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These data suggest that DNA methylation and the associated methyl-DNA binding proteins may not play a critical role in determining histone modification patterns on the mammalian inactive X chromosome at the sites analyzed.
Our results indicate, however, that these histones do have modifications typical of silenced genes, suggesting that methyl-DNA binding proteins may not be critical with respect to histone modification on the inactive X chromosome.
This could be because the mammalian response element is ineffective in plants or alternatively it may be due to the positioning of the augmented response elements close to the transcription start site where cGMP activated DNA binding proteins may not correctly modulate the transcriptional machinery as the cGMP response element is over 1000 bp upstream of NPR1/GCA in the mammalian system [ 22, 37].
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To the rescue is a recent demonstration that IAP-binding proteins may not necessarily require an IBM for their apoptogenic potential and therefore their apoptotic function is not mediated only through an interaction with the IAPs [18].
Interestingly, the term 'nucleic acid binding' suggests that the binding capabilities of LCR proteins may not be restricted to protein-protein interactions.
We further consider that the identified ice-binding residues of these proteins may not be identical to the residues that interact with the hydrate surface, but the way is now clear for such an investigation.
Alternatively, binding to certain FH family proteins may not be essential to the spirochetes, as previous studies indicate that B. burgdorferi are able to infect and cause disease in FH-deficient mice [57].
However, when measuring high molecular weight proteins these techniques may not be applicable because the proteins of interest may be bound to binding proteins in vivo, recombinant proteins may not have the same properties as the natural proteins in vivo, and plasma and tissue levels of the protein are not equal.
Furthermore, the common binding partners of TLR1 and TLR6, which drive the coevolution of these proteins, may not be the same as the binding partners of TLR10.
Clearance of cytokine binding proteins may be important in the resolution of inflammation.
This may not be surprising as most of the viral envelope proteins may not be folded properly in our YTH screen system, and therefore, may not possess the correct conformations for binding and interactions.
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