Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Stéphane Skouloubris"'
Autor:
Andreea Sodolescu, Cyril Dian, Laurent Terradot, Latifa Bouzhir-Sima, Roxane Lestini, Hannu Myllykallio, Stéphane Skouloubris, Ursula Liebl
Publikováno v:
PLoS ONE, Vol 13, Iss 12, p e0208850 (2018)
Serine hydroxymethyltransferase (SHMT), encoded by the glyA gene, is a ubiquitous pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the formation of glycine from serine. The thereby generated 5,10-methylene tetrahydrofolate (MTHF) is a maj
Externí odkaz:
https://doaj.org/article/948ddc00bab64642a468e1771d278205
Autor:
Stéphane Skouloubris, Kamel Djaout, Isabelle Lamarre, Jean-Christophe Lambry, Karine Anger, Julien Briffotaux, Ursula Liebl, Hilde de Reuse, Hannu Myllykallio
Publikováno v:
Open Biology, Vol 5, Iss 6 (2015)
ThyX is an essential thymidylate synthase that is mechanistically and structurally unrelated to the functionally analogous human enzyme, thus providing means for selective inhibition of bacterial growth. To identify novel compounds with anti-bacteria
Externí odkaz:
https://doaj.org/article/72786186d0a9436da8dd64ed0d2101d5
Autor:
Yoshizumi Ishino, Hanae Kudo, Asmae Es-Sadik, Caroline L'Hermitte-Stead, Sonoko Ishino, Jean Christophe Lambry, Stéphane Skouloubris, Hannu Myllykallio
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2018, ⟨10.1093/nar/gky460⟩
Nucleic Acids Research, Oxford University Press, 2018, ⟨10.1093/nar/gky460⟩
International audience; The mismatch repair (MMR) system, exemplified by the MutS/MutL proteins, is widespread in Bacteria and Eukarya. However, molecular mechanisms how numerous archaea and bacteria lacking the mutS/mutL genes maintain high replicat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::702e013dd7a9cb60801ba57aac779da2
https://hal.archives-ouvertes.fr/hal-01873297
https://hal.archives-ouvertes.fr/hal-01873297
Autor:
Hannu Myllykallio, Andreea Sodolescu, Ursula Liebl, Stéphane Skouloubris, Laurent Terradot, Latifa Bouzhir-Sima, Cyril Dian, Roxane Lestini
Publikováno v:
PLoS ONE, Vol 13, Iss 12, p e0208850 (2018)
PLoS ONE
PLoS ONE, Public Library of Science, 2018, 13 (12), pp.e0208850. ⟨10.1371/journal.pone.0208850⟩
PLoS ONE, 2018, 13 (12), pp.e0208850. ⟨10.1371/journal.pone.0208850⟩
'PloS One ', vol: 13, pages: e0208850-1-e0208850-23 (2018)
PLoS ONE
PLoS ONE, Public Library of Science, 2018, 13 (12), pp.e0208850. ⟨10.1371/journal.pone.0208850⟩
PLoS ONE, 2018, 13 (12), pp.e0208850. ⟨10.1371/journal.pone.0208850⟩
'PloS One ', vol: 13, pages: e0208850-1-e0208850-23 (2018)
Serine hydroxymethyltransferase (SHMT), encoded by the glyA gene, is a ubiquitous pyridoxal 5’-phosphate (PLP)-dependent enzyme that catalyzes the formation of glycine from serine. The thereby generated 5,10-methylene tetrahydrofolate (MTHF) is a m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7e8c828483fffb9ffabb73d05d4e77b
https://doaj.org/article/948ddc00bab64642a468e1771d278205
https://doaj.org/article/948ddc00bab64642a468e1771d278205
Autor:
Stéphane Skouloubris, Hannu Myllykallio, Djemel Hamdane, Gaston Hui-Bon-Hoa, David Cornu, Manuela Argentini, Béatrice Golinelli-Pimpaneau
Publikováno v:
Journal of Biological Chemistry. 286:36268-36280
The flavoprotein TrmFO methylates specifically the C5 carbon of the highly conserved uridine 54 in tRNAs. Contrary to most methyltransferases, the 1-carbon unit transferred by TrmFO derives from 5,10-methylenetetrahydrofolate and not from S-adenosyl-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::96013f6b397c5a9a8fcc07448f206a1e
https://doi.org/10.1074/jbc.m111.256966
https://doi.org/10.1074/jbc.m111.256966
Publikováno v:
Scientific Reports
Scientific Reports, Nature Publishing Group, 2015, ⟨10.1038/srep17356⟩
Sci. Rep. 5:17356 (2015)
Scientific Reports, 2015, ⟨10.1038/srep17356⟩
Scientific Reports, Nature Publishing Group, 2015, ⟨10.1038/srep17356⟩
Sci. Rep. 5:17356 (2015)
Scientific Reports, 2015, ⟨10.1038/srep17356⟩
International audience; Conservation of function across families of orthologous enzymes is generally accompanied by conservation of their active site electrostatic potentials. To study the electrostatic conservation in the highly conserved essential
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8fb9107513cd051751c65b66379db2b
http://europepmc.org/articles/PMC4661567
http://europepmc.org/articles/PMC4661567
Publikováno v:
Nucleic acids research, 33 (13
Nucleic Acids Research
Nucleic Acids Research
Formation of 5-methyluridine (ribothymidine) at position 54 of the T-psi loop of tRNA is catalyzed by site-specific tRNA methyltransferases (tRNA:m(5)U-54 MTase). In all Eukarya and many Gram-negative Bacteria, the methyl donor for this reaction is S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc966a17e35c953f45229bea40aabecb
https://doi.org/10.1093/nar/gki703
https://doi.org/10.1093/nar/gki703
Autor:
Jean-Michel Thiberge, Catherine Dauga, Hilde De Reuse, Agnès Labigne, Douglas E. Berg, Daiva Dailidiene, Stéphane Skouloubris, Stéphanie Bury-Moné
Publikováno v:
Infection and Immunity. 71:5613-5622
Ammonia production is of great importance for the gastric pathogen Helicobacter pylori as a nitrogen source, as a compound protecting against gastric acidity, and as a cytotoxic molecule. In addition to urease, H. pylori possesses two aliphatic amida
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89bf4a2d2b614a923667de05de46aa9f
https://doi.org/10.1128/iai.71.10.5613-5622.2003
https://doi.org/10.1128/iai.71.10.5613-5622.2003
Publikováno v:
Proceedings of the National Academy of Sciences. 100:11297-11302
Efforts to delineate the advent of many enzymes essential to protein translation are often limited by the fact that the modern genetic code evolved before divergence of the tree of life. Glutaminyl-tRNA synthetase (GlnRS) is one noteworthy exception
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a287d776f3f8aefbaecd279b10b47582
https://doi.org/10.1073/pnas.1932482100
https://doi.org/10.1073/pnas.1932482100