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 (original) (raw)

Processing sites in the human immunodeficiency virus type 1 (HIV1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates

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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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The virus-associated human immunodeficiency virus type 1 Gag-Pol carrying an active protease domain in the matrix region is severely defective both in autoprocessing and in trans processing of gag particles

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Comparison of Human Immunodeficiency Virus Type 1 Pr55 Gag and Pr160 Gag-Pol Processing Intermediates That Accumulate in Primary and Transformed Cells Treated with Peptidic and Nonpeptidic Protease Inhibitors

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Natural Variation in HIV1 Protease, Gag p7 and p6, and Protease Cleavage Sites within Gag/Pol Polyproteins: Amino Acid Substitutions in the Absence of Protease Inhibitors in Mothers and Children Infected by Human Immunodeficiency Virus Type 1

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Effect of sequence polymorphism and drug resistance on two HIV-1 Gag processing sites

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Drug-associated changes in amino acid residues in Gag p2, p7 NC, and p6 Gag/p6 Pol in human immunodeficiency virus type 1 (HIV1) display a dominant effect on replicative fitness and drug response

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Local and spatial factors determining HIV-1 protease substrate recognition

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