Structural models of ribonuclease H domains in reverse transcriptases from retroviruses
Author:
Publisher
Oxford University Press (OUP)
Subject
Genetics
Link
http://academic.oup.com/nar/article-pdf/19/8/1817/7059594/19-8-1817.pdf
Cited by 39 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Physiological magnesium concentrations increase fidelity of diverse reverse transcriptases from HIV-1, HIV-2, and foamy virus, but not MuLV or AMV;Journal of General Virology;2021-12-14
2. Physiological Magnesium Concentrations Increase Fidelity of Diverse Reverse Transcriptases from HIV-1, HIV-2, and Foamy Virus, but not MuLV or AMV;2021-08-05
3. Physiological Mg2+ Conditions Significantly Alter the Inhibition of HIV-1 and HIV-2 Reverse Transcriptases by Nucleoside and Non-Nucleoside Inhibitors in Vitro;Biochemistry;2016-12-27
4. Human Immunodeficiency Virus Reverse Transcriptase Displays Dramatically Higher Fidelity under Physiological Magnesium Conditions In Vitro;Journal of Virology;2014-05-21
5. Helicase dissociation and annealing of RNA-DNA hybrids by Escherichia coli Cas3 protein;Biochemical Journal;2011-09-14
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