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http://hub.abes.fr/acs/periodical/bichaw/1984/volume_23/issue_26/101021bi00321a050/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1986/volume_25/issue_2/101021bi00350a028/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1982/volume_21/issue_19/101021bi00262a037/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_24/101021bi00139a029/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/1995/volume_117/issue_19/101021ja00124a017/authorship/5
http://hub.abes.fr/oup/periodical/proeng/1994/volume_7/issue_5/101093protein75681/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1997/volume_36/issue_50/101021bi971636e/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1997/volume_36/issue_51/101021bi972155y/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_25/101021bi030041i/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1996/volume_35/issue_39/101021bi961354z/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1999/volume_38/issue_19/101021bi982894u/authorship/8
http://hub.abes.fr/acs/periodical/bichaw/1997/volume_36/issue_25/101021bi970020m/authorship/5
http://hub.abes.fr/acs/periodical/inocaj/1987/volume_26/issue_2/101021ic00249a021/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1988/volume_27/issue_16/101021bi00416a048/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_1/101021bi00001a024/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1993/volume_32/issue_38/101021bi00089a002/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_51/101021bi00051a028/authorship/1
http://hub.abes.fr/springer/periodical/10534/1994/volume_7/issue_4/B943381937DE5DE1E053120B220A297A/authorship/1
http://hub.abes.fr/springer/periodical/775/1996/volume_1/issue_1/B92A1D5D22006F61E053120B220A5EA3/authorship/1
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High-multiplicity spin states of 2[4Fe-4Se]+ clostridial ferredoxins
Detection and Classification of Hyperfine-Shifted 1H, 2H, and 15N Resonances from the Four Cysteines That Ligate Iron in Oxidized and Reduced Clostridium pasteurianum Rubredoxin
[4Fe-4X]2+ (X = sulfur, selenium) clusters in Clostridium pasteurianum ferredoxin and in synthetic analogs: structural data from resonance Raman spectroscopy
Effect of replacing conserved proline residues on the EPR and NMR properties of Clostridium pasteurianum 2[4Fe-4s] ferredoxin
Hydrogen-1 nuclear magnetic resonance of selenium-substituted clostridial ferredoxins
Characteristic features of the heterologous functional synthesis in Escherichia coli of a 2[4Fe-4S] ferredoxin
Sequence-specific assignments of the proton nuclear magnetic resonance spectra of reduced high-potential ferredoxin (HiPIP) from Chromatium vinosum
Probing the Role of Electrostatic Forces in the Interaction of Clostridium pasteurianum Ferredoxin with Its Redox Partners
Intramolecular Electron Transfer between [4Fe-4S] Clusters Studied by ProtonMagnetic Resonance Spectroscopy
Unusual NMR, EPR, and Mössbauer Properties of Chromatium vinosum 2[4Fe-4S]Ferredoxin
Site-Directed Mutagenesis of Rubredoxin Reveals the Molecular Basis of ItsElectron Transfer Properties
On the role of conserved proline residues in the structure and function of Clostridium pasteurianum 2[4Fe-4S] ferredoxin
Use of 1H Longitudinal Relaxation Times in the Solution Structure of ParamagneticProteins. Application to [4Fe-4S] Proteins
Atomic Resolution (0.94 Å) Structure of Clostridium acidurici Ferredoxin. DetailedGeometry of [4Fe-4S] Clusters in a Protein,
Peroxynitrite and Nitric Oxide Differently Target the Iron−Sulfur Cluster andAmino Acid Residues of Human Iron Regulatory Protein 1
The coordination sphere of iron-sulfur clusters: lessons from site-directed mutagenesis experiments
Characterization of the selenium-substituted 2[4Fe-4Se] ferredoxin from Clostridium pasteurianum
NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and impeded electron transfer between the two [4Fe-4S] clusters
Hydrogen-1 nuclear magnetic resonance of the nitrogenase iron protein (Cp2) from Clostridium pasteurianum
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