Year |
Citation |
Score |
2023 |
Ladeveze S, Zurek PJ, Kaminski TS, Emond S, Hollfelder F. Versatile Product Detection via Coupled Assays for Ultrahigh-Throughput Screening of Carbohydrate-Active Enzymes in Microfluidic Droplets. Acs Catalysis. 13: 10232-10243. PMID 37560191 DOI: 10.1021/acscatal.3c01609 |
0.368 |
|
2020 |
Emond S, Petek M, Kay EJ, Heames B, Devenish SRA, Tokuriki N, Hollfelder F. Accessing unexplored regions of sequence space in directed enzyme evolution via insertion/deletion mutagenesis. Nature Communications. 11: 3469. PMID 32651386 DOI: 10.1038/S41467-020-17061-3 |
0.382 |
|
2019 |
Daudé D, Vergès A, Cambon E, Emond S, Tranier S, André I, Remaud-Siméon M. Neutral Genetic Drift-Based Engineering of a Sucrose-Utilizing Enzyme toward Glycodiversification Acs Catalysis. 9: 1241-1252. DOI: 10.1021/Acscatal.8B03609 |
0.452 |
|
2017 |
Montanier CY, Chabot N, Emond S, Guieysse D, Remaud-Siméon M, Peruch F, André I. Engineering of Candida antarctica lipase B for poly(ε-caprolactone) synthesis European Polymer Journal. 95: 809-819. DOI: 10.1016/J.Eurpolymj.2017.07.029 |
0.669 |
|
2016 |
Gielen F, Hours R, Emond S, Fischlechner M, Schell U, Hollfelder F. Ultrahigh-throughput-directed enzyme evolution by absorbance-activated droplet sorting (AADS). Proceedings of the National Academy of Sciences of the United States of America. 113: E7383-E7389. PMID 27821774 DOI: 10.1073/Pnas.1606927113 |
0.475 |
|
2016 |
Kaltenbach M, Emond S, Hollfelder F, Tokuriki N. Functional Trade-Offs in Promiscuous Enzymes Cannot Be Explained by Intrinsic Mutational Robustness of the Native Activity. Plos Genetics. 12: e1006305. PMID 27716796 DOI: 10.1371/Journal.Pgen.1006305 |
0.414 |
|
2012 |
Theerachat M, Emond S, Cambon E, Bordes F, Marty A, Nicaud JM, Chulalaksananukul W, Guieysse D, Remaud-Siméon M, Morel S. Engineering and production of laccase from Trametes versicolor in the yeast Yarrowia lipolytica. Bioresource Technology. 125: 267-74. PMID 23026343 DOI: 10.1016/J.Biortech.2012.07.117 |
0.657 |
|
2012 |
Emond S, Guieysse D, Lechevallier S, Dexpert-Ghys J, Monsan P, Remaud-Siméon M. Alteration of enzyme activity and enantioselectivity by biomimetic encapsulation in silica particles Chemical Communications. 48: 1314-1316. PMID 22158825 DOI: 10.1039/C1Cc14478B |
0.628 |
|
2010 |
Mondon P, Grand D, Souyris N, Emond S, Bouayadi K, Kharrat H. Mutagen: a random mutagenesis method providing a complementary diversity generated by human error-prone DNA polymerases. Methods in Molecular Biology (Clifton, N.J.). 634: 373-86. PMID 20676997 DOI: 10.1007/978-1-60761-652-8_26 |
0.313 |
|
2010 |
Emond S, Montanier C, Nicaud JM, Marty A, Monsan P, André I, Remaud-Siméon M. New efficient recombinant expression system to engineer Candida antarctica lipase B. Applied and Environmental Microbiology. 76: 2684-7. PMID 20173074 DOI: 10.1128/Aem.03057-09 |
0.625 |
|
2008 |
Emond S, Mondeil S, Jaziri K, André I, Monsan P, Remaud-Siméon M, Potocki-Véronèse G. Cloning, purification and characterization of a thermostable amylosucrase from Deinococcus geothermalis. Fems Microbiology Letters. 285: 25-32. PMID 18522649 DOI: 10.1111/J.1574-6968.2008.01204.X |
0.589 |
|
2008 |
Emond S, André I, Jaziri K, Potocki-Véronèse G, Mondon P, Bouayadi K, Kharrat H, Monsan P, Remaud-Simeon M. Combinatorial engineering to enhance thermostability of amylosucrase. Protein Science : a Publication of the Protein Society. 17: 967-76. PMID 18441231 DOI: 10.1110/Ps.083492608 |
0.644 |
|
2008 |
Emond S, Mondon P, Pizzut-Serin S, Douchy L, Crozet F, Bouayadi K, Kharrat H, Potocki-Véronèse G, Monsan P, Remaud-Simeon M. A novel random mutagenesis approach using human mutagenic DNA polymerases to generate enzyme variant libraries Protein Engineering, Design and Selection. 21: 267-274. PMID 18287177 DOI: 10.1093/Protein/Gzn004 |
0.559 |
|
2007 |
Emond S, Potocki-Véronèse G, Mondon P, Bouayadi K, Kharrat H, Monsan P, Remaud-Simeon M. Optimized and automated protocols for high-throughput screening of amylosucrase libraries Journal of Biomolecular Screening. 12: 715-723. PMID 17517906 DOI: 10.1177/1087057107301978 |
0.616 |
|
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