Literature DB >> 2651157

Effective blocking of HIV-1 proteinase activity by characteristic inhibitors of aspartic proteinases.

A D Richards1, R Roberts, B M Dunn, M C Graves, J Kay.   

Abstract

Inhibitory constants (Ki) between 5 and 35 nM were derived (under different conditions of pH and ionic strength) for the interaction of HIV-1 proteinase with acetyl-pepstatin and H-261, two characteristic inhibitors of aspartic proteinases. Thus this enzyme, essential for replication of the AIDS virus, may be classified unequivocally as belonging to this proteinase family.

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Year:  1989        PMID： 2651157     DOI： 10.1016/0014-5793(89)81251-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  19 in total

1.  The selectivity of statine-based inhibitors against various human aspartic proteinases.

Authors:  R A Jupp; B M Dunn; J W Jacobs; G Vlasuk; K E Arcuri; D F Veber; D S Perlow; L S Payne; J Boger; S de Laszlo
Journal:  Biochem J       Date:  1990-02-01       Impact factor: 3.857

Review 2.  Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes.

Authors:  W G Dougherty; B L Semler
Journal:  Microbiol Rev       Date:  1993-12

3.  Solvent accessibility as a predictive tool for the free energy of inhibitor binding to the HIV-1 protease.

Authors:  V Nauchitel; M C Villaverde; F Sussman
Journal:  Protein Sci       Date:  1995-07       Impact factor: 6.725

Review 4.  Resistance to human immunodeficiency virus type 1 protease inhibitors.

Authors:  D Boden; M Markowitz
Journal:  Antimicrob Agents Chemother       Date:  1998-11       Impact factor: 5.191

5.  Mutational analysis of a native substrate of the human immunodeficiency virus type 1 proteinase.

Authors:  K Partin; H G Kräusslich; L Ehrlich; E Wimmer; C Carter
Journal:  J Virol       Date:  1990-08       Impact factor: 5.103

6.  Context surrounding processing sites is crucial in determining cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol polyprotein precursors by viral protease.

Authors:  Sook-Kyung Lee; Marc Potempa; Madhavi Kolli; Ayşegül Özen; Celia A Schiffer; Ronald Swanstrom
Journal:  J Biol Chem       Date:  2012-02-13       Impact factor: 5.157

7.  Inhibition of XMRV and HIV-1 proteases by pepstatin A and acetyl-pepstatin.

Authors:  Krisztina Matúz; János Mótyán; Mi Li; Alexander Wlodawer; József Tőzsér
Journal:  FEBS J       Date:  2012-08-17       Impact factor: 5.542

Review 8.  Positive and negative aspects of the human immunodeficiency virus protease: development of inhibitors versus its role in AIDS pathogenesis.

Authors:  K Ikuta; S Suzuki; H Horikoshi; T Mukai; R B Luftig
Journal:  Microbiol Mol Biol Rev       Date:  2000-12       Impact factor: 11.056

9.  The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions.

Authors:  S C Pettit; M D Moody; R S Wehbie; A H Kaplan; P V Nantermet; C A Klein; R Swanstrom
Journal:  J Virol       Date:  1994-12       Impact factor: 5.103

10.  Preparation and preliminary characterization of poly(ethylene glycol)-pepstatin conjugate.

Authors:  J Brygier; J Vincentelli; M Nijs; C Guermant; C Paul; D Baeyens-Volant; Y Looze
Journal:  Appl Biochem Biotechnol       Date:  1994-04       Impact factor: 2.926
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