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Binding partners that release WASp family proteins from their autoinhibited, conformationally closed state make them better substrates for tyrosine kinases by exposing a buried tyrosine that is the target of these kinases (33, 34).
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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.
In these experiments, we looked for ER-resident interaction partners that release very shortly after application of ER stressors.
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.
Likely it requires binding partners that aid in vesicle nucleation, localization, targeting and recycling.
We identified p33ING1 as a binding partner that interacts with CSIG.
This suggests that other binding partners exist that could modulate the IKK complex activity and function.
After immunoprecipitation, crosslinked binding partners are selectively released and all other components of the procedure (i.e. beads, antibody, and p120 itself) are discarded.
A consensus sequence for Arc binding identifies several additional partners that include genes implicated in schizophrenia.
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CEO of Professional Science Editing for Scientists @ prosciediting.com