Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Christine Allmang"'
Publikováno v:
Biomolecules, Vol 12, Iss 9, p 1268 (2022)
The synthesis of selenoproteins requires the co-translational recoding of an in-frame UGASec codon. Interactions between the Selenocysteine Insertion Sequence (SECIS) and the SECIS binding protein 2 (SBP2) in the 3′untranslated region (3′UTR) of
Externí odkaz:
https://doaj.org/article/0f3c6f7a26c847f6a90c3b5da8712971
Publikováno v:
Biomolecules; Volume 12; Issue 9; Pages: 1268
The synthesis of selenoproteins requires the co-translational recoding of an in-frame UGASec codon. Interactions between the Selenocysteine Insertion Sequence (SECIS) and the SECIS binding protein 2 (SBP2) in the 3′untranslated region (3′UTR) of
Autor:
Franck Martin, Lauriane Gross, Fatima Alghoul, Christine Allmang, Hassan Hayek, Laure Schaeffer, Gilbert Eriani
Publikováno v:
Methods
Methods, Elsevier, 2018, 137, pp.3-10. ⟨10.1016/j.ymeth.2017.12.019⟩
Methods, Elsevier, 2018, 137, pp.3-10. ⟨10.1016/j.ymeth.2017.12.019⟩
In eukaryotes, cap-dependent translation initiation is a sophisticated process that requires numerous trans-acting factors, the eukaryotic Initiation Factors (eIFs). Their main function is to assist the ribosome for accurate AUG start codon recogniti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14248ea8b70955c0edddc52aafa28514
https://hal-cnrs.archives-ouvertes.fr/hal-02118755
https://hal-cnrs.archives-ouvertes.fr/hal-02118755
Autor:
Lauriane, Gross, Laure, Schaeffer, Fatima, Alghoul, Hassan, Hayek, Christine, Allmang, Gilbert, Eriani, Franck, Martin
Publikováno v:
Methods (San Diego, Calif.). 137
In eukaryotes, cap-dependent translation initiation is a sophisticated process that requires numerous trans-acting factors, the eukaryotic Initiation Factors (eIFs). Their main function is to assist the ribosome for accurate AUG start codon recogniti
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1661
Several selenoprotein mRNAs undergo 5' cap maturation events whereby their classical monomethylated m
Publikováno v:
Methods in Molecular Biology ISBN: 9781493972579
Several selenoprotein mRNAs undergo 5' cap maturation events whereby their classical monomethylated m7G cap becomes trimethylated (m32,2,7G) by the trimethylguanosine synthase 1 (Tgs1). Here, we describe immunoprecipitation methods for the detection
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f71531feae9b2310ff0caf9a1f012c5
https://doi.org/10.1007/978-1-4939-7258-6_9
https://doi.org/10.1007/978-1-4939-7258-6_9
Autor:
Michael Leichter, Edouard Bertrand, Akiko Takeuchi, Alain Krol, Anne-Sophie Gribling-Burrer, Franck Martin, Christine Allmang, Laurence Wurth, Stéphanie Baudrey, Céline Verheggen
Publikováno v:
Nucleic Acids Research
Mammalian mRNAs are generated by complex and coordinated biogenesis pathways and acquire 5'-end m(7)G caps that play fundamental roles in processing and translation. Here we show that several selenoprotein mRNAs are not recognized efficiently by tran
Publikováno v:
Journal of Biological Chemistry. 278:2147-2156
Depletion of any of the essential Lsm proteins, Lsm2-5p or Lsm8p, delayed pre-rRNA processing and led to the accumulation of many aberrant processing intermediates, indicating that an Lsm complex is required to maintain the normally strict order of p
Publikováno v:
Gene. 291:279-285
Selenocysteine and selenoprotein synthesis require a complex molecular machinery in mammals. Among the key players is the RNA-protein complex formed by the selenocysteine insertion sequence (SECIS) binding protein (SBP2) and the SECIS element, an RNA
Publikováno v:
Allmang, C, Mitchell, P, Petfalski, E & Tollervey, D 2000, ' Degradation of ribosomal RNA precursors by the exosome ', Nucleic Acids Research, vol. 28, no. 8, pp. 1684-1691 . https://doi.org/10.1093/nar/28.8.1684
Scopus-Elsevier
Scopus-Elsevier
The yeast exosome is a complex of 3'-> 5' exonucleases involved in RNA processing and degradation. All 11 known components of the exosome are required during 3' end processing of the 5.8S rRNA. Here we report that depletion of each of the individual