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pro vyhledávání: '"Lenka, Skrisovska"'
Adenosine deaminases that act on RNA (ADARs) convert adenosine to inosine (A-to-I) by hydrolytic deamination in cellular and viral RNA transcripts containing either perfect or imperfect RNA duplexes (Bass, 2002). A-to-I editing can be either specific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ac41b20585450411fe734b0ba834a23
http://doc.rero.ch/record/311620/files/10858_2004_Article_6058.pdf
http://doc.rero.ch/record/311620/files/10858_2004_Article_6058.pdf
Publikováno v:
ChemBioChem. 14:457-466
Current solution NMR techniques enable structural investigations of proteins in molecular particles with sizes up to several hundred kDa. However, the large molecular weight of proteins in such systems results in increased numbers of NMR signals, and
Publikováno v:
Journal of Biomolecular NMR, 46 (1)
Journal of Biomolecular NMR, 46 (1)
ISSN:0925-2738
ISSN:1573-5001
ISSN:0925-2738
ISSN:1573-5001
Publikováno v:
Journal of Molecular Biology. 375:151-164
The study of multidomain or large proteins in solution by NMR spectroscopy has been made possible in recent years by the development of new spectroscopic methods. However, resonance overlap found in large proteins remains a limiting factor, making re
Autor:
Lu-Yun Lian, James Stévenin, Lenka Skrisovska, Stuart A. Wilson, Alexander P. Golovanov, Guillaume M. Hautbergue, Yann Hargous, Aura M. Tintaru, Frédéric H.-T. Allain
Publikováno v:
The EMBO Journal. 25:5126-5137
The sequence-specific RNA-binding proteins SRp20 and 9G8 are the smallest members of the serine- and arginine-rich (SR) protein family, well known for their role in splicing. They also play a role in mRNA export, in particular of histone mRNAs. We pr
Publikováno v:
Structure. 14:345-355
SummaryAdenosine deaminases that act on RNA (ADARs) site-selectively modify adenosines to inosines within RNA transcripts, thereby recoding genomic information. How ADARs select specific adenosine moieties for deamination is poorly understood. Here,
Publikováno v:
EMBO reports. 6:33-38
At all stages of its life (from transcription to translation), an RNA transcript interacts with many different RNA-binding proteins. The composition of this supramolecular assembly, known as a ribonucleoprotein particle, is diverse and highly dynamic
Autor:
Tatiana Kubičárová, Petra Procházková Schrumpfová, Milan Kuchar, Gabriela Mikova, Jiri Fajkus, Lenka Skrisovska
Publikováno v:
Genome. 47:316-324
Telomere-binding proteins participate in forming a functional nucleoprotein structure at chromosome ends. Using a genomic approach, two Arabidopsis thaliana genes coding for candidate Myb-like telomere binding proteins were cloned and expressed in E.
Autor:
Eulàlia Belloc, Raúl Méndez, Jordina Guillén-Boixet, Tariq Afroz, Frédéric H.-T. Allain, Lenka Skrisovska
Publikováno v:
Genes & development
Genes & Development, 28 (13)
Genes & Development, 28 (13)
Cytoplasmic changes in polyA tail length is a key mechanism of translational control and is implicated in germline development, synaptic plasticity, cellular proliferation, senescence, and cancer progression. The presence of a U-rich cytoplasmic poly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9780de615dba7db4ca0eb413de2866e4
Autor:
Sushma Nagaraja Grellscheid, Liliane Kister, Richard Štefl, Philipp Wenter, David J. Elliott, Lenka Skrisovska, James Stévenin, Cyril F. Bourgeois, Frédéric H.-T. Allain
Publikováno v:
EMBO Reports
EMBO Reports, EMBO Press, 2007, 8 (4), pp.372-9. ⟨10.1038/sj.embor.7400910⟩
EMBO Reports, 2007, 8 (4), pp.372-9. ⟨10.1038/sj.embor.7400910⟩
EMBO Reports, EMBO Press, 2007, 8 (4), pp.372-9. ⟨10.1038/sj.embor.7400910⟩
EMBO Reports, 2007, 8 (4), pp.372-9. ⟨10.1038/sj.embor.7400910⟩
The RBMY (RNA-binding motif gene on Y chromosome) protein encoded by the human Y chromosome is important for normal sperm development. Although its precise molecular RNA targets are unknown at present, it is suggested that human RBMY (hRBMY) particip
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a5e86d33e26d4cb0fe3aba58be3b06a
https://hal.archives-ouvertes.fr/hal-00166254
https://hal.archives-ouvertes.fr/hal-00166254