Parents
Sign in to add mentor| Jean-Marie Seigneurin | grad student | 1993 | Grenoble 1 | |
| (La protéine EBNA-2 du virus Epstein-Barr (EBV) : étude selon le type viral de la séquence nucléotidique du gène, de l'antigénicité et de la réponse anticorps chez les patients infectés par le virus de l'immunodéficience humaine) | ||||
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Publications
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| Habib M, Buisson M, Lupo J, et al. (2017) Lytic EBV infection investigated by detection of Soluble Epstein-Barr virus ZEBRA in the serum of patients with PTLD. Scientific Reports. 7: 10479 |
| Yabukarksi F, Leyrat C, Martinez N, et al. (2016) Ensemble Structure of the Highly Flexible Complex Formed between Vesicular Stomatitis Virus Unassembled Nucleoprotein and its Phosphoprotein Chaperone. Journal of Molecular Biology |
| Thierry E, Brennich M, Round A, et al. (2015) Production and characterisation of Epstein-Barr virus helicase-primase complex and its accessory protein BBLF2/3. Virus Genes. 51: 171-81 |
| Burmeister WP, Buisson M, Estrozi LF, et al. (2015) Structure determination of feline calicivirus virus-like particles in the context of a pseudo-octahedral arrangement. Plos One. 10: e0119289 |
| Horst D, Burmeister WP, Boer IG, et al. (2012) The "Bridge" in the Epstein-Barr virus alkaline exonuclease protein BGLF5 contributes to shutoff activity during productive infection. Journal of Virology. 86: 9175-87 |
| Lupo J, Germi R, Semenova T, et al. (2012) Performance of two commercially available automated immunoassays for the determination of Epstein-Barr virus serological status. Clinical and Vaccine Immunology : Cvi. 19: 929-34 |
| van Gent M, Griffin BD, Berkhoff EG, et al. (2011) EBV lytic-phase protein BGLF5 contributes to TLR9 downregulation during productive infection. Journal of Immunology (Baltimore, Md. : 1950). 186: 1694-702 |
| Larrat S, Morand P, Bas A, et al. (2009) Inhibition of Epstein-Barr virus replication by small interfering RNA targeting the Epstein-Barr virus protease gene. Antiviral Therapy. 14: 655-62 |
| Freeman L, Buisson M, Tarbouriech N, et al. (2009) The flexible motif V of Epstein-Barr virus deoxyuridine 5'-triphosphate pyrophosphatase is essential for catalysis. The Journal of Biological Chemistry. 284: 25280-9 |
| Buisson M, Géoui T, Flot D, et al. (2009) A bridge crosses the active-site canyon of the Epstein-Barr virus nuclease with DNase and RNase activities. Journal of Molecular Biology. 391: 717-28 |