[14]Subsite preferences of retroviral proteinases
- 1 January 1994
- book chapter
- Published by Elsevier
- Vol. 241, 254-IN12
- https://doi.org/10.1016/0076-6879(94)41068-2
Abstract
No abstract availableThis publication has 62 references indexed in Scilit:
- STRUCTURE-BASED INHIBITORS OF HIV-1 PROTEASEAnnual Review of Biochemistry, 1993
- Intrinsic activity of precursor forms of HIV‐1 proteinaseFEBS Letters, 1992
- Solid phase synthesis of the proteinase of bovine leukemia virus Comparison of its specificity to that of HIV‐2 proteinaseFEBS Letters, 1992
- Subsite specificity of the proteinase from myeloblastosis associated virusFEBS Letters, 1991
- Studies on the role of the S4 substrate binding site of HIV proteinasesFEBS Letters, 1991
- Comparison of inhibitor binding in HIV‐1 protease and in non‐viral aspartic proteases: the role of the flapFEBS Letters, 1990
- Hydrolysis of synthetic chromogenic substrates by HIV-1 and HIV-2 proteinasesBiochemical and Biophysical Research Communications, 1990
- Sub‐site preferences of the aspartic proteinase from the human immunodeficiency virus, HIV‐1FEBS Letters, 1990
- Structure of the aspartic protease from Rous sarcoma retrovirus refined at 2-.ANG. resolutionBiochemistry, 1990
- Substitutions at the P2′ site of gag p17–p24 affect cleavage efficiency by HIV-1 proteaseBiochemical and Biophysical Research Communications, 1990