Perturbed gap-filling synthesis in nucleotide excision repair causes histone H2AX phosphorylation in human quiescent cells.

Matsumoto, Megumi

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