Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Christophe Clouin"'
Autor:
Chloé Lescale, Hélène Lenden Hasse, Andrew N. Blackford, Gabriel Balmus, Joy J. Bianchi, Wei Yu, Léa Bacoccina, Angélique Jarade, Christophe Clouin, Rohan Sivapalan, Bernardo Reina-San-Martin, Stephen P. Jackson, Ludovic Deriano
Publikováno v:
Cell Reports, Vol 16, Iss 11, Pp 2967-2979 (2016)
Paralog of XRCC4 and XLF (PAXX) is a member of the XRCC4 superfamily and plays a role in nonhomologous end-joining (NHEJ), a DNA repair pathway critical for lymphocyte antigen receptor gene assembly. Here, we find that the functions of PAXX and XLF i
Externí odkaz:
https://doaj.org/article/506134640cca44fdb752c066f4b3376f
Autor:
Hélène Lenden Hasse, Chloé Lescale, Bernardo Reina-San-Martin, Stephen P. Jackson, Léa Bacoccina, Gabriel Balmus, Joy J. Bianchi, Ludovic Deriano, Rohan Sivapalan, Christophe Clouin, Angélique Jarade, Andrew N. Blackford, Wei Yu
Publikováno v:
Cell Reports
Cell Reports, Elsevier Inc, 2016, ⟨10.1016/j.celrep.2016.08.069⟩
Cell Reports, Vol 16, Iss 11, Pp 2967-2979 (2016)
Cell Reports, 2016, ⟨10.1016/j.celrep.2016.08.069⟩
Cell Reports, Elsevier Inc, 2016, ⟨10.1016/j.celrep.2016.08.069⟩
Cell Reports, Vol 16, Iss 11, Pp 2967-2979 (2016)
Cell Reports, 2016, ⟨10.1016/j.celrep.2016.08.069⟩
Summary Paralog of XRCC4 and XLF (PAXX) is a member of the XRCC4 superfamily and plays a role in nonhomologous end-joining (NHEJ), a DNA repair pathway critical for lymphocyte antigen receptor gene assembly. Here, we find that the functions of PAXX a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3b71045a3bd84fac2350e0b2ce23a1d
https://doi.org/10.1016/j.celrep.2016.08.069
https://doi.org/10.1016/j.celrep.2016.08.069
Autor:
Michael A. Lampson, Stephen S. Taylor, René H. Medema, Christophe Clouin, Rob Klompmaker, Michael B. Yaffe, Daniel Lim, Arne Lindqvist, Raimundo Freire, Libor Macůrek
Publikováno v:
Nature. 455(7209)
Polo-like kinase-1 (PLK1) is an essential mitotic kinase regulating multiple aspects of the cell division process. Activation of PLK1 requires phosphorylation of a conserved threonine residue (Thr 210) in the T-loop of the PLK1 kinase domain, but the