RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)80172-D/fullpdf
Reference21 articles.
1. HIV-1 RT-associated ribonuclease H displays both endonuclease and 3′----5′ exonuclease activity.
2. Characterization of Highly Immunogenic p66/p51 as the Reverse Transcriptase of HTLV-III/LAV
3. Structural characterization of reverse transcriptase and endonuclease polypeptides of the acquired immunodeficiency syndrome retrovirus
4. HIV-1 reverse transcriptase: crystallization and analysis of domain structure by limited proteolysis
5. Dimerization of human immunodeficiency virus type 1 reverse transcriptase. A target for chemotherapeutic intervention.
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1. Retroviral RNase H: Structure, mechanism, and inhibition;Viral Replication Enzymes and their Inhibitors Part B;2021
2. The β1′−β2′ Motif of the RNase H Domain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Is Responsible for Conferring Open Conformation to the p66 Subunit by Displacing the Connection Domain from the Polymerase Cleft;Biochemistry;2017-06-28
3. The Cellular Antiviral Protein APOBEC3G Interacts with HIV-1 Reverse Transcriptase and Inhibits Its Function during Viral Replication;Journal of Virology;2012-02-01
4. Targeting Protein-Protein and Protein-Nucleic Acid Interactions for Anti-HIV Therapy;Current Pharmaceutical Design;2011-11-01
5. Targeting the protein–protein interactions of the HIV lifecycle;Chem. Soc. Rev.;2011
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