Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Jonathan Bizarro"'
Autor:
Franck Vandermoere, Tiago M. Bandeiras, Ana C. F. Paiva, Edouard Bertrand, Bruno Charpentier, Xavier Manival, Céline Verheggen, Marie-Eve Chagot, Pedro M. F. Sousa, Marc Quinternet, Marie-Cécile Robert, Philippe Fort, Paulo E. Santo, Jonathan Bizarro, Yoann Abel
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, In press, 49 (2), pp.1094-1113. ⟨10.1093/nar/gkaa1226⟩
Nucleic Acids Research, 2021, 49 (2), pp.1094-1113. ⟨10.1093/nar/gkaa1226⟩
Nucleic Acids Research, Oxford University Press, In press, 49 (2), pp.1094-1113. ⟨10.1093/nar/gkaa1226⟩
Nucleic Acids Research, 2021, 49 (2), pp.1094-1113. ⟨10.1093/nar/gkaa1226⟩
The PAQosome is a large complex composed of the HSP90/R2TP chaperone and a prefoldin-like module. It promotes the biogenesis of cellular machineries but it is unclear how it discriminates closely related client proteins. Among the main PAQosome clien
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa3353ae141945db90b5fe30d422a6fb
https://doi.org/10.1093/nar/gkaa1226
https://doi.org/10.1093/nar/gkaa1226
Publikováno v:
Molecular Biology of the Cell
Cajal bodies (CBs) are nuclear organelles concentrating two kinds of RNA--protein complexes (RNPs), spliceosomal small nuclear (sn), and small CB-specific (sca)RNPs. Whereas the CB marker protein coilin is responsible for retaining snRNPs, the tether
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c54c096e5378ce36da51c47613c40f5
http://europepmc.org/articles/PMC6938241
http://europepmc.org/articles/PMC6938241
Autor:
Varun Gupta, Denis L. J. Lafontaine, Ludivine Wacheul, Joseph G. Gall, Jonathan Bizarro, Svetlana Deryusheva, U. Thomas Meier, Felix G.M. Ernst
Publikováno v:
bioRxiv
Genes Dev
Genes Dev
Spliceosomal small nuclear RNAs (snRNAs) are modified by small Cajal body (CB) specific ribonucleoproteins (scaRNPs) to ensure snRNP biogenesis and pre-mRNA splicing. However, the function and subcellular site of snRNA modification are largely unknow
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63a1912367c8febe8d29d57ced4fef94
https://pubmed.ncbi.nlm.nih.gov/33948588
https://pubmed.ncbi.nlm.nih.gov/33948588
Autor:
Aris N. Economides, Jonathan Bizarro, Yiyun Chen, Evangelos Pefanis, Carolina R. Batista, Jiguang Wang, Lijing Wu, Brice Laffleur, Junghyun Lim, Uttiya Basu, Wanwei Zhang
Publikováno v:
Nat Genet
Noncoding RNAs are exquisitely titrated by the cellular RNA surveillance machinery for regulating diverse biological processes. The RNA exosome, the predominant 3' RNA exoribonuclease in mammalian cells, is composed of nine core and two catalytic sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::467eb45542e4453444ca916491c5bc76
https://europepmc.org/articles/PMC8011275/
https://europepmc.org/articles/PMC8011275/
Autor:
Jonathan Bizarro, U. Thomas Meier
Publikováno v:
Molecular Genetics & Genomic Medicine
Background The inherited bone marrow failure syndrome dyskeratosis congenita (DC) is most frequently caused by mutations in DKC1 (MIM# 300126), the gene encoding NAP57 (aka dyskerin). The typically missense mutations modulate the interaction of NAP57
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68123eef71fc2a94d6ddd95eed987e0b
https://doi.org/10.1002/mgg3.314
https://doi.org/10.1002/mgg3.314
Autor:
Julie Rodor, Kenzo Nakamura, Manuel Echeverria, Jonathan Bizarro, Florence Vignols, Cristel C. Carles, Takamasa Suzuki, Edouard Jobet
Publikováno v:
The Plant Journal. 65:807-819
