Perturbed gap-filling synthesis in nucleotide excision repair causes histone H2AX phosphorylation in human quiescent cells. [electronic resource]
Producer: 20071127Description: 1104-12 p. digitalISSN:- 0021-9533
- Adaptor Proteins, Signal Transducing -- metabolism
- Ataxia Telangiectasia Mutated Proteins
- Cell Cycle -- physiology
- Cell Cycle Proteins -- metabolism
- Cells, Cultured
- Checkpoint Kinase 1
- Cytarabine -- pharmacology
- DNA Damage -- physiology
- DNA Polymerase II -- metabolism
- DNA Polymerase III -- metabolism
- DNA Repair -- physiology
- DNA, Single-Stranded -- physiology
- DNA-Binding Proteins
- Fibroblasts -- metabolism
- Histones -- metabolism
- Humans
- Phosphorylation
- Proliferating Cell Nuclear Antigen -- metabolism
- Protein Kinases -- metabolism
- Protein Serine-Threonine Kinases -- metabolism
- Replication Protein A -- metabolism
- Signal Transduction -- physiology
- Ultraviolet Rays -- adverse effects
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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