A fluorometric assay for HIV-protease activity using high-performance liquid chromatography
- 1 May 1990
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 186 (2) , 363-368
- https://doi.org/10.1016/0003-2697(90)90095-q
Abstract
No abstract availableThis publication has 24 references indexed in Scilit:
- Conserved Folding in Retroviral Proteases: Crystal Structure of Synthetic HIV-1 ProteaseScience, 1989
- Peptide substrates and inhibitors of the HIV-1 proteaseBiochemical and Biophysical Research Communications, 1989
- Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1Nature, 1989
- A rapid fluorometric assay for N-terminal glutaminyl cyclase activity using high-performance liquid chromatographyAnalytical Biochemistry, 1988
- HIV-1 protease specificity of peptide cleavage is sufficient for processing of gag and pol polyproteinsBiochemical and Biophysical Research Communications, 1988
- Enzymatic activity of a synthetic 99 residue protein corresponding to the putative HIV-1 proteaseCell, 1988
- A fluorometric assay for peptidyl α-amidation activity using high-performance liquid chromatographyAnalytical Biochemistry, 1988
- Inhibition of retroviral protease activity by an aspartyl proteinase inhibitorNature, 1987
- A convenient fluorescent assay for vertebrate collagenasesAnalytical Biochemistry, 1986
- Solid Phase Peptide Synthesis. I. The Synthesis of a TetrapeptideJournal of the American Chemical Society, 1963