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IL-7 binds to its receptor to mediate biological functions.
They interact either directly or indirectly with other proteins to synergistically mediate biological functions.
Several classes of small RNAs have been found to mediate biological functions in animals and plants [ 1- 5].
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However, in some cases the BH3 helix alone is not sufficient to mediate biological function, and further tools are required.
Currently the most successful approach to overcome this information gap is based on the assumption that sequences conserved between species (here human and mouse) would most likely mediate biological function [ 15- 19].
Currently the most successful approach to overcome this information gap is based on the assumption that gene sequences conserved between species (here Human and Mouse) would most likely mediate biological function [ 21- 25].
Although they lack the RNA-binding region and immunodominant core epitopes, the "mini-cores" seem to be important functional components of the HCV protein repertoire, as they might mediate some biological functions of core, such as binding to lipid droplets [43].
The mAb 3F8 and the peptidic GD2 ligands mediate similar biological functions in cell-based assays of calcium fluxes and src activation.
Both sTNF and tmTNF ligands interact with either of 2 distinct receptors TNF receptor 1 (TNFR1, p55, CD120a) and TNF receptor 2 (TNFR2, p75, CD120b)—on a wide variety of cell types to mediate their biological functions [2], [3].
Type I IFNs mediate their biological functions by binding to the receptor on the target cells, resulting in autophosphorylation and activation of the Janus kinases (JAKs), JAK1 and tyrosine kinase 2, leading to phosphorylation of the signaling molecules STAT1 and STAT2 [15], [15].
IL-17 family cytokines mediate their biological functions via surface receptors on target cells.
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