Retroviral integrase functions as a multimer and can turn over catalytically.
Open Access
- 1 August 1992
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (23) , 16037-16040
- https://doi.org/10.1016/s0021-9258(18)41960-6
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- HIV-1 reproduction is inhibited by peptides derived from the N- and C-termini of HIV-1 proteaseBiochemical and Biophysical Research Communications, 1991
- The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolutionCell, 1990
- Cooperativity mutants of the γδ resolvase identify an essential interdimer interactionCell, 1990
- Processive recombination by the phage Mu Gin system: Implications for the mechanisms of DNA strand exchange, DNA site alignment, and enhancer actionCell, 1990
- Unraveling retrovirus integrationCell, 1990
- Sedimentation equilibrium measurements of recombinant DNA-derived human interferon .gamma.Biochemistry, 1987
- Structure of bovine blood-coagulation factor Va. Determination of the subunit associations, molecular weights, and asymmetries by analytical ultracentrifugationBiochemistry, 1984
- Nucleotide sequence of rous sarcoma virusCell, 1983
- STUDIES OF SELF‐ASSOCIATING SYSTEMS BY EQUILIBRIUM ULTRACENTRIFUGATION *Annals of the New York Academy of Sciences, 1969
- The Specific Refractive Increment of Some Purified ProteinsJournal of the American Chemical Society, 1948