Zobrazeno 1 - 10 of 20 pro vyhledávání: '"Guillaume Stahl"'
1
Akademický článek
Genetic interactions show the importance of rRNA modification machinery for the role of Rps15p during ribosome biogenesis in S. cerevisiae.
Autor: Clément Bellemer, Pauline Chabosseau, Franck Gallardo, Pierre-Emmanuel Gleizes, Guillaume Stahl
Publikováno v: PLoS ONE, Vol 5, Iss 5, p e10472 (2010)
Rps15p, an essential ribosomal protein, was previously shown to be critical for nuclear export of small subunit pre-particles. We have designed a synthetic lethal screen in Saccharomyces cerevisiae to identify its genetic partners and further elucida
Externí odkaz: https://doaj.org/article/88ff1f62169e4ad3a1809b8e176cffa5
Zobrazit plný text záznamu
2
The eukaryotic ribosomal protein S15/uS19 is involved in fungal development and its C-terminal tail contributes to stop codon recognition
Autor: Tan-Trung Nguyen, Sylvie Hermann-Le Denmat, Guillaume Stahl, Veronique Contamine, Michelle Dequard-Chablat
SummaryS15/uS19 is one of the fifteen universally conserved ribosomal proteins of the small ribosomal subunit. While prokaryotic uS19 is located away from the mRNA decoding site, cross-linking studies identified eukaryotic uS19 C-terminal tail as con
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abfaef8e88a82bd7d05e8756f1aab291
https://doi.org/10.1101/2020.02.09.940346
Zobrazit plný text záznamu
4
The double life of the ribosome: When its protein folding activity supports prion propagation
Autor: Gary W. Jones, Reynald Gillet, Guillaume Stahl, Vincent Béringue, Stéphane Chédin, Marc Blondel, Cécile Voisset, Gaëlle Friocourt
Publikováno v: Prion
Prion, Taylor & Francis, 2017, 11 (2), pp.89-97. ⟨10.1080/19336896.2017.1303587⟩
Prion, 2017, 11 (2), pp.89-97. ⟨10.1080/19336896.2017.1303587⟩
Prion, Taylor & Francis, 2017, 11, pp.89-97. 〈10.1080/19336896.2017.1303587〉
International audience; It is no longer necessary to demonstrate that ribosome is the central machinery of protein synthesis. But it is less known that it is also key player of the protein folding process through another conserved function: the prote
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64cf94e66aa2cded6a8ba456c6f9aff1
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01517996
Zobrazit plný text záznamu
5
Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation
Autor: Cécile Voisset, Marc Blondel, Guillaume Stahl, Phu Hai Nguyen, Gaëlle Friocourt, Reynald Gillet, Stéphane Chédin, Justine Evrard, Gary W. Jones, Naushaba Hasin, Flavie Soubigou, Marie-Astrid Contesse
Publikováno v: Scientific Reports
Scientific Reports, Nature Publishing Group, 2016, 6, pp.32117. 〈10.1038/srep32117〉
Scientific Reports, Nature Publishing Group, 2016, 6 (1), pp.32117. ⟨10.1038/srep32117⟩
Scientific Reports (2045-2322) (Nature Publishing Group), 2016-09, Vol. 6, N. 32117, P. 1-14
Scientific Reports, 2016, 6 (1), pp.32117. ⟨10.1038/srep32117⟩
6AP and GA are potent inhibitors of yeast and mammalian prions and also specific inhibitors of PFAR, the protein-folding activity borne by domain V of the large rRNA of the large subunit of the ribosome. We therefore explored the link between PFAR an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73a16b95321c7df412a63f990b8470de
https://hal.archives-ouvertes.fr/hal-01394774
Zobrazit plný text záznamu
7
Translational Accuracy during Exponential, Postdiauxic, and Stationary Growth Phases in Saccharomyces cerevisiae
Autor: Samia N. Ben Salem, Lifeng Chen, Bing Zhao, Guillaume Stahl, Philip J. Farabaugh
Publikováno v: Eukaryotic Cell. 3:331-338
When the yeast Saccharomyces cerevisiae shifts from rapid growth on glucose to slow growth on ethanol, it undergoes profound changes in cellular metabolism, including the destruction of most of the translational machinery. We have examined the effect
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b81515d5438f2f67689df87ce129576
https://doi.org/10.1128/ec.3.2.331-338.2004
Zobrazit plný text záznamu
8
Gene Overexpression as a Tool for Identifying New trans-Acting Factors Involved in Translation Termination in Saccharomyces cerevisiae
Autor: Olivier Namy, Guillaume Stahl, Jean-Pierre Rousset, Laure Bidou, Stephanie Barnay, Isabelle Hatin, Hongmei Liu
Publikováno v: Genetics. 161:585-594
In eukaryotes, translation termination is dependent on the availability of both release factors, eRF1 and eRF3; however, the precise mechanisms involved remain poorly understood. In particular, the fact that the phenotype of release factor mutants is
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc0bf294da8d5817595dbcbc358ac782
https://doi.org/10.1093/genetics/161.2.585
Zobrazit plný text záznamu
9
Programmed +1 frameshifting stimulated by complementarity between a downstream mRNA sequence and an error-correcting region of rRNA
Autor: Philip J. Farabaugh, Zirong Li, Guillaume Stahl
Publikováno v: RNA. 7:275-284
Like most retroviruses and retrotransposons, the retrotransposon Ty3 expresses its pol gene analog (POL3) as a translational fusion to the upstream gag analog (GAG3). The Gag3-Pol3 fusion occurs by frameshifting during translation of the mRNA that en
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e9aa31ef896b251c358e5e150436f2d
https://doi.org/10.1017/s135583820100190x
Zobrazit plný text záznamu
10
Nonsense-mediated decay mutants do not affect programmed −1 frameshifting
Autor: Laure Bidou, Philip J. Farabaugh, Olivier Namy, Isabelle Hatin, Jean-Pierre Rousset, Guillaume Stahl
Publikováno v: RNA. 6:952-961
Sequences in certain mRNAs program the ribosome to undergo a noncanonical translation event, translational frameshifting, translational hopping, or termination readthrough. These sequences are termed recoding sites, because they cause the ribosome to
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35418baca3e47d6fb9ca6447f24b3845
https://doi.org/10.1017/s1355838200000443
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje