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c-Jun in combination with binding partners has a function in regulating the promoter activity positively or negatively.
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This result clearly shows that presenting multiple equivalent binding sites to the binding partner has a measurably positive effect on the effective affinity of the individual interaction site.
First, the interaction of BAX with a binding partner could be affected by low levels of BAX protein, especially if the binding partner had a reduced affinity for BAX in its globular conformation.
In the yeast protein-interaction network, the observed negative correlation between the connectivity of a protein and the average connectivity of its binding partners has been seen as a possible adaptation which allows the network to be resilient to the propagation of deleterious perturbations [ 14].
In the past 4 decades of desmin research, a growing number of desmin binding partners has been described (see also a previous review on desmin interactions [ 38]).
However, a lack of structural information characterizing CD59 with its binding partners has limited our ability to control complement susceptibility.
Although identification of binding partners has provided insight into LZAP function, satisfying mechanisms of pleiotropic LZAP activities have been lacking.
Structural analysis of IgG complexed with different binding partners has delineated several of these epitopes.
Direct experimental measurement of binding partners has typically focused on specific interactions driven by hypotheses relating to the precise signaling events under investigation.
The interaction of XPA and its binding partners has been extensively studied; however, the structures of the full-length XPA DNA complex remain to be defined.
Although the mapping of specific interaction sites between Mcm7 and its various binding partners has not yet been performed at high resolution, available evidence suggests that these sites likely overlap conserved ATPase motifs.
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CEO of Professional Science Editing for Scientists @ prosciediting.com