Eric Coïc相关文献与解析，生知库 | 链接生命科学的每一步

日期影响因子

Correction: Ma et al. Rad52 Oligomeric N-Terminal Domain Stabilizes Rad51 Nucleoprotein Filaments and Contributes to Their Protection against Srs2. Cells 2021, 10, 1467

更正：Ma 等人。Rad52 寡聚 N 端结构域可稳定 Rad51 核蛋白丝并有助于保护其免受 Srs2 的侵害。Cells 2021, 10, 1467

影响因子:5.1

doi:10.3390/cells10113207

Emilie Ma, Laurent Maloisel, Léa Le Falher, Raphaël Guérois, Eric Coïc

细胞生物学

发表日期：2021

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Rad52 Oligomeric N-Terminal Domain Stabilizes Rad51 Nucleoprotein Filaments and Contributes to Their Protection against Srs2

Rad52 寡聚 N 端结构域可稳定 Rad51 核蛋白丝并有助于保护其免受 Srs2 的侵害

影响因子:5.1

doi:10.3390/cells10061467

Emilie Ma, Laurent Maloisel, Léa Le Falher, Raphaël Guérois, Eric Coïc

发表日期：2021

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Rad52-Rad51 association is essential to protect Rad51 filaments against Srs2, but facultative for filament formation

Rad52-Rad51 相互作用对于保护 Rad51 丝状体免受 Srs2 损伤至关重要，但对于丝状体的形成并非必需。

影响因子:6.4

doi:10.7554/eLife.32744

Emilie Ma ,Pauline Dupaigne ,Laurent Maloisel ,Raphaël Guerois ,Eric Le Cam ,Eric Coïc

发表日期：2018

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Rad52 sumoylation prevents the toxicity of unproductive Rad51 filaments independently of the anti-recombinase Srs2

Rad52 SUMO化可独立于抗重组酶 Srs2 防止非生产性 Rad51 细丝的毒性

期刊:PLoS Genetics

doi:10.1371/journal.pgen.1003833

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

发表日期：2013

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