Peer-reviewed Publications:
43- Cutolo G., Didak B., Tomas J., Roubinet B, Lafite P., Nehmé R., Schuler M., Landemarre L., Tatibouët A., Carb. Res., 516, 2022, 108562. doi.org/10.1016/j.carres.2022.10856
42- Peyrot C.,Didak B.,Guillotin L.,Landemarre L.,Lafite P.,Lemiègre and R. Daniellou, European J. Org. Chem., 2021, 2021, 3812–3818. doi:10.1002/ejoc.202100672
41- Bretagne D., Pâris A., de Vaumas R., Lafite P., Daniellou R., Crystal structure of Dictyoglomus thermophilum β-d-xylosidase DtXyl unravels the structural determinants for efficient notoginsenoside R1 hydrolysis (2021) Biochimie. 18134–41. doi:10.1016/j.biochi.2020.11.017.
40- Domingues M., Jaszczyk J., Ismael M.I., Figueiredo J.A., Daniellou R., Lafite P., Schuler M., Tatibouët A. Conformationally Restricted Oxazolidin-2-one Fused Bicyclic Iminosugars as Potential Glycosidase Inhibitors, (2020) European J. Org. Chem. 2020 6109–6126. doi:10.1002/ejoc.202001053.
39- Papi, F., Pâris A., Lafite P., Daniellou R., Nativi C. Synthesis of an STnThr Analogue, Structurally Based on a TnThr Antigen Mimetic. (2020) Org. Biomol. Chem. 18 (37): 7366–72. https://doi.org/10.1039/D0OB01749C.
38- Kurdziel, M., Kopeć, M., Pâris, A., Lewiński, K., Lafite, P.*, Daniellou, R. Thioglycoligation of aromatic thiols using a natural glucuronide donor (2020) Org. Biomol. Chem. 18, 5582. https://doi.org/10.1039/d0ob00226g
37- Guillotin, L., Assaf, Z., Pistorio, S.G., Lafite, P., Demchenko, A. V., Daniellou, R. Hydrolysis of Glycosyl Thioimidates by Glycoside Hydrolase Requires Remote Activation for Efficient Activity. (2019) Catalysts 9, 826. https://doi.org/10.3390/catal9100826
36- Lafite P.*, Marroun S., Coadou G., Montaut S., Marquès S., Schuler M., Rollin P., Tatibouët A., Daniellou R., Oulyadi H. (2019) S-Glycosyltransferase UGT74B1 can glycosylate both S- and O-acceptors: mechanistic insights through substrate specificity. Mol. Catal. 479, 110631 https://doi.org/10.1016/j.mcat.2019.110631
35- Seničar M., Legentil L., Ferrières V., Eliseeva S.V., Petoud S., Takegawa K., Lafite P., Daniellou R. (2019). Galactofuranosidase from JHA 19 Streptomyces sp.: subcloning and biochemical characterization. Carbohyd. Res., 480, 35-41. https://www.doi.org/10.1016/j.carres.2019.05.011
34- Ferey J., Da Silva D., Colas C., Nehmé R., Lafite P., Roy V., Morin P., Daniellou R., Agrofoglio L., Maunit B. (2019). Monitoring of successive phosphorylations of thymidine using free and immobilized human nucleoside/nucleotide kinases by Flow Injection Analysis with High-Resolution Mass Spectrometry. Anal. Chim. Acta, 1049, 115-122. https://doi.org/10.1016/j.aca.2018.10.032
33- Guillotin, L., Kim, H., Traore, Y., Moreau, P., Lafite, P., Coquoin, V., Nuccio, S., de Vaumas, R. & Daniellou, R. (2019). Biochemical Characterization of the α-L-Rhamnosidase DtRha from Dictyoglomus thermophilum : Application to the Selective Derhamnosylation of Natural Flavonoids ACS Omega. 4, 1916–1922. https://www.doi.org/10.1021/acsomega.8b03186
32- Ati, J., Colas, C., Lafite, P., Sweeney, R. P., Zheng, R. B., Lowary T. L., Daniellou, R. (2018) The LPG1x family from Leishmania major is constituted of rare eukaryotic galactofuranosyltransferases with unprecedented catalytic properties. Sci. Rep., 8(1), 17566. https://www.doi.org/10.1038/s41598-018-35847-w
31- Ferey, J., Da Silva, D., Colas, C., Lafite, P., Topalis, D., Roy, V., Agrofoglio, L. A., Daniellou, R. & Maunit, B. Monitoring of phosphorylation using immobilized kinases by on-line enzyme bioreactors hyphenated with High-Resolution Mass Spectrometry (2019). Talanta. 205, 120120. https://www.doi.org/10.1016/j.talanta.2019.120120
