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Here, the potential glycosphingolipid receptors of enterotoxigenic F6-fimbriated E. coli were examined by binding of purified F6 fimbriae, and F6-expressing bacteria, to glycosphingolipids on thin-layer chromatograms.
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We used β2GPI purified from human plasma available from Haematologic Technologies, Inc. and analyzed the binding and inhibition of the binding of purified β2GPI by A1-A1 A1d A1 in the presence and in the absence of anti-β2GPI antibodies.
Our results demonstrated that the binding of purified GST-CTCF-ZFs to the biotin-labeled M1 oligo was competed by an excess amount of the unlabeled M1 oligo (Fig. 1C, lane 4).
The binding of purified His-tagged OxyR protein to the upstream region of the respective genes was verified in vitro by DNA band shift assays.
We found that Cdk1 strongly enhances the binding of purified Eg5 to microtubules.
Membrane binding of purified proteins showed that Endo-K8 had similar binding to Endo-WT.
Analytical gel filtration chromatography was employed for in vitro analysis of binding of purified FusB mutant proteins to EF-G, and eluted samples were analyzed by SDS-PAGE (11).
These data illustrate that the strong binding of purified C1q to dying cells shown in Figure 1e has no effect on their elimination by monocytes.
Transcription factor (TF) binding motifs in eukaryotes have been identified by examining binding sequences of purified TFs (e.g. SELEX and Protein Binding Microarrays) and by carrying out chromatin immunoprecipitation coupled with massively parallel sequencing (ChIP-seq) and microarray (ChIP-chip).
The binding activity of purified MBP-CCR3 was verified by binding with its endogenous ligands CCL11 and CCL24, with KD of 2.90 × 10−6 and 1.81 × 10−6 M, respectively.
RNA binding activity of purified recombinant proteins (Figure 5B) was tested by filter binding assay with radioactively labeled vector derived RNA.
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