dc.contributor.author | Redrejo-Rodriguez, M. | |
dc.contributor.author | Mursalimov, A. | |
dc.contributor.author | Koshenov, Z. | |
dc.contributor.author | Zhakupova, K. | |
dc.contributor.author | Saparbaev, M. K. | |
dc.contributor.author | Ishchenko, A. A. | |
dc.contributor.author | Matkarimov, B. | |
dc.date.accessioned | 2015-10-27T04:40:45Z | |
dc.date.available | 2015-10-27T04:40:45Z | |
dc.date.issued | 2014 | |
dc.identifier.isbn | 9786018046728 | |
dc.identifier.uri | http://nur.nu.edu.kz/handle/123456789/486 | |
dc.description.abstract | Human apurinic/apyrimidinic endonuclease 1 (APE1) is a key DNA repair enzyme involved in both base excision repair (BER) and nucleotide incision repair (NIR) pathways. In the BER pathway, APE1 cleaves DNA at AP sites and 3'-blocking moieties generated by DNA glycosylases. In the NIR pathway, APE1 incises DNA 5' to a number of oxidatively damaged bases. Here we propose to identify and characterize critical amino acids of APE1 involved in either BER and/or NIR functions by using the alignment of the known three-dimensional (or tertiary) structures of Xth family AP endonucleases including the Methanothermobacter thermautotrophicus Mth212, Bacillus subtilis ExoA (1), E. coli Xth and human APE1 proteins (2). | ru_RU |
dc.language.iso | en | ru_RU |
dc.publisher | Nazarbayev University | ru_RU |
dc.subject | DNA repair | ru_RU |
dc.subject | APE1 protein | ru_RU |
dc.subject | endonucleases | ru_RU |
dc.subject | glycosylases | ru_RU |
dc.subject | amino acid | ru_RU |
dc.subject | biochemical | ru_RU |
dc.title | Genetic dissection of the biochemical activities of human DNA repair protein, APE1 | ru_RU |
dc.type | Abstract | ru_RU |