Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Maria Victoria Botuyan"'
Autor:
Susan Kilgas, Aleem Syed, Patrick Toolan-Kerr, Michelle L. Swift, Shrabasti Roychoudhury, Aniruddha Sarkar, Sarah Wilkins, Mikayla Quigley, Anna R. Poetsch, Maria Victoria Botuyan, Gaofeng Cui, Georges Mer, Jernej Ule, Pascal Drané, Dipanjan Chowdhury
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024)
Abstract Tudor Interacting Repair Regulator (TIRR) is an RNA-binding protein (RBP) that interacts directly with 53BP1, restricting its access to DNA double-strand breaks (DSBs) and its association with p53. We utilized iCLIP to identify RNAs that dir
Externí odkaz:
https://doaj.org/article/a3262ed44e984be894b2ab228e2c52d3
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:
Jian Ma, Qing Shi, Gaofeng Cui, Haoyue Sheng, Maria Victoria Botuyan, Yingke Zhou, Yuqian Yan, Yundong He, Liguo Wang, Yuzhuo Wang, Georges Mer, Dingwei Ye, Chenji Wang, Haojie Huang
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Geminin-Cdt1 plays essential roles in the regulation of DNA replication. Here the authors reveal that the CULLIN3 E3 ubiquitin ligase adaptor protein SPOP prevents DNA replication over-firing and genome instability by affecting Geminin ubiquitination
Externí odkaz:
https://doaj.org/article/caf1ac2187f84e9cb816d00c2bdee890
Autor:
Brianna J. Klein, Xiaoyan Wang, Gaofeng Cui, Chao Yuan, Maria Victoria Botuyan, Kevin Lin, Yue Lu, Xiaolu Wang, Yue Zhao, Christiane J. Bruns, Georges Mer, Xiaobing Shi, Tatiana G. Kutateladze
Publikováno v:
Cell Reports, Vol 17, Iss 4, Pp 1158-1170 (2016)
PHF20 is a core component of the lysine acetyltransferase complex MOF (male absent on the first)-NSL (non-specific lethal) that generates the major epigenetic mark H4K16ac and is necessary for transcriptional regulation and DNA repair. The role of PH
Externí odkaz:
https://doaj.org/article/ec6c3e6e03384074a40e7c1146c1efdd
Publikováno v:
Chem. 9:1069-1071
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::761a5ccc9eb985db5a025555501d3937
https://doi.org/10.1016/j.chempr.2023.04.016
https://doi.org/10.1016/j.chempr.2023.04.016
Autor:
Yuqian Yan, Yuzhuo Wang, Haojie Huang, Gaofeng Cui, Dingwei Ye, Georges Mer, Maria Victoria Botuyan, Chenji Wang, Yingke Zhou, Jian Ma, Yundong He, Haoyue Sheng, Qing Shi, Liguo Wang
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Geminin and its binding partner Cdt1 are essential for the regulation of DNA replication. Here we show that the CULLIN3 E3 ubiquitin ligase adaptor protein SPOP binds Geminin at endogenous level and regulates DNA replication. SPOP promotes K27-linked
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fbe4d0b6d664eaef796a5d7ea27de1b
https://doi.org/10.1038/s41467-021-26049-6
https://doi.org/10.1038/s41467-021-26049-6
Autor:
Haojie Huang, Donglin Ding, Yingke Zhou, Yuqian Yan, Jiang Pei, Jian Ma, Gaofeng Cui, Maria Victoria Botuyan, Mark A. McNiven, Liguo Wang, Eugene W. Krueger, Xiaosheng Wu, Dingwei Ye, Dejie Wang, Georges Mer, Huadong Pei
Publikováno v:
Science Advances
SPOP mutation disables 53BP1 ubiquitination and exclusion from DNA double-strand break sites and causes genome instability.
53BP1 activates nonhomologous end joining (NHEJ) and inhibits homologous recombination (HR) repair of DNA double-strand b
53BP1 activates nonhomologous end joining (NHEJ) and inhibits homologous recombination (HR) repair of DNA double-strand b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8abdd3473fcd30248aca4bc5553ef4c8
https://doi.org/10.1126/sciadv.abd9208
https://doi.org/10.1126/sciadv.abd9208
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
Publikováno v:
Nature
The BRCA1–BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination1–10. The BRCA1–BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a698745d39a3c6a8857c2ae0b388885
https://pubmed.ncbi.nlm.nih.gov/34404953
https://pubmed.ncbi.nlm.nih.gov/34404953