Michel Véron, French citizen, Born in 1947, married, two children

1969-1974: DEA & Thesis: Unité de Biochimie Cellulaire. Head, Pr. Georges Cohen, Institut Pasteur, Paris. Study of the allosteric properties of Aspartokinase I-Homosérine deshydrogénase I, a bifunctionnal enzym from E. Coli.

1974-1976: Post-Doc I: Lab. of Pr. Bennet Shapiro, Dpt. of Biochemistry, University of Washington, Seattle, USA. Study of changes in membrane proteins upon fertilization of the sea urchin egg.

1976-1977: Post-Doc II: Institut de Microbiologie. Head, Pr. Jean-Claude Patte, University Paris Sud, Orsay, France. Study of cAMP binding proteins in Dictyostelium discoideum.

1977-1981: Post-Doc III: Unité de Différenciation Cellulaire. Head, Luiz Pereira da Silva, Institut Pasteur, Paris. Study of cAMP binding proteins in Dictyostelium discoideum.

1981-1988: PI of a group within the Unité de Biochimie Cellulaire. Head, Pr. Georges Cohen, Institut Pasteur, Paris. Main projects: (i) Biochemical properties of the cAMP dependant protein kinase from Dictyostelium; study of its role in differentiation and morphogenesis, (ii) Study of the enzyme S-adenosyl-homocysteine Hydrolase from Dictyostelium.

1988-1995: PI of a group within the Unité de Biochimie Cellulaire. Head, Pr. Michel Goldberg, Institut Pasteur, Paris. Main projects: (i): Dictyostelium cAMP dependant protein kinase: Biochemical & structural properties; role in development (ii) Cloning, purification and study of the structural properties of Nucleoside Diphosphate Kinase (NDP kinase).

1995-2000: Head of the Unité de Régulation Enzymatique des Activités cellulaires, Department of Molecular Biology, Institut Pasteur. Main projects: (i) Dictyostelium cAMP dependant protein kinase: properties and role in the development (ii) Role of NDP Kinase in the processing of nucleoside analogs used in multitherapies against AIDS. Attemps to design new analogs and mutant NDP kinases with better processing properties. Study of the DNA binding properties of Human NDP kinase.

2000-2007: Head of the Unité de Régulation Enzymatique des Activités cellulaires, Department of Structural Biology & Chemistry, Institut Pasteur, Paris. New main projects: (i) Study of the mechanism of recombination in HIV (PI, Matteo Negroni), (ii) Study of the protein NEMO, (NF-kB Essential Regulator), a non catalytic regulator of the IKK complex of the NF-kB signal tranduction pathway (Hayden and Ghosh. (2008) Cell 132: 344; Vallabhapurapu and Karin. (2009) Annu. Rev. Immunol 27: 693). Biochemical and structural studies coupled with functional cell biology approaches using cultured cells (PIs, Fabrice Agou and Michel Veron).

2008-2010: Head of the Unité de Biochimie Structurale & Cellulaire, Department of Structural Biology & Chemistry, Institut Pasteur, Paris. The Unit is composed of two independent groups: (i) The study of the protein NEMO (PI, Fabrice Agou), (ii) The study of Opiorphin, a new analgesic natural (PI, Catherine Rougeot).

          • Activity Report 2009

After graduating in physics (Université de Paris, 1969), I earned my PhD in biochemistry (1974) in the laboratory of Georges Cohen at the Institut Pasteur of Paris. During my thesis, I studied the allosteric bifunctional enzyme, aspartokinase I-homoserine dehydrogenase I from E. coli. I showed that the two activities of this enzyme, both of which are subject to feedback inhibition by threonine, are carried out by separate domains of the same polypeptide chain.

During my postdoc with Bennet Shapiro (Dept. of Biochemistry, University of Washington, Seattle, 1974), I studied the biochemical mechanisms linked to the formation of the “fertilization membrane” of sea urchin eggs. This membrane polymerizes around the egg upon contact with the fertilizing sperm, thus preventing polyspermy.

Upon my return to France in 1976, I became interested in the model system of Dictyostelium discoideum, which is a primitive eukaryote with very unusual properties. Dictyostelium cells live as unicellular amoebae as long as they are able to feed on bacteria by phagocytosis. During starvation, however, the cells undergo a sophisticated differentiation program. First, they respond chemotactically to extracellular cAMP signals to form a multicellular aggregate of about 105 cells. This aggregate then transforms into a migrating slug, which later develops into a fruiting body made up of a mass of spores supported by a stalk.

