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The present structural results convey a simultaneous description of both binding partners of an LRP ligand complex and open a route to a broader understanding of the binding specificity of the LRP receptor, which may involve a general four-residue receptor ligand recognition motif common to all LRP ligands.
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Under these specialized conditions, one might intuitively expect diffusion of both binding partners to be slowed, as the authors suggest.
Although the structural epitopes of BMPR-IA to both binding partners coincides, the structures of BMPR-IA in the two complexes differ significantly.
From chemical shift perturbations of both binding partners upon complex formation, a HADDOCK model of the complex between CR56 and RAPd1 has been obtained.
The Aβ:ZAβ3 interaction is characterized by extensive coupled folding and binding of both binding partners [ 33, 42].
Thus, we set out to identify the targets of Id inhibition by determining the direct binding partners of both Id and E proteins in ESCs.
Thus, we investigated binding partners of both the longest (Oxr1-FL) and the shortest (Oxr1-C) TLDc-containing isoforms of Oxr1 for a comprehensive study.
We initially identified both FTH1 and FTL as binding partners of NCOA4 and confirmed a reciprocal interaction by FTH1 pulldown (Mancias et al., 2014).
However, as Dact proteins are shared binding partners of both Dvl2 and Sestd1,, it remained possible that the Sestd1-Dvl2 complex formation observed in these cells might occur indirectly via mutual binding to endogenous Dact proteins.
We found that the overexpressed HA-zMcl1a and HA-zMcl1b were co-immunoprecipitated with zNoxa in embryonic cells, indicating that both zMcl1a and zMcl1b were binding partners of zNoxa.
Cul-3 binds to Kel in tissue culture (Hudson and Cooley, 2010): we confirmed this, finding that both Dbo and Kel were binding partners of Cul-3 in Drosophila S2 cells (Fig. 3B).
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