Intriguing structure-activity relations underlie the potent inhibition of HIV protease by norstatine-based peptides. | J Med Chem;35(7): 1318-20, 1992 Apr 03. | MEDLINE

Main content 1 Search 2 Footer 3

+A A -A High contrast

VHL Regional Portal

Information and Knowledge for Health

Subject descriptor lookup Advanced Search EVID@Easy

Intriguing structure-activity relations underlie the potent inhibition of HIV protease by norstatine-based peptides.

Tam, T F; Carrière, J; MacDonald, D; Castelhano, A L; Pliura, D H; Dewdney, N J; Thomas, E M; Bach, C; Barnett, J; Chan, H.

Affiliation

Tam TF; Syntex Research Canada, Mississauga, Ontario.

J Med Chem ; 35(7): 1318-20, 1992 Apr 03.

Article in En | MEDLINE | ID: mdl-1560443

Subject(s)

Aminocaproates/chemistry; HIV Protease Inhibitors; HIV-1/enzymology; Peptides/pharmacology; Aminocaproates/pharmacology; Molecular Structure; Peptides/chemistry; Protein Conformation; Structure-Activity Relationship

Search on Google

Collection: 01-internacional Database: MEDLINE Main subject: Peptides / HIV-1 / HIV Protease Inhibitors / Aminocaproates Language: En Journal: J Med Chem Journal subject: QUIMICA Year: 1992 Document type: Article Country of publication: United States

Search on Google

Collection: 01-internacional Database: MEDLINE Main subject: Peptides / HIV-1 / HIV Protease Inhibitors / Aminocaproates Language: En Journal: J Med Chem Journal subject: QUIMICA Year: 1992 Document type: Article Country of publication: United States