Ectopic expression of RNF168 and 53BP1 increases mutagenic but not physiological non-homologous end joining.
about
Writers, Readers, and Erasers of Histone Ubiquitylation in DNA Double-Strand Break RepairRole of Deubiquitinating Enzymes in DNA RepairTIRR regulates 53BP1 by masking its histone methyl-lysine binding functionTumors overexpressing RNF168 show altered DNA repair and responses to genotoxic treatments, genomic instability and resistance to proteotoxic stress.Repair Pathway Choices and Consequences at the Double-Strand BreakRetroviral insertional mutagenesis implicates E3 ubiquitin ligase RNF168 in the control of cell proliferation and survival.53BP1 fosters fidelity of homology-directed DNA repair.Regulatory cross-talk determines the cellular levels of 53BP1 protein, a critical factor in DNA repair.TIRR and 53BP1- partners in arms.
P2860
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P2860
Ectopic expression of RNF168 and 53BP1 increases mutagenic but not physiological non-homologous end joining.
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name
Ectopic expression of RNF168 a ...... al non-homologous end joining.
@ast
Ectopic expression of RNF168 a ...... al non-homologous end joining.
@en
type
label
Ectopic expression of RNF168 a ...... al non-homologous end joining.
@ast
Ectopic expression of RNF168 a ...... al non-homologous end joining.
@en
prefLabel
Ectopic expression of RNF168 a ...... al non-homologous end joining.
@ast
Ectopic expression of RNF168 a ...... al non-homologous end joining.
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P2093
P2860
P50
P356
P1476
Ectopic expression of RNF168 a ...... al non-homologous end joining.
@en
P2093
André Nussenzweig
Elsa Callén
P2860
P304
P356
10.1093/NAR/GKV336
P407
P577
2015-04-27T00:00:00Z