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http://hub.abes.fr/acs/periodical/bichaw/1996/volume_35/issue_15/101021bi9523466/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_4/101021bi011429l/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/1999/volume_121/issue_11/101021ja982280c/authorship/5
http://hub.abes.fr/oup/periodical/nar/1997/volume_25/issue_17/101093nar25173543/authorship/3
http://hub.abes.fr/oup/periodical/proeng/2010/volume_23/issue_8/101093proteingzq035/authorship/5
http://hub.abes.fr/oup/periodical/nar/1997/volume_25/issue_3/101093nar253648/authorship/3
http://hub.abes.fr/oup/periodical/nar/2008/volume_36/issue_1/101093nargkm1016/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1998/volume_37/issue_30/101021bi9806403/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/2004/volume_43/issue_24/101021bi036088l/authorship/7
http://hub.abes.fr/acs/periodical/jacsat/1996/volume_118/issue_34/101021ja960917r/authorship/7
http://hub.abes.fr/acs/periodical/jacsat/1996/volume_118/issue_19/101021ja953979a/authorship/3
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Unconventional GIY-YIG homing endonuclease encoded in group I introns in closely related strains of the Bacillus cereus group
Electron Magnetic Resonance of the Tyrosyl Radical inRibonucleotide Reductase from Escherichia coli
Subunit and small-molecule interaction of ribonucleotide reductases via surface plasmon resonance biosensor analyses
pH dependence of self-splicing by the group IA2 intron in a pre-mRNA derived from the nrdB gene of bacteriophage T4
Crystal Structure of the Di-iron/Radical Protein of Ribonucleotide Reductase fromCorynebacterium ammoniagenes,
Structural and Mutational Studies of the Carboxylate Cluster in Iron-FreeRibonucleotide Reductase R2
Metal Ion Interaction with Cosubstrate in Self-Splicing of Group I Introns
A Synthetic Model for Triple-Helical Domains in Self-Splicing Group I IntronsStudied by Ultraviolet and Circular Dichroism Spectroscopy
Electronic Structure of Neutral Tryptophan Radicals inRibonucleotide Reductase Studied by EPR and ENDORSpectroscopy
The Crystal Structure of an Azide Complex of the Diferrous R2Subunit of Ribonucleotide Reductase Displays a Novel CarboxylateShift with Important Mechanistic Implications for Diiron-CatalyzedOxygen Activation
Crystal Structures of Two Self-Hydroxylating Ribonucleotide Reductase Protein R2Mutants: Structural Basis for the Oxygen-Insertion Step of Hydroxylation ReactionsCatalyzed by Diiron Proteins,
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