Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Julie Goemaere"'
Autor:
Valérie Van der Eecken, André Clippe, Sophie Dekoninck, Julie Goemaere, Geoffroy Walbrecq, Paul P Van Veldhoven, Bernard Knoops
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e72844 (2013)
In human, the subcellular targeting of peroxiredoxin-5 (PRDX5), a thioredoxin peroxidase, is dependent on the use of multiple alternative transcription start sites and two alternative in-frame translation initiation sites, which determine whether or
Externí odkaz:
https://doaj.org/article/9f52ae0204ed4aeda6bfb531b3e1eccb
Publikováno v:
Antioxidants & Redox Signaling. 15:817-829
Peroxiredoxin 5 (PRDX5) was the last member to be identified among the six mammalian peroxiredoxins. It is also the unique atypical 2-Cys peroxiredoxin in mammals. Like the other five members, PRDX5 is widely expressed in tissues but differs by its s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4205c5f0e2f9b39376f2fdfb873ef78
https://doi.org/10.1089/ars.2010.3584
https://doi.org/10.1089/ars.2010.3584
Publikováno v:
Neuroscience Letters. 433:219-224
Peroxiredoxins (PRDXs) are a family of peroxidases well conserved throughout evolution. Human PRDX3 and PRDX5, two mitochondrial PRDXs, have been implicated in several pathologies associated with oxidative stress. However, the individual role of PRDX
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25462497c4b5ed0d4360de65b8a9ea45
https://doi.org/10.1016/j.neulet.2007.12.068
https://doi.org/10.1016/j.neulet.2007.12.068
Autor:
André Clippe, Fadel Tissir, Marie-Thérèse Ahn, Julie Goemaere, Olivier Schakman, Charlotte Lefort, Christine Galant, Vasiliki Argyropoulou, Philippe Gailly, Yves Guiot, Bernard Knoops
Publikováno v:
Free Radical Biology and Medicine. 100:S92
Peroxiredoxins are a superfamily of peroxidases widely distributed among prokaryotes and eukaryotes. Peroxiredoxin-5 (Prdx5) is the last isoform identified and characterized among the six mammalian peroxiredoxins. Prdx5 is ubiquitously expressed in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eeb3daa1840325dcee4948c4f8a7512d
https://doi.org/10.1016/j.freeradbiomed.2016.10.229
https://doi.org/10.1016/j.freeradbiomed.2016.10.229
Publikováno v:
Journal of neurochemistry. 125(3)
Peroxiredoxin-5 (PRDX5) is an antioxidant enzyme which differs from the other peroxiredoxins with regards to its enzymatic mechanism, its high affinity for organic peroxides and peroxynitrite and its wide subcellular distribution. In particular, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f42ffc5319c8c89c4eef19bd438fbeb
https://pubmed.ncbi.nlm.nih.gov/23216451
https://pubmed.ncbi.nlm.nih.gov/23216451
Autor:
Bernard Knoops, Julie Goemaere
Publikováno v:
The Journal of comparative neurology. 520(2)
Redox changes are observed in neurodegenerative diseases, ranging from increased levels of reactive oxygen/nitrogen species and disturbance of antioxidant systems, to nitro-oxidative damage. By reducing hydrogen peroxide, peroxynitrite and organic hy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a94d315a580db87c6e6756bcac4124f7
https://pubmed.ncbi.nlm.nih.gov/21674491
https://pubmed.ncbi.nlm.nih.gov/21674491
Publikováno v:
Antioxidants & Redox Signaling; Aug2011, Vol. 15 Issue 3, p817-829, 13p