Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Sylvie Auxilien"'
Autor:
Vedrana Andric, Alicia Nevers, Ditipriya Hazra, Sylvie Auxilien, Alexandra Menant, Marc Graille, Benoit Palancade, Mathieu Rougemaille
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
In fission yeast, the antagonistic RNA-binding proteins Mmi1 and Mei2 respectively promote and inhibit meiotic mRNA degradation during mitotic growth. Here the authors show that the lncRNA mamRNA scaffolds Mmi1 and Mei2 proteins to enable their mutua
Externí odkaz:
https://doaj.org/article/6ddfa8f1105c486a91070ee1f51cf5a5
Autor:
Mathieu Rougemaille, Sylvie Auxilien, Ditipriya Hazra, Vedrana Andric, Alicia Nevers, Marc Graille, Benoit Palancade, Alexandra Menant
Publikováno v:
Nature Communications
Nature Communications, Nature Publishing Group, 2021, 12 (1), ⟨10.1038/s41467-021-21032-7⟩
Nature Communications, Nature Publishing Group, 2021, 12, pp.770. ⟨10.1038/s41467-021-21032-7⟩
Nature Communications, 2021, 12 (1), pp.770. ⟨10.1038/s41467-021-21032-7⟩
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications, Nature Publishing Group, 2021, 12 (1), ⟨10.1038/s41467-021-21032-7⟩
Nature Communications, Nature Publishing Group, 2021, 12, pp.770. ⟨10.1038/s41467-021-21032-7⟩
Nature Communications, 2021, 12 (1), pp.770. ⟨10.1038/s41467-021-21032-7⟩
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Long non-coding RNAs (lncRNAs) contribute to the regulation of gene expression in response to intra- or extracellular signals but the underlying molecular mechanisms remain largely unexplored. Here, we identify an uncharacterized lncRNA as a central
Autor:
Stephen Douthwaite, Finn Kirpekar, Jesper F. Havelund, Simon Rose, Harald Huber, Sylvie Auxilien, Henri Grosjean
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, 2020, 48 (12), pp.6906--6918. ⟨10.1093/nar/gkaa411⟩
Rose, S, Auxilien, S, Havelund, J F, Kirpekar, F, Huber, H, Grosjean, H & Douthwaite, S 2020, ' The hyperthermophilic partners Nanoarchaeum and Ignicoccus stabilize their tRNA T-loops via different but structurally equivalent modifications ', Nucleic acids research, vol. 48, no. 12, pp. 6906-6918 . https://doi.org/10.1093/nar/gkaa411
Nucleic Acids Research, 2020, 48 (12), pp.6906--6918. ⟨10.1093/nar/gkaa411⟩
Rose, S, Auxilien, S, Havelund, J F, Kirpekar, F, Huber, H, Grosjean, H & Douthwaite, S 2020, ' The hyperthermophilic partners Nanoarchaeum and Ignicoccus stabilize their tRNA T-loops via different but structurally equivalent modifications ', Nucleic acids research, vol. 48, no. 12, pp. 6906-6918 . https://doi.org/10.1093/nar/gkaa411
Place: Oxford Publisher: Oxford Univ Press WOS:000574288800042; The universal L-shaped tertiary structure of tRNAs is maintained with the help of nucleotide modifications within the D- and T-loops, and these modifications are most extensive within hy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78b76e995c76b279dd947f01251ee9ff
https://hal.archives-ouvertes.fr/hal-02968376
https://hal.archives-ouvertes.fr/hal-02968376
Publikováno v:
Journal of Chromatography A
Journal of Chromatography A, 2018, 1537, pp.118--127. ⟨10.1016/j.chroma.2017.12.020⟩
Journal of Chromatography A, Elsevier, 2018, 1537, pp.118--127. ⟨10.1016/j.chroma.2017.12.020⟩
Journal of Chromatography A, 2018, 1537, pp.118--127. ⟨10.1016/j.chroma.2017.12.020⟩
Journal of Chromatography A, Elsevier, 2018, 1537, pp.118--127. ⟨10.1016/j.chroma.2017.12.020⟩
International audience; A method based on supercritical fluid chromatography coupled to high resolution mass spectrometry for the profiling of canonical and modified nucleosides was optimized, and compared to classical reverse-phase liquid chromatogr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5ee5c0705625601d8e50a9f0793e2d6
https://hal.science/hal-02180790
https://hal.science/hal-02180790
Autor:
Kalliopi Trachana, Céline Brochier-Armanet, Béatrice Golinelli-Pimpaneau, Hélène Walbott, Sylvie Auxilien, Henri Grosjean, Jaunius Urbonavičius
Publikováno v:
