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Compared with Fe2+, the native cofactor of JHDMs, Ni2+ can stabilize JHDMs without impairing the binding of JHDMs with its ligands.
We proceeded to investigate whether ORF73 would be functioning at the nuclear level by impairing the binding of NF-κB to DNA κB sites.
These findings suggest that PDB-related SQSTM1 mutations may confer a higher susceptibility to development of the disease by impairing the binding of the p62 protein to a ubiquitinated target.
Increase/decrease in the number of cytosine residues in the poly-C region may affect the rate of DNA replication by impairing the binding of polymerase and other trans-acting factors (Fliss et al, 2000).
These data suggest that Pin1 protects TAp63 α from degradation via binding to its phospho-Thr538-Pro peptidyl-prolyl bonds and impairing the binding of WWP1 to the P540PxY543 motif of TAp63 α; T538A mutation in TAp63 α abolishes the action of Pin1 on this site and it makes TAp63 α(T538A) proteins vulnerable to WWP1-mediated degradation.
Recently, it was shown that melatonin acts as a calmodulin antagonist, inducing conformational changes in the ERα calmodulin complex and thus impairing the binding of 17β-estradiol (E2) and the ERα calmodulin complex to DNA and therefore preventing ERα-dependent transcription [ 15].
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MDV3100 also reduces the efficiency of AR translocation to the nucleus and impairs the binding of AR to the androgen response element and other factors that bind to AR [ 99].
Moreover, we show that the association of NP with the host transporter does not impair the binding of NP to RNA.
This finding from our analysis is consonant with an experimentally identified functional role of residue E428 in hDAT71: the E428Q substitution in hDAT expressed in HEK293 cells was found to impair the binding of the inhibitor CFT, suggesting that this mutation favors an inward-open state in hDAT over the outward-open conformation to which CFT binds.
In contrast, the AA →Glu mutations of the hydrophilic residues Gln148, Lys156 and Lys159, known for their interactions with LTRs (long terminal repeats) and inhibitors (5 CITEP, for instance), significantly impaired the binding of K156 to the antibody.
We found that HbF impairs the binding of parasitized RBCs to human microvascular endothelial cells (MVECs), monocytes, and nonparasitized erythrocytes – cytoadherence interactions that contribute to the development of high parasite densities and the symptoms of malaria.
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