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The characterization of the structural determinants of protein protein recognition represents an important step for the development of molecular entities able to modulate these interactions.
Although efforts to modulate these interactions are more challenging and much less mature than work on conventional drug discovery pathways, significant progress has been made on several fronts.
As activation of TRPV4 results in high Ca2+-influx, we tested if higher concentration of Ca2+ could modulate these interactions.
However, in vivo there are many other proteins able to modulate these interactions to add specificity.
Unknown ways in which Fringe proteins could modulate these interactions are indicated by question marks.
We found that Dll1 and Jag1 can cis-inhibit Notch1, and Fringe proteins modulate these interactions in a way that parallels their effects on trans interactions.
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Supramolecular polymers are ideal systems to generate polyvalent architectures for studying and modulating these interactions: the inherent reversibility of the self-assembling process and the translation of monomers into polymers provide control over ligand density and assembly architecture.
We show that Pat-C is essential for the interaction with mRNA decapping factors (i.e. DCP2, EDC4 and LSm1 7), whereas the P-rich region and Mid domain have distinct functions in modulating these interactions.
In the past decade, our understanding of protein recognition has served as solid basis for the design of synthetic mimetics to modulate these protein protein interactions.
Together, these results raise the possibility that Ran can modulate the interactions between impβ and the NPC.
Different activation signals regulate ERM proteins functions by modulating these intramolecular interactions.
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