A 3′-5′ exonuclease activity embedded in the helicase core domain of Candida albicans Pif1 helicase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep42865.pdf
Reference33 articles.
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3. Singleton, M. R., Dillingham, M. S., Gaudier, M., Kowalczykowski, S. C. & Wigley, D. B. Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks. Nature 432, 187–193 (2004).
4. Dillingham, M. S., Spies, M. & Kowalczykowski, S. C. RecBCD enzyme is a bipolar DNA helicase. Nature 423, 893–897 (2003).
5. Taylor, A. F. & Smith, G. R. RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity. Nature 423, 889–893 (2003).
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1. Dynamic regulation of Pif1 acetylation is crucial to the maintenance of genome stability;Current Genetics;2020-10-20
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3. The helicase Pif1 functions in the template switching pathway of DNA damage bypass;Nucleic Acids Research;2018-08-10
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