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The two most promising Affibody variants were shown to selectively and efficiently bind to Aβ peptides, but not to the control proteins.
All four variants were shown to be monomeric, as judged by analytical ultracentrifugation, and highly helical as measured by far-UV CD.
The sites location and nucleotide substitution patterns of all the alternative splicing and RNA-editing variants were shown in Table 1.
For instance, SLCO1B1 variants block the uptake of flavonoids present in grapefruit juice and statins and missense variants were shown to be associated with simvastatin-induced myopathy [61, 62].
Certain CD44 variants were shown to be causally involved in metastasis formation [18].
The UTI prone children expressed less CXCR1 protein than the pediatric controls (p<0.0001) and two sequence variants were shown to impair transcription.
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The novel variants are shown in Table 1.
Reported genes that harbored somatic variants are shown (c).
Only SNPs associated with significant differences (p < 0.05 using the Mann-Whitney U-test) in the adhesion or invasion abilities of variants are shown.
Similarities between product variants are shown on each level by multidimensional scaling, which allows a simple visual evaluation.
Effects of several buffers on protein solubility and solubility curves of different insulin variants are shown as examples of relevant screening parameters.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com