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1. Synthesis and biochemical evaluation of new 3-amido-4-substituted monocyclic ß-lactams as inhibitors of penicillin-binding protein(s)

Author

Grabrijan Katarina, Benedik Nika Strašek, Krajnc Alen, Bozovičar Krištof, Knez Damijan, Proj Matic, Zdovc Irena, Sosič Izidor, Contreras-Martel Carlos, Dessen Andréa, Rambaher Martina Hrast, and Gobec Stanislav

Subjects
antibacterial agents, monocyclic-β-lactams, penicillin-binding proteins, covalent inhibitors, transpeptidase, Pharmaceutical industry, HD9665-9675
Abstract

In the final phases of bacterial cell wall synthesis, penicillin-binding proteins (PBPs) catalyze the cross-linking of peptidoglycan. For many decades, effective and non-toxic β-lactam antibiotics have been successfully used as mimetics of the d-Ala-d-Ala moiety of the natural substrate and employed as irreversible inhibitors of PBPs. In the years following their discovery, the emergence of resistant bacteria led to a decline in their clinical efficacy. Using Staudinger cycloaddition, we synthesized a focused library of novel monocyclic β-lactams in which different substituents were introduced at the C4 position of the β-lactam ring, at the C3 amino position, and at the N1 lactam nitrogen. In biochemical assays, the compounds were evaluated for their inhibitory effect on the model enzyme PBP1b from Streptococcus pneumoniae. Upon investigation of the antibacterial activity of the newly prepared compounds against ESKAPE pathogens, some compounds showed moderate inhibition. We also examined their reactivity and selectivity in a biochemical assay with other enzymes that have a catalytic serine in the active site, such as human cholinesterases, where they also showed no inhibitory activity, highlighting their specificity for bacterial targets. These compounds form the basis for further work on new monocyclic β-lactams with improved antibacterial activity.

Published
2024
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8. Structural insights into ring-building motif domains involved in bacterial sporulation

Author

Liu, Bowen, primary, Chan, Helena, additional, Bauda, Elda, additional, Contreras-Martel, Carlos, additional, Bellard, Laure, additional, Villard, Anne-Marie, additional, Mas, Caroline, additional, Neumann, Emmanuelle, additional, Fenel, Daphna, additional, Favier, Adrien, additional, Serrano, Monica, additional, Henriques, Adriano O., additional, Rodrigues, Christopher D.A., additional, and Morlot, Cecile, additional

Published
2022
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14. Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae

Author

Morlot, Cécile, Straume, Daniel, Peters, Katharina, Hegnar, Olav A., Simon, Nolwenn, Villard, Anne-Marie, Contreras-Martel, Carlos, Leisico, Francisco, Breukink, Eefjan, Gravier-Pelletier, Christine, Le Corre, Laurent, Vollmer, Waldemar, Pietrancosta, Nicolas, Håvarstein, Leiv Sigve, Zapun, André, Sub Membrane Biochemistry & Biophysics, Membrane Biochemistry and Biophysics, Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Department of Chemical Biology and Organic Chemistry, Utrecht University [Utrecht], Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601), Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS), Centre for Bacterial Cell Biology, Newcastle University [Newcastle], Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Systèmes glutamatergiques normaux et pathologiques = Normal and Pathologic Glutamatergic Neurons (NPS), Neuroscience Paris Seine (NPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Analyse, Interactions Moléculaires et Cellulaires (LBM-E2), Laboratoire des biomolécules (LBM UMR 7203), Chimie Moléculaire de Paris Centre (FR 2769), École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Département de Chimie - ENS Paris, Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Chimie Moléculaire de Paris Centre (FR 2769), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Universidade Nova de Lisboa (NOVA), Bijvoet Centre for Biomolecular Research [Utrecht, The Netherlands], Laboratoire d'Ingénierie des Macromolécules (LIM), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), IMMI INSERM AstraZeneca, Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Staphylococcus aureus, MurT ligase, amidation, Glutamine, Science, GatD glutaminase, Glutamic Acid, Peptidoglycan, peptidoglycan, ammonia, Article, Bacterial Proteins, Glutaminase, Protein Domains, Cell Wall, Catalytic Domain, enzyme kinetics, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Sulfhydryl Compounds, lcsh:Science, ComputingMilieux_MISCELLANEOUS, carboxy terminal sequence, nonhuman, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], pH, zinc, article, ligase, glutaminase, Mycobacterium tuberculosis, Staphylococcal Infections, Lipids, [INFO.INFO-MO]Computer Science [cs]/Modeling and Simulation, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, operon, Anti-Bacterial Agents, unclassified drug, enzyme activity, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Streptococcus pneumoniae, glutamine, enzyme active site, lcsh:Q, Oxidoreductases
Abstract

