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Thus, the cellular proteins identified in VLPs without viral genomes are important in the normal virus life cycle during virus assembly and budding from the host cells.
Enveloped viruses acquire their envelope by budding from the host cell.
The cellular proteins identified in our VLPs might be actively involved in the normal virus life cycle, especially during virus assembly and budding from the host cells.
This complex is surrounded by a matrix consisting of VP40 and VP24, which is packaged by a lipid membrane envelope obtained during budding from the host cell.
The Gag protein is cleaved by viral protease into P17, P24, P7, and P6 proteins shortly after budding from the host cell [ 1].
M protein connects the VSV nucleoprotein capsule and cellular plasma membrane in the assembly of viral particles [40], [42], [45] and plays a role in the release of the viral particles by budding from the host cells [45].
Similar(54)
In addition, when newly formed virus particles bud from the host cell membrane after virus replication, the NA present on the virus membrane facilitates the release of particles.
The Gag (p55) and Gag-Pol (p160) polyproteins also associate with the inner surface of the plasma membrane along with the HIV genomic RNA as the forming virion begins to bud from the host cell.
While neuraminidase cleaves N-acetylneuramic acid from ascent viral glycoproteins on host cell membrane and facilitates viral budding from the infected host cells [ 105].
Infectious and non-infectious influenza virions are released by budding from the apical surface of their host cells, which is preceded by viral genome replication and intracellular virus protein accumulation.
In budding yeast, Sec14 is essential for vesicle budding from the Golgi apparatus.
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