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By increasing the rate of macrophage cell death, an infection with the hypercytotoxic mutants may induce a proinflammatory response and as a result, diminish the virulence of the strain.
Overexpression of wild-type or activated SRC mutants may induce phosphorylation of this broader subset of targets distinct from the substrates of endogenous c-SRC activated by an upstream growth factor receptor.
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The H1047R (exon 20) mutation may induce an allosteric change that mimics Ras-GTP binding, making this mutant independent of interaction with Ras-GTP [ 5].
In many cases an increase in ethanol production rate is also accompanied by an increase in glycerol formation [ 50] but in this case the evolved tolerant mutant may have induced an inherent higher glycerol production rate as a general stress response.
Blocking one type of endocytosis may up-regulate alternative mechanisms, over-expression of mutant proteins may induce non-physiological cellular responses, and small GTPases may, via different sets of effectors, directly or indirectly control the activity of multiple endocytic pathways.
One possible explanation is that the chronic loss of NE in dbh mutant mice may induce compensatory mechanisms during development that do not occur in response to chronic loss of NE in zebrafish.
Alternatively, PIK3CA mutations might only moderately activate the pathway and/or constitutive activity of mutant PIK3CA may induce negative feedback loops that preclude a more pronounced activation of the pathway [ 14].
As the inhibition for those tumor-associated mutant IDH proteins may induce differentiation of those cancer cells, these tumor-associated mutant IDH proteins can be treated as a drug target proteins for a differentiation therapy against cancers.
The inhibition for those tumor-associated mutant IDH proteins may induce differentiation of those cancer cells.
PP1-binding deficient mutants may strongly induce cell retraction although they retain the cell spreading activity.
This appears very likely as mycobactin and carboxymycobactin follow the same synthetic pathway and the higher cytosolic levels of carboxymycobactin, due to the inability of irtAB mutant to secrete it out, may induce mycobactin production to a higher rate.
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