Sentence examples for export domains from inspiring English sources

Functional validation of common putative export domains of malaria parasites in P. berghei provides an alternative and simpler system compared to P. falciparum to investigate export mechanisms.

Functional validation of common putative export domains of malaria parasites in P. berghei provides an alternative and simpler system to investigate export mechanisms.

To determine if export pathways are conserved in plasmodia and to develop an experimental system for studying these processes, we investigated export of GFP fused with N- and C-terminus putative export domains in the rodent malaria parasite P. berghei.

The first step (the formation of the tubular export domains) also includes the segregation of the cargo proteins from the Golgi resident enzymes.

These export domains usually contain TGN markers; i.e. they are part of the TGN (Polishchuk et al. 2003; Puertollano et al. 2003).

These experiments, as those in previous figures, were done with isoform NFAT5a, which has a nuclear localization sequence (NLS) and an auxiliary export domain (AED), but lacks the nuclear export signal (NES) exclusive of the longer isoform NFAT5c [20].

However, since one consequence of the retention of NFAT5 mutants in mitotic chromatin was that they were localized in the nucleus in the next interphase, we used the alternative approach of testing whether a constitutively nuclear NFAT5a (export domain mutant FL5AED, Figure 6A) had greater basal transcriptional activity than wild-type NFAT5 in isotonic conditions.

Furthermore, we identify the C-terminal domain of the FMRP as a nuclear export domain, perhaps explaining why naturally occurring nuclear isoforms of FMRP are generated by alternative splicing in the C-terminus.

As indicated above, this process comprises the formation, the extrusion and the fission of the export domain from the TGN, thus generating the free carrier (Polishchuk et al. 2003; see also Fig.  1).

For example, ScyD, ScyE, and ScyF, none of which had been assigned a protein function by annotation, each contain a signal peptide export domain in their derived protein sequence.

While the protein sequence of NpR1268 does not have an N-terminal export domain, the fact that it resembles dsbA, a dithiol-disulfide isomerase (oxidoreductase) that facilitates the formation of disulfide bridges in the folding of periplasmic proteins [ 19], suggests that it may also localize to the periplasm.