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Experiments were designed to reproduce the antiepileptic effects of low frequency stimulation (LFS) during the amygdala kindling process and to examine LFS-induced changes in receptor binding levels of different neurotransmitters in normal brain.
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(A ) Genome-wide profiling of Pol II (N20) and CTD isoforms (as in Figure 2 ) for different classes of binding levels indicate a distribution of Tyr1P more prominent at promoters vs gene bodies as compared to Pol II and Ser7P, but comparable to that of Ser5P.
Here, we identify the expression level of different FK506-binding proteins (FKBPs), primarily FKBP12 and FKBP51, as the key determinants for rapamycin-mediated inhibition of mTORC2.
These different binding levels were a consequence of the higher density of VEGFR1 and the higher binding affinity of VEGF for this receptor (Table 2).
Next, the different binding levels were generated by varying k3 from 0.2 to 2.6 min−1.
The expression levels of the different isoforms, as assessed using an antibody against the common DNA binding domain of the protein (pan-AP-2α, 3B5), were consistently similar.
This also suggests that the binding of miRNA biogenesis factors to the assembling miRNA transcript might be a regulatory step controlling the levels of the different miRNA forms.
Whilst replicate measurements within a single portion of tumour were reproducible (intra-assay coefficient of variation was between 4.5 and 7.8% and that for inter-assay variation was between 2.1 and 4.0%) there were often considerable differences in levels of binding proteins between different portions of the same tumour.
We provide functional validation of these genomic binding events by modulating levels of BRA within different signalling environments in differentiating hESCs and by analysing the expression pattern of BRA target genes in mouse embryos that lack brachyury.
SA displayed negligible bias (0.14%), independent of the binding level.
Therefore, σfactors and recombinant proteins compete to bind chaperon complexes, and different levels of binding affinity of recombinant proteins to chaperon complexes change the evolution of the system state.
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