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The extraordinary stability of the Smac dimer supports the idea that the posttranslational modification(s) that attenuates dimerization specifically targets a critical regulatory motif.
An important future achievement will be to identify the posttranslational modification(s) that monomerizes Smac and destroys the epitope recognized by the monoclonal antibody and the enzyme(s) involved.
These findings suggest that the IBM of Smac is a recognition point for a posttranslational modification(s) that blocks homodimerization and IAP interaction, and that amino acids 62 105 are required for the proapoptotic function of Smac.
Hence, persistent cytosolic expression of wild type Smac56, but not Smac60, predisposes it to a posttranslational modification(s) that blocks dimer formation without affecting its mobility by SDS-PAGE (Fig. 7A, anti-V5, lanes 2 and 5) or 8 M urea PAGE (Fig. 6B, lanes 1 and 4).
Both proteins could require post-translational modification(s) that stabilize and activate them in the nucleus.
We have tried to identify the UVR-induced modification(s) that initiate and/or promote aggregation.
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These results suggest that a posttranslational modification(s) at or near the dimer interface, which includes residues V78 to F88, is responsible for the loss of immunoreactivity.
The algorithm does not require the adjustment or modification of the alignment scoring scheme(s) that is usually tuned for a particular alignment purpose, e.g. cross-species, contig or read alignments.
To identify the kinase(s) that may phosphorylate PAGE4, we used a commercial service to screen for modification by 190 S/T protein kinases that were expressed in Sf9 cells as human recombinant GST-fusion proteins or His-tagged proteins by means of the baculovirus expression system (ProQuinase, GmbH).
The synthetic miRNAs require chemical modification(s) so that they can be stable in systems' fluid and can also be tissue specific.
This finding suggests that covalent modification(s) by small chemical group(s), which we believe cause the slight molecular weight shift of the 32-kDa procaspase-3-D3A, could have a major role in the Photofrin-PDT-mediated suppression of caspase-3 activity.
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