Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Frederic Langevin"'
Autor:
Lee Mulderrig, Naomi Park, Serena Nik-Zainal, Frederic Langevin, Juan I. Garaycoechea, Guillaume Guilbaud, Fentang Yang, Gerry P. Crossan, Ketan J. Patel, Sophie Roerink, Sandra Louzada, Michael R. Stratton
Publikováno v:
Nature. 553:171-177
Haematopoietic stem cells renew blood. Accumulation of DNA damage in these cells promotes their decline, while misrepair of this damage initiates malignancies. Here we describe the features and mutational landscape of DNA damage caused by acetaldehyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a8c4f41485eb2814ca4ed75f1c67c97
https://doi.org/10.1038/nature25154
https://doi.org/10.1038/nature25154
Autor:
Etsuro Ito, Seiji Kojima, Kenichi Yoshida, Rui Yu, Camille Nadler, Paul S. Monks, Asuka Hira, Nicola K. Wilson, Motohiro Kato, Ashley N. Kamimae-Lanning, Satoru Miyano, Hiromasa Yabe, Tomoo Osumi, Minako Mori, Miharu Yabe, Michael R. G. Hodskinson, Minoru Takata, Hideki Muramatsu, Lucas B. Pontel, Seishi Ogawa, Toshinori Moriguchi, Christopher L. Millington, Yusuke Okamoto, Masayuki Kobayashi, Yuichi Shiraishi, Meng Wang, Ketan J. Patel, Frederic Langevin, Berthold Göttgens, Yusuke Okuno, Sam Watcham, Felix A. Dingler, Rebecca Cordell, Keitaro Matsuo, Nina Oberbeck, Anfeng Mu
Publikováno v:
Molecular Cell
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Summary Reactive aldehydes arise as by-products of metabolism and are normally cleared by multiple families of enzymes. We find that mice lacking two aldehyde detoxifying enzymes, mitochondrial ALDH2 and cytoplasmic ADH5, have greatly shortened lifes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79d65d6f96b03ddf58df2484332f40f7
http://hdl.handle.net/2433/255881
http://hdl.handle.net/2433/255881
Autor:
Meng Wang, Gillian L. Dornan, Vibe H. Oestergaard, Ketan J. Patel, Eeson Rajendra, Lori A. Passmore, Frederic Langevin
Publikováno v:
Molecular Cell
Rajendra, E, Østergaard, V H, Langevin, F, Wang, M, Dornan, G L, Patel, K J & Passmore, L A 2014, ' The genetic and biochemical basis of FANCD2 Monoubiquitination ', Molecular Cell, vol. 54, no. 5, pp. 858-869 . https://doi.org/10.1016/j.molcel.2014.05.001
Rajendra, E, Østergaard, V H, Langevin, F, Wang, M, Dornan, G L, Patel, K J & Passmore, L A 2014, ' The genetic and biochemical basis of FANCD2 Monoubiquitination ', Molecular Cell, vol. 54, no. 5, pp. 858-869 . https://doi.org/10.1016/j.molcel.2014.05.001
Summary Fanconi anaemia (FA) is a cancer predisposition syndrome characterized by cellular sensitivity to DNA interstrand crosslinkers. The molecular defect in FA is an impaired DNA repair pathway. The critical event in activating this pathway is mon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc897ac6045bb202e976d341868da36a
http://europepmc.org/articles/PMC4051986
http://europepmc.org/articles/PMC4051986
Autor:
Juan I. Garaycoechea, Gerry P. Crossan, Mark J. Arends, Frederic Langevin, Ketan J. Patel, Maria Daly
Publikováno v:
Nature. 489:571-575
The function of haematopoietic stem and progenitor cells is impaired by damaged DNA; here, endogenously generated aldehydes are found to be one source of such damage, which is repaired by the Fanconi anaemia pathway. Haematopoietic stem cells handle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7a0d93666d83ccd453f1f0124b020c9
https://doi.org/10.1038/nature11368
https://doi.org/10.1038/nature11368
Publikováno v:
Nature. 475:53-58
Reactive aldehydes are common carcinogens. They are also by-products of several metabolic pathways and, without enzymatic catabolism, may accumulate and cause DNA damage. Ethanol, which is metabolised to acetaldehyde, is both carcinogenic and teratog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::302e8a07b6d4a5773946145b2b2b009c
https://doi.org/10.1038/nature10192
https://doi.org/10.1038/nature10192
Autor:
