Fluorimetric analysis of recombinant p15 HIV-1 ribonuclease H
Open Access
- 1 July 1993
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 268 (20) , 14743-14749
- https://doi.org/10.1016/s0021-9258(18)82395-x
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous latticePublished by Elsevier ,2004
- Analysis of the backbone dynamics of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase using nitrogen-15 relaxation measurementsBiochemistry, 1992
- Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolutionJournal of Molecular Biology, 1992
- Secondary structure of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase in solution using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopyJournal of Molecular Biology, 1991
- Crystal Structure of the Ribonuclease H Domain of HIV-1 Reverse TranscriptaseScience, 1991
- Mutations within the RNase H Domain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Abolish Virus InfectivityJournal of General Virology, 1991
- Purification and characterization of the RNase H domain of HIV‐1 reverse transcriptase expressed in recombinant Escherichia coliFEBS Letters, 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
- Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA PolymeraseScience, 1988
- Thermodynamics and kinetics of co-operative protein-nucleic acid bindingJournal of Molecular Biology, 1983