Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Benoît Bragantini"'
Autor:
Sowmiya Palani, Yuka Machida, Julia R. Alvey, Vandana Mishra, Allison L. Welter, Gaofeng Cui, Benoît Bragantini, Maria Victoria Botuyan, Anh T. Q. Cong, Georges Mer, Matthew J. Schellenberg, Yuichi J. Machida
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract FAM111A, a serine protease, plays roles in DNA replication and antiviral defense. Missense mutations in the catalytic domain cause hyper-autocleavage and are associated with genetic disorders with developmental defects. Despite the enzyme’
Externí odkaz:
https://doaj.org/article/04b6d5d1449d4892b6e3d297c8272f1f
Autor:
Gaofeng Cui, Maria Victoria Botuyan, Pascal Drané, Qi Hu, Benoît Bragantini, James R. Thompson, David J. Schuller, Alexandre Detappe, Michael T. Perfetti, Lindsey I. James, Stephen V. Frye, Dipanjan Chowdhury, Georges Mer
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-11 (2023)
Abstract The recruitment of 53BP1 to chromatin, mediated by its recognition of histone H4 dimethylated at lysine 20 (H4K20me2), is important for DNA double-strand break repair. Using a series of small molecule antagonists, we demonstrate a conformati
Externí odkaz:
https://doaj.org/article/0f5b7e97b6324cda80e7ab7f47fa3f98
Autor:
Benoît Bragantini, Christophe Charron, Maxime Bourguet, Arnaud Paul, Decebal Tiotiu, Benjamin Rothé, Hélène Marty, Guillaume Terral, Steve Hessmann, Laurence Decourty, Marie-Eve Chagot, Jean-Marc Strub, Séverine Massenet, Edouard Bertrand, Marc Quinternet, Cosmin Saveanu, Sarah Cianférani, Stéphane Labialle, Xavier Manival, Bruno Charpentier
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-17 (2021)
Biogenesis of small nucleolar RNAs ribonucleoproteins (snoRNPs) requires dedicated assembly machinery. Here, the authors show that a subset of snoRNP assembly factors interacts, genetically or directly, with factors modulating chromatin architecture,
Externí odkaz:
https://doaj.org/article/334ab11b5a9d40c685790e1db511ecac
Autor:
Chloé Maurizy, Marc Quinternet, Yoann Abel, Céline Verheggen, Paulo E. Santo, Maxime Bourguet, Ana C.F. Paiva, Benoît Bragantini, Marie-Eve Chagot, Marie-Cécile Robert, Claire Abeza, Philippe Fabre, Philippe Fort, Franck Vandermoere, Pedro M.F. Sousa, Jean-Christophe Rain, Bruno Charpentier, Sarah Cianférani, Tiago M. Bandeiras, Bérengère Pradet-Balade, Xavier Manival, Edouard Bertrand
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-16 (2018)
R2TP is an HSP90 co-chaperone composed of an RPAP3-PIH1D1 heterodimer, which binds two essential AAA+ ATPases RUVBL1/RUVBL2. Here authors use a structural approach to study RPAP3 and find an RPAP3-like protein (SPAG1) which also forms a co-chaperone
Externí odkaz:
https://doaj.org/article/f9bce095aa2a4c49a49a7a66e4c6ecf6
Autor:
Dario Neri, Huib Ovaa, Sibylle Burger, Tatiana Gubser, Matthias Altmeyer, Marco Gatti, Alessandra Villa, Benoît Bragantini, Monique P. C. Mulder, Lorenza Penengo, Maria Victoria Botuyan, Franziska Walser, Georges Mer
Publikováno v:
Molecular Cell, 80(3), 423-436.e9. CELL PRESS
Mol Cell
Mol Cell
The ubiquitin system regulates the DNA damage response (DDR) by modifying histone H2A at Lys15 (H2AK15ub) and triggering downstream signaling events. Here, we find that phosphorylation of ubiquitin at Thr12 (pUbT12) controls the DDR by inhibiting the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0441d9a872227385a1dce6ed80d8480
https://doi.org/10.1016/j.molcel.2020.09.017
https://doi.org/10.1016/j.molcel.2020.09.017
Autor:
Catarina Oliveira, Dipanjan Chowdhury, Nishita Parnandi, J. Ross Chapman, James R. Thompson, Benoît Bragantini, Gaofeng Cui, Maria Victoria Botuyan, Debiao Zhao, Alexandre Detappe, Shweta Chaubey, Georges Mer, Pascal Drané, Marie Eve Brault
Dynamic protein interaction networks such as DNA double-strand break (DSB) signaling are modulated by post-translational modifications (PTMs). The DNA repair factor 53BP1 is a rare example of a protein whose PTM binding function can be switched on an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4fe4c237e6413f1742a0c5b8650b051
https://doi.org/10.1038/s41594-018-0083-z
https://doi.org/10.1038/s41594-018-0083-z