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By generating a homology model of LeuRS while in the editing conformation, we conclude that structural changes within the ZN-1 domain play a central role in LeuRS's catalytic cycle.
But it looks more like a domain play.
Being sparse, the coefficients in the transformed domain play a key role in the performance of any thresholding methods.
Furthermore, mutation experiments showed that both the RPEL-repeat domain and the PP1-binding domain play crucial roles in these morphological changes.
These results indicate that the HSPG binding domain play an important role for VEGF interactions on the surface of the cells.
Combined with our previous findings that deletion of the C-terminal sugar-binding domain of LevQ alone resulted in loss of function of this pathway [9], these results indicate that LevQ, and in particular its sugar-binding domain, play essential roles in the function of the LevQRST signal transduction complex.
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Recently, we observed that the KS domain plays a role in product processing27.
Another experiment replicated this effect in a different domain: playing a computer game.
SH3 domain plays an important role in maintaining autoinhibition of BCR-ABL protein.
It has been postulated that this hydrophilic domain plays an important role in controlling the self-assembly behavior of rM179.
We demonstrate that the ZN-1 domain plays a central role in the catalytic cycle of E. coli LeuRS.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com