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Exact(28)
We show that, for the constructed EGFP variants, the C2 mutation is sufficient to facilitate the production of fluorescence in both bacterial and mammalian cells.
Using model constructs in which an isolated δ-helix is engineered into a bona fide membrane protein, we find that, for two δ-helices originating from secreted proteins, at least three single-nucleotide mutations are necessary to obtain efficient membrane insertion, whereas one mutation is sufficient in a δ-helix from the cytosolic protein P450BM-3.
The presence of c.2746delCA mutation is sufficient to introduce the alternative splicing process because for individuals alone with the c.2749+51A>G mutation alternatively spliced cDNA could not be shown.
We have assumed the shortest genetic distance possible between wildtype and fully drug resistant mutants (one mutation is sufficient to create full resistance against a single drug, three distinct mutations are required for full resistance against a triple-drug combination).
We have shown previously that a nemR mutation is sufficient to suppress the absence of RutE [3] and hence that the nemR and nemR promoter mutations present in strains NCM4299 and 4300, respectively, are sufficient to account for their phenotypes.
This is also the case for NUMT30 (that fully overlaps ARS1635) whose partial deletion or mutation is sufficient to reduce the efficiency of replication to the levels of empty vectors.
Similar(31)
However, the aliphatic-to-aspartic mutation was sufficient to make V5-MKK4cr_46 and both of the V5-MKK7cr mutants resistant to cleavage (Figure 2E and F).
The latter mutation was sufficient to double YFP expression by itself.
The assumption that a single point mutation was sufficient for the parasite to become resistant to the treatment may raise some concerns.
Together, these results are consistent with the observation that the addition of the Y197C mutation was sufficient to restore activity when combined with the V266H mutation because the double mutant more closely resembles the wild-type protein.
However, one distinction from our in vitro results is that the R28D mutation was sufficient to block leading-edge localization in vivo, whereas the 2×KE mutant Coro1C still retained leading edge localization.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com