Structural and kinetic analysis of drug resistant mutants of HIV-1 protease (Q27619254)

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J M Louis

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C C Reed

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J M Adomat

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J Krouse

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Y F Wang

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R W Harrison

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I T Weber

Structural basis for specificity of retroviral proteases

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language of work or name

English

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publication date

July 1999

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published in

FEBS Journal

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volume

263

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issue

1

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page(s)

238-45

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cites work

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Molecular basis of HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with cyclic urea inhibitors

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The HIV-1 protease as a therapeutic target for AIDS

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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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The p2gag peptide, AEAMSQVTNTATIM, processed from HIV-1 Pr55gag was found to be a suicide inhibitor of HIV-1 protease

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Multiple concurrent reverse transcriptase and protease mutations and multidrug resistance of HIV-1 isolates from heavily treated patients

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Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure

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Human immunodeficiency virus. Mutations in the viral protease that confer resistance to saquinavir increase the dissociation rate constant of the protease-saquinavir complex

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Influence of flanking sequences on the dimer stability of human immunodeficiency virus type 1 protease

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Inhibition of porcine pepsin by two substrate analogues containing statine. The effect of histidine at the P2 subsite on the inhibition of aspartic proteinases.

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Structural basis of drug resistance for the V82A mutant of HIV-1 proteinase

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Role of arginine 67 in the stabilization of chymotrypsin inhibitor 2: examination of amide proton exchange rates and denaturation thermodynamics of an engineered protein

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Complete mutagenesis of the HIV-1 protease

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