Rad51 paralogs Rad55-Rad57 balance the anti-recombinase Srs2 in Rad51 filament formation

Por Liu, Jie, Renault, Ludovic, Veaute, Xavier, Fabre, Francis, Stahlberg, Henning, Heyer, Wolf-Dietrich
Publicado em 2011

Srs2 removes deadly recombination intermediates independently of its interaction with SUMO-modified PCNA

Por Le Breton, Cyrille, Dupaigne, Pauline, Robert, Thomas, Le Cam, Eric, Gangloff, Serge, Fabre, Francis, Veaute, Xavier
Publicado em 2008

The translesion DNA polymerases Pol ζ and Rev1 are activated independently of PCNA ubiquitination upon UV radiation in mutants of DNA polymerase δ

Por Tellier-Lebegue, Carine, Dizet, Eléa, Ma, Emilie, Veaute, Xavier, Coïc, Eric, Charbonnier, Jean-Baptiste, Maloisel, Laurent
Publicado no PLoS Genet (2017)

Correction: The translesion DNA polymerases Pol ζ and Rev1 are activated independently of PCNA ubiquitination upon UV radiation in mutants of DNA polymerase δ

Por Tellier-Lebegue, Carine, Dizet, Eléa, Ma, Emilie, Veaute, Xavier, Coïc, Eric, Charbonnier, Jean-Baptiste, Maloisel, Laurent
Publicado no PLoS Genet (2018)

Rad52 Sumoylation Prevents the Toxicity of Unproductive Rad51 Filaments Independently of the Anti-Recombinase Srs2

Por Esta, Aline, Ma, Emilie, Dupaigne, Pauline, Maloisel, Laurent, Guerois, Raphaël, Le Cam, Eric, Veaute, Xavier, Coïc, Eric
Publicado em 2013

UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli

Por Veaute, Xavier, Delmas, Stéphane, Selva, Marjorie, Jeusset, Josette, Le Cam, Eric, Matic, Ivan, Fabre, Francis, Petit, Marie-Agnès
Publicado em 2005

Srs2 promotes synthesis-dependent strand annealing by disrupting DNA polymerase δ-extending D-loops

Por Liu, Jie, Ede, Christopher, Wright, William D, Gore, Steven K, Jenkins, Shirin S, Freudenthal, Bret D, Todd Washington, M, Veaute, Xavier, Heyer, Wolf-Dietrich
Publicado no eLife (2017)

A role for Tau protein in maintaining ribosomal DNA stability and cytidine deaminase-deficient cell survival

Por Bou Samra, Elias, Buhagiar-Labarchède, Géraldine, Machon, Christelle, Guitton, Jérôme, Onclercq-Delic, Rosine, Green, Michael R., Alibert, Olivier, Gazin, Claude, Veaute, Xavier, Amor-Guéret, Mounira
Publicado no Nat Commun (2017)

Structural basis for the substrate selectivity of Helicobacter pylori NucT nuclease activity

Por Celma, Louisa, Corbinais, Christopher, Vercruyssen, Julien, Veaute, Xavier, de la Sierra-Gallay, Inès Li, Guérois, Raphaël, Busso, Didier, Mathieu, Aurélie, Marsin, Stéphanie, Quevillon-Cheruel, Sophie, Radicella, J. Pablo
Publicado no PLoS One (2017)