Literature DB >> 3052448

HIV-1 protease specificity of peptide cleavage is sufficient for processing of gag and pol polyproteins.

P L Darke1, R F Nutt, S F Brady, V M Garsky, T M Ciccarone, C T Leu, P K Lumma, R M Freidinger, D F Veber, I S Sigal.   

Abstract

The mature proteins of retroviruses originate as a result of proteolytic cleavages of polyprotein precursors. Retroviruses encode proteases responsible for several of these processing events, making them potential antiviral drug targets. A 99-amino acid HIV-1 protease, produced by chemical synthesis or by expression in bacteria, is shown here to hydrolyze peptides corresponding to all of the known cleavage sites in the HIV-1 gag and pol polyproteins. It does not hydrolyze peptides corresponding to an env cleavage site or a distantly related retroviral gag cleavage site.

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Year:  1988        PMID： 3052448     DOI： 10.1016/s0006-291x(88)80839-8

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  46 in total

1.  Human immunodeficiency virus type 1 protease cleavage site mutations associated with protease inhibitor cross-resistance selected by indinavir, ritonavir, and/or saquinavir.

Authors:  H C Côté; Z L Brumme; P R Harrigan
Journal:  J Virol       Date:  2001-01       Impact factor: 5.103

2.  Altered substrate specificity of drug-resistant human immunodeficiency virus type 1 protease.

Authors:  Deborah S Dauber; Rainer Ziermann; Neil Parkin; Dustin J Maly; Sami Mahrus; Jennifer L Harris; Jon A Ellman; Christos Petropoulos; Charles S Craik
Journal:  J Virol       Date:  2002-02       Impact factor: 5.103

3.  Local and spatial factors determining HIV-1 protease substrate recognition.

Authors:  S Hazebrouck; V Machtelinckx-Delmas; J J Kupiec; P Sonigo
Journal:  Biochem J       Date:  2001-09-01       Impact factor: 3.857

4.  Binding of human immunodeficiency virus type 1 (HIV-1) RNA to recombinant HIV-1 gag polyprotein.

Authors:  J Luban; S P Goff
Journal:  J Virol       Date:  1991-06       Impact factor: 5.103

5.  Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.

Authors:  Yunfeng Tie; Peter I Boross; Yuan-Fang Wang; Laquasha Gaddis; Fengling Liu; Xianfeng Chen; Jozsef Tozser; Robert W Harrison; Irene T Weber
Journal:  FEBS J       Date:  2005-10       Impact factor: 5.542

6.  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.

Authors:  Steve C Pettit; Gavin J Henderson; Celia A Schiffer; Ronald Swanstrom
Journal:  J Virol       Date:  2002-10       Impact factor: 5.103

7.  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

8.  Effect of linker insertion mutations in the human immunodeficiency virus type 1 gag gene on activation of viral protease expressed in bacteria.

Authors:  J Luban; C Lee; S P Goff
Journal:  J Virol       Date:  1993-06       Impact factor: 5.103

9.  Development of activity assays for high-volume evaluation of human immunodeficiency virus (HIV) protease inhibitors in rat serum: results with ditekiren.

Authors:  K F Wilkinson; B D Rush; S K Sharma; D B Evans; M J Ruwart; J M Friis; M J Bohanon; P K Tomich
Journal:  Pharm Res       Date:  1993-04       Impact factor: 4.200

10.  Sensitive, hydrosoluble, macromolecular fluorogenic substrates for human immunodeficiency virus 1 proteinase.

Authors:  F Anjuère; M Monsigny; Y Lelièvre; R Mayer
Journal:  Biochem J       Date:  1993-05-01       Impact factor: 3.857
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