, Travis W. Young, Susan J. Stafford, Zheng Wu, John E. Wiktorowicz, Anthony M. Haag, Robert D. English, Kizhake V. Soman et Alexander Kurosky, « Toward the proteome of the human peripheral blood eosinophil », Proteomics Clinical Applications, vol. 3, no 10, , p. 1151-1173 (PMID21048890, PMCID2967046, DOI10.1002/prca.200900043, lire en ligne)
(en) Martina Ulrich, Alina Petre, Nikolay Youhnovski, Franziska Prömm, Markus Schirle, Michael Schumm, Ralph S. Pero, Alfred Doyle, James Checkel, Hirohito Kita, Nethaji Thiyagarajan, K. Ravi Acharya, Peter Schmid-Grendelmeier, Hans-Uwe Simon, Heinz Schwarz, Masato Tsutsui, Hiroaki Shimokawa, Gabriel Bellon, James J. Lee, Michael Przybylski et Gerd Döring, « Post-translational Tyrosine Nitration of Eosinophil Granule Toxins Mediated by Eosinophil Peroxidase », Journal of Biological Chemistry, vol. 283, no 42, , p. 28629-28640 (PMID18694936, PMCID2661412, DOI10.1074/jbc.M801196200, lire en ligne)
rsc.org
pubs.rsc.org
(en) Martina Zederbauer, Paul G. Furtmüller, Silvia Brogioni, Christa Jakopitsch, Giulietta Smulevich et Christian Obinger, « Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties », Natural Product Reports, vol. 24, , p. 571-584 (PMID17534531, DOI10.1039/B604178G, lire en ligne)
rupress.org
jem.rupress.org
(en) R. M. Ten, L. R. Pease, D. J. McKean, M. P. Bell et G. J. Gleich, « Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family », The Journal of Experimental Medicine, vol. 169, no 5, , p. 1757-1769 (PMID2541222, PMCID2189302, DOI10.1084/jem.169.5.1757, lire en ligne)
sciencedirect.com
(en) Paul G. Furtmüller, Martina Zederbauer, Walter Jantschko, Jutta Helm, Martin Bogner, Christa Jakopitsch et Christian Obinger, « Active site structure and catalytic mechanisms of human peroxidases », Archives of Biochemistry and Biophysics, vol. 445, no 2, , p. 199-213 (PMID16288970, DOI10.1016/j.abb.2005.09.017, lire en ligne)
springer.com
link.springer.com
(en) De Gioia, Elena M. Ghibaudi, Enzo Laurenti, Mario Salmona et R. P. Ferrari, « A theoretical three-dimensional model for lactoperoxidase and eosinophil peroxidase, built on the scaffold of the myeloperoxidase X-ray structure », JBIC Journal of Biological Inorganic Chemistry, vol. 1, no 5, , p. 476-485 (DOI10.1007/s007750050081, lire en ligne)
wiley.com
onlinelibrary.wiley.com
(en) Christof Straub, Konrad Pazdrak, Travis W. Young, Susan J. Stafford, Zheng Wu, John E. Wiktorowicz, Anthony M. Haag, Robert D. English, Kizhake V. Soman et Alexander Kurosky, « Toward the proteome of the human peripheral blood eosinophil », Proteomics Clinical Applications, vol. 3, no 10, , p. 1151-1173 (PMID21048890, PMCID2967046, DOI10.1002/prca.200900043, lire en ligne)