Switching 53BP1 on and off via Tudors

[1]  M. Botuyan,et al.  Mechanism of 53BP1 activity regulation by RNA-binding TIRR and a designer protein , 2018, Nature Structural & Molecular Biology.

[2]  Zihua Gong,et al.  Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR , 2018, Nature Communications.

[3]  J. Harper,et al.  TIRR regulates 53BP1 by masking its histone methyl-lysine binding function , 2017, Nature.

[4]  D. Durocher,et al.  The structural basis of modified nucleosome recognition by 53BP1 , 2016, Nature.

[5]  E. Appella,et al.  Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. , 2015, Structure.

[6]  Stéphanie Panier,et al.  Double-strand break repair: 53BP1 comes into focus , 2013, Nature Reviews Molecular Cell Biology.

[7]  D. Durocher,et al.  53BP1 is a reader of the DNA damage-induced H2A Lys15 ubiquitin mark , 2013, Nature.

[8]  R. Greenberg,et al.  Acetylation Limits 53BP1 Association with Damaged Chromatin to Promote Homologous Recombination , 2012, Nature Structural &Molecular Biology.

[9]  Derryck H. Smith.  Competing interests of authors , 2009, Canadian Medical Association Journal.

[10]  E. Appella,et al.  Role for 53BP1 Tudor Domain Recognition of p53 Dimethylated at Lysine 382 in DNA Damage Signaling* , 2008, Journal of Biological Chemistry.

[11]  Min Gyu Lee,et al.  p53 is regulated by the lysine demethylase LSD1 , 2007, Nature.

[12]  Georges Mer,et al.  Structural Basis for the Methylation State-Specific Recognition of Histone H4-K20 by 53BP1 and Crb2 in DNA Repair , 2006, Cell.