Sentence examples for support splice from inspiring English sources

Based on whether the aligner support splice reads alignment, we can divide aligner into two categories: unspliced aligner and spliced aligner.

Auxiliary signals, so-called splicing regulatory elements (SREs) located near the splice sites, were discovered to support splice site recognition (Matlin et al. 2005; Pozzoli and Sironi 2005; Wang and Burge 2008).

An example appears in Figure 5, showing ESTs that support splice variants for the gene encoding rubisco activase (AGI code AT2G39730), one of the earliest characterized examples of AS in Arabidopsis [ 14].

GLEAN uses transcript alignments to support splice predictions, but does not merge or split genes based on transcript alignments, while MAKER2 creates gene models that best agree with transcript alignments, and works best with highly reliable transcript assemblies.

Curiously, the R8E mutation, but not the V6A/I7A/R8A or R8A mutations, abrogated the inhibitory effects of the N-terminus on the ability of ΔRS to support splicing of IgM M1-M2 (Figure 1C).

The phosphorylation state of the RS domain has a significant influence on SR protein function, as both hyper- and hypophosphorylated SR proteins are unable to support splicing [37], [38], [39].

As the number of constitutive substrates that can be spliced without an SR protein RS domain continues to grow, it seems increasingly improbable that SR proteins lacking their RS domains can only support splicing in contexts where recruitment functions of SR proteins are dispensable.

We had previously characterized an N-terminally His-tagged SF2/ASF lacking the RS domain as unable to complement S100 for constitutive splicing [40], but omitting this N-terminal tag allowed the same protein to support splicing of some pre-mRNAs [42].

An N-terminally His-tagged ΔRS protein was found to be unable to perform ESE-independent SR protein function(s) in this context [27]; however, we demonstrate using ΔNΔRS as the sole source of SR protein in our complementation assays that the RS domain is also not required for this additional SR protein function(s) to support splicing of IgM M1-M2.

These support splicing, clipping, multi-part and padded alignments.

Our in vivo splicing results (fig. 8) demonstrate that TIA1 and HNRNPF can equally support splicing of the same intron.