Life Sciences


  • Klein S., Sommer A., Distel L., Hazemann J.-L., et al., “Superparamagnetic iron oxide nanoparticles as novel X-ray enhancer for low-dose radiation therapy”, J. Phys. Chem. B 118 (2014) 6159–6166
  • Bissardon C., Proux O., Bureau S., Suess E. et al., “Sub-ppm high energy resolution fluorescence detected X-ray absorption spectroscopy of selenium in articular cartilage”, Analyst144 (2019) 3488-3493


  • Préaubert L., Tassistro V., Auffan M., Sari-Minodier I., Rose J., et al., “Very low concentration of cerium dioxide nanoparticles induce DNA damage, but no loss of vitality, in human spermatozoa”, Toxicol. in Vitro 50(2018) 236-241
  • Oliveira P.N., Moussa A., Milhau N., Dosciatti Bini R., Prouillac C., et al., “In situ synthesis of Fe3O4 nanoparticles coated by chito-oligosaccharides: physico-chemical characterizations and cytotoxicity evaluation for biomedical applications”, Nanotechnology 31 (2020) 175602


  • Hemmann J.L., Wagner T., Shima S., Vorholt J.A., “Methylofuran is a prosthetic group of the formyltransferase/hydrolase complex and shuttles one-carbon units between two active sites”, Proc. Natl. Acad. Sci. U.S.A.116 (2019), 25583–25590
  • Huang G., Wagner T., Wodrich M.D., Ataka K., Bill E., Ermler U., Hu X., Shima S. “The atomic-resolution crystal structure of activated [Fe]-hydrogenase”, Nat. Catal.2 (2019), 537–543
  • Liu W.Q., Amara P., Mouesca J.M., Ji X., Renoux O., et al. “1,2-diol dehydration by the radical SAM enzyme AprD4: A matter of proton circulation and substrate flexibility”, J. Am. Chem. Soc. 140 (2018) 1365-1371
  • Wagner T., Huang G., Ermler U., Shima S. “How [Fe]-hydrogenase from Methanothermobacter is protected against light and oxidative stress”, Angew. Chem. Int. Ed.57 (2018), 15056-15059
  • Rohac R., Amara P., Benjdia A., Martin L., Ruffié P., et al. “Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE”, Nat. Chem.8 (2016), 491-500
  • Volbeda A., Darnault C., Renoux O., Nicolet Y., Fontecilla-Camps J.C. “The crystal structure of the global anaerobic transcriptional regulator FNR explains its extremely fine-tuned monomer-dimer equilibrium”, Sci. Adv.1 (2015), e1501086
  • Cheignon C., Jones M., Atrian-Blasco E., Kieffer I., Faller P., et al., “Identification of key structural features of the elusive Cu-Aβ complex generating ROS in Alzheimer’s Disease”, Chem. Sci.8 (2017) 5107-5118
  • Thomas S.A., Catty P., Hazemann J.-L., Michaud-Soret I., Gaillard J.-F.., “The role of cysteine and sulfide in the interplay between microbial Hg(II) uptake and sulfur metabolism”, Metallomics 11 (2019) 1219-1229

Ligand screening

  • Ahmed-Belkacem A., Colliandre L., Ahnou N., Nevers Q., Gelin M., et al. “Fragment-based discovery of a new family of non-peptidic small-molecule cyclophilin inhibitors with potent antiviral activities”, Nat. Commun.7 (2016) 12777
  • Gelin M., Delfosse V., Allemand F., Hoh F., Sallaz-Damaz Y., et al. “Combining ‘dry’ co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography”, Acta Crystallogr. D Biol. Crystallogr.71 (2015), 1777-1787


  • De S., Chi B., Granier T., Qi T., Maurizot V., Huc I. “Designing cooperatively folded abiotic uni- and multimolecular helix bundles”, Nature Chem.10 (2018), 51-57
  • Ziach K., Chollet C., Parissi V., Prabhakaran P., Marchivie M., et al. “Single helically folded aromatic oligoamides that mimic the charge surface of double-stranded B-DNA”, Nature Chem. 10 (2018) 511–518
  • Lopez S., Rondot L., Lepretre C., Marchi-Delapierre C., Menage S. et al. “Cross-linked artificial enzyme crystals as heterogeneous catalysts for oxidation reactions”, J. Am. Chem. Soc.139 (2017), 17994-18002
  • Chandramouli N., Ferrand Y., Lautrette G., Kauffmann B. et al. “Iterative design of a helically folded aromatioligoamide sequence for the selective encapsulation of fructose”, Nat. Chem.7 (2015), 334-341

Elucidation of biological mechanisms

  • Halloum I., Carrère-Kremer S., Blaise M., Viljoen A., Bernut A., et al. “Deletion of a dehydratase important for intracellular growth and cording renders rough Mycobacterium abscessus avirulent”, Proc. Natl. Acad. Sci. U.S.A.113 (2016), E4228-E4237
  • Bui S., von Stetten D., Jambrina P.G., Prangé T., Colloc’h N., et al. “Direct evidence for a peroxide intermediate and a reactive enzyme-substrate-dioxygen configuration in a cofactor-free oxidase”, Angew. Chem. Int. Ed.53 (2014), 13710-13714
  • Siponen M.I., Legrand P., Widdrat M., Jones S.R., Chang M.C.Y., et al. “Structural insight into magnetochrome-mediated magnetite biomineralization”, Nature502 (2013), 681-684