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TRAF6 may mediate interaction of active TBK1/IKKi with IRF7 but not with IRF3.
Suppression of BRCA1-induced lethality in spt4Δ and spt5 yeast strains suggests that the DSIF complex may mediate interaction of BRCA1 with RNAPII.
It is these TPRs that are postulated to form complimentary interacting surfaces for their TBDR partners, but we also posit that this may mediate interaction with the cognate sialidase NanH as well.
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In addition, recent data have suggested that paracrine Hh signaling may mediate interactions between tumor cells and non-transformed stromal cells through multiple mechanisms [5], [26], [41], [42].
Nevertheless, it is not clear so far, if there is a limited repertoire of structurally conserved motifs that may mediate interactions among death domain superfamily members.
The high degree of conservation of cysteine residues in these extracellular domains suggests that the tertiary structure of this region is critical for the function of most channel subunits and may mediate interactions with extracellular structures.
The FDF domain may mediate interactions that are specific to these RNP complexes.
Furthermore, it may be speculated that the ARM repeats may mediate interactions with large number of proteins, conferring substrate versatility to the proteasomal degradation pathway.
These hub SNPs may mediate interactions at an unknown gene regulatory level, e.g. as non-coding RNAs, miRNAs or cis-regulatory elements.
This indicates that the N-terminal half of Swr1 extends across the complex and may mediate interactions between the N-Module and the Rvb1/Rvb2 ring.
The MRG domain is less well characterized, but it has been reported to contain HLH and leucine-zipper motifs, suggesting that the MRG domain may mediate interactions with other proteins (Bertram and Pereira-Smith 2001; Chen et al. 2010).
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