scholarly journals Use of novel assays to measure in vivo base excision DNA repair

2009 ◽  
Author(s):  
Preethi Sundaresakumar
2004 ◽  
Vol 64 (3) ◽  
pp. 1050-1057 ◽  
Author(s):  
Ivan Rusyn ◽  
Shoji Asakura ◽  
Brian Pachkowski ◽  
Blair U. Bradford ◽  
Mikhail F. Denissenko ◽  
...  

Oncogene ◽  
2002 ◽  
Vol 21 (5) ◽  
pp. 731-737 ◽  
Author(s):  
Young R Seo ◽  
Melissa L Fishel ◽  
Sally Amundson ◽  
Mark R Kelley ◽  
Martin L Smith

F1000Research ◽  
2017 ◽  
Vol 6 ◽  
pp. 279 ◽  
Author(s):  
Upasna Thapar ◽  
Bruce Demple

Since the discovery of the base excision repair (BER) system for DNA more than 40 years ago, new branches of the pathway have been revealed at the biochemical level by in vitro studies. Largely for technical reasons, however, the confirmation of these subpathways in vivo has been elusive. We review methods that have been used to explore BER in mammalian cells, indicate where there are important knowledge gaps to fill, and suggest a way to address them.


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

2016 ◽  
Vol 113 (28) ◽  
pp. 7792-7797 ◽  
Author(s):  
Chenxu Zhu ◽  
Lining Lu ◽  
Jun Zhang ◽  
Zongwei Yue ◽  
Jinghui Song ◽  
...  

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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