A
Aude Smeets
Researcher at Université catholique de Louvain
Publications - 6
Citations - 272
Aude Smeets is an academic researcher from Université catholique de Louvain. The author has contributed to research in topics: Peroxiredoxin & Thioredoxin fold. The author has an hindex of 5, co-authored 6 publications receiving 255 citations. Previous affiliations of Aude Smeets include University College London.
Papers
More filters
Journal ArticleDOI
Pre-steady state kinetic characterization of human peroxiredoxin 5: Taking advantage of Trp84 fluorescence increase upon oxidation
Madia Trujillo,André Clippe,Bruno Manta,Gerardo Ferrer-Sueta,Aude Smeets,Jean-Paul Declercq,Bernard Knoops,Rafael Radi +7 more
TL;DR: The order of reactivities between PRDX5 towards oxidizing substrates differ from other PRDXs studied, pointing to a selective action ofPRDXs with respect to peroxide detoxification, helping to rationalize the multiple enzyme isoforms present even in the same cellular compartment.
Journal ArticleDOI
Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2
Aude Smeets,Christine Evrard,Marie Landtmeters,Cécile Marchand,Bernard Knoops,Jean-Paul Declercq +5 more
TL;DR: The first crystal structures of a mammalian mitochondrial thioredoxin 2 are reported, and possible interaction domains with human peroxiredoxin 5 are revealed, a substrate protein of human thiOREDoxin 2 in mitochondria.
Journal ArticleDOI
The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins.
TL;DR: Three crystal forms in which this intramolecular disulfide bond is indeed observed are reported in which the enzyme was not oxidized in the same way and the influence of the oxidizing conditions is discussed.
Journal ArticleDOI
The crystal structure of the C45S mutant of annelid Arenicola marina peroxiredoxin 6 supports its assignment to the mechanistically typical 2-Cys subfamily without any formation of toroid-shaped decamers.
Aude Smeets,Eléonore Loumaye,André Clippe,Jean-François Rees,Bernard Knoops,Jean-Paul Declercq +5 more
TL;DR: Structural features of typical 2‐Cys PRDXs without any formation of toroid‐shaped decamers are presented, suggesting that it should function more like a cytoprotective antioxidant enzyme or a modulator of peroxide‐dependent cell signaling rather than a molecular chaperone.
Journal ArticleDOI
Crystal structure of the C47S mutant of human peroxiredoxin 5
TL;DR: In this paper, the crystal structure of the reduced form of the C47S mutant of the same enzyme has been crystallized in the tetragonal system, space group P4(1)2(1)-2(2)2, with a = 65.65 Angstrom, c = 122.04 Angstrom.