In all eukaryotes, C/D small nucleolar ribonucleoproteins (C/D snoRNPs) are essential for methylation and processing of ribosomal RNAs. They consist of a box C/D small nucleolar RNA (C/D snoRNA) associated with four highly conserved nucleolar protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::837ec669b019cfe066de583bdcddd02d
https://doi.org/10.1111/j.1365-313x.2010.04468.x
https://doi.org/10.1111/j.1365-313x.2010.04468.x
Autor:
Christiane Branlant, Séverine Massenet, Jonathan Bizarro, Alexandra Huttin, Maxime Dodré, Céline Verheggen, Bruno Charpentier, Edouard Bertrand, Florence Schlotter
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2015, 43 (18), pp.8973-8989. ⟨10.1093/nar/gkv809⟩
Nucleic Acids Research, Oxford University Press, 2015, 43 (18), pp.8973-8989. 〈10.1093/nar/gkv809〉
Nucleic Acids Research, Oxford University Press, 2015, 43 (18), pp.8973-8989. ⟨10.1093/nar/gkv809⟩
Nucleic Acids Research, Oxford University Press, 2015, 43 (18), pp.8973-8989. 〈10.1093/nar/gkv809〉
International audience; The Sm proteins are loaded on snRNAs by the SMN complex, but how snRNP-specific proteins are assembled remains poorly characterized. U4 snRNP and box C/D snoRNPs have structural similarities. They both contain the 15.5K and pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af29aaf647240546e7458e8bddb342ce
https://hal.univ-lorraine.fr/hal-01451914
https://hal.univ-lorraine.fr/hal-01451914
Autor:
Christophe Charron, Xavier Manival, Céline Verheggen, Belinda J. Westman, Marie Eve Chagot, Heinrich Leonhardt, Angus I. Lamond, Séverine Boulon, Yasmeen Ahmad, Marie Hallais, Christiane Branlant, Jonathan Bizarro, Bérengère Pradet-Balade, Edouard Bertrand, Bruno Charpentier, Franck Vandermoere
Publikováno v:
Journal of Cell Biology
Journal of Cell Biology, Rockefeller University Press, 2014, 207 (4), pp.463-480. 〈10.1083/jcb.201404160〉
Journal of Cell Biology, Rockefeller University Press, 2014, 207 (4), pp.463-480. ⟨10.1083/jcb.201404160⟩
The Journal of Cell Biology
Journal of Cell Biology, Rockefeller University Press, 2014, 207 (4), pp.463-480. 〈10.1083/jcb.201404160〉
Journal of Cell Biology, Rockefeller University Press, 2014, 207 (4), pp.463-480. ⟨10.1083/jcb.201404160⟩
The Journal of Cell Biology
During small nucleolar ribonucleoprotein complex assembly, a pre-snoRNP complex consisting only of protein components forms first, followed by displacement of the ZNHIT3 subunit when C/D snoRNAs bind and dynamic loading and unloading of RuvBL AAA+ AT
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a47ac7571e44d3181b0c8b14bc9eb56
https://hal.univ-lorraine.fr/hal-01453204
https://hal.univ-lorraine.fr/hal-01453204
Autor:
Bruno Charpentier, Xavier Manival, Régis Back, Magali Blaud, Edouard Bertrand, Marie Cécile Robert, Marc Quinternet, Jonathan Bizarro, Christophe Romier, Christiane Branlant, Benjamin Rothé
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2014, 42 (3), pp.2015-2036. ⟨10.1093/nar/gkt1091⟩
Nucleic Acids Research, 2014, 42 (3), pp.2015-2036. ⟨10.1093/nar/gkt1091⟩
Nucleic Acids Research, Oxford University Press, 2014, 42 (3), pp.2015-2036. 〈10.1093/nar/gkt1091〉
Nucleic Acids Research, Oxford University Press, 2014, 42 (3), pp.2015-2036. ⟨10.1093/nar/gkt1091⟩
Nucleic Acids Research, 2014, 42 (3), pp.2015-2036. ⟨10.1093/nar/gkt1091⟩
Nucleic Acids Research, Oxford University Press, 2014, 42 (3), pp.2015-2036. 〈10.1093/nar/gkt1091〉
International audience; The yeast Snu13p protein and its 15.5K human homolog both bind U4 snRNA and box C/D snoRNAs. They also bind the Rsa1p/NUFIP assembly factor, proposed to scaffold immature snoRNPs and to recruit the Hsp90-R2TP chaperone complex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a4314b00e12424db89ef224598723e0
https://hal.univ-lorraine.fr/hal-01452718
https://hal.univ-lorraine.fr/hal-01452718