457 citations
Counting papers with at most 25 authors, so collaboration author lists do not stand in for the people here.
- Centre National de la Recherche ScientifiqueFR24 papers
- CEA GrenobleFR22 papers
- Commissariat à l'Énergie Atomique et aux Énergies AlternativesFR22 papers
- Université Joseph FourierFR12 papers
- Université Grenoble AlpesFR7 papers
- CEA Paris-SaclayFR3 papers
- InsermFR3 papers
- Institut de Chimie PhysiqueFR3 papers
- Institut Pluridisciplinaire Hubert CurienFR3 papers
- Université Paris-SudFR3 papers
- Institut de Biologie StructuraleFR2 papers
- Institut de Recherches en Technologies et Sciences pour le VivantFR2 papers
29 papers
Revisiting Out-of-Distribution Detection in Real-time Object Detection: From Benchmark Pitfalls to a New Mitigation Paradigm
Changshun Wu, Weicheng He, Chih-Hong Cheng +2
Out-of-distribution (OoD) inputs pose a persistent challenge to deep learning models, often triggering overconfident predictions on non-target objects. While prior work has primari…
Biomimetic hydrogel based on HET-s amyloïd fibers for long-term culture of primary hippocampal neurons
Julien Hurtaud, Cécile Delacour, Carole Mathevon +1
Historically, amyloid fibers (AF) in research has always been linked to degenerative diseases. However, HET-s AF, by their morphology and function, have only little in common to pa…
Zinc oxide induces the stringent response and major reorientations in the central metabolism of Bacillus subtilis
Sylvie Luche, Elise Eymard-Vernain, Hélène Diemer +3
Microorganisms, such as bacteria, are one of the first targets of nanoparticles in the environment. In this study, we tested the effect of two nanoparticles, ZnO and TiO2, with the…
A single step protein assay that is both detergent and reducer compatible: The cydex blue assay
Thierry Rabilloud
Determination of protein concentration in often an absolute pre-requisite in preparing samples for biochemical and proteomic analyses. However, current protein assay methods are no…
Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii
Christelle Mathé, Tony A Mattioli, Olivier Horner +4
The active site of superoxide reductase SOR consists of an Fe2+ center in an unusual [His4 Cys1] square-pyramidal geometry. It specifically reduces superoxide to produce H2O2. Here…
A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor
Julien Valton, Laurent Filisetti, Marc Fontecave +1
The two-component flavin-dependent monooxygenases belong to an emerging class of enzymes involved in oxidation reactions in a number of metabolic and biosynthetic pathways in micro…
The flavin reductase ActVB from Streptomyces coelicolor: characterization of the electron transferase activity of the flavoprotein form
Laurent Filisetti, Julien Valton, Marc Fontecave +1
The flavin reductase ActVB is involved in the last step of actinorhodin biosynthesis in Streptomyces coelicolor. Although ActVB can be isolated with some FMN bound, this form was n…
Pulse radiolysis studies on superoxide reductase from Treponema pallidum
V Nivière, M. Lombard, M. Fontecave +1
Superoxide reductases (SORs) are small metalloenzymes, which catalyze reduction of O2*- to H2O2. The reaction of the enzyme from Treponema pallidum with superoxide was studied by p…
Superoxide reductase from Desulfoarculus baarsii: reaction mechanism and role of glutamate 47 and lysine 48 in catalysis
M. Lombard, C. Houée-Levin, D. Touati +2
Superoxide reductase (SOR) is a small metalloenzyme that catalyzes reduction of O(2)(*)(-) to H(2)O(2) and thus provides an antioxidant mechanism against superoxide radicals. Its a…
The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotides
V. Nivière, F. Fieschi, J. L. Dećout +1
The NAD(P)H:flavin oxidoreductase from Escherichia coli, named Fre, is a monomer of 26.2 kDa that catalyzes the reduction of free flavins using NADPH or NADH as electron donor. The…
Hydrogen bonding to the cysteine ligand of superoxide reductase: acid--base control of the reaction intermediates
Emilie Tremey, Florence Bonnot, Yohann Moreau +6