At first, I focused on studying the Dictyostelium cAMP-dependent protein kinase (PKA) and showed that this enzyme is composed of catalytic (C) and regulatory (R) subunits, similarly to its mammalian ortholog. In 1981, I started my own group on this project, in which we purified the enzyme, cloned its gene, and characterized the biochemical properties of both subunits. In parallel, we studied the role of PKA in Dictyostelium development using newly established methods of reverse genetics. In particular, we generated a dominant negative mutant and used it in transformation experiments to investigate the various roles of Dictyostelium PKA in differentiation and morphogenesis.

In 1989, we were the first to clone the gene for nucleoside diphosphate (NDP) kinase in Dictyostelium, which is an ubiquitous enzyme that catalyzes the synthesis of triphospho-nucleotides from diphospho precursors. We showed that NDP kinase was the product of the human gene nm23 which had just been reported as a metastasis suppresor gene. This exciting discovery led us to embark in a thorough structure/function study of the protein. We solved the 3D structure of the protein at high-resolution using x-ray crystallograpy and studied the catalytic mechanism in detail at the atomic scale. Yet, the report of the involvement of NDP kinase in tumor metastasis remained very ellusive ever since.

But NDP kinase has another major interest as playing an important role in processing nucleoside analogs used in AIDS treatments such as such as AZT (Zidovudine), d4T (Stavudine) or ddI (didanosine). Indeed, since phosphorylated nucleotides cannot cross the cell membrane, nucleoside analogs are thus provided to patients as unphosphorylated precursors, which are then successively phosphorylated within cells into their mono-, di- and triphosphate derivatives. NDP kinase catalyzes the last step of this metabolic pathway to provide active compounds (AZT-triphosphate, for example), which can act as a reverse transcriptase inhibitor and thus disrupt viral replication. By combining methods of protein biochemistry and structural biology, we studied the problem of why diphospho-derivatives of nucleoside analogs are poor substrates for NDP kinase. We determined the high-resolution 3D structure of AZT-diphosphate bound to the catalytic site of NDP kinase. As a result, we were able to demonstrate the existence of a substrate-assisted catalytic mechanism, in which a crucial H-bond is formed within the nucleotide substrate between the 3’-OH of the ribose and the gamma-phosphate while it is bound to the enzyme’s catalytic site.

Since 2000, new themes have emerged in the laboratory. The major current project is the study of the NEMO (NF-kB Essential Modulator) protein, which plays a crucial role in regulating the activity of the “IKK complex” involved in NF-kB signal transduction.

