Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Laure Jobert"'
Autor:
Lene Alsøe, Antonio Sarno, Sergio Carracedo, Diana Domanska, Felix Dingler, Lisa Lirussi, Tanima SenGupta, Nuriye Basdag Tekin, Laure Jobert, Ludmil B. Alexandrov, Anastasia Galashevskaya, Cristina Rada, Geir Kjetil Sandve, Torbjørn Rognes, Hans E. Krokan, Hilde Nilsen
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
Abstract Both a DNA lesion and an intermediate for antibody maturation, uracil is primarily processed by base excision repair (BER), either initiated by uracil-DNA glycosylase (UNG) or by single-strand selective monofunctional uracil DNA glycosylase
Externí odkaz:
https://doaj.org/article/200ff99a0e8a48df8df9562bc5e8eec8
Autor:
Penelope Kroustallaki, Lisa Lirussi, Sergio Carracedo, Panpan You, Q. Ying Esbensen, Alexandra Götz, Laure Jobert, Lene Alsøe, Pål Sætrom, Sarantis Gagos, Hilde Nilsen
Publikováno v:
Cell Reports, Vol 28, Iss 7, Pp 1690-1702.e10 (2019)
Summary: Telomerase biogenesis is a complex process where several steps remain poorly understood. Single-strand-selective uracil-DNA glycosylase (SMUG1) associates with the DKC1-containing H/ACA ribonucleoprotein complex, which is essential for telom
Externí odkaz:
https://doaj.org/article/c1b2bb7b8be24fc3b74be5042f5e16cb
Autor:
Lisa Lirussi, Dilara Ayyildiz, Yan Liu, Nicola P Montaldo, Sergio Carracedo, Miriam R Aure, Laure Jobert, Xavier Tekpli, Joel Touma, Torill Sauer, Emiliano Dalla, Vessela N Kristensen, Jürgen Geisler, Silvano Piazza, Gianluca Tell, Hilde Nilsen
Publikováno v:
Nucleic acids research. 50(18)
Single-strand selective uracil–DNA glycosylase 1 (SMUG1) initiates base excision repair (BER) of uracil and oxidized pyrimidines. SMUG1 status has been associated with cancer risk and therapeutic response in breast carcinomas and other cancer types
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cbdd1390fcc468684dc5a6a5f8b66d2
https://pubmed.ncbi.nlm.nih.gov/36156150
https://pubmed.ncbi.nlm.nih.gov/36156150
Autor:
Lisa Lirussi, Geir Kjetil Sandve, Laure Jobert, Lene Alsøe, Sergio Carracedo, Ludmil B. Alexandrov, Anastasia Galashevskaya, Torbjørn Rognes, Felix A. Dingler, Hans E. Krokan, Hilde Nilsen, Nuriye Basdag Tekin, Diana Domanska, Cristina Rada, Antonio Sarno, Tanima SenGupta
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
Both a DNA lesion and an intermediate for antibody maturation, uracil is primarily processed by base excision repair (BER), either initiated by uracil-DNA glycosylase (UNG) or by single-strand selective monofunctional uracil DNA glycosylase (SMUG1).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e98397a8d938a392115c1db5e0851309
https://pubmed.ncbi.nlm.nih.gov/28775312
https://pubmed.ncbi.nlm.nih.gov/28775312
Autor:
Laure Jobert, Hanne Kim Skjeldam, Anastasia Galashevskaya, Bjørn Dalhus, Magnar Bjørås, Cathrine Broberg Vågbø, Hilde Nilsen
Publikováno v:
Molecular Cell. 49:339-345
Single-strand-selective monofunctional uracil-DNA glycosylase 1 (SMUG1) is a base excision repair enzyme that removes uracil and oxidised pyrimidines from DNA. We show that SMUG1 interacts with the pseudouridine synthase Dyskerin (DKC1) and colocaliz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a21c802dc53c30fefe796ff5ebe7f89
https://doi.org/10.1016/j.molcel.2012.11.010
https://doi.org/10.1016/j.molcel.2012.11.010
Publikováno v:
Oncogene
Oncogene, Nature Publishing Group, 2012, epub ahead of print. ⟨10.1038/onc.2012.490⟩
Oncogene, Nature Publishing Group, 2012, epub ahead of print. ⟨10.1038/onc.2012.490⟩
International audience; TAF15 (formerly TAFII68) is a member of the FET (FUS, EWS, TAF15) family of RNA- and DNA-binding proteins whose genes are frequently translocated in sarcomas. By performing global gene expression profiling, we found that TAF15
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20074ed88dbda476df0464bccf5737a4
https://hal.archives-ouvertes.fr/hal-00853421
https://hal.archives-ouvertes.fr/hal-00853421
Autor:
Laure Jobert, Beáta E. Jády, Laszlo Tora, Elodie Van Herreweghe, Apostolia Guialis, Natalia Pinzón, Tamás Kiss
Publikováno v:
EMBO Reports
EMBO Reports, EMBO Press, 2009, 10 (5), pp.494-500. ⟨10.1038/embor.2009.24⟩
EMBO Reports, 2009, 10 (5), pp.494-500. ⟨10.1038/embor.2009.24⟩
EMBO Reports, EMBO Press, 2009, 10 (5), pp.494-500. ⟨10.1038/embor.2009.24⟩
EMBO Reports, 2009, 10 (5), pp.494-500. ⟨10.1038/embor.2009.24⟩
International audience; The U1 small nuclear RNA (snRNA)--in the form of the U1 spliceosomal Sm small nuclear ribonucleoprotein particle (snRNP) that contains seven Sm and three U1-specific RNP proteins-has a crucial function in the recognition and r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c2c28b84680a69afd2de4f74a9a579e
https://www.hal.inserm.fr/inserm-00384441
https://www.hal.inserm.fr/inserm-00384441
Publikováno v:
Experimental Cell Research
Experimental Cell Research, 2009, 315 (7), pp.1273-86. ⟨10.1016/j.yexcr.2008.12.008⟩
Experimental Cell Research, Elsevier, 2009, 315 (7), pp.1273-86. ⟨10.1016/j.yexcr.2008.12.008⟩
Experimental Cell Research, 2009, 315 (7), pp.1273-86. ⟨10.1016/j.yexcr.2008.12.008⟩
Experimental Cell Research, Elsevier, 2009, 315 (7), pp.1273-86. ⟨10.1016/j.yexcr.2008.12.008⟩
International audience; TAF15 (formerly TAF(II)68) is a nuclear RNA-binding protein that is associated with a distinct population of TFIID and RNA polymerase II complexes. TAF15 harbours an N-terminal activation domain, an RNA recognition motif (RRM)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf9f178fe2287d2bb75db79dcdf34a9a
https://www.hal.inserm.fr/inserm-00384438
https://www.hal.inserm.fr/inserm-00384438