Sentence examples for binding to the type from inspiring English sources

Upon binding to the type II IFN receptor on tumour cells, IFN-γ triggers the JAK/STAT signalling cascade as well as PI3K and mTOR pathways24.

Upon binding to the type II IFN receptor, IFN-γ triggers the JAK/STAT signalling cascade that leads to the expression of a large array of interferon induced genes which can cause growth arrest, cell death or make tumour cells to upregulate MHC-I expression and antigen presentation, thus becoming more susceptible to MHC-restricted cytolytic killing24,25.

The TGF-beta signal is mediated by ligand binding to the type II receptor, leading to the recruitment and activation of the type I receptor, and subsequent activation of a family of intracellular signal transducing proteins called Smads.

In fact, BV does not form a single H bond with the H epitope in binding to the type 2 Ley antigen, while only one water mediated H epitope between D349′ of the P-loop and the H epitope was seen in BV binding to the type 1 Leb antigen (Fig. 6).

TGF-ß signaling is initiated by ligand binding to the type II TGF-ß receptor (TßRII), which leads to activation of the type I TGF-ß receptor (TßRI).

To determine the effects of pharmacologic inhibition of TGF-β signaling on bone, mice were treated for 6 weeks with either of two doses of SD-208, a small molecule that blocks ATP binding to the type I TGF-β receptor to specifically inhibit its kinase activity [17].

Upon ligand binding to the TGFβ type II receptor (TGFβRII), the type I receptor (TGFβRI or ALK5) is recruited into the complex and phosphorylated.

TGFβ signal transduction begins with ligand binding to the TGFβ type II receptor, which recruits and activates the type I receptor.

Binding of hEBV321 to VEGF-G88A resembled its binding to the wild type VEGF, but binding of Bevacizumab to VEGF-G88A was substantially reduced as compared to hEBV321 (Figure 3D).

In comparing to proteins binding to the wild type eIF5B, several proteins were found to preferentially bind to eIF5B-S214E mutant, but not eIF5B-S214A mutast as displayed in Fig. 2C.

However, the effects reported by Petersen and co-workers are direct: they result from fibrinogen binding to the BMP type I receptor protein ACVR1 on the surface of OPCs to stimulate the BMP signalling cascade in these cells (Fig. 1).