Mutations of a conserved residue within HIV-1 ribonuclease H affect its exo- and endonuclease activities
- 1 August 1991
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 220 (3), 801-818
- https://doi.org/10.1016/0022-2836(91)90119-q
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Cleavage of the HIV-1 p66 reverse transcriptase/RNase H by the p9 protease in vitro generates active p15 RNase HArchiv für die gesamte Virusforschung, 1991
- Mutations within the RNase H Domain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Abolish Virus InfectivityJournal of General Virology, 1991
- Interaction of HIV-1 ribonuclease H with polypurine tract containing RNA-DNA hybridsBiochemistry, 1990
- Endoribonucleolytic cleavage of RNA: Oligodeoxynucleotide hybrids by the ribonuclease H activity of HIV-1 reverse transcriptaseBiochemical and Biophysical Research Communications, 1990
- Point mutations in conserved amino acid residues within the C‐terminal domain of HIV‐1 reverse transcriptase specifically repress RNase H functionFEBS Letters, 1989
- Plus-strand priming by Moloney murine leukemia virusJournal of Molecular Biology, 1989
- HIV-1 reverse transcriptase: crystallization and analysis of domain structure by limited proteolysisBiochemistry, 1988
- Enzymatically Active Forms of Reverse Transcriptase of the Human Immunodeficiency VirusAIDS Research and Human Retroviruses, 1988
- Characterization of Highly Immunogenic p66/p51 as the Reverse Transcriptase of HTLV-III/LAVScience, 1986
- A detailed model of reverse transcription and tests of crucial aspectsCell, 1979