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These results identifying cell-type-specific functions and multiple presynaptic binding partners for different LRRTM family members reveal an unexpected complexity in the design and function of synapse-organizing proteins.
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One clear mechanism of modulation is through tyrosine phosphorylation acting as a molecular switch to regulate different binding partners for dystroglycan and hence control its function.
Their differences define the concentrations of binding partners for effectors whose binding site phosphorylations are described in different layers.
Through this approach, we identified different members of the mammalian ATG8 family of proteins as binding partners for the C-terminal domain of MAPK15, raising the possibility that this MAP kinase may be involved in the control of autophagy.
It is also notable that the binding partners for the Sp domains and CysR domain of the two aggrecanases, ADAMTS-4 and ADAMTS-5, are different in that the Sp domain of ADAMTS-4 binds to sulfated GAGs [ 27, 28].
We will discuss the binding partners for these motifs and how their interactions and regulation can modulate the involvement of dystroglycan in a range of different adhesion structures and functions depending on context.
These two proteins may represent novel binding partners for Tspan9.
Electrostatic interactions can facilitate macromolecular recognition by enhancing the collision frequency of the binding partners and by orienting the binding partners for subsequent short-range interactions.
At least 20 proteins (besides G-alpha subunits) have now been identified as direct binding partners for RGS proteins, and additional binding partners remain to be found [ 4].
We observed a strong reduction of HP1c mRNA in two different woc heteroallelic mutant backgrounds, suggesting that besides being a binding partner for Woc, HP1c is also transcriptionally regulated by Woc (Figure 3B).
Moreover, Smad1/Mad is a direct binding partner for YAP/Yki in both Drosophila and humans [11, 36].
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