• Chiaravalli, J., Fontan, E., Fsihi, H., Coïc, Y.-M., Baleux, F., Véron, M. and Agou (2011) F. Direct inhibition of NF-kB activation by peptide targeting the NOA ubiquitin binding domain of NEMO. Biochem. Pharmacol., 82, 1163-1174.
• Grubisha, O., Kaminska, M., Duquerroy, S., Fontan, E., Cordier, F., Haouz, A., Raynal, B., Chiaravalli, J., Delepierre, M., Israël, A., Véron, M. and Agou, F. (2010) DARPin-assisted crystallography of the CC2-LZ domain of NEMO reveals a coupling between dimerization and ubiquitin-binding. J. Mol. Biol., 395, 89-104.
• Laplantine, E., Fontan, E., Chiaravalli, J., Lopez, T., Lakisic, G., Véron, M., Agou, F. and Israël, A. (2009) NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain. EMBO J., 28, 2885-2895.
• Cordier, F., Grubisha, O., Traincard, F., Véron, M., Delepierre, M. and Agou, F. (2009) The Zinc Finger of NEMO is a functional ubiquitin-binding domain. J. Biol. Chem., 284, 2902-2907.
• Cordier, F., Vinolo, E., Véron, M., Delepierre, M. and Agou, F. (2008) Solution structure of NEMO Zinc Finger and impact of an anhidrotic Ectodermal Dysplasia with immunodeficiency-related point mutation. J. Mol. Biol., 377, 1419-1432.
• Wyler, E., Kaminska, M., Coïc, Y.-M., Baleux, F., Véron, M. and Agou, F. (2007) Inhibition of NF-kB activation with designed ankyrin-repeat proteins targeting the ubiquitin-binding/oligomerization domain of NEMO. Protein Sci., 16, 2013-2022.
• Fontan, E., Traincard, F., Lévy, S. G., Yamaoka, S., Véron, M. and Agou, F. (2007) NEMO oligomerization in the dynamic assembly of the IkappaB kinase complex. FEBS J., 274, 2540-2551.
• Carvalho, G., Fabre, C., Braun, T., Grosjean, J., Ades, L., Agou, F., Tasdemir, E., Boehrer, S., Israël, A., Véron, M., Fenaux, P. and Kroemer, G. (2007) Inhibition of NEMO, the regulatory subunit of the IKK complex, induces apoptosis in high-risk myelodysplastic syndrome and acute myeloid leukemia. Oncogene, 26, 2299-2307.
• Santos, O. F., Bustamante, J., Haverkamp, M., Vinolo, E., Ku, C.-K., Puel, A., Frucht, D., Senechal, B., Feinberg, J., Fieschi, C., Durandy, A., Christel, K., Chapgier, A., Vogt, G., de Beaucoudrey, L., von Bernuth, H., Picard, C., Kutukculer, N., Plebani, A., Notarangelo, L., Bodemer, C., Geissmann, F., Israel, A., Veron, M., Knackstedt, M., Magdorf, K., Gendrel, D., Agou, F., Holland, S. M. and Casanova, J.-L. (2006) X-linked susceptibility to mycobacteria is caused by mutations in NEMO impairing CD40-dependent IL-12 production. J. Exp. Med., 203, 1745-1759.
• Vinolo, E., Sebban, H., Chaffotte, A., Israël, A., Courtois, G., Véron M. and Agou, F. (2006) A point mutation in NEMO associated with anhidrotic ectodermal dysplasia with immunodeficiency pathology results in destabilization of the oligomer and reduces lipopolysaccharide- and tumor necrosis factor-mediated NF-kappa B activation. J. Biol. Chem., 281, 6334-6348.
• Galetto, R., Giacomoni, V., Véron, M. and Negroni, M. (2006) Dissection of a circumscribed recombination hot spot in HIV-1 after a single infectious cycle. J. Biol. Chem., 281, 2711-2720.
• Chen, Y., Morera, S., Pasti, C., Angusti, A., Solaroli, N., Véron, M., Janin, J., Manfredini, S. and Deville-Bonne, D. (2005) Adenosine phosphonoacetic acid is slowly metabolized by NDP Kinase. Med. Chem., 1, 529-536.
• Agou, F., Courtois, G., Chiaravalli, J., Baleux, F., Coïc, Y.-M., Traincard, F., Israël, A. and Véron, M. (2004) Inhibition of NF-kB activation by peptides targeting NEMO oligomerisation. J. Biol. Chem., 279, 54248-54257.
  
• Galetto, R., Moumen, A. Giacomoni, V., Véron, M., Charneau, P. and Negroni, M. (2004) The structure of HIV-1 genomic RNA in ghe gp120 gene determines a recombination hot spot in vivo. J. Biol. Chem., 279, 36625-36632.
• Agou, F., Traincard, F., Vinolo, E., Courtois, G., Yamaoka, S., Israël, A., Véron, M. (2004) The trimerization domain of NEMO is composed of the interacting C terminal CC2 and LZ coiled-coil subdomains. J. Biol. Chem., 279, 27861-27869.
  
• Chen, Y. Gallois-Montbrun, S., Schneider, B., Véron, M., Moréra, S., Deville Bonne, D. & Janin, J. (2003) Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK A in complex with ADP and a comparison to protein kinases. J. Mol. Biol., 332, 915-926
• Moumen, A., Polomack, L., Unge, T., Veron, M., Buc, H. and Negroni, M. (2003) Evidence for a mechanism of recombination during reverse transcription dependent on the structure of the acceptor RNA. J. Biol. Chem., 278, 15973-15982
• Pasti, C., Gallois-Montbrun, S., Munier-Lehman, H., Véron, M., Gilles, A.-M., and Deville-Bonne, D. (2003) Reaction of human UMP-CMP kinase with natural and analog substrates. Eur. J. Biochem., 270, 1784-1790.
  
