The virus-associated human immunodeficiency virus type 1 Gag-Pol carrying an active protease domain in the matrix region is severely defective both in autoprocessing and in trans processing of gag particles
- 1 January 2004
- Vol. 318 (2) , 534-541
- https://doi.org/10.1016/j.virol.2003.08.043
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- The Dimer Interfaces of Protease and Extra-Protease Domains Influence the Activation of Protease and the Specificity of GagPol CleavageJournal of Virology, 2003
- Coding Sequences Upstream of the Human Immunodeficiency Virus Type 1 Reverse Transcriptase Domain in Gag-Pol Are Not Essential for Incorporation of the Pr160
gag-pol
into Virus ParticlesJournal of Virology, 2002
- Gag-Pol Supplied in trans Is Efficiently Packaged and Supports Viral Function in Human Immunodeficiency Virus Type 1Journal of Virology, 2001
- Maintenance of the Gag/Gag-Pol Ratio Is Important for Human Immunodeficiency Virus Type 1 RNA Dimerization and Viral InfectivityJournal of Virology, 2001
- HIV-1 Gag Proteins: Diverse Functions in the Virus Life CycleVirology, 1998
- Extensive Regions ofpolAre Required for Efficient Human Immunodeficiency Virus Polyprotein Processing and Particle MaturationVirology, 1996
- Macromolecular interactions in the assembly of HIV and other retrovirusesSeminars in Virology, 1994
- Form, function, and use of retroviral Gag proteinsAIDS, 1991
- Cleavage of HIV-1gagPolyprotein Synthesized In Vitro: Sequential Cleavage by the Viral ProteaseAIDS Research and Human Retroviruses, 1989
- Characterization of ribosomal frameshifting in HIV-1 gag-pol expressionNature, 1988