Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Valérie Van der Eecken"'
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:
Mitochondrion. 11:973-981
Peroxiredoxin 5 (PRDX5) is a thioredoxin peroxidase able to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. In human, PRDX5 was reported to be localized in the cytosol, the mitochondria, the peroxisomes and the nucleus. Mitochondria
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::537573aa9e892cf85223e6754b490567
https://doi.org/10.1016/j.mito.2011.06.013
https://doi.org/10.1016/j.mito.2011.06.013
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:
Sub-cellular biochemistry. 44
Peroxiredoxins compose a superfamily of peroxidases ubiquitously found throughout evolution in prokaryotes, archaea and eukaryotes. These enzymes contain a conserved catalytic peroxidatic cysteine (Cp) in the N-terminal region of the protein. The res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::72b7f3ad3ff76ea3bdfd84f45cb07e4f
https://pubmed.ncbi.nlm.nih.gov/18084888
https://pubmed.ncbi.nlm.nih.gov/18084888
Publikováno v:
Subcellular Biochemistry ISBN: 9781402060502
Peroxiredoxins compose a superfamily of peroxidases ubiquitously found throughout evolution in prokaryotes, archaea and eukaryotes. These enzymes contain a conserved catalytic peroxidatic cysteine (Cp) in the N-terminal region of the protein. The res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1c9cd79cc4e023fee521d802092676d8
https://doi.org/10.1007/978-1-4020-6051-9_2
https://doi.org/10.1007/978-1-4020-6051-9_2
Autor:
Valérie Van der Eecken, André Clippe, Jehanne Berck, Elee Duconseille, Alfred Bernard, C Boone, Bernard Knoops, Ingrid Banmeyer, Nhu Tiên Nguyên-nhu, H. Cherif
Publikováno v:
Biochimica et biophysica acta. 1769(7-8)
Peroxiredoxin 5 (PRDX5) is a mammalian thioredoxin peroxidase ubiquitously expressed in tissues. Its role as antioxidant enzyme has been previously supported in different pathological situations. In this study, we determined the complete human PRDX5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5154cde9f08fc00176f7c98201353843
https://pubmed.ncbi.nlm.nih.gov/17628720
https://pubmed.ncbi.nlm.nih.gov/17628720
Publikováno v:
Antioxidants & Redox Signaling; Aug2011, Vol. 15 Issue 3, p817-829, 13p