• Gallois-Montbrun, S., Schneider, B., Chen, Y., Giacomoni-Fernandes, V., Mulard, L., Morera, S., Janin, J., Deville Bonne, D. and Véron, M. (2002) Improving nucleotide diphosphate kinase for antiviral nucleotide analogs activation. J. Biol. Chem., 277, 39953-39959.
• Schneider, B., Norda, A., Karlsson, A., Veron, M. and Deville-Bonne, D. (2002) Nucleotide affinity for a stable phosphorylated intermediate of nucleoside diphosphate kinase. Prot. Sci., 11, 1648-1656.
• Agou, F., Ye, F., Goffinont, S., Courtois, G. Yamaoka, S., Israël, A. and Véron, M. (2002) NEMO trimerizes though its coiled-coil C-terminal domain. J. Biol. Chem., 277, 17464-17475.
• Traincard, F., Ponte, E., Pun, J., Coukell, B. and Veron, M. (2001) The NF-kB like DNA binding activity observed in Dictyostelium nuclear extracts is due to the GBF transcription factor. J. Cell Sci., 114,  3767-3769.
  
• Raveh, S., Vinh, J., Rossier J., Agou, F., and Véron, M. (2001) Peptidic determinants and structural model of human NDP-kinase B (Nm23-H2) bound to single stranded DNA. Biochemistry, 40, 5882-5893.
• Schneider, B., Babolat, M., Xu, Y. W., Janin, J., Véron, M. and Deville-Bonne, D. (2001) Mechanism of phosphoryl transfer by Nucleoside Diphosphate Kinase : pH-dependence and role of the active site Lys 16 and Tyr 56 residues. Eur. J. Biochem., 268, 1964-1971
• Meyer, P., Schneider, B., Sarfati, S., Deville-Bonne, D., Guerreiro, C., Boretto, J., Janin, J., Véron, M. and Canard, B. (2000) Structural basis for activation of α-boranophosphate nucleotide analogues targeting drug-resistant reverse transcriptase. EMBO J., 19, 3520-3529.
  
• Traincard, F., Ponte, E., Pun, J., Coukell, B. and Véron, M. (1999) Evidence for the presence of a NF-kB signal transduction system in Dictyostelium discoideum. J. Cell Sci., 112, 3529-3535.
  
• Admiraal, S. J., Schneider, B., Meyer, P., Janin, J., Veron, M., Deville-Bonne, D. and Herschlag, D. (1999) Nucleophilic activation by positioning in phosphoryl transfer catalyzed by Nucleoside Diphosphate Kinase. Biochemistry, 38, 4701-4711.
• Agou, F., Raveh, S., Mesnildrey, S. and Véron, M. (1999) Single strand DNA specificity analysis of human NDP kinase B. J. Biol. Chem., 274, 19630-19638.
• Biondi, R. M., Baehler, P. J., Reymond, C. D. and Véron, M. (1998). Random insertion of GFP into the cAMP dependent protein kinase regulatory subunit from Dictyostelium discoideum. Nucleic Acid Res., 26, 4946-4952.
• Schneider, B., Xu, Y. W., Janin, J., Veron, M. and Deville-Bonne, D. (1998). 3’ phosphorylated nucleotides : tight binding inhibitors of NDP kinase activity. J. Biol. Chem., 273, 28773-28778.
• Schneider, B., Xu, Y., Sellam, O., Sarfati, R., Janin, J., Véron, M. and Deville-Bonne, D. (1998) Pre-steady state of reaction of Nucleoside Diphosphate Kinase with anti-HIV nucleotides. J. Biol. Chem., 273, 11491-11497.
• Mesnildrey, S., Agou, F., Karlsson, A., Deville-Bonne, D. and Véron, M. (1998) Coupling between catalysis and oligomeric structure in NDP kinase. J. Biol. Chem., 273, 4436-4442.
• Xu, Y., Sellam, O., Moréra, S., Sarfati, S., Biondi, R., Véron, M. and Janin, J. (1997) Nucleoside diphosphate kinase and the activation of AZT. Proc. Natl. Acad. Sci. USA, 94, 7162-7165.
  
