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Six of the new compounds which displayed high in vitro CB1 binding affinities were assayed for binding to CB2 receptor.
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Relative binding affinities were tested by radioligand displacement assays versus PMP-BSA (pentamannosyl phosphate-bovine serum albumin).
The binding affinities were determined using isolated receptor binding assays where the different integrins (α5 β1, α v β3, and α IIb β3) were immobilised and [I]echistatin was replaced by increasing amounts of the different peptides tested.
Two anti-TNT antibodies with differing binding affinities were compared in the reversed-displacement assay format, and a correlation between affinity and detection limits was observed.
ER binding affinities were evaluated by a fluorescent polarization assay with the corresponding inactive In III) complex or iodinated peptide.
The PSMA binding affinities were determined in a competitive binding assay using LNCaP human prostate carcinoma cells and the known high affinity PSMA ligand ([125I]I-BA KuE [125I]I-BA KuEnM) as the radioligand.
Peptide binding affinities were predicted, and the affinities of 4 distinct high binders were determined using flow-based MHC stabilization assays (Table 3a).
Compounds with predicted binding affinity were then screened by various assays with purified p300 acetyltransferase domain.
After identifying several aptamer sequences capable of binding adenine, the highest affinity aptamers were assayed with molecules structurally similar to adenine.
In vitro GRPR-binding affinities were determined with competitive binding assays on PC3 human prostate cancer cells.
The αvβ3-binding affinities were determined by a competitive cell-binding assay using I-echistatin (PerkinElmer) as the αvβ3-specific radioligand.
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