Sentence examples for binding of soluble ligands from inspiring English sources
Some TNF receptors are strongly activated by the binding of soluble ligands, whereas others bind soluble ligands but then fail to trigger intracellular signaling.
In analogy to LRP1, this might occur through binding of soluble ligands in the extracellular space [27].
This pathway is commonly activated by binding of soluble ligands to death receptors (reviewed in [ 28]).
Now, the interaction of TNF receptors with membrane-bound TNF ligands always results in strong receptor activation, whereas TNF receptors respond differently to binding of soluble ligand molecules.
While interaction with a membrane-bound TNFSF ligand in any case results in strong receptor activation, TNFRSF receptors differ in their response to binding of soluble ligand trimers.
TNFRSF receptors that fail to signal properly in response to binding of soluble ligand trimers, typically respond quite well when the ligand molecules become secondarily oligomerized (Table 2).
In a subset of members of the TNF receptor superfamily, including TRAILR2, the binding of soluble ligand trimers is less efficient in receptor activation than interaction with the corresponding membrane-bound form of the ligand.
The latter reflects that some members of the TNF receptor family are potently activated by the membrane-bound form of their ligand but fail to respond properly to binding of soluble ligand trimers.
We and others have shown earlier for the TRAIL death receptors and some other members of the TNF receptor family that their per se poor response to binding of soluble ligand trimers can be overcome by anchoring the latter to cell surface antigens.
This system consists of soluble ligands (including IGFI and IGFII), cell surface transmembrane receptors (including IGFI receptor (IGF-IR) and IGFII receptor (IGF-IIR)) and soluble binding proteins (IGFBP1 (IGF binding protein-1) through IGFBP-6).
In this context, it is of interest to note that the discovery of soluble ligand binding versions of the β-GF points to a noteworthy structure-function analogy with the RNA-recognition motif (RRM -like fold.
