Effect of substrate residues on the P2' preference of retroviral proteinases (Q28372993)

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P Bagossi

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T D Copeland

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S Oroszlan

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J M Louis

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J Tözsér

Three-dimensional structures of HIV-1 and SIV protease product complexes

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language of work or name

English

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publication date

September 1999

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published in

FEBS Journal

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volume

264

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issue

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page(s)

921-9

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cites work

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Structural basis for specificity of retroviral proteases

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Closing in on human immunodeficiency virus-1.

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Subsite preferences of retroviral proteinases

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Specificity of retroviral proteases: an analysis of viral and nonviral protein substrates

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Comparison of the HIV-1 and HIV-2 proteinases using oligopeptide substrates representing cleavage sites in Gag and Gag-Pol polyproteins

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Kinetic and modeling studies of S3-S3' subsites of HIV proteinases

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Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobic*hydrophobic- or -aromatic*pro- cleavage sites

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On the size of the active site in proteases. I. Papain

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Extensive polymorphisms observed in HIV-1 clade B protease gene using high-density oligonucleotide arrays.

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The p2 Peptide, AEAMSQVTNTATIM, Processed from HIV-1 Pr55 Was Found to Be a Suicide Inhibitor of HIV-1 Protease

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Crystal structure of human immunodeficiency virus (HIV) type 2 protease in complex with a reduced amide inhibitor and comparison with HIV-1 protease structures

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Crystallographic analysis of human immunodeficiency virus 1 protease with an analog of the conserved CA-p2 substrate -- interactions with frequently occurring glutamic acid residue at P2' position of substrates

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Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli

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Selective phosphinate transition-state analogue inhibitors of the protease of human immunodeficiency virus

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Moloney murine leukemia virus protease: bacterial expression and characterization of the purified enzyme.

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Studies on the substrate specificity of the proteinase of equine infectious anemia virus using oligopeptide substrates

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Human immunodeficiency virus, type 1 protease substrate specificity is limited by interactions between substrate amino acids bound in adjacent enzyme subsites

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Substrate-dependent mechanisms in the catalysis of human immunodeficiency virus protease

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X-ray crystallographic structure of a complex between a synthetic protease of human immunodeficiency virus 1 and a substrate-based hydroxyethylamine inhibitor

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Activity of linked HIV-1 proteinase dimers containing mutations in the active site region

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Structure of equine infectious anemia virus proteinase complexed with an inhibitor

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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The effect of salt on the Michaelis Menten constant of the HIV-1 protease correlates with the Hofmeister series.

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The HIV-1 protease as enzyme and substrate: mutagenesis of autolysis sites and generation of a stable mutant with retained kinetic properties.

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Predicting human immunodeficiency virus protease cleavage sites in proteins by a discriminant function method

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Natural variation in HIV-1 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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