Sentence examples for mutually exclusive sites from inspiring English sources

Estradiol metabolism proceeds by hydroxylation at one of two mutually exclusive sites at C-2 and C-16 alpha.

Therefore, the partial inhibition observed here may be more complex than simple partial competitive inhibition, with the inhibitor and l-serine competing at two distinct sites, the catalytic and effector sites, rather than mutually exclusive sites.

Binding of a molecule to one such site will result in hiding of the mutually exclusive binding site by sterically blocking its accessibility and thereby inhibit binding of the competing molecule.

The 4E-binding proteins [4E-BP; also called phosphorylated heat-and-stable protein, insulin-stimulated (PHAS-I)] compete with eIF4G for a mutually exclusive binding site on the dorsal surface of eIF4E by way of a shared eIF4E-recognition motif, YxxxxLФ (where x is any amino acid and Ф is an aliphatic residue, usually L, M or F) [19] and consequently inhibit cap-dependent translation [20].

However, it has recently emerged that CBX proteins are in direct competition with two additional factors, RYBP/YAF2, for a mutually exclusive binding site on RING1A/B (Wang et al., 2010).

These results led us to conclude that AChE directly interacts with PrP unstructured N-terminus and more precisely with two mutually exclusive sub-sites that are included between residues 23 and 99 and residues 100 and 120.

To determine the PrP region involved in the AChE-PrP fibril interaction, we used SLS to investigate the interaction between AChE and two fibrillar samples obtained from two N-terminally truncated PrP variants lacking either residues 23 99 or 100 120, the two mutually exclusive sub-sites for the AChE-PrP interaction that we previously identified using monomeric PrP.

Using several truncated PrP variants and specific tight-binding AChE inhibitors (AChEis), we then demonstrate that the PrP-AChE interaction requires two mutually exclusive sub-sites in PrP N-terminal domain and an aromatic-rich region at the entrance of AChE active center gorge.

Therefore, we conducted re-ChIP experiments in Kasumi-1 cells to test at known RUNX1/ETO binding sites whether the two factors co-occupy single sites or whether binding is mutually exclusive at such sites.

Concatenating these mutually exclusive selections of sites produces a composite alignment that preserves a maximal amount of information for reconstructing the placement of the rare SerRS and ThrRS types (see Additional file 3).

These data, together with computer docking simulations, lead us to conclude that both the type I PAM NS1738 and the type II PAM PNU-120596 bind competitively at a mutually exclusive intrasubunit transmembrane site.