Zobrazeno 1 - 10
of 11
pro vyhledávání: '"MESH : Ribonucleoproteins, Small Nuclear"'
Publikováno v:
Journal of Cell Science
Journal of Cell Science, 2004, 117 (Pt 19), pp.4551-8. ⟨10.1242/jcs.01329⟩
Journal of Cell Science, Company of Biologists, 2004, 117 (Pt 19), pp.4551-8. ⟨10.1242/jcs.01329⟩
Journal of Cell Science, Company of Biologists, 2004, 117 (Pt 19), pp.4551-8. 〈10.1242/jcs.01329〉
Journal of Cell Science, 2004, 117 (Pt 19), pp.4551-8. ⟨10.1242/jcs.01329⟩
Journal of Cell Science, Company of Biologists, 2004, 117 (Pt 19), pp.4551-8. ⟨10.1242/jcs.01329⟩
Journal of Cell Science, Company of Biologists, 2004, 117 (Pt 19), pp.4551-8. 〈10.1242/jcs.01329〉
International audience; Exposure of cells to stressful conditions results in the rapid synthesis of a subset of specialized proteins termed heat shock proteins (HSPs) which function in protecting the cell against damage. The stress-induced activation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::233afbbb32c1a077f04eaee9a809e05f
https://doi.org/10.1242/jcs.01329
https://doi.org/10.1242/jcs.01329
Publikováno v:
Molecular Cell
Molecular Cell, Elsevier, 2010, 37 (5), pp.597-606. ⟨10.1016/j.molcel.2010.01.032⟩
Molecular Cell, Elsevier, 2010, 37 (5), pp.597-606. ⟨10.1016/j.molcel.2010.01.032⟩
International audience; Box H/ACA RNAs represent an abundant, evolutionarily conserved class of small noncoding RNAs. All H/ACA RNAs associate with a common set of proteins, and they function as ribonucleoprotein (RNP) enzymes mainly in the site-spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9cff5c71ec41f1a21fcbce7081acdbfa
https://doi.org/10.1016/j.molcel.2010.01.032
https://doi.org/10.1016/j.molcel.2010.01.032
Autor:
Pilar, Bustos-Sanmamed, Carole, Laffont, Florian, Frugier, Christine, Lelandais-Brière, Martin, Crespi
Publikováno v:
Methods in Molecular Biology (Clifton then Totova)
Methods in Molecular Biology (Clifton then Totova), Humana Press (Springer Imprint), 2013, 959, pp.317-22. 〈10.1007/978-1-62703-221-6_21〉
Methods in Molecular Biology
Methods in Molecular Biology, Humana Press/Springer Imprint, 2013, 959, pp.317-22. ⟨10.1007/978-1-62703-221-6_21⟩
Methods in Molecular Biology (Clifton then Totova), Humana Press (Springer Imprint), 2013, 959, pp.317-22. 〈10.1007/978-1-62703-221-6_21〉
Methods in Molecular Biology
Methods in Molecular Biology, Humana Press/Springer Imprint, 2013, 959, pp.317-22. ⟨10.1007/978-1-62703-221-6_21⟩
International audience; Proteins are distributed in different cellular compartments. Our group studies the role of non-coding RNAs and associated RNPs in the development and stress response in legumes. Ribonucleoproteins (RNPs) are RNA-protein comple
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::188fa6c1e7781790ea38f2bfee4235d7
https://hal.archives-ouvertes.fr/hal-00856158
https://hal.archives-ouvertes.fr/hal-00856158
Autor:
Cordin, Olivier, Hahn, Daniela, Alexander, Ross, Gautam, Amit, Saveanu, Cosmin, Barrass, J David, Beggs, Jean D
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2014, 42 (22), pp.13897-910. ⟨10.1093/nar/gku1238⟩
Nucleic Acids Research, 2014, 42 (22), pp.13897-910. ⟨10.1093/nar/gku1238⟩
Cordin, O, Hahn, D, Alexander, R, Gautam, A, Saveanu, C, Barrass, J D & Beggs, J D 2014, ' Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase ', Nucleic Acids Research, vol. 42, no. 22, pp. 13897-13910 . https://doi.org/10.1093/nar/gku1238
Nucleic Acids Research, Oxford University Press, 2014, 42 (22), pp.13897-910. ⟨10.1093/nar/gku1238⟩
Nucleic Acids Research, 2014, 42 (22), pp.13897-910. ⟨10.1093/nar/gku1238⟩
Cordin, O, Hahn, D, Alexander, R, Gautam, A, Saveanu, C, Barrass, J D & Beggs, J D 2014, ' Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase ', Nucleic Acids Research, vol. 42, no. 22, pp. 13897-13910 . https://doi.org/10.1093/nar/gku1238
International audience; RNA helicases are essential for virtually all cellular processes, however, their regulation is poorly understood. The activities of eight RNA helicases are required for pre-mRNA splicing. Amongst these, Brr2p is unusual in hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::cb6235d4e78a079e50d1f4389c35a698
https://hal-pasteur.archives-ouvertes.fr/pasteur-01427502/file/gku1238.pdf
https://hal-pasteur.archives-ouvertes.fr/pasteur-01427502/file/gku1238.pdf
Publikováno v:
Nature Genetics
