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Here, only those peptides can bind where the binding does not depend on the P1 pocket.
In contrast, CPBF1 binds to the mature portion of EhCP-A5, and its binding does not depend on carbohydrate modifications.
RIG-I can also bind to RNA molecules made by the host cell, but this binding does not cause RIG-I to activate the immune response.
Such binding does not, however, unequivocally identify NMD substrates, as Upf1 also binds many non-NMD targets (Hogg and Goff 2010; Zünd et al. 2013).
Therefore, Bcl-w binds to Akt and is a direct substrate of Akt; however, this binding does not alter the activity of Akt on other substrates.
However, UTP binding does not cause significant conformational change of cGAS.
This RMSD indicates that the H3K4me0 peptide binding does not induce major conformational changes to the backbone of PHD1KDM5B.
Based on the results of pull-down assays, Mx2-CA binding requires the higher-order assembled capsid lattice, just as TRIM5α-CA binding does.
From an overall bioaccumulation perspective, protein binding does not provide additional information about the quantitative bioaccumulation of substances beyond log K OW.
If the types of the required and provided interfaces are incompatible, the binding does not occur and an error message is generated.
However, the results of the data analysis show that protein binding does not correlate with increased bioaccumulation beyond log K OW.
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