Molecular Microbiology. 67:323-335
The Pyrococcus abyssi genome displays two genes possibly coding for S-adenosyl-l-methionine-dependent RNA(uracil, C5)-methyltransferases (PAB0719 and PAB0760). Their amino acid sequences are more closely related to Escherichia coli RumA catalysing th
Autor:
C. Simon, Henri Grosjean, D. Foiret, Y. Corda, Marjorie Fournier, Sylvie Auxilien, Hubert F. Becker, Annie Morin, Y.X. Jin, Jean-Louis Fourrey, F. Constantinesco
Publikováno v:
Biochimie. 78:488-501
Inosine (6-deaminated adenosine) is a characteristic modified nucleoside that is found at the first anticodon position (position 34) of several tRNAs of eukaryotic and eubacterial origins, while N1-methylinosine is found exclusively at position 37 (3
Publikováno v:
RNA Biology
RNA Biology, Taylor & Francis, 2012, 9 (11), pp.1331-1338. ⟨10.4161/rna.22180⟩
RNA Biology, Taylor & Francis, 2012, 9 (11), pp.1331-1338. ⟨10.4161/rna.22180⟩
The human tRNA m ( 5) C methyltransferase Misu is a novel downstream target of the proto-oncogene Myc that participates in controlling cell division and proliferation. Misu catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to carb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c9cd56e35bf6291a32d9e4bfa6ecd06
https://hal.archives-ouvertes.fr/hal-03280465/document
https://hal.archives-ouvertes.fr/hal-03280465/document
Autor:
Sylvie Auxilien, Céline Brochier-Armanet, Simon Rose, Stephen Douthwaite, Clotilde Husson, Henri Grosjean, Anette Rasmussen, Dominique Fourmy
Publikováno v:
RNA
RNA, Cold Spring Harbor Laboratory Press, 2011, 17 (1), pp.45-53. ⟨10.1261/rna.2323411⟩
Auxilien, S, Rasmussen, A, Rose, S, Brochier-Armanet, C, Husson, C, Fourmy, D, Grosjean, H & Douthwaite, S R 2011, ' Specificity shifts in the rRNA and tRNA nucleotide targets of archaeal and bacterial m5U methyltransferases ', R N A, vol. 17, no. 1, pp. 45-53 . https://doi.org/10.1261/rna.2323411
RNA, Cold Spring Harbor Laboratory Press, 2011, 17 (1), pp.45-53. ⟨10.1261/rna.2323411⟩
Auxilien, S, Rasmussen, A, Rose, S, Brochier-Armanet, C, Husson, C, Fourmy, D, Grosjean, H & Douthwaite, S R 2011, ' Specificity shifts in the rRNA and tRNA nucleotide targets of archaeal and bacterial m5U methyltransferases ', R N A, vol. 17, no. 1, pp. 45-53 . https://doi.org/10.1261/rna.2323411
Methyltransferase enzymes that use S-adenosylmethionine as a cofactor to catalyze 5-methyl uridine (m5U) formation in tRNAs and rRNAs are widespread in Bacteria and Eukaryota, but are restricted to the Thermococcales and Nanoarchaeota groups amongst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e537a57003667278300b99b45f5ef3f
https://hal.archives-ouvertes.fr/hal-00580893
https://hal.archives-ouvertes.fr/hal-00580893
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 282 (32), pp.23663-23671. ⟨10.1074/jbc.M703818200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 282 (32), pp.23663-23671. ⟨10.1074/jbc.M703818200⟩
International audience; The human tRNA m(5)C methyltransferase is a potential target for anticancer drugs because it is a novel downstream target of the proto-oncogene myc, mediating Myc-induced cell proliferation. Sequence comparisons of RNA m(5)C m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04ae3f13a8bd689f654dda00cc006cf4
https://hal.archives-ouvertes.fr/hal-02287273/document
https://hal.archives-ouvertes.fr/hal-02287273/document
Publikováno v:
RNA
RNA, Cold Spring Harbor Laboratory Press, 2007, 13 (7), pp.967-973. ⟨10.1261/rna.515707⟩
RNA, Cold Spring Harbor Laboratory Press, 2007, 13 (7), pp.967-973. ⟨10.1261/rna.515707⟩
Sequence comparison of several RNA m5C methyltransferases identifies two conserved cysteine residues that belong to signature motifs IV and VI of RNA and DNA methyltransferases. While the cysteine of motif IV is used as the nucleophilic catalyst by D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a37228386297819b79c686bfaf8a6e1
https://hal.archives-ouvertes.fr/hal-02287307/document
https://hal.archives-ouvertes.fr/hal-02287307/document