The universality of peptidoglycan in bacteria underlies the broad spectrum of many successful antibiotics. However, in our times of widespread resistance, the diversity of peptidoglycan modifications offers a variety of new antibacterials targets. In some Gram-positive species such as Streptococcus pneumoniae, Staphylococcus aureus, or Mycobacterium tuberculosis, the second residue of the peptidoglycan precursor, D-glutamate, is amidated into iso-D-glutamine by the essential amidotransferase MurT/GatD complex. Here, we present the structure of this complex at 3.0 Å resolution. MurT has central and C-terminal domains similar to Mur ligases with a cysteine-rich insertion, which probably binds zinc, contributing to the interface with GatD. The mechanism of amidation by MurT is likely similar to the condensation catalyzed by Mur ligases. GatD is a glutaminase providing ammonia that is likely channeled to the MurT active site through a cavity network. The structure and assay presented here constitute a knowledge base for future drug development studies., The amidotransferase MurT/GatD complex catalyzes peptidoglycan precursor amidation in some Gram-positive bacteria. Here the authors present the crystal structure of the Streptococcus pneumoniae MurT/GatD complex and provide mechanistic insights, which are of interest for drug development.

Published
2018
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19. Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae

Author

Sub Membrane Biochemistry & Biophysics, Membrane Biochemistry and Biophysics, Morlot, Cécile, Straume, Daniel, Peters, Katharina, Hegnar, Olav A., Simon, Nolwenn, Villard, Anne-Marie, Contreras-Martel, Carlos, Leisico, Francisco, Breukink, Eefjan, Gravier-Pelletier, Christine, Le Corre, Laurent, Vollmer, Waldemar, Pietrancosta, Nicolas, Håvarstein, Leiv Sigve, Zapun, André, Sub Membrane Biochemistry & Biophysics, Membrane Biochemistry and Biophysics, Morlot, Cécile, Straume, Daniel, Peters, Katharina, Hegnar, Olav A., Simon, Nolwenn, Villard, Anne-Marie, Contreras-Martel, Carlos, Leisico, Francisco, Breukink, Eefjan, Gravier-Pelletier, Christine, Le Corre, Laurent, Vollmer, Waldemar, Pietrancosta, Nicolas, Håvarstein, Leiv Sigve, and Zapun, André

Published
2018

20. Molecular architecture of the PBP2–MreC core bacterial cell wall synthesis complex

Author

Contreras-Martel, Carlos, Martins, Alexandre, Ecobichon, Chantal, Trindade, Daniel Maragno, Matteï, Pierre-Jean, Hicham, Samia, Hardouin, Pierre, Ghachi, Meriem El, Boneca, Ivo G., Dessen, Andréa, Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Biologie et Génétique de la Paroi bactérienne - Biology and Genetics of Bacterial Cell Wall (BGPB), Institut Pasteur [Paris] (IP), Groupe Avenir [Dijon], Programme ATIP - Avenir, Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Brazilian Biosciences National Laboratory (LNBio), National Center for Research in Energy and Materials, This work was supported by ANR-13-BSV8-0015-01 (to A.D. and I.G.B.), the Laboratoire International Associé BACWALL (CNRS), by grants 11/52067-6 from FAPESP (Fundação de Amparo à Pesquisa do Estado de São Paulo) and DEQ20090515390 from the FRM (Fondation pour la Recherche Médicale) to A.D., and by ERC Starting Grant (PGNfrom SHAPEtoVIR-202283) and FRM Grant Programme d’Urgence (DBF20160635726) to I.G.B. This study received funding from the French Government’s Investissement d’Avenir program, Laboratoire d’Excellence 'Integrative Biology of Emerging Infectious Diseases' (grant no ANR-10-LABX-62-IBEID). We acknowledge the platforms of the Grenoble Instruct center (ISBG, UMS 3518 CNRS-CEA-UGA-EMBL) with support from FRISBI (ANR-10-INSB-05-02) and GRAL (ANR-10-LABX-49-01) within the Grenoble Partnership for Structural Biology (PSB). We also acknowledge the Spectroscopy and Calorimetry Facility (LEC) of the Brazilian Biosciences National Laboratory, CNPEM, Campinas, Brazil for support and help with circular dichroism experiments., ANR-13-BSV8-0015,BACSCREEN,Assemblage et structure de complexes macromoléculaires essentiels pour la biosynthèse de la paroi bactérienne(2013), ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010), ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), ANR-10-LABX-0049,GRAL,Grenoble Alliance for Integrated Structural Cell Biology(2010), Thomas, Frank, Blanc 2013 - Assemblage et structure de complexes macromoléculaires essentiels pour la biosynthèse de la paroi bactérienne - - BACSCREEN2013 - ANR-13-BSV8-0015 - Blanc 2013 - VALID, Integrative Biology of Emerging Infectious Diseases - - IBEID2010 - ANR-10-LABX-0062 - LABX - VALID, Infrastructure Française pour la Biologie Structurale Intégrée - - FRISBI2010 - ANR-10-INBS-0005 - INBS - VALID, Grenoble Alliance for Integrated Structural Cell Biology - - GRAL2010 - ANR-10-LABX-0049 - LABX - VALID, Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), and Institut Pasteur [Paris]

