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These studies prove that CT-DNA binding of the complexes follows the intercalation mode.
The binding of the complexes with CT-DNA was analyzed by electronic absorption spectroscopy, viscosity measurement, and cyclic voltammetry.
The binding of the complexes with CT-DNA were studied by UV-vis, fluorescence and time-resolved nanosecond transient absorption (ns-TA) spectroscopy.
As can be seen in Tables 1 and 2, the ∆Eele of binding of the complexes with capping in the polarisable simulations is more negative compared to the results obtained with the non-polarisable simulations.
When the particles from fruiting bodies of A. blazei Murill (ABP-F) were reacted with human serum, the formation of complement-opsonized ABP, iC3b-ABP-F complexes, and binding of the complexes to human peripheral blood monocytes, were demonstrated in vitro by immunofluorescence.
In most cases, DNA damages caused by platinum complexes are attributed to the binding of the complexes to DNA, which leads to DNA conformational changes that block the normal replication and transcription processes.
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It has previously been shown that RUNX3 binds to TCF4/β-catenin complex, which suppresses the binding of the complex to the Wnt target gene promoters.
This interaction was specific and not an artifact of non-specific binding of the complex to beads (Figure S4).
While increasing amounts of the KSC, p53, and WT oligonucleotides disrupted binding of the complex, the MT oligonucleotide was unable to compete (Figure 2 lanes 2 9).
Upon binding of the complex to the cell surface of SKOV-3 cells, the gold particles were deposited on protrusions and smooth parts of the cell membrane (Figure 4, A D).
The HAP2 and HAP3 proteins enable DNA binding of the complex, whereas HAP4 contains the transcriptional activation domain.
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