Mutations Effects on Inhibition of HIV Protease

Tang, Jordan J.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Allergy and Infectious Diseases (NIAID)
• Type: Research Project (R01)
• Project #: 5R01AI038189-02
• Application #: 2075143
• Study Section: Special Emphasis Panel (ZRG5-ARRB (05))
• Project Start: 1995-08-01
• Project End: 1998-07-31
• Budget Start: 1996-08-01
• Budget End: 1997-07-31
• Support Year: 2
• Fiscal Year: 1996

Institution

• Name: Oklahoma Medical Research Foundation
• DUNS #: 937727907
• City: Oklahoma City
• State: OK
• Country: United States
• Zip Code: 73104

Publications

Judd, D A; Nettles, J H; Nevins, N et al. (2001) Polyoxometalate HIV-1 protease inhibitors. A new mode of protease inhibition. J Am Chem Soc 123:886-97

Hong, L; Zhang, X C; Hartsuck, J A et al. (2000) Crystal structure of an in vivo HIV-1 protease mutant in complex with saquinavir: insights into the mechanisms of drug resistance. Protein Sci 9:1898-904

Hong, L; Hartsuck, J A; Foundling, S et al. (1998) Active-site mobility in human immunodeficiency virus, type 1, protease as demonstrated by crystal structure of A28S mutant. Protein Sci 7:300-5

Ermolieff, J; Lin, X; Tang, J (1998) The effect of substrates on the kinetics and the in vivo threshold activity of mutant HIV-1 proteases. Adv Exp Med Biol 436:47-51

Hong, L; Zhang, X J; Foundling, S et al. (1997) Structure of a G48H mutant of HIV-1 protease explains how glycine-48 replacements produce mutants resistant to inhibitor drugs. FEBS Lett 420:11-6

Ermolieff, J; Lin, X; Tang, J (1997) Kinetic properties of saquinavir-resistant mutants of human immunodeficiency virus type 1 protease and their implications in drug resistance in vivo. Biochemistry 36:12364-70

Hong, L; Treharne, A; Hartsuck, J A et al. (1996) Crystal structures of complexes of a peptidic inhibitor with wild-type and two mutant HIV-1 proteases. Biochemistry 35:10627-33