30- Lafite, P., André, F., Graves, J., Zeldin, D., Dansette, P., Mansuy, D. (2018) Role of Arginine 117 in Substrate Recognition by Human Cytochrome P450 2J2. Int. J. Mol. Sci. 19, 2066. https://www.doi.org/10.3390/ijms19072066
29- Guillotin, L., Richet, N., Lafite, P.*, Daniellou, R. (2017). Is the acid/base catalytic residue mutation in β-D-mannosidase DtMan from Dictyoglomus thermophilum sufficient to provide thioglycoligase activity? Biochimie, 137, 190–196. https://www.doi.org/10.1016/j.biochi.2017.03.020
28- Guillotin, L., Cancellieri, P., Lafite, P., Landemarre, L., Daniellou, R., Corzo, N., Daniellou, R. (2017). Chemo-enzymatic synthesis of 3-O-(β-D-glycopyranosyl)-sn-glycerols and their evaluation as preservative in cosmetics. Pure App. Chem., 89(9), 11302. https://www.doi.org/10.1515/pac-2016-1210
27- Ferey, J., Da Silva, D., Lafite, P., Daniellou, R., Maunit, B. (2017). TLC-UV hyphenated with MALDI-TOFMS for the screening of invertase substrates in plant extracts. Talanta, 170, 419–424.https://www.doi.org/10.1016/j.talanta.2017.04.040
26- Ortmayer, M., Lafite, P., Menon, B. R. K., Tralau, T., Fisher, K., Denkhaus, L., Leys, D. (2016). An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme. Nature, 539(7630), 593–597. https://www.doi.org/10.1038/nature20159
25- Marroun, S., Montaut, S., Marquès, S., Lafite, P., Coadou, G., Rollin, P., Jousset, G., Tatibouët A, Oulyadi, H, Daniellou, R. (2016). UGT74B1 from Arabidopsis thaliana as a versatile biocatalyst for the synthesis of desulfoglycosinolates. Org. Biomol. Chem., 14(26), 6252–6261. https://www.doi.org/10.1039/c6ob01003b
24- Ferey, J., Da Silva, D., Bravo-Veyrat, S., Lafite, P., Daniellou, R., Maunit, B. (2016). Validation of a thin-layer chromatography/densitometry method for the characterization of invertase activity. J. Chrom. A, 1477, 108-113. https://www.doi.org/ 10.1016/j.chroma.2016.11.049
23- Sauvageot, E., Lafite, P., Duverger, E., Marion, R., Hamel, M., Gaillard, S., Daniellou, R. (2016). Iridium complexes inhibit tumor necrosis factor-alpha by utilizing light and mixed ligands. J. Organomet. Chem., 808, 122–127. https://www.doi.org/ 10.1016/j.jorganchem.2016.02.001
22- Belaz, S., Rattier, T., Lafite, P., Moreau, P., Routier, F. H., Robert-Gangneux, F., Gangneux, J-P., Daniellou, R. (2015). Identification, biochemical characterization, and in-vivo expression of the intracellular invertase BfrA from the pathogenic parasite Leishmania major. Carbohydr. Res., 415, 31–38. https://www.doi.org/ 10.1016/j.carres.2015.07.001
21- Fayad, S., Nehmé, R., Lafite, P., & Morin, P. (2015). Assaying human neutrophil elastase activity by capillary zone electrophoresis combined with laser-induced fluorescence. J. Chrom. A. 1419, 116-124. https://www.doi.org/ 10.1016/j.chroma.2015.09.084
20- François-Heude, M., Méndez-Ardoy, A., Cendret, V., Lafite, P., Daniellou, R., Ortiz Mellet, C., Garcìa Fernandez, J. M., Moreau, V., Djedaïni-Pilard, F. (2015). Synthesis of High-Mannose Oligosaccharide Analogues through Click Chemistry: True Functional Mimics of Their Natural Counterparts Against Lectins? Chem. Eur. J., 21(5), 1978–1991. https://www.doi.org/10.1002/chem.201405481
19- Guillotin, L., Lafite, P., Daniellou, R. (2014). Unraveling the Substrate Recognition Mechanism and Specificity of the Unusual Glycosyl Hydrolase Family 29 BT2192 from Bacteroides thetaiotaomicron. Biochemistry, 53(9), 1447–1455. https://www.doi.org/10.1021/bi400951q
