Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Juliette Létoquart"'
Autor:
Kilian Dekoninck, Juliette Létoquart, Cédric Laguri, Pascal Demange, Robin Bevernaegie, Jean-Pierre Simorre, Olivia Dehu, Bogdan I Iorga, Benjamin Elias, Seung-Hyun Cho, Jean-Francois Collet
Publikováno v:
eLife, Vol 9 (2020)
OmpA, a protein commonly found in the outer membrane of Gram-negative bacteria, has served as a paradigm for the study of β-barrel proteins for several decades. In Escherichia coli, OmpA was previously reported to form complexes with RcsF, a surface
Externí odkaz:
https://doaj.org/article/4bedf222626847969d447bd6eb2047aa
Publikováno v:
Biomolecules, Vol 7, Iss 1, p 7 (2017)
Post-transcriptional and post-translational modifications are very important for the control and optimal efficiency of messenger RNA (mRNA) translation. Among these, methylation is the most widespread modification, as it is found in all domains of li
Externí odkaz:
https://doaj.org/article/6c834670354347f4a4a2217ea5909dca
Autor:
Kilian Dekoninck, Juliette Létoquart, Cédric Laguri, Pascal Demange, Robin Bevernaegie, Jean-Pierre Simorre, Olivia Dehu, Bogdan I Iorga, Benjamin Elias, Seung-Hyun Cho, Jean-Francois Collet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::60c4327958f718a84fa6b527845646df
https://doi.org/10.7554/elife.60861.sa2
https://doi.org/10.7554/elife.60861.sa2
Autor:
Antonio N. Calabrese, Gwennaelle Louis, Sheena E. Radford, Raquel Rodríguez-Alonso, Han Remaut, Bogdan I. Iorga, Juliette Létoquart, Van Son Nguyen, Seung-Hyun Cho, Jean-François Collet
Publikováno v:
Nature Chemical Biology
Nature chemical biology
Nature Chemical Biology, Nature Publishing Group, 2020, 16, pp.1019-1025. ⟨10.1038/s41589-020-0575-0⟩
Nature chemical biology, Vol. 16, no. 9, p. 1019-1025 (2020)
Nature chemical biology
Nature Chemical Biology, Nature Publishing Group, 2020, 16, pp.1019-1025. ⟨10.1038/s41589-020-0575-0⟩
Nature chemical biology, Vol. 16, no. 9, p. 1019-1025 (2020)
International audience; The β-barrel assembly machinery (BAM) inserts outer membrane β-barrel proteins (OMPs) in the outer membrane of Gram-negative bacteria. In Enterobacteriacea, BAM also mediates export of the stress sensor lipoprotein RcsF to t
Autor:
Seung-Hyun Cho, Raquel Rodríguez-Alonso, Han Remaut, Jean-François Collet, Gwennaelle Louis, Juliette Létoquart, Sheena E. Radford, Van Son Nguyen, Antonio N. Calabrese
The β-barrel assembly machinery (BAM) inserts outer membrane β-barrel proteins (OMPs) in the outer membrane of Gram-negative bacteria. In Enterobacteriacea, BAM also mediates export of the stress sensor lipoprotein RcsF to the cell surface by assem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b8b74e92b35e52938831ce7e7cbe3a6
Autor:
Dominique Liger, W. Zhang, Tamara Basta, Herman van Tilbeurgh, Patrick Forterre, Juliette Létoquart, Inès Li de la Sierra-Gallay, A. Pichard-Kostuch, M.C. Daugeron, Bruno Collinet
Publikováno v:
RNA
RNA, 2018, 24 (7), pp.926--938. ⟨10.1261/rna.066092.118⟩
RNA, Cold Spring Harbor Laboratory Press, 2018, 24 (7), pp.926--938. ⟨10.1261/rna.066092.118⟩
RNA, 2018, 24 (7), pp.926--938. ⟨10.1261/rna.066092.118⟩
RNA, Cold Spring Harbor Laboratory Press, 2018, 24 (7), pp.926--938. ⟨10.1261/rna.066092.118⟩
N6-threonyl-carbamoyl adenosine (t6A) is a universal tRNA modification found at position 37, next to the anticodon, in almost all tRNAs decoding ANN codons (where N = A, U, G, or C). t6A stabilizes the codon–anticodon interaction and hence promotes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ee66c60104d2f3e1fa2590339d8904a
https://hal.science/hal-02183256/file/RNA-2018-Pichard-Kostuch-926-38.pdf
https://hal.science/hal-02183256/file/RNA-2018-Pichard-Kostuch-926-38.pdf
Autor:
Adeline, Pichard-Kostuch, Wenhua, Zhang, Dominique, Liger, Marie-Claire, Daugeron, Juliette, Létoquart, Ines, Li de la Sierra-Gallay, Patrick, Forterre, Bruno, Collinet, Herman, van Tilbeurgh, Tamara, Basta
Publikováno v:
RNA (New York, N.Y.). 24(7)
N(6)-threonyl-carbamoyl adenosine (t(6)A) is a universal tRNA modification found at position 37, next to the anticodon, in almost all tRNAs decoding ANN codons (where N = A, U, G, or C). t(6)A stabilizes the codon–anticodon interaction and hence pr
Autor:
Nhan, van Tran, Leslie, Muller, Robert L, Ross, Roxane, Lestini, Juliette, Létoquart, Nathalie, Ulryck, Patrick A, Limbach, Valérie, de Crécy-Lagard, Sarah, Cianférani, Marc, Graille
Publikováno v:
Nucleic acids research. 46(16)
Protein synthesis is a complex and highly coordinated process requiring many different protein factors as well as various types of nucleic acids. All translation machinery components require multiple maturation events to be functional. These include
Publikováno v:
Biomolecules
Biomolecules, MDPI, 2017, 7 (1), pp.7. ⟨10.3390/biom7010007⟩
Biomolecules, Vol 7, Iss 1, p 7 (2017)
Biomolecules, MDPI, 2017, 7 (4), pp.7. ⟨10.3390/biom7010007⟩
Biomolecules, MDPI, 2017, 7 (1), pp.7. ⟨10.3390/biom7010007⟩
Biomolecules, Vol 7, Iss 1, p 7 (2017)
Biomolecules, MDPI, 2017, 7 (4), pp.7. ⟨10.3390/biom7010007⟩
International audience; Post-transcriptional and post-translational modifications are very important for the control and optimal efficiency of messenger RNA (mRNA) translation. Among these, methylation is the most widespread modification, as it is fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05727d9e0703d106d18bdfbfa281c929
https://hal.archives-ouvertes.fr/hal-03295436/document
https://hal.archives-ouvertes.fr/hal-03295436/document
Autor:
Gabrielle Bourgeois, Juliette Létoquart, Denis L. J. Lafontaine, Emmeline Huvelle, Marc Graille, Christiane Zorbas, Ludivine Wacheul, Valérie Heurgué-Hamard
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2014, 111 (51), pp.E5518-E5526. ⟨10.1073/pnas.1413089111⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2014, 111 (51), pp.E5518-E5526. ⟨10.1073/pnas.1413089111⟩
The eukaryotic small ribosomal subunit carries only four ribosomal (r) RNA methylated bases, all close to important functional sites. N(7)-methylguanosine (m(7)G) introduced at position 1575 on 18S rRNA by Bud23-Trm112 is at a ridge forming a steric
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5fdef49ba7ae7dab433698ca82583a2
https://hal.archives-ouvertes.fr/hal-01107275
https://hal.archives-ouvertes.fr/hal-01107275