• Etchebehere, L., Van Bemmellen, M., Anjard, C., Traincard, F., Assemat, K., Reymond, C., and Véron, M. (1997) The C subunit of Dictyostelium cAMP protein kinase: Role of the amino terminal domain and of the carboxy-terminal residues in catalytic activity and stability. Eur. J. Biochem., 248, 820-826.
• Deville-Bonne, D., Sellam, O., Merola, F., Lascu, I., Desmadril, M. and Véron, M. (1996) Phosphorylation of Nucleoside Diphosphate Kinase at the active site studied by steady-state and time-resolved fluorescence. Biochemistry, 35, 14643-14650.
• Kraeft, S., Traincard, F., Mesnildrey, S., Bourdais, J., Véron, M. and Chen, LB. (1996) Immunofluorescent localization of NDP kinase (NM23) in cultured cell lines. Exp. Cell Res., 227, 63-69.
• Xu, J., Liu, L.Z., Deng, X.F., Timmons, L., Hersperger, E., Steeg, P., Veron, M. and Shearn, A. (1996) The enzymatic activity of Drosophila AWD/NDP kinase is necessary but not sufficient for its biological function. Develop. Biol., 177, 544-557.
• Karlsson, A. Mesnildrey, S., Xu, Y., Morera, S. Janin, J. and Véron, M. (1996) Nucleoside Diphosphate Kinase. Investigation of the intersubunit contacts by site-directed mutagenesis and crystallography. J. Biol. Chem., 271, 19928-19934.
• Easty, D. J., Maung, K., Lascu, I., Véron, M., Fallowfield, M. E., Hart, I. R. and Bennett, D. C. (1996) Expression of NM23 in human melanoma progression and metastasis. British J. Cancer, 74, 109-114.
• Bourdais, J., Biondi, R., Lascu, I., Sarfati, S., Guerreiro, C., Janin, J. and Véron, M. (1996) Cellular phosphorylation of anti-HIV nucleosides: role of NDP kinase. J. Biol. Chem., 271, 7887-7890.
• Engel, M., Véron, M., Theisinger, B., Lacombe, M-L., Seib, T., Dooley, S. and Welter, C. (1996) A novel serine/threonine specific protein phosphotransferase activity of Nm23/ NDP kinase. Eur. J. Biochem., 234, 200-207.
• Gutlich, M., Witter, K., Bourdais, J., Rodl, W., Véron, M. and Ziegler, I. (1996) Control of Dictyopterin (D-threo-Biopterin) synthesis during aggregation of Dictyostelium. Biochem. J., 314, 95-101.
• Hildebrandt, M., Lacombe, M-L., Mesnildrey, S. and Véron, M. (1995) Human NDP-Kinase B binds specifically to single-stranded poly-pyrimidine DNA sequences. Nucleic Acid Res., 23, 3858-3864.
• Lecroisey, A., Lascu, I., Bominaar, A., Véron, M. and Delepierre, M. (1995) Phosphorylation mechanism of Nucleoside Diphosphate Kinase: 31P-nuclear magnetic resonance studies. Biochemistry, 34, 12445-12450.
• Aryee, D. N. T., Ströbel, T., Kos, K., Salzer-Kuntschik, M., Zoubek, A., Véron, M., Ambros, I. M., Traincard, F., Gadner, H. and Kovar, H. (1995) High NM23-H1/NDPK-a expression in Ewing tumors: paradoxical immunohistochemical reactivity and lack of prognostic significance. Int. J. Cancer, 64, 104-111.
• Tepper, A.D., Dammann, H., Bominaar, A.A. and Véron, M. (1994) Investigation of the active site and conformational stability of nucleoside diphosphate kinase by site-directed mutagenesis. J. Biol. Chem., 269, 32175-32180.
• Bominaar, A. A., Tepper, A.D. and Véron, M. (1994) Autophosphorylation of Nucleoside Diphosphate Kinase on non histidine residues. FEBS Lett., 353, 5-8.
• Morera, S., Dumas, C., Lascu, I., Lacombe, M-L., Véron, M. and Janin, J. (1994) X-ray Structure of Dictyostelium Nucleoside Diphosphate Kinase at 1.8 Å resolution. J. Mol. Biol., 243, 373-390.
• Véron, M., Radsio-Andzelm, E., Tsigelny, I. and Taylor, S.S. (1994) The Protein kinases share a common structural motif outsite the conserved catalytic domain. Cell. Mol. Biol., 40, 587-596.
• Cherfils, J., Moréra, S., Lascu, I., Véron, M. and Janin, J. (1994) X-ray structure of nucleoside diphosphate kinase complexed with dTDP and Mg++ at 2Å resolution. Biochemistry, 33, 9062-9069.
• Moréra, S., Lascu, I., Dumas, C., LeBras, G., Briozzo, P., Véron, M. and Janin, J. (1994) ADP binding and the active site of nucleoside diphosphate kinase. Biochemistry, 33, 459-467.
• Sawan, A., Lascu, I., Véron, M., Anderson, J.J., Wright, C., Horne, C.H.W. and Angus, B. (1994) NDP-K/NM23 expression in human breast cancer in relation to relapse, survival, and other prognostic factors: an immunohistochemical study. J. Pathol., 172, 27-34.
• Chiadmi, M., Moréra, S., Lascu, I., Dumas, C., LeBras, G., Véron, M. and Janin, J. (1993) The Awd Nucleoside Diphosphate Kinase from Drosophila. Structure, 1, 283-293.
• Véron, M., Radsio-Andzelm, E., Tsigelny, I., Ten Eyck, L.F. and Taylor, S.S. (1993) A conserved helix motif complements the Protein Kinase core. Proc. Natl. Acad. Sci. USA, 90, 10618-10622.
• Anjard, C., Etchebehere, L., Pinaud, S., Véron, M. and Reymond, C.D. (1993) An unsual catalytic subunit for the cAMP dependent protein kinase of Dictyostelium discoideum. Biochemistry, 32, 9532-9538.
• Etchebehere, L., Simon, M-N., Ballego Campanha, R., Veron, M. and Da Costa Maia, J.C. (1993) Developmental regulation of hexosamine synthesis by protein phosphatases 2A and 2C in Blastocladiella emersonii. J. Bact., 175, 5022-5027.
• Hopper, N. A. Harwood, AJ., Bouzid, S., Véron, M. and Williams, J.G. (1993) Activation of the prespore and spore cell pathway of Dictyostelium differentiation by cAMP-dependent protein kinase and evidence for its upstream regulation by ammonia. EMBO J., 12, 2459-2466.
• Troll, H., Winkler, T., Lascu, I., Müller, N., Véron, M. and Mutzel, R. (1993) Separate nuclear genes encode cytosolic and mitochondrial Nucleoside Diphosphate Kinase in Dictyostelium discoideum. J. Biol. Chem., 34, 25469-25475.
• Lascu, I., Deville-Bonne, D., Glazer, P. and Véron, M. (1993) Equilibrium dissociation and unfolding of nucleoside diphosphate kinase from Dictyostelium discoideum. Role of proline 100 in the stability of the hexameric enzyme. J. Biol. Chem., 268,  20268-20275.
• Bominaar, A.A., Molijn, A.C., Pestel, M., Véron, M. and Van Haastert, P.J.M. (1993) GTP formation and activation of G-proteins by receptor-stimulated NDP-Kinase in Dictyostelium. EMBO J., 12, 2275-2279.
• Wetterauer, B., Véron, M., Miginiac-Maslow, M., Decottignies, P. and Jacquot, J-P. (1992) Biochemical characterization of Thioredoxin 1 from Dictyostelium discoideum. Eur. J. Biochem., 209, 643-649.
• Wetterauer, B., Jacquot, J-P. and Véron, M. (1992) Thioredoxins from Dictyostelium discoideum are a developmentally regulated multigene familly. J. Biol. Chem., 267, 9895-9904.
  
