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Recombinant peroxiredoxin 5 protects against excitotoxic brain lesions in newborn mice.
Plaisant F, Clippe A, Vander Stricht D, Knoops B, Gressens P. Plaisant F, et al. Among authors: clippe a. Free Radic Biol Med. 2003 Apr 1;34(7):862-72. doi: 10.1016/s0891-5849(02)01440-5. Free Radic Biol Med. 2003. PMID: 12654475
Peroxiredoxins are a family of peroxidases widely distributed in eukaryotes and prokaryotes. Peroxiredoxin 5 (PRDX5) is a recently discovered mammalian member of this family of antioxidant enzymes that is able to reduce hydrogen peroxide and alkyl hydroperoxides. .. …
Peroxiredoxins are a family of peroxidases widely distributed in eukaryotes and prokaryotes. Peroxiredoxin 5 (PRDX5) is a rece …
Cloning and characterization of Arenicola marina peroxiredoxin 6, an annelid two-cysteine peroxiredoxin highly homologous to mammalian one-cysteine peroxiredoxins.
Loumaye E, Andersen AC, Clippe A, Degand H, Dubuisson M, Zal F, Morsomme P, Rees JF, Knoops B. Loumaye E, et al. Among authors: clippe a. Free Radic Biol Med. 2008 Aug 15;45(4):482-93. doi: 10.1016/j.freeradbiomed.2008.04.033. Epub 2008 May 2. Free Radic Biol Med. 2008. PMID: 18503776
This intermediate is reduced by forming a disulfide bond either with a resolving Cys of another monomeric entity (typical 2-Cys) or of the same molecule (atypical 2-Cys). ...Thus, A. marina PRDX6 belongs to a transient group exhibiting sequence homolog …
This intermediate is reduced by forming a disulfide bond either with a resolving Cys of another monomeric entity (typical 2-Cy …
Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide.
Banmeyer I, Marchand C, Clippe A, Knoops B. Banmeyer I, et al. Among authors: clippe a. FEBS Lett. 2005 Apr 25;579(11):2327-33. doi: 10.1016/j.febslet.2005.03.027. FEBS Lett. 2005. PMID: 15848167
Peroxiredoxin 5 is a thioredoxin peroxidase ubiquitously expressed in mammalian tissues. Peroxiredoxin 5 can be addressed intracellularly to mitochondria, peroxisomes, the cytosol and the nucleus. ...
Peroxiredoxin 5 is a thioredoxin peroxidase ubiquitously expressed in mammalian tissues. Peroxiredoxin 5 can be addressed intracellul …
Human peroxiredoxin 5 is a peroxynitrite reductase.
Dubuisson M, Vander Stricht D, Clippe A, Etienne F, Nauser T, Kissner R, Koppenol WH, Rees JF, Knoops B. Dubuisson M, et al. Among authors: clippe a. FEBS Lett. 2004 Jul 30;571(1-3):161-5. doi: 10.1016/j.febslet.2004.06.080. FEBS Lett. 2004. PMID: 15280035
We report here that human peroxiredoxin 5 is also a peroxynitrite reductase. Analysis of peroxiredoxin 5 mutants, in which each of the cysteine residues was mutated, suggests that the nucleophilic attack on the O-O bond of peroxynitrite is performed by the N-terminal perox …
We report here that human peroxiredoxin 5 is also a peroxynitrite reductase. Analysis of peroxiredoxin 5 mutants, in which each of th …
Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution.
Declercq JP, Evrard C, Clippe A, Stricht DV, Bernard A, Knoops B. Declercq JP, et al. Among authors: clippe a. J Mol Biol. 2001 Aug 24;311(4):751-9. doi: 10.1006/jmbi.2001.4853. J Mol Biol. 2001. PMID: 11518528
We report here the 1.5 A resolution crystal structure of human PRDX5 in its reduced form. The crystal structure reveals that PRDX5 presents a thioredoxin-like domain. ...Moreover, the presence of a benzoate ion, a hydroxyl radical scavenger, was noted …
We report here the 1.5 A resolution crystal structure of human PRDX5 in its reduced form. The crystal structure reveals that PRDX5 pr …
Crystal structure of a dimeric oxidized form of human peroxiredoxin 5.
Evrard C, Capron A, Marchand C, Clippe A, Wattiez R, Soumillion P, Knoops B, Declercq JP. Evrard C, et al. Among authors: clippe a. J Mol Biol. 2004 Apr 9;337(5):1079-90. doi: 10.1016/j.jmb.2004.02.017. J Mol Biol. 2004. PMID: 15046979
Here, a new crystal form of human peroxiredoxin 5 is described at 2.0 A resolution. The asymmetric unit contains three polypeptide chains. ...The oxidized polypeptide chain forms an homodimer with a symmetry-related one through intermolecular disulfide bonds …
Here, a new crystal form of human peroxiredoxin 5 is described at 2.0 A resolution. The asymmetric unit contains three polypep …
Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family.
Knoops B, Clippe A, Bogard C, Arsalane K, Wattiez R, Hermans C, Duconseille E, Falmagne P, Bernard A. Knoops B, et al. Among authors: clippe a. J Biol Chem. 1999 Oct 22;274(43):30451-8. doi: 10.1074/jbc.274.43.30451. J Biol Chem. 1999. PMID: 10521424
Using two-dimensional electrophoresis, we have recently identified in human bronchoalveolar lavage fluid a novel protein, termed B166, with a molecular mass of 17 kDa. ...Indeed, the deduced amino acid sequence reveals that AOEB166 represents a new mammalian …
Using two-dimensional electrophoresis, we have recently identified in human bronchoalveolar lavage fluid a novel protein, termed B166 …
Deconstructing the catalytic efficiency of peroxiredoxin-5 peroxidatic cysteine.
Portillo-Ledesma S, Sardi F, Manta B, Tourn MV, Clippe A, Knoops B, Alvarez B, Coitiño EL, Ferrer-Sueta G. Portillo-Ledesma S, et al. Among authors: clippe a. Biochemistry. 2014 Sep 30;53(38):6113-25. doi: 10.1021/bi500389m. Epub 2014 Sep 18. Biochemistry. 2014. PMID: 25184942
Kinetic studies of peroxiredoxin 6 from Arenicola marina: rapid oxidation by hydrogen peroxide and peroxynitrite but lack of reduction by hydrogen sulfide.
Loumaye E, Ferrer-Sueta G, Alvarez B, Rees JF, Clippe A, Knoops B, Radi R, Trujillo M. Loumaye E, et al. Among authors: clippe a. Arch Biochem Biophys. 2011 Oct;514(1-2):1-7. doi: 10.1016/j.abb.2011.07.002. Epub 2011 Jul 13. Arch Biochem Biophys. 2011. PMID: 21767527
Its antioxidant systems include a cytosolic peroxiredoxin, peroxiredoxin 6 (AmPrx6 or AmPRDX6) that shows high homology to the mammalian 1-Cys peroxiredoxin. ...Our data indicate that in this annelid, Prx6 could contribute to peroxide detoxification in the presence of a
Its antioxidant systems include a cytosolic peroxiredoxin, peroxiredoxin 6 (AmPrx6 or AmPRDX6) that shows high homology to the mammal …
SOS response activation and competence development are antagonistic mechanisms in Streptococcus thermophilus.
Boutry C, Delplace B, Clippe A, Fontaine L, Hols P. Boutry C, et al. Among authors: clippe a. J Bacteriol. 2013 Feb;195(4):696-707. doi: 10.1128/JB.01605-12. Epub 2012 Nov 30. J Bacteriol. 2013. PMID: 23204467 Free PMC article.
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