INHIBITION OF THE ASPARTIC PROTEINASE FROM HIV-2

[1] GENOME ORGANIZATION AND TRANSACTIVATION OF THE HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-2 [J]. NATURE, 1987, 326 (6114) : 662 - 669

[2] HTLV-III GAG PROTEIN IS PROCESSED IN YEAST-CELLS BY THE VIRUS POL-PROTEASE [J]. SCIENCE, 1986, 231 (4745) : 1580 - 1584

[3] LEGRICE SFJ, 1989, IN PRESS J BIOL CHEM

[4] 3-DIMENSIONAL STRUCTURE OF ASPARTYL PROTEASE FROM HUMAN IMMUNODEFICIENCY VIRUS HIV-1 [J]. NATURE, 1989, 337 (6208) : 615 - 620

[5] EFFECTIVE BLOCKING OF HIV-1 PROTEINASE ACTIVITY BY CHARACTERISTIC INHIBITORS OF ASPARTIC PROTEINASES [J]. FEBS LETTERS, 1989, 247 (01) : 113 - 117

[6] MOLECULAR MODELING OF THE HIV-1 PROTEASE AND ITS SUBSTRATE BINDING-SITE [J]. SCIENCE, 1989, 243 (4893) : 928 - 931

[1] GENOME ORGANIZATION AND TRANSACTIVATION OF THE HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-2 [J]. NATURE, 1987, 326 (6114) : 662 - 669

[2] HTLV-III GAG PROTEIN IS PROCESSED IN YEAST-CELLS BY THE VIRUS POL-PROTEASE [J]. SCIENCE, 1986, 231 (4745) : 1580 - 1584

[3] LEGRICE SFJ, 1989, IN PRESS J BIOL CHEM

[4] 3-DIMENSIONAL STRUCTURE OF ASPARTYL PROTEASE FROM HUMAN IMMUNODEFICIENCY VIRUS HIV-1 [J]. NATURE, 1989, 337 (6208) : 615 - 620

[5] EFFECTIVE BLOCKING OF HIV-1 PROTEINASE ACTIVITY BY CHARACTERISTIC INHIBITORS OF ASPARTIC PROTEINASES [J]. FEBS LETTERS, 1989, 247 (01) : 113 - 117

[6] MOLECULAR MODELING OF THE HIV-1 PROTEASE AND ITS SUBSTRATE BINDING-SITE [J]. SCIENCE, 1989, 243 (4893) : 928 - 931