Nature Genetics, Nature Publishing Group, 1997, 16 (3), pp.277-282. ⟨10.1038/ng0797-277⟩
Nature Genetics, 1997, 16 (3), pp.277-282. ⟨10.1038/ng0797-277⟩
Nature Genetics, Nature Publishing Group, 1997, 16 (3), pp.277-282. ⟨10.1038/ng0797-277⟩
Nature Genetics, 1997, 16 (3), pp.277-282. ⟨10.1038/ng0797-277⟩
International audience; The genome of the yeast Saccharomyces cerevisiae is now completely sequenced. Despite successful genetic work in recent years, 60% of yeast genes have no assigned function and half of those encode putative proteins without any
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd285f1e20a58c233821d411dbde257c
https://doi.org/10.1038/ng0797-277
https://doi.org/10.1038/ng0797-277
Publikováno v:
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, 2010, 17 (2), pp.216-21. ⟨10.1038/nsmb.1718⟩
Nature Structural and Molecular Biology, Nature Publishing Group, 2010, 17 (2), pp.216-21. ⟨10.1038/nsmb.1718⟩
Nature Structural and Molecular Biology, 2010, 17 (2), pp.216-21. ⟨10.1038/nsmb.1718⟩
Nature Structural and Molecular Biology, Nature Publishing Group, 2010, 17 (2), pp.216-21. ⟨10.1038/nsmb.1718⟩
International audience; Reversible protein phosphorylation has an essential role during pre-mRNA splicing. Here we identify two previously unidentified phosphoproteins in the human spliceosomal B complex, namely the pre-mRNA processing factors PRP6 a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f42cdf5b02f9546aae8d269e3422a7e0
https://www.hal.inserm.fr/inserm-00461778
https://www.hal.inserm.fr/inserm-00461778
Autor:
Elodie Van Herreweghe, Bernard Monsarrat, Isabelle Goiffon, Sylvain Egloff, Tamás Kiss, Beáta E. Jády, Carine Froment
Publikováno v:
EMBO Journal
EMBO Journal, EMBO Press, 2007, 26 (15), pp.3570-80. ⟨10.1038/sj.emboj.7601783⟩
EMBO Journal, EMBO Press, 2007, 26 (15), pp.3570-80. ⟨10.1038/sj.emboj.7601783⟩
The 7SK small nuclear RNA (snRNA) regulates RNA polymerase II transcription elongation by controlling the protein kinase activity of the positive transcription elongation factor b (P-TEFb). In cooperation with HEXIM1, the 7SK snRNA sequesters P-TEFb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1478fd21300fad531486e676470e25fc
https://pubmed.ncbi.nlm.nih.gov/17611602
https://pubmed.ncbi.nlm.nih.gov/17611602
Publikováno v:
RNA
RNA, Cold Spring Harbor Laboratory Press, 2006, 12 (1), pp.40-52. ⟨10.1261/rna.2221606⟩
RNA, Cold Spring Harbor Laboratory Press, 2006, 12 (1), pp.40-52. ⟨10.1261/rna.2221606⟩
The H/ACA small nucleolar ribonucleoprotein (snoRNP) complexes guide the modification of uridine to pseudouridine at conserved sites in rRNA. The H/ACA snoRNPs each comprise a target-site-specific snoRNA and four core proteins, Nop10p, Nhp2p, Gar1p,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7006aa34831316849b4d2160776cd5bf
https://hal.archives-ouvertes.fr/hal-00109511
https://hal.archives-ouvertes.fr/hal-00109511
Autor:
Claire Torchet, Michel Werner, Frédéric Devaux, Gwenael Badis, Ginny Costanzo, Alain Jacquier
Publikováno v:
RNA
RNA, 2005, 11 (6), pp.928-938. ⟨10.1261/rna.2100905⟩
RNA, Cold Spring Harbor Laboratory Press, 2005, 11 (6), pp.928-938. ⟨10.1261/rna.2100905⟩
RNA, 2005, 11 (6), pp.928-938. ⟨10.1261/rna.2100905⟩
RNA, Cold Spring Harbor Laboratory Press, 2005, 11 (6), pp.928-938. ⟨10.1261/rna.2100905⟩
International audience; Conversion of uridines into pseudouridines (Psis) is the most frequent base modification in ribosomal RNAs (rRNAs). In eukaryotes, the pseudouridylation sites are specified by base-pairing with specific target sequences within
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50a3fdfe0c6c2c90246cd4796e51b92d
https://hal.science/hal-03032770
https://hal.science/hal-03032770
Autor:
Anthony K. Henras
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2011, 411 (5), pp.925-6. ⟨10.1016/j.jmb.2011.07.008⟩
Journal of Molecular Biology, Elsevier, 2011, 411 (5), pp.925-6. ⟨10.1016/j.jmb.2011.07.008⟩
H/ACA small nucleolar and Cajal body ribonucleoproteins (RNPs) function in site-specific pseudouridylation of eukaryotic rRNA and snRNA, rRNA processing, and vertebrate telomerase biogenesis. Nhp2, one of four essential protein components of eukaryot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dae0b860b8d2be82caa04348515325d7
https://doi.org/10.1016/j.jmb.2011.07.008
https://doi.org/10.1016/j.jmb.2011.07.008