• Harwood, A.J., Simon, M-N., Hopper, N.A., Driscoll, D., Véron, M. and Williams, J.G. (1992) Culmination in Dictyostelium is regulated by the cAMP dependent protein kinase. Cell, 69, 615-624.
• Simon, M-N., Pellegrini, O., Veron, M. and Kay, R. (1992) Mutation of protein kinase A causes heterochronic development of Dictyostelium. Nature, 356, 171-172.
• Harwood, A.J. , Hopper, N.A., Simon, M-N., Bouzid, S., Veron, M. and Williams, J.G. (1992) Multiples roles for cAMP dependent protein kinase during Dictyostelium development. Develop. Biol., 149, 90-99.
• Lascu, I., Chaffotte, A., Limbourg-Bouchon, B. and Véron, M. (1992) A Pro/Ser substitution in nucleoside diphosphate kinase of Drosophila melanogaster (mutation Killer of prune) affects stability but not catalytic efficiency of the enzyme. J. Biol. Chem., 267, 12775-12781.
• Sastre-Gareau, X., Lacombe, M-L., Jouve, M., Véron, M. and Magdelenat, H. (1992) Nucleoside Diphosphate Kinase/NM23 expression in breast cancers : lack of correlation with lymph node metastasis. Int. J. Cancer, 50, 533-538.
• Keim, D., Hailat, N., Melhem, R., Zhu,X.X., Lascu, I., Veron, M., Strahler, J. and Hanash, S.M. (1992) Proliferation related expression of P19/NM23 Nucleoside Diphosphate Kinase. J. Clinic. Invest., 89, 919-924.
• Lacombe, M-L., Sastre-Gareau, X., Lascu, I., Wallet, V., Thiery, J-P. and Veron, M. (1991) Overexpression of Nucleoside Diphosphate Kinase (Nm23) in human solid tumors. Eur. J. Cancer, 27, 1302-1307.
  
• Dumas, C., Lebras, G., Wallet, V., Lacombe, M-L., Véron, M. and Janin, J. (1991) Crystallisation and preliminary X-ray diffraction studies of Nucleoside Diphosphate Kinase from Dictyostelium discoideum. J. Mol. Biol., 217, 239-240.
• Wallet, V., Mutzel, R., Troll, H., Barzu, O., Wurster, B., Véron, M. and Lacombe, M-L. (1990) A developmentally regulated Dictyostelium nucleoside diphosphate kinase is highly homologous to the Nm23/Awd proteins involved in mammalian tumor metastasis and Drosophila development. J. Nat. Cancer Inst., 82, 1199-1202.
• Lacombe, M.-L., Wallet, V., Troll, H. and Véron, M. (1990) Functional cloning of a nucleoside diphosphate kinase from Dictyostelium discoideum. J. Biol. Chem., 265, 10012-10018.
• Simon, M.N., Driscoll, D., Mutzel, R., Part, D., Wiliams, J. and Veron, M. (1989) Overexpression of the regulatorry subunit of the cAMP-dependent protein kinase blocks the differentiation of Dictyostelium discoideum. EMBO J., 8, 2039-2043.
• Guitton, M.-C., Part, D. and Veron, M. (1988) Cloning of a cDNA for the S-adenosyl-L-homocysteine hydrolase from Dictyostelium discoideum. Biochimie, 70, 835-840.
  
• Mutzel, R., Simon, M.-N., Lacombe, M.-L., and Veron, M. (1988) Expression and properties of the regulatory subunit of Dictyostelium discoideum cAMP-dependent protein kinase encoded by lgt11 cDNA clones. Biochemistry, 27, 481-486.
• Lacombe, M.-L., Ladant, D., Mutzel, R. and Véron, M. (1987) Gene isolation by direct in situ cAMP binding. Gene, 58, 29-36.
• Mutzel, R., Lacombe, M.-L., Simon, M.-N., de Gunzburg, J. and Véron, M. (1987) cAMP-dependent protein kinase from Dictyostelium discoideum: cloning and cDNA sequence of the regulatory subunit. Proc. Natl. Acad. Sci. USA, 84, 6-10.
• De Gunzburg, J., Franke, J., Kessin, R. and Véron, M. (1986) Detection and developmental regulation of the mRNA for the regulatory subunit of the cAMP-dependent protein kinase of Dictyostelium discoideum by cell-free translation. EMBO J., 5, 363-367.
  
• Hohman, R.J., Guitton, M.C. and Véron, M. (1985) Inactivation of S-adenosyl-L-homocysteine hydrolase by cAMP results from dissociation of enzyme-bound NAD+. Proc. Natl. Acad. Sci. USA, 82, 4578-4581.
  
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• Agou, F., Courtois, G., Israël, A., Véron, M., Traincard, F., Yamaoka, S., Baleux, F. and Coïc, Y.-M.: Selective inhibition of NF-κB activation by peptides designed to disrupt NEMO oligomerization – International application : PCT/IB2004/003352 edited on 24-09-2004 N° W0/2005/027959
• Traincard, F., Véron, M. and Agou, F.: Identification of substances that inhibit NEMO oligomerization – USA application : US 2009-0269748 deposited on 13-06-2008
• Chiaravalli, J., Coïc, Y.-M., Baleux, F., Israël, A., Véron, M. and Agou, F.: Method for screening for selective inhibitor of the NF-κB activation – International application : PCT/IB2008/00263 edited on 20-06-2008 N° WO/2009/001222
• Grubisha, O., Duquerroy, S., Chiaravalli, J., Kaminska, M., Fontan, E., Véron, M., Agou F. and Cordier, F.: Structure cristalline du domaine CC2-LZ de NEMO – International application : PCT/FR2009/00127 edited on 05-02-2009 N° WO/2009/115664


Last Update : February 2011