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This novel human CKIdelta mutation may alter the physiological role and enhance the transforming ability of CKIdelta through a Wnt/beta-catenin independent mechanism and thereby influence colonic adenoma development.
This mutation may alter the folding of ENT1, thereby reducing the uptake and binding activity of the transporter.
Hence, this mutation may alter salt bridge patterns and stability in a region of the HA oligomerization interface that is important for membrane fusion.
Alternatively, the acj6-GAL4 mayalter may alter connectivity, as reported for acj6 mutation in photoreceptors and projection neurons [20], [21], [22].
However, the observed band represents only a small portion of the protein and other scenarios remain equally possible, for example, the mutation may alter a protein-protein interaction with another member of the forkhead transcription factor family, perhaps a FOXO protein, which binds to the DNA element instead of FOXL2.
Extrapolating back to FGFR4, we propose that the Glu681Lys mutation may alter the functional properties of the TK catalytic domain by reversing the charge of residue 681, potentially disrupting an ionic bond with residue Arg650, and thereby disrupting normal function of FGFR4 (Figure 5).
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Cancer results from the sequential acquisition of a number of genetic and epigenetic alterations, and these mutations may alter the expression of specific isoforms but not the others of a gene.
Several lines of evidence have indicated that CFTR mutations may alter major signaling pathways through altered expression of miRNAs (Xu et al., 2011) or by modulation of proteostasis network (Balch et al., 2011).
The etiology of DBA is not completely understood; however, the ribosomal nature of the genes involved has led to speculation that these mutations may alter the landscape of messenger RNA (mRNA) translation.
Some of these mutations may alter genes so that they code for small stretches of abnormal proteins that the immune system sees as foreign proteins, or antigens.
For example, mutations of the four positively charged residues, R1639G, R1642S, R1645Q, and R1648C, are present in the domain IV S4 segment (Table 2), suggesting that these EIEE6 mutations may alter the voltage sensing behavior of the channel.
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