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All 20 P. falciparum paralogs possess a canonical Plasmodium export element downstream of a signal / anchor sequence required for exportation outside the parasitophorous vacuole.
All functional studies of the HT motif or closely related, but distinct, Plasmodium export element (PEXEL) have been done in P. falciparum.
In two elegant studies, Hiller et al. [2] and Marti et al. [3] identified a short peptide sequence, referred to as the vacuolar transport signal (VTS) or Plasmodium export element (PEXEL), respectively.
Swanson et al [12] recently demonstrated that altering the RNA nuclear export element used by HIV-1 gag-pol mRNA from the RRE to the CTE resulted in efficient trafficking and assembly of Gag at cellular membranes in murine cells, which are notable for their inability to support HIV-1 assembly and budding [12], [15], [16].
These proteins are called exported proteins; and a large number of such proteins have been predicted for Plasmodium falciparum based on the presence of an N-terminal motif known as the Plasmodium export element (PEXEL) or vacuolar transport signal (VTS), which has been shown to mediate export.
Interestingly, we found no Pf-aaRS sequences with specific PEXEL (Plasmodium export element) motifs.
Similar(43)
Here, we demonstrated that efficient expression of S from the wild-type spike gene in cultured cells required the use of improved plasmid vectors containing donor and acceptor splice sites, as well as heterologous viral RNA export elements, such as the CTE of Mazon-Pfizer monkey virus or the PRE of Woodchuck hepatitis virus (WPRE).
As examples, Rius identified two provisions that she said would "export" elements of U.S. laws protecting drug companies from competition.
We performed a bioinformatical analysis of protein export elements (PEXEL) in the putative proteome of the malaria parasite Plasmodium falciparum.
It was previously demonstrated that perturbation of the RNA export elements of avian leucosis virus is associated with budding and genome packaging [34].
Identification of export elements mediating transport of PfEMP1 to the surface of P. berghei-infected erythrocytes may allow studies on PfEMP1-associated virulence in mice.
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