Perturbed gap-filling synthesis in nucleotide excision repair causes histone H2AX phosphorylation in human quiescent cells. [electronic resource]
- Journal of cell science Mar 2007
- 1104-12 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0021-9533
10.1242/jcs.03391 doi
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