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After incorporation into the oocyte cytoplasm during fertilization, ubiquitinated sperm mitochondria are detectable in the oocyte cytoplasm whereupon the intensity of ubiquitin binding appears to increase, as detected by immunofluorescence imaging [ 51].
The contrasting chromatin-binding dynamics of CBX8 and PHC1 in response to signaling are in good agreement with our previous observation that PHC1/chromatin binding appears to increase globally in the context of cell cycle progression or cell stress, whereas detection of other PRC1 members in PcG-NB (like BMI1, CBX4 and RNF2) is reduced [ 5, 11].
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Specifically, Red1 binding appeared to increase on large chromosomes and close to centromeres.
We note, however, that Red1 binding appeared to increase at some positions (see next section).
In addition, the polyethylene glycol covering decreased protein binding and appears to increase the time of circulation within the systemic compartment.
To date, there is little information about the relationship between enolase structure and plasminogen binding, although one mutation that partially dissociates enolase appears to increase binding [18].
C-terminal deletion of Syx appears to increase Rnd3 binding, indicating an intramolecular N- to C-terminal auto-inhibition that might be relieved by Rnd3 association as seen for other RhoGEFs [39], [40].
VEGF induction appears to increase DNA binding of HIF-1 to hypoxia-responsive elements in the VEGF gene promoter.
Although I3C decreased the amount of p-MDM2, this natural indole carbinol compound appears to increase significantly the binding efficiency between phosphorylated MDM2 and nucleostemin.
These results indicate that the binding of silica particles to albumin and IgG appears to increase as the particle size decreases.
The effect of binding allosterically inhibits the binding of the CREB KID domain, inhibits CREB-mediated gene induction, but appears to increase histone acetylation.
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