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K. W. Caldecott
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The region of XRCC1 which harbours the three most common nonsynonymous polymorphic variants, is essential for the scaffolding function of XRCC1
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Topoisomerase I poisoning results in PARP-mediated replication fork reversal
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The genesis of cerebellar interneurons and the prevention of neural DNA damage require XRCC1
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Poly(ADP-ribose) polymerase-1 modulates DNA repair capacity and prevents formation of DNA double strand breaks
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PARP-1 ensures regulation of replication fork progression by homologous recombination on damaged DNA
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Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells
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Poly(ADP-ribose) polymerase 1 accelerates single-strand break repair in concert with poly(ADP-ribose) glycohydrolase
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End-damage-specific proteins facilitate recruitment or stability of X-ray cross-complementing protein 1 at the sites of DNA single-strand break repair
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DNA polymerase β promotes recruitment of DNA ligase IIIα-XRCC1 to sites of base excision repair
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Ablation of PARP-1 does not interfere with the repair of DNA double-strand breaks, but compromises the reactivation of stalled replication forks
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A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage
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Spatial and temporal cellular responses to single-strand breaks in human cells
S Okano et al.
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Poly(ADP-ribose) polymerase-1 (PARP-1) is required in murine cell lines for base excision repair of oxidative DNA damage in the absence of DNA polymerase β
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Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1
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A monomeric red fluorescent protein
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Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
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Base excision repair is efficient in cells lacking poly(ADP-ribose) polymerase 1
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XRCC1 keeps DNA from getting stranded
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