Sentence examples for supported wild type from inspiring English sources

Exact(1)

In general, sensitivity of sgn3 to growth conditions is such that we observed everything from a near absence of phenotypes to severely dwarfed plants that did not reproduce when grown in different, standard growth chambers that all well supported wild type growth.

Similar(59)

Strains containing SpoIIIE-GFP-SsrA* without SspBEc or expressing SspBEc with untagged-SpoIIIE supported wild-type sporulation, chromosome translocation and membrane fission (Supplemental data).

Since the wrky25-1 and wrky25-2 mutantsupporteded wild-type levels of bacterial growth, PR1 expression and SA accumulation, it is possible that WRKY25 exerts its negative effect(s) primarily by promoting disease symptom development.

Substitutions of Glu1.35 by Asp, Gln or Arg were incapable of supporting wild-type OTR agonist binding or signaling.

viciae supports wild-type rates of nitrogen fixation.

Remarkably, a version of the Atf1 protein that is not detectably phosphorylated [40] supports wild-type levels of hotspot recombination under conditions where Atf1 is rate limiting (Figure 3).

However, KHC1-910 does not support wild-type localization of oskar or wild-type streaming.

The MalF-TM-SpoIIE chimera does not support wild-type sporulation efficiency and we have added these data to the table in Figure 4 source data 1.

The best model to fit all of the data is that these charge swap mutants support wild-type levels of Cdc13p– Est1p interaction, but the resulting complex is somehow defective in vivo such that it is unable to support wild-type levels of telomerase telomere interaction or telomerase extension.

The fact that FBM neurons lacking scrib and vangl2 failed to migrate in a pk1b morphant host, which has the environmental cues to support wild-type FBM neuron migration, reveals an essential cell-autonomous requirement for these core PCP components in addition to their function in the polarized environment.

We have found that a fusion of the cellular protein, high-mobility group A (HMGA) 1a, to EBNA1's DNA-binding and dimerization domain, which deletes EBNA1's binding site for EBP2 (Altmann et al, 2006), or a second derivative of EBNA1 that cannot bind EBP2, 2XLR1 (Mackey and Sugden, 1999; Shire et al, 1999), supports wild-type levels of plasmid synthesis and partitioning (Supplementary Figure 5).

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