Zobrazeno 1 - 7
of 7
pro vyhledávání: '"genetics [Glutathione Peroxidase]"'
Autor:
Martin Jastroch, Florencio Porto Freitas, Carsten Berndt, Daniel Lamp, Marcus Conrad, Antonella Roveri, Sabine Schmitt, Ulrich Schweizer, Lisa Mehr, Wolfgang Wurst, Fulvio Ursini, Axel Walch, Katalin Buday, Elias S.J. Arnér, Tobias Seibt, Xiaoxiao Peng, Sebastian Doll, José Pedro Friedmann Angeli, Noelia Fradejas-Villar, Michaela Aichler, Irina Ingold, Gereon Poschmann, Sayuri Miyamoto, Hans Zischka
Publikováno v:
Cell 172, 409–422.e21 (2018)
Cell 172(3), 409-422.e21 (2018). doi:10.1016/j.cell.2017.11.048
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Cell 172(3), 409-422.e21 (2018). doi:10.1016/j.cell.2017.11.048
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Selenoproteins are rare proteins among all kingdoms of life containing the 21 st amino acid, selenocysteine. Selenocysteine resembles cysteine, differing only by the substitution of selenium for sulfur. Yet the actual advantage of selenolate- versus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b35109d677be425e4813bd942813598d
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=52658
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=52658
Autor:
Axel Walch, Irina Ingold, Antonella Roveri, Marcus Conrad, Katalin Buday, Michaela Aichler, Fulvio Ursini, Nils Hoffard, Wolfgang Wurst, Elena Yefremova, Adrianne Tasdemir, Sebastian Doll, José Pedro Friedmann Angeli
Publikováno v:
The journal of biological chemistry 290(23), 14668-14678 (2015). doi:10.1074/jbc.M115.656363
J. Biol. Chem. 290, 14668-14678 (2015)
J. Biol. Chem. 290, 14668-14678 (2015)
The selenoenzyme Gpx4 is essential for early embryogenesis and cell viability for its unique function to prevent phospholipid oxidation. Recently, the cytosolic form of Gpx4 was identified as an upstream regulator of a novel form of non-apoptotic cel
Publikováno v:
Journal of cellular physiology / Supplement 227(4), 1420-1427 (2012). doi:10.1002/jcp.22857
The nuclear isoform of the selenoprotein Phospholipid Hydroperoxide Glutathione Peroxidase (nGPx4) is expressed in haploid male germ cells, contains several cysteines and is able to oxidize protein thiols, besides glutathione. In this study we have i
Autor:
Heidi Förster, Rob Hooft van Huijsduijnen, Arne Östman, Pontus Aspenström, Åsa Sandin, Frank Böhmer, Alexander Seiler, Georg W. Bornkamm, Jeroen Frijhoff, Marcus Conrad, Olof Rådmark, Markus Dagnell
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America 107(36), 15774-15779 (2010). doi:10.1073/pnas.1007909107
Protein tyrosine phosphatases (PTPs) are regulated through reversible oxidation of the active-site cysteine. Previous studies have implied soluble reactive oxygen species (ROS), like H 2 O 2 , as the mediators of PTP oxidation. The potential role(s)
Autor:
Noblanc, Anaïs, Peltier, Manon, Damon-Soubeyrand, Christelle, Kerchkove, Nicolas, Chabory, Eléonore, Vernet, Patrick, Saez, Fabrice, Cadet, Rémi, Janny, Laurent, Pons-Rejraji, Hanae, Conrad, Marcus, Drevet, Joël, Kocer, Ayhan, Bishop, Alexander James Roy
Publikováno v:
PLoS ONE
PLoS ONE, Public Library of Science, 2012, 7 (6), pp.e38565. ⟨10.1371/journal.pone.0038565⟩
PLoS ONE, 2012, 7 (6), pp.e38565. ⟨10.1371/journal.pone.0038565⟩
PLoS ONE 7:e38565 (2012)
PLOS ONE 7(6), e38565 (2012). doi:10.1371/journal.pone.0038565
PLoS ONE, Vol 7, Iss 6, p e38565 (2012)
PLoS ONE, Public Library of Science, 2012, 7 (6), pp.e38565. ⟨10.1371/journal.pone.0038565⟩
PLoS ONE, 2012, 7 (6), pp.e38565. ⟨10.1371/journal.pone.0038565⟩
PLoS ONE 7:e38565 (2012)
PLOS ONE 7(6), e38565 (2012). doi:10.1371/journal.pone.0038565
PLoS ONE, Vol 7, Iss 6, p e38565 (2012)
We report here that spermatozoa of mice lacking both the sperm nucleus glutathione peroxidase 4 (snGPx4) and the epididymal glutathione peroxidase 5 (GPx5) activities display sperm nucleus structural abnormalities including delayed and defective nucl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2680fb2aef4c23e568eb5b6f0e9ad344
https://hal.archives-ouvertes.fr/hal-02083321
https://hal.archives-ouvertes.fr/hal-02083321
Publikováno v:
The FASEB journal 25(7), 2135-2144 (2011). doi:10.1096/fj.10-177147
Selenoproteins are expressed in many organisms, including bacteria, insects, fish, and mammals. Yet, it has remained obscure why some organisms rely on selenoproteins while others, like yeast and plants, express Cys-containing homologues. This study
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57fca697400939d36b4c4e1ee8debe04
http://hdl.handle.net/11577/157236
http://hdl.handle.net/11577/157236
Autor:
Ulrike Lichti, Andrew Ryscavage, Christophe Cataisson, Stuart H. Yuspa, Dolph L. Hatfield, Marcus Conrad, Susan M. Fischer, Bradley A. Carlson, Carol Mikulec, Aniruddha Sengupta
Publikováno v:
The journal of investigative dermatology 133(7), 1731-1741 (2013). doi:10.1038/jid.2013.52
J. Invest. Dermatol. 133, 1731-1741 (2013)
J. Invest. Dermatol. 133, 1731-1741 (2013)
Selenoproteins are essential molecules for the mammalian antioxidant network. We previously demonstrated that targeted loss of all selenoproteins in mouse epidermis disrupted skin and hair development, and caused premature death. In the current study