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In particular, it has been suggested that the miRNA binds preferentially to the 3′UTR of the mRNA and that the binding is determined by the "seed" at the 5′-end of the miRNA [ 23– 25].
Substrate binding is determined by hydrogen bonds with the substrate backbone.
However, these estimates of false positive rate may be exaggerated, because functional binding is determined by not only the cis element but several other genomic and epigenomic markers in the vicinity and the proximal promoters are enriched for these additional markers.
The rate of binding is determined by EF-Tu interactions with the ribosome: this step proceeds much more slowly with aa-tRNA alone [ 19].
Selective binding is determined by interactions with more than 60 different cofactors, which turn SRF into a versatile transcription factor translating cell- and stimulus-specific signaling into selective target gene expression [ 1, 2].
A TF is modulated by the binding of a ligand, which is either molecule A (light blue circle) or molecule X (dark blue circle), and the strength of this binding is determined by the corresponding constant of dissociation.
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Nonspecific binding was determined by carrying out parallel determinations in the presence of excess unlabeled competitive antagonist (10 µM naloxone).
After protein purification, we incubated equal amounts of E194 and E194GAGmut with Chinese hamster ovary K1 (CHO-K1) and HeLa cells, and binding was determined by immunofluorescence and flow cytometry using anti-V5 antibodies.
In the in vitro study, citrated blood was incubated with different concentrations of etamsylate, and P-selectin expression and annexin V binding were determined by flow cytometry.
The effect of these mutations on membrane binding was determined by a quantitative phospholipid ELISA assay and compared to wild-type α-Syn and to the Parkinson's disease-causing mutations, A30P, E46K and A53T.
Plasma protein binding was determined by using human plasma according to Patila et al. (2007).
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