Rapid kinetic analysis of a point mutant of HIV-1 reverse transcriptase lacking ribonuclease H activity
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00074a025
Reference18 articles.
1. A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity
2. Crystal Structure of the Ribonuclease H Domain of HIV-1 Reverse Transcriptase
3. Polymerization and RNase H activities of the reverse transcriptases from avian myeloblastosis, human immunodeficiency, and Moloney murine leukemia viruses are functionally uncoupled.
4. Analysis of the RNA- and DNA-dependent DNA polymerase activities of point mutants of HIV-1 reverse transcriptase lacking ribonuclease H activity
5. Reverse transcriptase.RNase H from the human immunodeficiency virus. Relationship of the DNA polymerase and RNA hydrolysis activities.
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1. Tighter Binding of HIV Reverse Transcriptase to RNA−DNA versus DNA−DNA Results Mostly from Interactions in the Polymerase Domain and Requires Just a Small Stretch of RNA−DNA;Biochemistry;2006-05-24
2. Combining mutations in HIV-1 reverse transcriptase with mutations in the HIV-1 polypurine tract affects RNase H cleavages involved in PPT utilization;Virology;2006-05
3. Mutations at position 184 of human immunodeficiency virus type-1 reverse transcriptase affect virus titer and viral DNA synthesis;Virology;2004-04
4. A 5'-3' long-range interaction in Ty1 RNA controls its reverse transcription and retrotransposition;The EMBO Journal;2002-08-15
5. Replication of Phenotypically Mixed Human Immunodeficiency Virus Type 1 Virions Containing Catalytically Active and Catalytically Inactive Reverse Transcriptase;Journal of Virology;2001-07-15
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