Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Martín, Hugo"'
Autor:
Martín, Hugo, Alejandra, Martínez, Madia, Trujillo, Damián, Estrada, Mauricio, Mastrogiovanni, Edlaine, Linares, Ohara, Augusto, Federico, Issoglio, Ari, Zeida, Darío A, Estrín, Harry F G, Heijnen, Lucía, Piacenza, Rafael, Radi
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 114(8)
Trypanosoma cruzi, the causative agent of Chagas disease, affects 8–10 million people in Latin America. Parasite antioxidant systems are essential for parasite survival and infectivity in the vertebrate host. Herein, we characterized the enzymic pr
Autor:
Ohara Augusto, Madia Trujillo, Ari Zeida, Martín Hugo, Edlaine Linares, Damián Estrada, Alejandra Martínez, Mauricio Mastrogiovanni, Harry F. G. Heijnen, Lucía Piacenza, Federico Issoglio, Rafael Radi, Darío A. Estrin
Publikováno v:
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Universidade de São Paulo (USP)
instacron:USP
The Trypanosoma cruzi ascorbate peroxidase is, by sequence analysis, a hybrid type A member of class I heme peroxidases [TcAPx-cytochrome c peroxidase (CcP)], suggesting both ascorbate (Asc) and cytochrome c (Cc) peroxidase activity. Here, we show th
Autor:
Thiago Geronimo Pires Alegria, Napoleão Fonseca Valadares, Ohara Augusto, Paolo Di Mascio, Raphael Ferreira Queiroz, José Renato Rosa Cussiol, Rafael Radi, Richard Charles Garratt, Sayuri Miyamoto, Madia Trujillo, Martín Hugo, Diogo de Abreu Meireles, Marcos Antonio de Oliveira, Luis Eduardo Soares Netto
Publikováno v:
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Universidade de São Paulo (USP)
instacron:USP
Organic hydroperoxide resistance (Ohr) enzymes are unique Cys-based, lipoyl-dependent peroxidases. Here, we investigated the involvement of Ohr in bacterial responses toward distinct hydroperoxides. In silico results indicated that fatty acid (but no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::121c48fff0ad4536a75d4d8cf1563254
Autor:
Madia Trujillo, Carlos Batthyány, Bruno Manta, Ana Denicola, Magdalena Gil, Lía M. Randall, Martín Hugo, Leslie B. Poole
Publikováno v:
Journal of Biological Chemistry. 289:15536-15543
Peroxiredoxins (Prx) are efficient thiol-dependent peroxidases and key players in the mechanism of H2O2-induced redox signaling. Any structural change that could affect their redox state, oligomeric structure, and/or interaction with other proteins c
Autor:
Diego S. Vazquez, Madia Trujillo, Martín Hugo, Rafael Radi, Javier Santos, Darío A. Estrin, María Inés De Armas, M. Dolores Piñeyro, Aníbal M. Reyes, Ari Zeida
Publikováno v:
Advances in Free Radical Biology & Medicine
Advances in Free Radical Biology & Medicine, Elsevier, 2015, 101, pp.249-260. ⟨10.1016/j.freeradbiomed.2016.10.005⟩
Advances in Free Radical Biology & Medicine, Elsevier, 2015, 101, pp.249-260. ⟨10.1016/j.freeradbiomed.2016.10.005⟩
Mycobacterium tuberculosis (M. tuberculosis) is the intracellular bacterium responsible for tuberculosis disease (TD). Inside the phagosomes of activated macrophages, M. tuberculosis is exposed to cytotoxic hydroperoxides such as hydrogen peroxide, f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::042d66280e8ec1abf7a3e210176328d6
https://www.sciencedirect.com/science/article/pii/S0891584916304476
https://www.sciencedirect.com/science/article/pii/S0891584916304476
Autor:
Aníbal M. Reyes, Madia Trujillo, Pablo Lichtig, Darío A. Estrin, F. Luis González Flecha, Rafael Radi, Martín Hugo, Diego S. Vazquez, Javier Santos, Ari Zeida
Peroxiredoxins (Prxs) constitute a ubiquitous family of Cys-dependent peroxidases that play essential roles in reducing hydrogen peroxide, peroxynitrite and organic hydroperoxides in almost all organisms. Members of the Prx subfamilies show different
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58889b2a5eb4c09c34b8d4cd80d02415
Publikováno v:
Archives of Biochemistry and Biophysics. 484:146-154
Peroxiredoxin 2 (Prx2) is a 2-Cys peroxiredoxin extremely abundant in the erythrocyte. The peroxidase activity was studied in a steady-state approach yielding an apparent K(M) of 2.4 microM for human thioredoxin and a very low K(M) for H2O2 (0.7 micr
Autor:
Joris Messens, Koen Van Laer, Aníbal M. Reyes, Didier Vertommen, Rafael Radi, Martín Hugo, Madia Trujillo
Mycobacterium tuberculosis (M. tuberculosis), the pathogen responsible for tuberculosis, detoxifies cytotoxic peroxides produced by activated macrophages. M. tuberculosis expresses alkyl hydroxyperoxide reductase E (AhpE), among other peroxiredoxins.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e97601bb66d8ade0da5acc2f860a76a3
https://biblio.vub.ac.be/vubir/mycothiolmycoredoxin-1dependent-reduction-of-the-peroxiredoxin-ahpe-from-mycobacterium-tuberculosis(8e448b93-f224-43f7-af46-eec26f4456c5).html
https://biblio.vub.ac.be/vubir/mycothiolmycoredoxin-1dependent-reduction-of-the-peroxiredoxin-ahpe-from-mycobacterium-tuberculosis(8e448b93-f224-43f7-af46-eec26f4456c5).html
Autor:
Gunnar Wingsle, Vaibhav Srivastava, Madia Trujillo, Martín Hugo, Rafael Radi, Benjamin Selles, Nicolas Rouhier, Jean-Pierre Jacquot
Publikováno v:
The Biochemical journal
The Biochemical journal, 2012, 442 (2), pp.369-380. ⟨10.1042/BJ20111378⟩
Biochemical Journal
Biochemical Journal, Portland Press, 2012, 442 (2), pp.369-380. ⟨10.1042/BJ20111378⟩
The Biochemical journal, 2012, 442 (2), pp.369-380. ⟨10.1042/BJ20111378⟩
Biochemical Journal
Biochemical Journal, Portland Press, 2012, 442 (2), pp.369-380. ⟨10.1042/BJ20111378⟩
Gpxs (glutathione peroxidases) constitute a family of peroxidases, including selenocysteine- or cysteine-containing isoforms (SeCys-Gpx or Cys-Gpx), which are regenerated by glutathione or Trxs (thioredoxins) respectively. In the present paper we sho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b99eeb1d93986c76c65d537045a688bc
https://hal.archives-ouvertes.fr/hal-01268025
https://hal.archives-ouvertes.fr/hal-01268025