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Consequently, a yeast two-hybrid cDNA library screen was performed with the VAMP7 longin domain in an attempt to identify new candidate binding partners that could act as cargo-selective devices for VAMP7.
Further structural characterization of eIF4E complexes revealed unique binding elements in different eIF4E binding partners that could be fused into a chimeric '4E-BP-like' mimic and dampen translational activity [ 98].
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There are binding partners that demonstrate preference for each of the known arrestin conformations: free, receptor-bound, and microtubule-bound.
There are no known binding partners that would interact with the periplasmic domain of AmtB.
These co-factors can have other binding partners that are themselves regulated by different signalling pathways.
Likely it requires binding partners that aid in vesicle nucleation, localization, targeting and recycling.
Phosphorylation of R2/B itself could trigger release of APC's Arm rpts from the Axin complex, or alternately, phosphorylation may create a binding site for a binding partner that carries out this function.
This suggests that other binding partners exist that could modulate the IKK complex activity and function.
We identified p33ING1 as a binding partner that interacts with CSIG.
Our data indicated that BI-1 is a binding partner of IP3R that could upregulate IP3R expression in the retina.
We used yeast 2 hybrid screens to identify novel binding partners of R-Ras that could mediate its effects on integrin function.
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