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The TM4 G153R mutation perturbs the closing of the outward metal-permeation pathway and alters the selectivity of the conserved metal-binding site.
Functional testing of this allele in vivo and in vitro showed that the mutation perturbs the relative dosage of two PUF60 isoforms and, subsequently, the splicing efficiency of downstream PUF60 targets.
As demonstrated by small-angle x-ray scattering comparative analysis of wild-type and mutant forms, the F241L mutation perturbs the oligomerization state and the global architecture of Lg-ECD.
In this study, we demonstrated that heterozygous dOpa1 mutation perturbs the visual function and an ERG profile of the Drosophila compound eye.
This provides further evidence that the T183A mutation perturbs the glycosylation at the second site.
This single amino acid mutation perturbs the folding and tertiary structure of AAT, leading to spontaneous polymerization and cellular retention.
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The D2-K317R mutation perturbed the bands in the regions of the COO– stretching and backbone amide vibrations in the FTIR difference spectrum upon the S1 → S2 transition.
Thus it seems that the S129R mutation perturbed the dimer interface of βB1-crystallin and led to a shift to the monomeric state in the dimer-monomer equilibrium.
Tested singly in a yeast two-hybrid test, each mutation perturbed the interaction of Vac14p with Vac7p and Atg18p, without disrupting interaction with its other binding partners (not shown).
To test whether this mutation perturbed the interaction with STIL, we purified WT and various other mutant forms of D. rerio CPAP937 1124 in which we valine substituted residues that our crystal structure suggested to be important for binding.
Finally, we could identify 40 cancer mutations in addition to the PKD1 D665N mutation perturbing the αD1 site, eight of which containing the same amino acid substitution D to N (PKCb D427N, TSSK1 D97N, TTBK1 D116N, CDK11b D507N, CDK8 D103N, PFTAIRE1 D198N, PDGFRa D681N, and STYK1 D201N) and thereby constituting high-confidence downstream rewiring mutants.
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