Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Martina, Zederbauer"'
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 33, Iss 1, Pp 1529-1536 (2018)
There is an increasing interest in developing novel eosinophil peroxidase (EPO) inhibitors, in order to provide new treatment strategies against chronic inflammatory and neurodegenerative diseases caused by eosinophilic disorder. Within this study, a
Externí odkaz:
https://doaj.org/article/fbffca2cf5c94eb8b384f2e2d5caa111
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 33, Iss 1, Pp 1529-1536 (2018)
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 33, Iss 1, Pp 1529-1536 (2018)
There is an increasing interest in developing novel eosinophil peroxidase (EPO) inhibitors, in order to provide new treatment strategies against chronic inflammatory and neurodegenerative diseases caused by eosinophilic disorder. Within this study, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d273d90c47b643fed424b4236728abb
https://doi.org/10.1080/14756366.2018.1512598
https://doi.org/10.1080/14756366.2018.1512598
Autor:
Martina Zederbauer, Christa Jakopitsch, Johanna Stampler, Nicole Moguilevsky, Paul G. Furtmüller, Marzia Bellei, Christian Obinger, Gianantonio Battistuzzi
Publikováno v:
Journal of Biological Chemistry. 282:17041-17052
In human heme peroxidases the prosthetic group is covalently attached to the protein via two ester linkages between conserved glutamate and aspartate residues and modified methyl groups on pyrrole rings A and C. Here, monomeric recombinant myeloperox
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85053238285fe522eb8a89d70bcd84ae
https://doi.org/10.1074/jbc.m610685200
https://doi.org/10.1074/jbc.m610685200
Autor:
Martina Zederbauer, Paul G. Furtmüller, Marzia Bellei, Gianantonio Battistuzzi, Christian Obinger, Marco Sola
Publikováno v:
Biochemistry. 45:12750-12755
Myeloperoxidase (MPO) (donor, hydrogen peroxide oxidoreductase, EC 1.11.1.7) is the most abundant neutrophil enzyme and catalyzes predominantly the two-electron oxidation of ubiquitous chloride (Cl-), to generate the potent bleaching oxidant hypochlo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf4fb527a7ce8075532eb81ee04ed6e2
https://doi.org/10.1021/bi061647k
https://doi.org/10.1021/bi061647k
Autor:
Jürgen Arnhold, Enrico Monzani, Martina Zederbauer, Luigi Casella, Christian Obinger, Paul G. Furtmüller
Publikováno v:
European Journal of Inorganic Chemistry. 2006:3801-3811
The human heme peroxidases myeloperoxidase (MPO),eosinophil peroxidase (EPO) and lactoperoxidase (LPO) are able to oxidise (pseudo)halides and nitrite to reactive species that participate in host defence against foreign microorganisms as well as in i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eae1e92fa786e43c394553084fe2b38b
https://doi.org/10.1002/ejic.200600436
https://doi.org/10.1002/ejic.200600436
Autor:
Martina Zederbauer, Silvia Brogioni, Alessandro Feis, Christian Obinger, Mario P. Marzocchi, Giulietta Smulevich, Paul G. Furtmüller
Publikováno v:
Journal of Raman Spectroscopy. 37:263-276
Resonance Raman (RR) spectra have been acquired for human myeloperoxidase (MPO), and its Met243Thr and Asp94Val mutants with different excitation wavelengths and in polarized light. The proteins were characterized as ferric, ferrous and ferric–CN c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b01ca552da7c7fe102f9e7fc5670af9
https://doi.org/10.1002/jrs.1442
https://doi.org/10.1002/jrs.1442
Autor:
Christa Jakopitsch, Christian Obinger, Paul G. Furtmüller, Jutta Helm, Walter Jantschko, Martin Bogner, Martina Zederbauer
Publikováno v:
Archives of Biochemistry and Biophysics. 445:199-213
Myeloperoxidase (MPO), eosinophil peroxidase, lactoperoxidase, and thyroid peroxidase are heme-containing oxidoreductases (EC 1.7.1.11), which bind ligands and/or undergo a series of redox reactions. Though sharing functional and structural homology,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22bd967646e2ddb5b684c84d74df8576
https://doi.org/10.1016/j.abb.2005.09.017
https://doi.org/10.1016/j.abb.2005.09.017
Autor:
Martina Zederbauer, Jürgen Arnhold, Christa Jakopitsch, Walter Jantschko, Paul G. Furtmüller, Christian Obinger
Publikováno v:
Journal of Inorganic Biochemistry. 99:1220-1229
Lactoperoxidase (LPO) is found in mucosal surfaces and exocrine secretions including milk, tears and saliva and has physiological significance in antimicrobial defense. Its predominant physiological role is to convert hydrogen peroxide and thiocyanat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60666bbf5a8e341e7c8ef5f509bf1c37
https://doi.org/10.1016/j.jinorgbio.2005.02.021
https://doi.org/10.1016/j.jinorgbio.2005.02.021
Autor:
Paul G. Furtmüller, Martina Zederbauer, Karin Neugschwandtner, Christian Obinger, Christa Jakopitsch, Walter Jantschko, Nicole Moguilevsky
Publikováno v:
Biochemistry. 44:6482-6491
In human myeloperoxidase the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu242 and Asp94 and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8253d5159531614d2684a1b01e89f73
https://doi.org/10.1021/bi0501737
https://doi.org/10.1021/bi0501737
Autor:
Paul G. Furtmüller, Martina Zederbauer, Giulietta Smulevich, Silvia Brogioni, Christian Obinger, Christa Jakopitsch
Publikováno v:
ChemInform. 38
Covering: 1966 to 2007The mammalian peroxidases myeloperoxidase, eosinophil peroxidase, lactoperoxidase and thyroid peroxidase participate in host defense against infection, hormone synthesis and pathogenesis. The most striking feature of these heme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0e9f43dc9c885cacc58e9f5d53762ce
https://doi.org/10.1002/chin.200736272
https://doi.org/10.1002/chin.200736272