18- Nehmé, R., Nehmé, H., Saurat, T., de-Tauzia, M.-L., Buron, F., Lafite, P., Verrelle, P., Chautard, E., Morin, P., Routier, S., Bénédetti, H. (2014). New in-capillary electrophoretic kinase assays to evaluate inhibitors of the PI3k/Akt/mTOR signaling pathway. Anal. Bioanal. Chem., 406(15), 3743–3754. https://www.doi.org/ 10.1007/s00216-014-7790-z
17- Amaral, M., Levy, C., Heyes, D. J., Lafite, P., Outeiro, T. F., Giorgini, F., Leys, D., Scrutton, N. S. (2013). Structural basis of kynurenine 3-monooxygenase inhibition. Nature, 496(7445), 382–385. https://www.doi.org/10.1038/nature12039
16- Barkauskaite, E., Brassington, A., Tan, E. S., Warwicker, J., Dunstan, M. S., Banos, B., Lafite P., Ahel I., Leys, D. (2013). Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities. Nat. Commun., 4, 2164. https://www.doi.org/10.1038/ncomms3164
15- Nehmé, H., Nehmé, R., Lafite, P., Routier, S., & Morin, P. (2013). In-capillary reactant mixing for monitoring glycerol kinase kinetics by capillary electrophoresis. J. Sep. Sci., 36(13), 2151–2157. https://www.doi.org/10.1002/jssc.201300063
14- Nehmé, H., Nehmé, R., Lafite, P., Duverger, E., Routier, S., Morin, P. (2013). Electrophoretically mediated microanalysis for in-capillary electrical cell lysis and fast enzyme quantification by capillary electrophoresis. Anal. Bioanal. Chem., 405(28), 9159–9167. https://www.doi.org/10.1007/s00216-013-7332-0
13- Nehmé, H., Nehmé, R., Lafite, P., Routier, S., Morin, P. (2013). Human protein kinase inhibitor screening by capillary electrophoresis using transverse diffusion of laminar flow profiles for reactant mixing. J. Chrom. A, 1314, 298–305. https://www.doi.org/ 10.1016/j.chroma.2013.08.046
12- Dunstan, M. S., Barkauskaite, E., Lafite, P., Knezevic, C. E., Brassington, A., Ahel, M., Hergenrother, P.J., Leys, D., Ahel, I. (2012). Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase. Nat. Comm., 3, 878. https://www.doi.org/10.1038/ncomms1889
11- Nehmé, H., Nehmé, R., Lafite, P., Routier, S., & Morin, P. (2012). New development in in-capillary electrophoresis techniques for kinetic and inhibition study of enzymes. Anal. Chim. Acta, 722, 127–135. https://www.doi.org/10.1016/j.aca.2012.02.003
10- Slade, D., Dunstan, M. S., Barkauskaite, E., Weston, R., Lafite, P., Dixon, N., Hergenrother, P. J., Leys, D., Ahel, I. (2011). The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase. Nature, 477(7366), 616–620. https://www.doi.org/10.1038/nature10404
9- Driscoll, M. D., McLean, K. J., Levy, C., Mast, N., Pikuleva, I. A., Lafite, P., Rigby, S. E. J., Leys, D., Munro, A. W. (2010). Structural and biochemical characterization of Mycobacterium tuberculosis CYP142. J. Biol. Chem., 285(49), 38270–38282. https://www.doi.org/10.1074/jbc.M110.164293
8- Heyes, D.J., Levy, C., Lafite, P., Roberts, I. S., Goldrick, M., Stachulski, A.V., Rossington, S.B., Stanford, D., Rigby, S.E., Scrutton, N.S., Leys, D. (2009). Structure-based mechanism of CMP-2-keto-3-deoxymanno-octulonic acid synthetase: convergent evolution of a sugar-activating enzyme with DNA/RNA polymerases. J. Biol. Chem., 284(51), 35514–35523. https://www.doi.org/10.1074/jbc.M109.056630
7- McLean, K. J., Lafite, P., Levy, C., Cheesman, M. R., Mast, N., Pikuleva, I. A., Leys, D, Munro, A. W. (2009). The structure of Mycobacterium tuberculosis CYP125 molecular basis for cholesterol binding in a P450 needed for host infection. J. Biol. Chem., 284(51), 35524–35533. https://www.doi.org/10.1074/jbc.M109.032706
