@misc{oai:repo.qst.go.jp:00077520,
 author = {中野, 敏彰 and Nakano, Toshiaki},
 month = {Nov},
 note = {Proteins are covalently trapped on DNA to form DNA-protein cross- links (DPCs) when cells are exposed to DNA damaging agents. Aldehydes are highly electrophilic and readily react with DNA and proteins and hamper their functions. The reactions of aldehydes with DNA give rise to DPCs without an undisrupted DNA strand might be repaired by FANC pathway. Some DNA metabolizinge enzymes also form intermediates that are irreversibly trapped during abortive reactions or in the presence of inhibitors to produce DPCs. Topoisomerase 1 (TOPO1)  relaxes supercoiling and torsion of DNA by transiently introducing a single-strand break (SSB) and rejoining the break. Camptothecin blocks the rejoining step by trapping TOPO1 on DNA (TOPO1-DNA trap) and induces SSBs. Tyrosyl-DNA phosphodiesterase 1 (TDP1) is a DNA 3’-end processing enzyme that repair removes the TOPO1-DNA trap. Recently it has been shown that TDP1 is capable of removing a broad range of 3’-end blocking lesions associated with DNA single- strand breaks and with DNA double- strand breaks. However, substrate specificity of TDP1 is still controversial. In this study, we have analyzed how TDP1 exert repair mechanism of DPC through TOPO1-DNA trap and formaldehyde-induced DPCs., アジア環境変異原学会第6回大会/日本環境変異原学会第48回大会合同大会},
 title = {TDP1はどのようにしてDNAタンパク質クロスリンク損傷の修復機構に関与するのか？},
 year = {2019}
}