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To determine whether BVFP, when bound to PGRN, disrupts full-length PGRN and SORT1 binding, we devised a SORT1-dependent rprecipitationassay assay utilizing the Meso-Scale DiSupplementary systeMaterialementary Material, Fig. S4A and B).
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Combining these mutant Kv7.2 CaM binding domains, we devised an assay to follow the adoption of the trans-binding mode in vitro, which involves monitoring D-CaM fluorescence while sequentially adding the mutant proteins.
To quantitatively substantiate that MeCP2 binding tracks with DNA methylation at exons, we devised a sensitive rank-based test to determine the overlap between MeCP2 binding and DNA methylation.
With these requirements in mind, we devised a new protein binding ligand called a synthetic antibody or synbody that is composed of two peptides linked by a scaffold to create a high-affinity binding agent (Figure 1B).
In this study, we devised a bifunctional ligand of E6 that simultaneously targets its LxxLL binding pocket and its PDZ-binding motif.
To measure in vivo the relative transcriptional activation potential of activated Stat92E GFP at these sites, we devised a luciferase reporter plasmid containing either four 3 n- or 4 n-binding sites (Fig 3D; Methods).
To change that, we devised a little experiment.
Employing global protein expression profiling by quantitative proteomics, we devised a strategy to identify the degradation substrates of ubiquitin ligases and using this strategy, identified the Myb-binding protein p160 as a novel substrate of VHL.
We devised a permutation test to evaluate this possibility.
In this study, we devised a two-stage mapping protocol.
13 We devised a positively worded two-item version.
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