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Characterisation of mutated proteinases derived from HIV-positive patients: enzime activity, vitality and inhibition

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    0100873 - UOCHB-X 20043061 RIV CZ eng J - Journal Article
    Kožíšek, Milan - Prejdová, Jana - Souček, Milan - Machala, L. - Staňková, M. - Linka, M. - Brůčková, M. - Konvalinka, Jan
    Characterisation of mutated proteinases derived from HIV-positive patients: enzime activity, vitality and inhibition.
    [Charakterisace mutantních proteas odvozených z HIV-positivních pacientů: enzymová aktivita, vitalita a inhibice.]
    Collection of Czechoslovak Chemical Communications. Roč. 69, č. 3 (2004), s. 703-714. ISSN 0010-0765
    R&D Projects: GA MZd NI6339
    Grant - others:5th Framework(XE) QLK2-CT-2001-02360
    Institutional research plan: CEZ:AV0Z4055905
    Keywords : enzyme inhibitors * HIV protease * enzyme kinetics
    Subject RIV: CE - Biochemistry
    Impact factor: 1.062, year: 2004

    In this paper we describe kinetic characterisation of two highly resistant proteases isolated from HIV-positive patients undergoing higly active antiretroviral therapy including protease inhibitors. Kinetic analysis revealed that second-generation PI lopinavir and pseudopeptide inhibitor QF34 retained their subnanomolar potency against both multidrug resistant PR variants

    V této publikaci popisujeme kinetickou charakterisaci dvou vysoce resistentních proteas isolovaných z HIV-positivních pacientů procházejících vysoce aktivní antiretrovirovou terapií zahrnující proteasové inhibitory. Kinetická analysa prokázala, že lopinavir, inhibitor proteasy druhé generace, a pseudopeptidový inhibitor QF34, si udržují svou subnanomolární aktivitu proti vysoce resistentním variantám proteasy
    Permanent Link: http://hdl.handle.net/11104/0008357

     
     

Number of the records: 1  

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