6- Pudney, C. R., McGrory, T., Lafite, P., Pang, J. Y., Hay, S., Leys, D., Sutcliffe, M. J. , Scrutton, N. S. (2009). Parallel pathways and free-energy landscapes for enzymatic hydride transfer probed by hydrostatic pressure. Chembiochem, 10(8), 1379–1384. https://www.doi.org/10.1002/cbic.200900071
5- Tralau, T., Lafite, P., Levy, C., Combe, J. P., Scrutton, N. S., Leys, D. (2009). An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde. J. Biol. Chem., 284(26), 17826–17834. https://www.doi.org/ 10.1074/jbc.M109.006262
4- Lafite, P., André, F., Zeldin, D. C., Dansette, P. M., Mansuy, D. (2007). Unusual regioselectivity and active site topology of human cytochrome P450 2J2. Biochemistry, 46(36), 10238–10247. https://www.doi.org/10.1021/bi700876a
3- Lafite, P., Dijols, S., Zeldin, D. C., Dansette, P. M., Mansuy, D. (2007). Selective, competitive and mechanism-based inhibitors of human cytochrome P450 2J2. Arch. Biochem. Biophys., 464(2), 155–168. https://www.doi.org/10.1016/j.abb.2007.03.028
2- Lafite, P., Dijols, S., Buisson, D., Macherey, A. C., Zeldin, D. C., Dansette, P. M., Mansuy, D. (2006). Design and synthesis of selective, high-affinity inhibitors of human cytochrome P450 2J2. Bioorg. Med. Chem. Lett., 16(10), 2777–2780. https://www.doi.org/10.1016/j.bmcl.2006.02.004
1- Pfister, S. L., Spitzbarth, N., Zeldin, D. C., Lafite, P., Mansuy, D., Campbell, W. B. (2003). Rabbit aorta converts 15-HPETE to trihydroxyeicosatrienoic acids: potential role of cytochrome P450. Arch. Biochem. Biophys., 420(1), 142–152. https://doi.org/10.1016/j.abb.2003.09.026
Patent:
1- Yaacoub K., Guillaudeux T., Daniellou R., Lafite P., Aci-Sèche S., Bonnet P., Selective c-FLIP Inhibitors as anticancer agents. Eur. Pat. EP 3323428 (23/05/18); Int. Pat. WO 2018/091647 (24/05/18).
Reviews:
4- Seničar, M. ; Lafite, P. ; Eliseeva, S. ; Petoud, S. ; Landemarre, L. ; Daniellou, R. Galactofuranose-related enzymes: challenges and hopes (2020) Int. J. Mol. Sci. 21, 3465. https://dx.doi.org/10.3390/ijms21103465
3- Ati, J, Lafite P., Daniellou R (2017). Enzymatic synthesis of glycosides: from natural O- and N-glycosides to rare C- and S-glycosides. Belstein J. Org. Chem., 13, 1857-1865. https://www.doi.org/10.3762/bjoc.13.180
2- Lafite, P., Daniellou, R. (2012). Rare and unusual glycosylation of peptides and proteins. Nat. Prod. Rep., 29(7), 729–738. https://www.doi.org/10.1039/c2np20030a
1- Mansuy, D., Lafite, P. (2007). Great adaptability of the heme-cysteinate monooxygenases family to very diverse substrates and sophisticated reactions. J Porphyr. Phtalocyan., 11(3–4), 258–268. https://www.doi.org/ 10.1142/S108842460700031X
Book Chapters:
3- Bretagne D, Wagner G.K., Lafite P., Daniellou R. (2021) In situ formation of nucleotide-sugars from simple substrates for glycosyltransferase-catalyzed reactions. In Carbohydrate Chemistry: Volume 45 (Vol. 45, pp. 336-351). The Royal Society of Chemistry. doi.org/10.1039/9781839164538-00336
2- Peyrot C., Lafite, P., Lemiègre L., Daniellou, R. (2017) Low molecular weight carbohydrate-based hydrogelators In Carbohydrate Chemistry: Volume 43 (Vol. 43, pp. 245-265). The Royal Society of Chemistry. https://www.doi.org/ 10.1039/9781788010641-00245
1- Guillotin, L., Lafite, P., Daniellou, R. (2014). Chapter 10 : Enzymatic thioglycosylation: current knowledge and challenges. In Carbohydrate Chemistry: Volume 40 (Vol. 40, pp. 178–194). The Royal Society of Chemistry. https://www.doi.org/ 10.1039/9781849739986-00178
