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We then mutated the three critical tyrosines (Tyr232, 253 or 257) individually to glutamic acid, which mimics phosphorylation, in the BCR63-ABLKD context and found that each Y/E substitution alone is sufficient to block the nuclear import of this kinase-defective BCR63-ABLKD protein (Figure 5B).
Thus, we mutated the three hydrophobic residues (I162, L159 and I170) contacted by L41 and M42 of the N terminus.
To further investigate the role of the AT motif in ZFHX3-dependent transcription, we mutated the three most conserved residues (residues 6, 8, and 10) within the Avp and Vip promoter constructs.
To test whether disruption of zinc coordination would result in a similar phenotype as deleting C33, we mutated the three cysteines in the CHCC motif of endogenous Dcr1 into serines (Dcr1-CHCC to Dcr1-SHSS).
To investigate the importance of this sequence, we mutated the three core bases of the Ets site either singly or in combination within the context of the 508 bp reporter.
To investigate whether disruption of the binding of PP1βMYPT1 to NUAK1 might also promote NUAK1 phosphorylation and hence interaction with SCFβTrCP, we mutated the three GILK motifs in NUAK1 that mediate PP1βMYPT1 phosphatase binding [ 6] and observed that this significantly enhanced binding of βTrCP.
Similar(53)
These results suggest that AP-2α also regulates PP2A-Aα To further confirm the AP-2α control on PP2A-Aα gene promoter, we again mutated the two AP-2α binding sites either individually or in combination (the mutation of the two AP-2α sites are shown in Fig. 5A) and assayed the relative luciferase activity from the two constructs in both ARPE-19 and FHL124 cells.
We mutated the four aforementioned residues to alanine and generated four stable mutant ArgRSs (D118A, Y313A, D317A and R324A).
In this study, we mutated the two sites, expressed four resulting mutants in Escherichia coli and characterized.
Therefore, we mutated the two UIMs in the Atx3(1 263) fragment in order to compromise their functionality [Atx3(1 263)(S236A,S256A)].
To identify the CK2 phosphorylation sites, we mutated the four CK2 consensus sites to Ala either individually or in groups (Fig. 2D I).
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