Subjects
Models, Molecular, Binding Sites, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Helicobacter pylori, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Science, Crystallography, X-Ray, Article, Protein Structure, Tertiary, Bacterial Proteins, Cell Wall, Penicillin-Binding Proteins, lcsh:Q, Amino Acid Sequence, lcsh:Science, Sequence Alignment
Abstract

Bacterial cell wall biosynthesis is an essential process that requires the coordinated activity of peptidoglycan biosynthesis enzymes within multi-protein complexes involved in cell division (the “divisome”) and lateral wall growth (the “elongasome”). MreC is a structural protein that serves as a platform during wall elongation, scaffolding other essential peptidoglycan biosynthesis macromolecules, such as penicillin-binding proteins. Despite the importance of these multi-partite complexes, details of their architecture have remained elusive due to the transitory nature of their interactions. Here, we present the crystal structures of the soluble PBP2:MreC core elongasome complex from Helicobacter pylori, and of uncomplexed PBP2. PBP2 recognizes the two-winged MreC molecule upon opening of its N-terminal region, revealing a hydrophobic zipper that serves as binding platform. The PBP2:MreC interface is essential both for protein recognition in vitro and maintenance of bacterial shape and growth. This work allows visualization as to how peptidoglycan machinery proteins are scaffolded, revealing interaction regions that could be targeted by tailored inhibitors., Bacterial wall biosynthesis is a complex process that requires the coordination of multiple enzymes. Here, the authors structurally characterize the PBP2:MreC complex involved in peptidoglycan elongation and cross-linking, and demonstrate that its disruption leads to loss of H. pylori shape and inability to sustain growth.

Published
2017
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21. Substitutions in PBP2b from β-lactam resistant Streptococcus pneumoniae have different effects on enzymatic activity and drug reactivity

Author

Calvez, Philippe, Breukink, Eefjan, Roper, David I., Dib, Mélanie, Contreras-Martel, Carlos, Zapun, André, Sub Membrane Biochemistry & Biophysics, and Membrane Biochemistry and Biophysics

Subjects
antibiotic resistance, enzyme kinetics, QR180, polycyclic compounds, cell wall, Streptococcus, peptidoglycan
Abstract

Pneumococcus resists β-lactams by expressing variants of its target enzymes, the penicillin-binding proteins (PBPs), with many amino acid substitutions. Up to 10% of the sequence can be modified. These altered PBPs have a much reduced reactivity with the drugs but retain their physiological activity of cross-linking the peptidoglycan, the major constituent of the bacterial cell wall. However, as β-lactams are chemical and structural mimics of the natural substrate, resistance mediated by altered PBPs raises the following paradox: how PBPs that react poorly with the drugs maintain a sufficient level of activity with the physiological substrate? This question is addressed for the first time in this study, which compares the peptidoglycan cross-linking activity of PBP2b from susceptible and resistant strains with their inhibition by different β-lactams. Unexpectedly, the enzymatic activity of the variants did not correlate with their antibiotic reactivity. This finding indicates that some of the numerous amino acid substitutions were selected to restore a viable level of enzymatic activity by a compensatory molecular mechanism.

Published
2017

24. Découverte et structure cristallographique d'une apolipoprotéine humaine

Author

Morales, R., Berna, A., Carpentier, P., Contreras-Martel, Carlos, Renault, F., Nicodeme, M., Chesne-Seck, M.L., Bernier, F., Dupuy, J., Schaeffer, C., Diemer, H., Van-Dorsselaer, A., Fontecilla-Camps, J.C., Masson, P., Chabriere, E., Laboratoire de Cristallographie et modélisation des matériaux minéraux et biologiques (LCM3B), and Université Henri Poincaré - Nancy 1 (UHP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[PHYS.COND.CM-GEN]Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other], ComputingMilieux_MISCELLANEOUS
Abstract

