Human immunodeficiency virus type 1 Vif binds the viral protease by interaction with its N-terminal region (original) (raw)
Abrogation of Vif function by peptide derived from the N-terminal region of the human immunodeficiency virus type 1 (HIV-1) protease
marina hutoran
Virology, 2004
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Human immunodeficiency virus type 1 Vif-derived peptides inhibit the viral protease and arrest virus production
Nissim Chen
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Peptides derived from HIV-1 vif: a non-substrate based novel type of HIV-1 protease inhibitors 1 1 Edited by J. Karn
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J Mol Biol, 1999
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Charles Craik
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Journal of Virology, 2001
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Journal of Molecular Structure: THEOCHEM, 1998
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Replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral protease
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Initial Cleavage of the Human Immunodeficiency Virus Type 1 GagPol Precursor by Its Activated Protease Occurs by an Intramolecular Mechanism
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The role of lysine residue at amino acid position 165 of human immunodeficiency virus type 1 CRF01_AE Gag in reducing viral drug susceptibility to protease inhibitors
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Virological Importance of the Protease-Cleavage Site in Human Immunodeficiency Virus Type 1 Nef Is Independent of both Intravirion Processing and CD4 Down-regulation
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