Sentence examples similar to terminal version from inspiring English sources

In particular, the introduction of a truncated N-terminal version of this protein resulted in baseline expression of the LevQRST targets in the presence of inducing substrates, but higher levels of expression of these genes in the presence of carbohydrates that do not normally induce expression.

The N-terminal version contains two silent point mutations at the 5′ end of the full coding sequence to render the transcript unrecognizable to Xbra3 MO2.

The C-terminal version contains the last 22 bp of the 5′ UTR in addition to the coding sequence of Xbra3 without stop codon.

For the co-purification of interaction partners with NirF, the STrEP-tagged (C-terminal) version of NirF was produced in the P. aeruginosa PAO1 strain RM301 lacking the native NirF.

In order to experimentally verify the bioinformatic prediction that NirF from P. aeruginosa is a membrane attached lipoprotein, we produced the STrEP-tagged (C-terminal) version of NirF in P. aeruginosa PAO1 RM301 lacking the native NirF as described above for the affinity co-purification experiments.

Thus we initially generated the following for both isoforms: the GFP labeled full length construct; an (aPKCΔcatalytic) construct missing the whole kinase domain including a nuclear export sequence (NES); an N-terminal version (aPKC AA1-176(177*)) including the PB1 (Phox and Bem1) and a C1 (cystein-rich) domain but excluding the hinge region.

To test this, we performed chromatin immunoprecipitation (ChIP) assays with MOVAS cells transiently transfected with a plasmid encoding a FLAG-tagged (N-terminal) version of HOXC11 (F-HOXC11); endogenous Hoxc11 expression was not detected in MOVAS cells by semi-quantitative PCR (supplementary material Fig. S3).

Similar results were obtained whenever an N-terminal or a C-terminal tagged version of the proteins was used.

The telomere capping role of POT1B was inferred from an experiment in which a C-terminal truncated version of the POT1B protein harboring only the N-terminal OB domains was expressed in wild-type plants [77].

This mode of recognition is consistent with our results that demonstrated similar trimming kinetics between a model peptide and its C-terminal extended version and very different trimming kinetics between the peptide and its N-terminal extended version (Figure 8).

It is a member of the glucagon/secretin superfamily of peptides [6, 13, 14] and is endogenously present in two isoforms namely; PACAP1 38 and the C-terminal truncated version PACAP1 27.