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The ligand binding domain (LBD) can also be mutated to bind a synthetic small molecule that can reversibly regulate expression of genes.
We demonstrated that multiple loops of EETI-II can be mutated to bind with high affinity to tumor-associated integrin receptors.
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Specifically, the 3′ UTR bases predicted to be part of the mRNA miRNA seed base pairing were mutated to the complementary base, A to T, C to G, G to C, and U to A, such that mir-34 and mir-83 loaded miRISCs would no longer to be able to bind the mutated 3′ UTRs.
Ubiquitin E3 ligases RNF168 and BRCA1 exhibit defective ubiquitylation when the acidic patch is mutated and IL-33 binds to the acidic patch, likely in a manner similar to the LANA nucleosome targeting peptide.
The sites where Pin1 binds were mutated and examined if Pin1 bound the sites or not.
Theoretically, mutated HN protein whose receptor-binding site is occupied by sialic acid should not be able to bind additional ligands.
Accordingly, we designed and constructed a RIG-I Q299A mutant, and found that the mutated protein is unable to bind significantly to biotinylated leader RNA (Figure 5G).
According to our results, neither native VvMYB5bR nor mutated VvMYB5bL were able to bind MBS sequences in EMSA experiments.
Since the PfI2 mutated proteins are able to bind PP1 but unable to inhibit its function we sought to determine whether the pre-injection of deleted or mutated PfI2 proteins may block the role of wild PfI2.
The authors of the original paper conclude that PIAS3, being unable to bind the mutated MITF, is accessible for binding and thus inhibition of STAT3.
As an alternative approach to block the actions of IL-6 Ciliberto and colleagues generated a number of IL-6 receptor antagonists, which were mutated forms of IL-6, that can bind to the IL-6R but block it in an inactive configuration (Demartis et al, 1996).
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