Substitution mutations of the highly conserved arginine 87 of HIV-1 protease result in loss of proteolytic activity
- 1 October 1989
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 164 (1) , 30-38
- https://doi.org/10.1016/0006-291x(89)91678-1
Abstract
No abstract availableThis publication has 27 references indexed in Scilit:
- Chemical synthesis and expression of the HIV-1 protease gene in E.coliBiochemical and Biophysical Research Communications, 1989
- 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
- Genetic locus, primary structure, and chemical synthesis of human immunodeficiency virys proteaseGene Analysis Techniques, 1988
- The Human Immunodeficiency Virus: Infectivity and Mechanisms of PathogenesisScience, 1988
- A structural model for the retroviral proteasesNature, 1987
- Immunological and Chemical Analysis of P6, the Carboxyl-Terminal Fragment of HIV P15AIDS Research and Human Retroviruses, 1987
- Characterization of Highly Immunogenic p66/p51 as the Reverse Transcriptase of HTLV-III/LAVScience, 1986
- Frequent Detection and Isolation of Cytopathic Retroviruses (HTLV-III) from Patients with AIDS and at Risk for AIDSScience, 1984
- Isolation of a T-Lymphotropic Retrovirus from a Patient at Risk for Acquired Immune Deficiency Syndrome (AIDS)Science, 1983