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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.
Receptor-ligand binding affinities were determined by SPR using Biacore T100.
The number of receptors and binding affinities were determined as previously described (Obiri et al, 1993; Puri et al, 1991).
In these cases the apparent binding affinities were determined from the dose dependency of equilibrium binding (KD (eq)).
These results are well correlated with those from experiments where no binding affinities were determined in the BPA-D/ERRγ complex.
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.
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It should be noted that these metal binding affinities are determined using various methods [e.g., isothermal titration calorimetry (ITC), equilibrium dialysis, and absorbance or fluorescence spectroscopy] under various conditions, some which are thermodynamic and others of which are based on metal site activity.
Method: A lactam bridge-cyclized H-Cys-Ahx-βAla3-c[Lys4-Glu-His-D-Phe-Arg-Trp-Glu10]-Arg11-Pro-Val-NH2 (NandNS2) and the corresponding linear H-Cys-Ahx-βAla-Nle-Asp-His-D-Phe-Arg-Trp-Gly-NH2 (NAP-NS1) peptide were synthetized, characterized by ESI-MS spectroscopy and their MC1R binding affinity were determined in B16/F10 melanoma cells.
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.
Nucleotide-binding affinities were determined by equilibrium titration of Irga6 in the range of 0 to 100 μM against 0.5 mM mant nucleotide in B1 buffer/2 mM DTT at 20°C.
More suggestions(19)
binding affinities were mirrored
binding parameters were determined
binding mechanisms were determined
binding affinities were predicted
binding profiles were determined
binding affinities were obtained
binding models were determined
binding affinities were used
binding affinities were interpreted
binding affinities were compared
binding affinities were evaluated
binding values were determined
binding affinities were computed
binding affinities were assayed
binding affinities were observed
binding affinities were estimated
binding affinities were chosen
binding affinities were analyzed
binding regions were determined
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