Sentence examples for mutants bind to from inspiring English sources

This phosphorylation might explain why the binding of VRK2 inactive mutants to JIP1 is more robust, since these kinase inactive mutants bind to the substrate but are unable to transfer the phosphate and therefore the substrate cannot be released, causing the formation of a stable intermediate [40].

In the presence of Ca2+, the wild-type protein and both mutants bind to both PS and phosphorylated PtdIns's with the exception of PtdIns 3,4,5 P3.

The profiles of proteins identified in wild-type and mutant Rab7 were qualitatively identical, suggesting that Rab7 mutants bind to the same complement of interactors as wild-type Rab7 (Fig.  4A and B, Supplementary Material, Fig. S4).

Instead, the newly termed "superbinder" Keap1 mutants bind to Nrf2 with a greater affinity than wild-type Keap1, yet are unable to inhibit Nrf2-mediated gene expression (Hast et al., 2014).

To identify which of the Myo Va mutants bind to full length NF-L, we co-immunoprecipitated (co-IP) each of these Myo Va mutant proteins (Fig. 1A and Fig. S1A-E) in equimolar quantities with an excess of NF-L, using the antibodies NR-4 or 21.4 for purified NF-L and 9E10 for Myc tagged NF-L (Fig. S1F).

10.7554/eLife.06942.013 Figure 2. NKX2-5 mutants bind to hundreds of targets in HL-1 cells.

All three mutants bound to PG like the wild-type, and no significant differences in the binding affinity were observed.

These mutants bound to both FADD and caspase-8, but could not block apoptosis or the formation of death effector filaments.

We have determined the three-dimensional structures of selected mutants bound to the substrate analogue nicotinic acid, using X-ray crystallography.

All pyrin mutants bound to PSTPIP1 and reticularized PSTPIP1 filaments in a manner similar to wildtype pyrin (Figure 6A R).

Right panel: comparative efficiency of SUMO chain pull-down by MBP-Wss1 mutants bound to the same amount of amylose beads.