Sentence examples for binding of dimeric ligands from inspiring English sources

All known RTKs become activated by the selective binding of dimeric ligands to their extracellular domains, resulting in their dimerization and autophosphorylation [1], [2].

By contrast, statistical thermodynamics also predicts that binding of a dimeric ligand to membrane-anchored receptors will occur via a stepwise process, since the direct binding of ligand to two receptors simultaneously (with respect to the timing of the binding events) involves a trimolecular reaction, which is a very rare event.

Biological evaluation of the compounds shows no discrimination between monomeric and dimeric-ligands in respect to binding affinities, however, the dimeric ligands appear to have different functional properties.

BMP signaling, induced through the binding of a dimeric BMP ligand to type I and type II BMP receptors, has a key role in the pathogenesis of RA [ 32].

The presence of four receptor binding epitopes in the dimeric ligand creates the possibility of a whole set of individual ligand-receptor interactions on cell surfaces.

This paper mainly focused on the development of structure-based dimeric ligands that target CXCL12 CXCR4 interaction and signaling.

A stoichiometry of 1 molecule of ligand per mole of dimeric enzyme was obtained for the binding of these ligands.

However, measuring the kinetic binding parameters or in vitro activity of the Fab-12 fragment does not take into account potential avidity interactions of bivalent antibodies, especially when the binding partner is a dimeric ligand such as VEGF-A.

As shown by the structures of several ligand-receptor complexes, the dimeric ligands are capable of interacting simultaneously with two receptor molecules of either subtype.

In fact, binding of bivalent ligands shows a considerable avidity effect; affinity of a dimeric myosin 5a fragment has been recently reported to be ∼40 nM [20].

Taken together, these results support the idea that dimeric ligands can cooperatively bind the two antigen-binding sites of an antibody, resulting in significant improvement of binding affinity between ligand and antibody.