Going APE over ref-1

• Published in: Mutation research Vol. 461; no. 2; pp. 83 - 108
• Main Authors: Evans, Angela R., Limp-Foster, Melissa, Kelley, Mark R.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier 16.10.2000
• Subjects: Animals; Ape1/ref-1 protein; base excision repair; Biological and medical sciences; Carbon-Oxygen Lyases - chemistry; Carbon-Oxygen Lyases - genetics; Carbon-Oxygen Lyases - physiology; DNA Repair - physiology; DNA-(Apurinic or Apyrimidinic Site) Lyase; Endodeoxyribonucleases - physiology; Fos protein; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation; Humans; Models, Molecular; Molecular and cellular biology; Molecular genetics; Mutagenesis. Repair; NF-^KB protein; Oxidation-Reduction; Tissue Distribution; Transcription Factors - metabolism; Oxidation reduction; Excision; Molecular structure; Nucleotide sequence; Enzyme; DNA-(apurinic or apyrimidinic site) lyase; Homology; Gene organization; Lyases; Review; Malignant tumor; Gene expression; Regulation(control); Gene; DNA; Molecular complex; Lesion; Transcription factor; Repair; Carbon-oxygen lyases

The DNA base excision repair (BER) pathway is responsible for the repair of cellular alkylation and oxidative DNA damage. A crucial and the second step in the BER pathway involves the cleavage of baseless sites in DNA by an AP endonuclease. The major AP endonuclease in mammalian cells is Ape1/ref-1....