Gerry P. Crossan, Mikko I. Kettunen, Frederic Langevin, Mark J. Arends, David Y. Lewis, Sanger Mouse Genetics, Iván V. Rosado, David J. Adams, Louise van der Weyden, Pierre-Henri L. Gaillard, Ferdia A. Gallagher, Ketan J. Patel, Kevin M. Brindle, Rebecca E. McIntyre
Publikováno v:
Nature Genetics
Nature Genetics, Nature Publishing Group, 2011, 43 (2), pp.147-152. ⟨10.1038/ng.752⟩
Crossan, G P, van der Weyden, L, Rosado, I V, Langevin, F, Gaillard, P-H L, McIntyre, R E, Gallagher, F, Kettunen, M I, Lewis, D Y, Brindle, K, Arends, M J & Adams, D J & Patel, K J 2011, ' Disruption of mouse Slx4, a regulator of structure-specific nucleases, phenocopies Fanconi anemia ', Nature Genetics, vol. 43, no. 2, pp. 147-152 . https://doi.org/10.1038/ng.752
Nature genetics
Nature Genetics, Nature Publishing Group, 2011, 43 (2), pp.147-152. ⟨10.1038/ng.752⟩
Crossan, G P, van der Weyden, L, Rosado, I V, Langevin, F, Gaillard, P-H L, McIntyre, R E, Gallagher, F, Kettunen, M I, Lewis, D Y, Brindle, K, Arends, M J & Adams, D J & Patel, K J 2011, ' Disruption of mouse Slx4, a regulator of structure-specific nucleases, phenocopies Fanconi anemia ', Nature Genetics, vol. 43, no. 2, pp. 147-152 . https://doi.org/10.1038/ng.752
Nature genetics
The evolutionarily conserved SLX4 protein, a key regulator of nucleases, is critical for DNA damage response. SLX4 nuclease complexes mediate repair during replication and can also resolve Holliday junctions formed during homologous recombination. He
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81175b7943a670092081f0bdd7fd2d8b
https://doi.org/10.1038/ng.752
https://doi.org/10.1038/ng.752
Autor:
Arno F. Alpi, Georgina Mosedale, Frederic Langevin, Yuichi J. Machida, Anindya Dutta, Ketan J. Patel
Publikováno v:
Molecular and Cellular Biology. 27:8421-8430
The Fanconi anemia (FA) nuclear core complex and the E2 ubiquitin-conjugating enzyme UBE2T are required for the S phase and DNA damage-restricted monoubiquitination of FANCD2. This constitutes a key step in the FA tumor suppressor pathway, and much a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c3c33d5d00ed16c2249cca27a10751a
https://doi.org/10.1128/mcb.00504-07
https://doi.org/10.1128/mcb.00504-07
Autor:
Frederic Langevin, Mioko Ohzeki, Laura J. Simpson, Julian E. Sale, Hendrik J. Kuiken, Wojciech Niedzwiedz, Ketan J. Patel, Minoru Takata, Paul E. Pace, Vibe H. Oestergaard
Publikováno v:
Molecular Cell
Summary Monoubiquitination of FANCD2 and PCNA promotes DNA repair. It causes chromatin accumulation of FANCD2 and facilitates PCNA's recruitment of translesion polymerases to stalled replication. USP1, a protease that removes monoubiquitin from FANCD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82bfd5d03dd78296515fb680645a2b4a
Autor:
Arno F. Alpi, Georgina Mosedale, Frederic Langevin, Mark S. Johnson, Paul E. Pace, Wojciech Niedzwiedz, Ketan J. Patel, José B. Pereira-Leal, Franco Perrina
Publikováno v:
Nature Structural & Molecular Biology. 12:763-771
The helicase-associated endonuclease for fork-structured DNA (Hef) is an archaeabacterial protein that processes blocked replication forks. Here we have isolated the vertebrate Hef ortholog and investigated its molecular function. Disruption of this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a161fc60ff03b714c007650cd7ca835c
https://doi.org/10.1038/nsmb981
https://doi.org/10.1038/nsmb981
Autor:
Niels de Wind, Gerry P. Crossan, Gareth King, Frederic Langevin, Nina Oberbeck, Ketan J. Patel
Publikováno v:
Molecular Cell, 55(6), 807-817
Maternal metabolism provides essential nutrients to enable embryonic development. However, both mother and embryo produce reactive metabolites that can damage DNA. Here we discover how the embryo is protected from these genotoxins. Pregnant mice lack
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f29542053506f431b1430ad1cd5c6458
https://pubmed.ncbi.nlm.nih.gov/25238193
https://pubmed.ncbi.nlm.nih.gov/25238193