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Human immunodeficiency virus type 1 (HIV-1) protease (PR) permits viral maturation by processing the gag and gag-pro-pol polyproteins.
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This enzyme performs an essential role in viral maturation by processing specific cleavage sites in the Gag and Gag-Pol precursor polyproteins so as to release their mature forms.
Before having the ability to infect another cell, the virion undergoes a morphological change known as maturation that includes proteolytic processing of the Gag and Gag-Pol polyproteins by viral enzyme PR and a less well defined function of Vif [ 8].
Therefore, increased viral protease-mediated processing of the Gag polyproteins from CIITA-expressing cells may be due to an increase in overall viral protease levels, due to increased Gag-Pol synthesis.
This study examines the effect of drug resistant mutations on HIV-1 protease, which is involved in the processing of the Gag and Gag-Pol viral polyproteins.
GAG chemical exchange saturation transfer (gagCEST) measures GAG concentrations by using the GAG molecules as endogenous contrast agents [ 25– 28].
Following budding, HIV maturation is initiated by proteolytic processing of Gag, which induces conformational changes in the CA domain and results in the assembly of the distinctive conical capsid.
The annealing of tRNALys3 to 5′-terminal sequences of viral RNA is multi-staged, with an initial poor quality, cytoplasmic annealing promoted by the Gag precursor protein, followed by a more effective annealing imposed upon the Gag-annealed tRNALys3 that occurs after viral protein processing, and that is facilitated by mature nucleocapsid (NCp7).
She was still troubled by the gag order, however.
Protease (PR) is a dimer of identical subunits, and is involved in the processing of Gag and GagPol during the process of maturation.
Next we demonstrated that CIITA increased Gag processing through the viral protease and evaluated whether this enhancement was a consequence of CIITA-mediated transcriptional activation.
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