scholarly journals New oligonucleotide derivatives as unreactive substrate analogues and potential inhibitors of human apurinic/apyrimidinic endonuclease APE1

2016 ◽  
Vol 12 (1) ◽  
pp. 67-75 ◽  
Author(s):  
Nikita A. Kuznetsov ◽  
Maxim S. Kupryushkin ◽  
Tatyana V. Abramova ◽  
Alexandra A. Kuznetsova ◽  
Anastasia D. Miroshnikova ◽  
...  
Keyword(s):  
Dna Repair ◽  
Repair System ◽  
Key Enzymes ◽  
Substrate Analogues ◽  
System P ◽  
Base Excision ◽  
Potential Inhibitors ◽  
Base Excision Dna Repair ◽  
Oligonucleotide Derivatives

Human apurinic/apyrimidinic endonuclease APE1 is one of the key enzymes of the base excision DNA repair system.

scholarly journals Molecular Mechanisms of the Whole DNA Repair System: A Comparison of Bacterial and Eukaryotic Systems

2010 ◽  
Vol 2010 ◽  
pp. 1-32 ◽  
Author(s):  
Rihito Morita ◽  
Shuhei Nakane ◽  
Atsuhiro Shimada ◽  
Masao Inoue ◽  
Hitoshi Iino ◽  
...  
Keyword(s):  
Dna Repair ◽  
Molecular Mechanisms ◽  
Excision Repair ◽  
Thermus Thermophilus ◽  
Repair System ◽  
System A ◽  
Recombination Repair ◽  
Repair Mechanisms ◽  
Repair Pathways ◽  
Base Excision

DNA is subjected to many endogenous and exogenous damages. All organisms have developed a complex network of DNA repair mechanisms. A variety of different DNA repair pathways have been reported: direct reversal, base excision repair, nucleotide excision repair, mismatch repair, and recombination repair pathways. Recent studies of the fundamental mechanisms for DNA repair processes have revealed a complexity beyond that initially expected, with inter- and intrapathway complementation as well as functional interactions between proteins involved in repair pathways. In this paper we give a broad overview of the whole DNA repair system and focus on the molecular basis of the repair machineries, particularly inThermus thermophilusHB8.

scholarly journals Base excision DNA repair and cancer

Oncotarget ◽  
2014 ◽  
Vol 6 (2) ◽  
pp. 584-585 ◽  
Author(s):  
Gianluca Tell ◽  
Bruce Demple
Keyword(s):  
Dna Repair ◽  
Base Excision ◽  
Base Excision Dna Repair

scholarly journals Expression of Base Excision DNA Repair Genes Is a Sensitive Biomarker for in Vivo Detection of Chemical-induced Chronic Oxidative Stress

2004 ◽  
Vol 64 (3) ◽  
pp. 1050-1057 ◽  
Author(s):  
Ivan Rusyn ◽  
Shoji Asakura ◽  
Brian Pachkowski ◽  
Blair U. Bradford ◽  
Mikhail F. Denissenko ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Dna Repair ◽  
Dna Repair Genes ◽  
In Vivo Detection ◽  
Chronic Oxidative Stress ◽  
Base Excision ◽  
Base Excision Dna Repair ◽  
Repair Genes

scholarly journals Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair

2016 ◽  
Vol 113 (28) ◽  
pp. 7792-7797 ◽  
Author(s):  
Chenxu Zhu ◽  
Lining Lu ◽  
Jun Zhang ◽  
Zongwei Yue ◽  
Jinghui Song ◽  
...  
Keyword(s):  
Dna Repair ◽  
Excision Repair ◽  
Mammalian Genome ◽  
Dna Bases ◽  
Repair Pathway ◽  
Thymine Glycol ◽  
Base Excision ◽  
Oxidation Damage ◽  
Biochemical Analyses ◽  
Base Excision Dna Repair

NEIL1 (Nei-like 1) is a DNA repair glycosylase guarding the mammalian genome against oxidized DNA bases. As the first enzymes in the base-excision repair pathway, glycosylases must recognize the cognate substrates and catalyze their excision. Here we present crystal structures of human NEIL1 bound to a range of duplex DNA. Together with computational and biochemical analyses, our results suggest that NEIL1 promotes tautomerization of thymine glycol (Tg)—a preferred substrate—for optimal binding in its active site. Moreover, this tautomerization event also facilitates NEIL1-catalyzed Tg excision. To our knowledge, the present example represents the first documented case of enzyme-promoted tautomerization for efficient substrate recognition and catalysis in an enzyme-catalyzed reaction.

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