National audience

Published
2007

25. Conformational versatility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate

Author

Cavazza, C., Contreras-Martel, Carlos, Pieulle, L., Chabriere, E., Hatchikian, E.C., Fontecilla-Camps, J.C., Laboratoire de Cristallographie et modélisation des matériaux minéraux et biologiques (LCM3B), Université Henri Poincaré - Nancy 1 (UHP)-Centre National de la Recherche Scientifique (CNRS), and Clausse, Anne

Subjects
[PHYS.COND.CM-GEN] Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other], [PHYS.COND.CM-GEN]Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2006

26. Crystallization and preliminary X-ray diffraction analysis of the Human Phosphate Binding Protein

Author

Contreras-Martel, Carlos, Carpentier, P., Morales, R., Renault, F., Chesne-Seck, M.L., Rochu, D., Masson, P., Fontecilla-Camps, J.C., Chabriere, E., Laboratoire de Cristallographie et modélisation des matériaux minéraux et biologiques (LCM3B), and Université Henri Poincaré - Nancy 1 (UHP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[PHYS.COND.CM-GEN]Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2006

29. Dual Inhibitor of MurD and MurE Ligases from Escherichia coli and Staphylococcus aureus

Author

Tomašić, Tihomir, primary, Šink, Roman, additional, Zidar, Nace, additional, Fic, Anja, additional, Contreras-Martel, Carlos, additional, Dessen, Andréa, additional, Patin, Delphine, additional, Blanot, Didier, additional, Müller-Premru, Manica, additional, Gobec, Stanislav, additional, Zega, Anamarija, additional, Kikelj, Danijel, additional, and Mašič, Lucija Peterlin, additional

Published
2012
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31. The full-length Streptococcus pneumoniae major pilin RrgB crystallizes in a fibre-like structure, which presents the D1 isopeptide bond and provides details on the mechanism of pilus polymerization

Author

El Mortaji, Lamya, primary, Contreras-Martel, Carlos, additional, Moschioni, Monica, additional, Ferlenghi, Ilaria, additional, Manzano, Clothilde, additional, Vernet, Thierry, additional, Dessen, Andrea, additional, and Di Guilmi, Anne Marie, additional

Published
2012
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33. Structure-Guided Design of Cell Wall Biosynthesis Inhibitors That Overcome β-Lactam Resistance in Staphylococcus aureus (MRSA)

Author

Contreras-Martel, Carlos, primary, Amoroso, Ana, additional, Woon, Esther C. Y., additional, Zervosen, Astrid, additional, Inglis, Steven, additional, Martins, Alexandre, additional, Verlaine, Olivier, additional, Rydzik, Anna M., additional, Job, Viviana, additional, Luxen, André, additional, Joris, Bernard, additional, Schofield, Christopher J., additional, and Dessen, Andréa, additional

Published
2011
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34. Structure-Based Design of a New Series of d-Glutamic Acid Based Inhibitors of Bacterial UDP-N-acetylmuramoyl-l-alanine:d-glutamate Ligase (MurD)

Author

Tomašić, Tihomir, primary, Zidar, Nace, additional, Šink, Roman, additional, Kovač, Andreja, additional, Blanot, Didier, additional, Contreras-Martel, Carlos, additional, Dessen, Andréa, additional, Müller-Premru, Manica, additional, Zega, Anamarija, additional, Gobec, Stanislav, additional, Kikelj, Danijel, additional, and Peterlin Mašič, Lucija, additional

Published
2011
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43. Structural and Functional Characterization of Enantiomeric Glutamic Acid Derivatives as Potential Transition State Analogue Inhibitors of MurD Ligase

Author

Kotnik, Miha, primary, Humljan, Jan, additional, Contreras-Martel, Carlos, additional, Oblak, Marko, additional, Kristan, Katja, additional, Hervé, Mireille, additional, Blanot, Didier, additional, Urleb, Uroš, additional, Gobec, Stanislav, additional, Dessen, Andréa, additional, and Solmajer, Tom, additional

Published
2007
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45. Serendipitous Discovery and X-Ray Structure of a Human Phosphate Binding Apolipoprotein

Author

Morales, Renaud, primary, Berna, Anne, additional, Carpentier, Philippe, additional, Contreras-Martel, Carlos, additional, Renault, Frédérique, additional, Nicodeme, Murielle, additional, Chesne-Seck, Marie-Laure, additional, Bernier, François, additional, Dupuy, Jérôme, additional, Schaeffer, Christine, additional, Diemer, Hélène, additional, Van-Dorsselaer, Alain, additional, Fontecilla-Camps, Juan C., additional, Masson, Patrick, additional, Rochu, Daniel, additional, and Chabriere, Eric, additional

Published
2006
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