Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Adeline Derouaux"'
Autor:
Adrien Boes, Jean Michel Brunel, Adeline Derouaux, Frédéric Kerff, Ahmed Bouhss, Thierry Touze, Eefjan Breukink, Mohammed Terrak
Publikováno v:
Antibiotics, Vol 9, Iss 7, p 373 (2020)
Peptidoglycan (PG) is an essential polymer of the bacterial cell wall and a major antibacterial target. Its synthesis requires glycosyltransferase (GTase) and transpeptidase enzymes that, respectively, catalyze glycan chain elongation and their cross
Externí odkaz:
https://doaj.org/article/a8126a6e31d2404a824835bca431e117
Autor:
Eric Sauvage, Adeline Derouaux, Claudine Fraipont, Marine Joris, Raphaël Herman, Mathieu Rocaboy, Marie Schloesser, Jacques Dumas, Frédéric Kerff, Martine Nguyen-Distèche, Paulette Charlier
Publikováno v:
PLoS ONE, Vol 9, Iss 5, p e98042 (2014)
In Escherichia coli, penicillin-binding protein 3 (PBP3), also known as FtsI, is a central component of the divisome, catalyzing cross-linking of the cell wall peptidoglycan during cell division. PBP3 is mainly periplasmic, with a 23 residues cytopla
Externí odkaz:
https://doaj.org/article/d19d6b7d9fdf4f26802af6ec423fa307
Autor:
Rob Till, Joe W. Gray, Waldemar Vollmer, Yves V. Brun, Adrien Ducret, Erkin Kuru, R. Elizabeth Sockett, Jacob Biboy, Michael S. VanNieuwenhze, Carey Lambert, Jonathan Rittichier, Adeline Derouaux
Publikováno v:
Nature microbiology
Modification of essential bacterial peptidoglycan (PG) containing cell walls can lead to antibiotic resistance, for example β-lactam resistance by L,D-transpeptidase activities. Predatory Bdellovibrio bacteriovorus are naturally antibacterial and co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bae9d9f3ab0a21e4743563f9480ba83
https://doi.org/10.1038/s41564-017-0029-y
https://doi.org/10.1038/s41564-017-0029-y
Autor:
Mohammed Terrak, Piet Herdewijn, André Piette, Eveline Lescrinier, Adeline Derouaux, Bernard Joris, Shrinivas G. Dumbre
Publikováno v:
Journal of the American Chemical Society. 134:9343-9351
The peptidoglycan glycosyltransferases (GTs) are essential enzymes that catalyze the polymerization of glycan chains of the bacterial cell wall from lipid II and thus constitute a validated antibacterial target. Their enzymatic cavity is composed of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c888697f5a5720dd2d9130610465c6c8
https://doi.org/10.1021/ja302099u
https://doi.org/10.1021/ja302099u
Autor:
Martine Nguyen-Distèche, Nick K. Olrichs, Ana Maria Amoroso, Samo Turk, Jean-Marie Frère, Bernard Joris, Julieanne M. Bostock, Ian Chopra, Julien Offant, Katherine R. Mariner, Eefjan Breukink, Stanislav Gobec, Thierry Vernet, Adeline Derouaux, Mohammed Terrak, Astrid Zervosen
Publikováno v:
Biochemical Pharmacology
Biochemical Pharmacology, Elsevier, 2011, 81 (9), pp.1098. ⟨10.1016/j.bcp.2011.02.008⟩
Biochemical Pharmacology, Elsevier, 2011, 81 (9), pp.1098. ⟨10.1016/j.bcp.2011.02.008⟩
International audience; Bacterial peptidoglycan glycosyltransferases (GTs) of family 51 catalyze the polymerization of the lipid II precursor into linear peptidoglycan strands. This activity is essential to bacteria and represents a validated target
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55834dee6b61204793b307e3fa63e73a
https://doi.org/10.1016/j.bcp.2011.02.008
https://doi.org/10.1016/j.bcp.2011.02.008
Autor:
