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The reduced IgE binding of both hybrids translated into decreased receptor cross-linking on passively sensitized RBL cells.
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We found that the binding of porphyrin hybrids occured through intercalation and groove binding mode in addition interaction with the amino acid residues constituting the active cavity of Topo IIβ.
Estrogen treatment increased shell thickness of both hybrids.
Fig. 3 Integrin αVβ3 receptor binding of the hybrid probe.
In the blocking study, the cellular uptake decreased to 72.2 % in the presence of RGD2 (10 μM), indicating specific binding of the hybrid probe to the integrin αVβ3 expressed on tumor cells (Fig. 4b).
Immunofluorescence staining showed the formation of new blood vessels in tumor tissues, suggesting that the tumor uptake was due to specific binding of the hybrid probe to integrin αVβ3 expressed on tumor cells.
A control experiment with Na3[Fe(OH)6Mo6O18] up to two molar equivalents showed no quenching of the tryptophan signal at either pH value (5.5 and 7.4), which revealed no binding in the vicinity of tryptophan 214 and thus indicated the importance of the aromatic moieties in the binding of the hybrid POMs reported herein.
This meant that there was simultaneous binding of both metals with the same binding sites.
Furthermore, simultaneous DNA and transition metal binding of hybrid 4 is indicated.
Therefore, we performed ChIP to measure the occupancy of several candidate partners for C/EBPβ, and found robust binding of ATF4 at hybrid motifs.
In particular, recent cross-species ChiP-seq analysis of transcription factor binding (Schmidt et al. 2010) suggests a way to explicitly test our predictions at the level of actual binding affinities of hybrid TF TFBS combinations for recently diverged species, such as in the Drosophila family.
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