Assay ID | Title | Year | Journal | Article |
AID1795283 | Protease Inhibition Assay from Article 10.1021/jm00041a005: \\Crystal-structure-based design and synthesis of novel C-terminal inhibitors of HIV protease.\\ | 1994 | Journal of medicinal chemistry, Jul-22, Volume: 37, Issue:15
| Crystal-structure-based design and synthesis of novel C-terminal inhibitors of HIV protease. |
AID160777 | Binding affinity to HIV-1 protease | 1994 | Journal of medicinal chemistry, Jun-10, Volume: 37, Issue:12
| Three-dimensional pharmacophores from binding data. |
AID239453 | Binding affinity towards human immunodeficiency virus type 1 protease determined using continuum electrostatics solvation | 2004 | Journal of medicinal chemistry, Nov-04, Volume: 47, Issue:23
| Efficient evaluation of binding free energy using continuum electrostatics solvation. |
AID1811 | Experimentally measured binding affinity data derived from PDB | 1993 | Biochemistry, Dec-07, Volume: 32, Issue:48
| Three-dimensional structure of a simian immunodeficiency virus protease/inhibitor complex. Implications for the design of human immunodeficiency virus type 1 and 2 protease inhibitors. |
AID977610 | Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB | 1993 | Biochemistry, Dec-07, Volume: 32, Issue:48
| Three-dimensional structure of a simian immunodeficiency virus protease/inhibitor complex. Implications for the design of human immunodeficiency virus type 1 and 2 protease inhibitors. |
AID977610 | Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB | 1992 | The Journal of biological chemistry, Nov-15, Volume: 267, Issue:32
| The crystal structures at 2.2-A resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations. |
AID1811 | Experimentally measured binding affinity data derived from PDB | 1992 | The Journal of biological chemistry, Nov-15, Volume: 267, Issue:32
| The crystal structures at 2.2-A resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations. |
AID1811 | Experimentally measured binding affinity data derived from PDB | 1992 | Biochemistry, Jul-28, Volume: 31, Issue:29
| Hydroxyethylene isostere inhibitors of human immunodeficiency virus-1 protease: structure-activity analysis using enzyme kinetics, X-ray crystallography, and infected T-cell assays. |
AID977610 | Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB | 1992 | Biochemistry, Jul-28, Volume: 31, Issue:29
| Hydroxyethylene isostere inhibitors of human immunodeficiency virus-1 protease: structure-activity analysis using enzyme kinetics, X-ray crystallography, and infected T-cell assays. |
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023] |