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pro vyhledávání: '"Martín, Hugo"'
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
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