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This situation is somewhat similar to that of glycan-array binding studies, in which the probe that binds best on the glycan array does not necessarily bind the same glycan on the array as on cells and the identification of the glycan structure does not always result in the identification of the relevant biosynthetic enzyme.
These results are in good agreement with the ELISA binding studies, in which antibody binding to surface-immobilized PA was impaired compared to that of soluble PA (indirect format), indicating that the epitope recognized by this antibody is probably disrupted when the PA is used as the capture moiety.
In addition, we did not detect differences in the affinity binding of mutants that mimic phosphorylation by Erk and Src, which contrast our previous binding studies in which a mutant that mimics phosphorylation by Erk was found to bind preferentially to N-WASP [ 14].
Receptor binding studies in which the Ig-labelled polysaccharide-binding domains of dectin-1 were used to detect glucan binding have demonstrated that dectin-1 preferentially binds to the β-(1→3) part of the glucan, and that the minimal length required to allow binding to dectin-1 is 10 11 glucose residues [ 63].
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In our study (Oehlmann et al. 2006), we did not intend to deliver a complete binding study in which saturation experiments with Scatchard analysis are needed, but to provide indications for the presence of estrogen receptors by a specific binding of ligands to cytosolic extracts (a widely used practice).
In this regard, a significantly higher percentage of receptor-positive cases could be identified by autoradiography (Gugger and Reubi, 1999), compared with binding studies in cell lines, in which a 33% incidence of GRP receptor-positive breast carcinomas was found.
This is confirmed by binding studies in vitro for Wnt3a and YW211.31 antibody, which bind competitively within the E3-E4 regiof of LRP6, and for Wnt9b and YW210.09 antibody, which compete for binding within the E1-E2 region.
Isotopic labeling of the I-CreI meganuclease is demonstrated opening the way for structural and ligand binding studies in solution by nuclear magnetic resonance (NMR 2 which was previously hampered by the problems associated with the toxicity of the enzyme for Escherichia coli limiting its growth.
This correlated well with the binding and activation studies, in which 50 50 TBECH-γδ displayed a higher activation/binding than TBECH-αβ.
The %AD is corrected for unspecific binding determined by blocking studies in which 10−6 M of the unlabeled agonist or antagonist was added.
Ticagrelor binds to the P2Y12 receptor at a site distinct from the ADP-binding site, as initially shown in studies in which CPTP did not prevent binding of ADP [ 34], and appears to inhibit ADP-induced receptor signaling in a noncompetitive manner [ 35].
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com