Thierry Vernet, Martine Nguyen-Distèche, André Zapun, Mohammed Terrak, Julien Offant, Eefjan Breukink, Adeline Derouaux
Publikováno v:
FEBS Journal. 277:4290-4298
Cell wall biosynthesis is a key target for antibacterial drugs. The major constituent of the bacterial wall, peptidoglycan, is a netlike polymer responsible for the size and shape of the cell and for resisting osmotic pressure. It consists of glycan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e33e867ce49df9651e016043c6352d94
https://doi.org/10.1111/j.1742-4658.2010.07817.x
https://doi.org/10.1111/j.1742-4658.2010.07817.x
Autor:
Rob Till, Yves V. Brun, Erkin Kuru, Jacob Biboy, Carey Lambert, Joe W. Gray, Jonathan Rittichier, Michael S. VanNieuwenhze, Adrien Ducret, R. Elizabeth Sockett, Adeline Derouaux, Waldemar Vollmer
Publikováno v:
Nature Microbiology. 3:254-254
In the original version of this Article, a grant number and acknowledgement were omitted. The Acknowledgements section should have stated that one of the 3D SIM microscopes used for this research was supported by Medical Research Council UK grant (MR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b01e27c6c3cf1e4062b653869fa1b20
https://doi.org/10.1038/s41564-017-0087-1
https://doi.org/10.1038/s41564-017-0087-1
Autor:
Irena Mlinarič Raščan, Martina Gobec, Eefjan Breukink, Mohammed Terrak, Adeline Derouaux, Izidor Sosič, Marko Anderluh, Matej Sova, Stanislav Gobec, Ana Maria Amoroso
Publikováno v:
Journal of medicinal chemistry. 58(24)
Penicillin-binding proteins represent well-established, validated, and still very promising targets for the design and development of new antibacterial agents. The transglycosylase domain of penicillin-binding proteins is especially important, as it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d317047db57dc808e0a065094433f2b
https://pubmed.ncbi.nlm.nih.gov/26588190
https://pubmed.ncbi.nlm.nih.gov/26588190
Autor:
Adeline Derouaux, Jean-Pierre Simorre, Waldemar Vollmer, Catherine M. Bougault, Gilles Callens, Nicolas L. Jean
Publikováno v:
Biomolecular NMR Assignments
Biomolecular NMR Assignments, 2015, pp.11
Biomolecular NMR Assignments, Springer, 2015, pp.11
Biomolecular NMR Assignments, 2015, pp.11
Biomolecular NMR Assignments, Springer, 2015, pp.11
International audience; The peptidoglycan is a major component of the bacterial cell wall and is essential to maintain cellular integrity and cell shape. Penicillin-Binding Proteins (PBPs) catalyze the final biosynthetic steps of peptidoglycan synthe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a599e9790fbcc1e9092d6ecfb9a5e7e8
https://hal.univ-grenoble-alpes.fr/hal-01119762
https://hal.univ-grenoble-alpes.fr/hal-01119762
Autor:
Georgios Moutzourelis, Harald Nothaft, Serkan Halici, Fritz Titgemeyer, Jozef Van Beeumen, Jean Dusart, Fabrizio Giannotta, Dominique Dehareng, Adeline Derouaux, Elke Lecocq, Sébastien Rigali, Bart Devreese
Publikováno v:
Biochemical and Biophysical Research Communications. 325:983-990
The chromosomal inactivation of the unique transcription factor of Streptomyces coelicolor that displays a cyclic-nucleotide-binding domain, Crp(Sco), led to a germination-defective phenotype similar to the mutant of the adenylate cyclase gene (cya)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3e9e593adfee095b0260695db121c0a
https://doi.org/10.1016/j.bbrc.2004.10.143
https://doi.org/10.1016/j.bbrc.2004.10.143