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Further experiments revealed that while these antibodies preferentially bind to mono and unglycosylated PrP, they also bind to diglycosylated molecules with reduced binding strength (e.g. in Supplementary Figure S4A).
These experiments revealed that while both wild-type and mutated proteins were expressed at equivalent levels in transfected cells, there was a significant reduction in the surface expression of the mutated protein.
Their experiments revealed that while the first 26 N-terminal residues of histone H3 were greatly sensitive to trypsin digestion, H3K36 was resistant to the enzyme (Bohm et al., 1981).
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Results of experiments reveal that while the error rate of the RF classifier is relatively insensitive to mislabelled training data (in the multiclass experiment, overall 78.3% Kappa with no mislabelled instances to 70.1% with 25% mislabelling in each class), the level of associated confidence falls at a faster rate than overall accuracy with increasing amounts of mislabelled training data.
The experiments reveal that while OSNs respond to an increasing odor concentration by signaling its rate of change, they stop firing in response to decreasing odor concentrations.
In support of this hypothesis, EGS crosslinking experiments reveal that while wild-type HSF1 exists predominantly in the monomeric form, the active HSF1 mutants identified were all enriched in the trimer form.
However, individual-male mating and laboratory-swarm experiments revealed that hybrid males, while inseminating fewer females than older inbred males, were significantly more fertile, producing larger mating plugs and drastically increasing female fecundity.
No other isomer was detected, while spiking experiments revealed that their detection sensitivity was comparable or even better than for 4,4ʹ-BPF.
While control experiments revealed that as much as 30% of Y could be reduced in the crude cell extract if left for ∼3 h at 4 °C, loading onto the affinity column within 30 min at 4 °C minimized this loss.
In vivo experiments using S. enterica strains carrying wild-type PhilD or the mutant variant PhilD* showed that Fur activates hilD expression, while in vitro experiments revealed that the Fur·Mn2+ protein is sufficient to increase hilD transcription.
PCR experiments revealed that four of the five encoded shrimp genes while the fifth was likely to be a TSV gene.
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