High-level expression of self-processed HIV-1 protease in Escherichia coli using a synthetic gene
- 31 May 1989
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 161 (3), 1056-1063
- https://doi.org/10.1016/0006-291x(89)91350-8
Abstract
No abstract availableThis publication has 38 references indexed in Scilit:
- Crystal structure of a retroviral protease proves relationship to aspartic protease familyNature, 1989
- Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1Nature, 1989
- Enzymatic activity of a synthetic 99 residue protein corresponding to the putative HIV-1 proteaseCell, 1988
- VIRAL PROTEINASESAnnual Review of Biochemistry, 1988
- Codon usage patterns inEscherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melanogasterandHomo sapiens; a review of the considerable within-species diversityNucleic Acids Research, 1988
- A structural model for the retroviral proteasesNature, 1987
- Solid-phase assembly of cow colostrum trypsin inhibitor geneNucleic Acids Research, 1987
- Murine leukemia virus maturation: Protease region required for conversion from “immature” to “Mature” core form and for virus infectivityVirology, 1985
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- Complete nucleotide sequence of the AIDS virus, HTLV-IIINature, 1985