mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivo

To protect cells from oxidative DNA damage and mutagenesis, organisms possess multiple glycosylases to recognize the damaged bases and to initiate the Base Excision Repair pathway. Three DNA glycosylases have been identified in mammals that are homologous to the Escherichia coli Fpg and Nei proteins...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2010-03, Vol.107 (11), p.4925-4930
Hauptverfasser:	Liu, Minmin, Bandaru, Viswanath, Bond, Jeffrey P, Jaruga, Pawel, Zhao, Xiaobei, Christov, Plamen P, Burrows, Cynthia J, Rizzo, Carmelo J, Dizdaroglu, Miral, Wallace, Susan S
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Base excision repair Biochemistry Biological Sciences Cells DNA DNA - metabolism DNA Damage DNA glycosylase DNA Glycosylases - chemistry DNA Glycosylases - metabolism DNA repair E coli Endodeoxyribonucleases - chemistry Endodeoxyribonucleases - metabolism Enzymes Escherichia coli Escherichia coli - genetics Gamma Rays Genetic mutation Guanidines - metabolism Guanosine - analogs & derivatives Guanosine - metabolism Hydantoins - metabolism Kinetics Lesions Mice Molecular Sequence Data Molecular structure Mus musculus Mutagenesis Mutation Mutation - genetics Nei protein Nucleophiles Proline Proteins purines Pyrimidines - metabolism Rodents Schiff bases Schiff Bases - metabolism Sequence Alignment Sequence Homology, Amino Acid Spiro Compounds - metabolism Substrate Specificity - radiation effects valine Valine - metabolism
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