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Research | 27 November 2017
Inhibition of 53BP1 favors homology-dependent DNA repair and increases CRISPR–Cas9 genome-editing efficiency
- Marella D Canny
- , Nathalie Moatti
- , Leo C K Wan
- , Amélie Fradet-Turcotte
- , Danielle Krasner
- , Pedro A Mateos-Gomez
- , Michal Zimmermann
- , Alexandre Orthwein
- , Yu-Chi Juang
- , Wei Zhang
- , Sylvie M Noordermeer
- , Eduardo Seclen
- , Marcus D Wilson
- , Andrew Vorobyov
- , Meagan Munro
- , Andreas Ernst
- , Timothy F Ng
- , Tiffany Cho
- , Paula M Cannon
- , Sachdev S Sidhu
- , Frank Sicheri
- & Daniel Durocher
Nature Biotechnology 36 , 95–102

Rights & permissionsfor article Inhibition of 53BP1 favors homology-dependent DNA repair and increases CRISPR–Cas9 genome-editing efficiency . Opens in a new window.
Research | 27 July 2016
The structural basis of modified nucleosome recognition by 53BP1
Nature 536 , 100–103

Rights & permissionsfor article The structural basis of modified nucleosome recognition by 53BP1 . Opens in a new window.
Research | 12 June 2013
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark
Nature 499 , 50–54

Rights & permissionsfor article 53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark . Opens in a new window.

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Inhibition of 53BP1 favors homology-dependent DNA repair and increases CRISPR–Cas9 genome-editing efficiency

The structural basis of modified nucleosome recognition by 53BP1

53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark

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