Superoxide reductase SOR is a non-heme iron metalloenzyme that detoxifies superoxide radical in microorganisms. Its active site consists of an unusual non-heme Fe2+ center in a [Hi…
Fe(3+)-eta(2)-peroxo species in superoxide reductase from Treponema pallidum. Comparison with Desulfoarculus baarsii
Christelle Mathé, Vincent Nivière, Chantal Houée-Levin +1
Superoxide reductases (SORs) are superoxide (O2-)-detoxifying enzymes that catalyse the reduction of O2- into hydrogen peroxide. Three different classes of SOR have been reported o…
Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme
Gergely Katona, Philippe Carpentier, Vincent Nivière +5
Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (…
Reaction of the NAD(P)H:flavin oxidoreductase from Escherichia coli with NADPH and riboflavin: identification of intermediates
V Nivière, M. A. Vanoni, G. Zanetti +1
Flavin reductase catalyzes the reduction of free flavins by NAD(P)H. As isolated, Escherichia coli flavin reductase does not contain any flavin prosthetic group but accommodates bo…
Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity
M Lombard, M Fontecave, D Touati +1
Desulfoferrodoxin is a small protein found in sulfate-reducing bacteria that contains two independent mononuclear iron centers, one ferric and one ferrous. Expression of desulfofer…
Fe3+-hydroxide ligation in the superoxide reductase from Desulfoarculus baarsii is associated with pH dependent spectral changes
Christelle Mathé, Vincent Nivière, Tony A Mattioli
Superoxide reductase (SOR) catalyzes the reduction of O2*- to H2O2. Its active site consists of a non-heme Fe2+ center in an unusual square-pyramidal [His4 Cys] coordination. Like…
M{ö}ssbauer characterization of an unusual high-spin side-on peroxo-Fe3+ species in the active site of superoxide reductase from Desulfoarculus Baarsii. Density functional calculations on related models
Olivier Horner, Jean-Marie Mouesca, Jean-Louis Oddou +9
Superoxide reductase (SOR) is an Fe protein that catalyzes the reduction of superoxide to give H(2)O(2). Recently, the mutation of the Glu47 residue into alanine (E47A) in the acti…
Superoxide reductase from Desulfoarculus baarsii
Vincent Nivière, Murielle Lombard
Superoxide radical (O2.-) is the univalent reduction product of molecular oxygen and belongs to the group of the so-called toxic oxygen derivatives. For years the only enzymatic sy…
Discovery of superoxide reductase: an historical perspective
Vincent Nivière, Marc Fontecave
For more than 30 years, the only enzymatic system known to catalyze the elimination of superoxide was superoxide dismutase, SOD. SOD has been found in almost all organisms living i…
Paleoproteomics explained to youngsters: how did the wedding of two-dimensional electrophoresis and protein sequencing spark proteomics on: Let there be light
Thierry Rabilloud
Taking the opportunity of the 20th anniversary of the word "proteomics", this young adult age is a good time to remember how proteomics came from enormous progress in protein separ…
The proteomic to biology inference, a frequently overlooked concern in the interpretation of proteomic data: A plea for functional validation
Thierry Rabilloud, Pierre Lescuyer
Proteomics will celebrate its 20th year in 2014. In this relatively short period of time, it has invaded most areas of biology and its use will probably continue to spread in the f…
How to use 2D gel electrophoresis in plant proteomics
Thierry Rabilloud
Two-dimensional electrophoresis has nurtured the birth of proteomics. It is however no longer the exclusive setup used in proteomics, with the development of shotgun proteomics tec…
Multidimensional separation prior to mass spectrometry: Getting closer to the bottom of the iceberg
Manuel Mayr, Thierry Rabilloud
While prefractionation has previously been shown to improve results in MS analysis, a novel combination provides an additional dimension of separation: protein fractionation by SDS…
When 2D is not enough, go for an extra dimension
Thierry Rabilloud
The use of an extra SDS separation in a different buffer system provide a technique for deconvoluting 2D gel spots made of several proteins (Colignon et al. Proteomics, 2013, 13, 2…