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Functional binding and transcription activation of this region by viral BZLF-1 protein binding (functionally equivalent to host AP-1 binding) was confirmed in these studies.
Specificity of W-box binding was confirmed in competition experiments, wherein only an excess of the W-box probe was able to compete for binding of the protein.
Binding was confirmed in cells using pull-downs, while in vitro binding assays showed direct, high affinity (apparent dissociation coefficient of c. 0.25 nM) binding of Dp71d to IMPα/β.
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All peptides were less than fifty amino acids in length and the binding was confirmed by in vivo as well as in vitro studies.
The specificity of Twist1 binding was confirmed by ChIP qPCR in each tissue.
The Sia dependence of bacterial binding was confirmed by a considerable reduction in the binding of desialylated FITC-PA with CHO-siglec-7,-9.
Involvement of the C-terminal region of Hsp70 in M1 binding was confirmed; thus, to identify the region of the M1 protein involved in this binding, deletion mutants of M1 were constructed based on a previous report.
The in vitro binding was confirmed by overlay of the blotted membranes with radio-labeled HAMLET (Figure 2A, right panel).
Consequently, the role and influence of position H58 for antigen binding was confirmed and correlated with each hapten in terms of its chemical structure and polarity.
AP-2α binding was confirmed by chromatin immunoprecipitation (ChIP) analysis in the region including the three high score sites, as shown in Figure 8a, using three different anti-AP-2α antibodies.
The essential role of Phe313 and Trp305 in N-6 binding was confirmed by our SPR assays, showing that N-6 had much lower binding affinity to two RXRα-LBD point mutants with Ala substitution of Phe313 or Trp305 (Fig. 4D and 4E).
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