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ROCKs are small guanosine triphosphate binding proteins which mediate smooth muscle contraction, cell migration, and proliferation by inhibition of eNOS [ 36].
Hearts rely predominantly on lipids for their energy supply [ 42] and FABP3 is the cardiac/muscle-isoform of fatty acid binding proteins, which mediate the intracellular transport of long-chain fatty acids.
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Pentatricopeptide repeat (PPR) proteins are a large family of modular RNA-binding proteins which mediate several aspects of gene expression primarily in organelles but also in the nucleus.
Furthermore, it interacts with nuclear and cytoplasmic cap-binding proteins which mediate additional 7mG functions (Table 1 and Figure 3).
CfrA (CJSA_0711) is the ferri-enterobactin receptor (Zeng et al. 2009); ChuA (CJSA_1526) is the heme-containing compound receptor and ChuZ (CJSA_1525) encodes an iron-responsive cellular hemoxygenase (Ridley et al. 2006); and P19 (CJSA_1570) is a periplasmic binding protein which mediates iron acquisition from the fungal hydroxamate siderophore ferri-rhodotorulic acid (Janvier et al. 1998).
8– 10 Activation of the mTOR pathway results in the phosphorylation of two downstream targets, the ribosomal p70 S6 kinase and the eukaryotic translation initiation factor 4E-binding protein, which mediate the translation of proteins involved in regulation of cell growth and proliferation.
As previous studies (Katz et al. 2008) have shown that the CreA DNA-binding protein, which mediates carbon catabolite repression, may modulate XprG activity, it is a likely candidate.
It is a member of the LOV-domain subfamily of PER, ARNT and SIM (PAS -domain PAS -domainich mediate both ligand binding and proteinsprotein interactions [ 18].
This gene product belongs to the 14-3-3 14-3-3 14-3-3teins which mediate signal transduction by binding to phosphoserine-containing proteins.
Subsequently, phosphorylated AS160 interacts with the 14-3-3 14-3-3 14-3-3sphoprotein-binding proteins, which is mainly mediated by phosphorylated Thr [ 4, 5].
These interactions are mediated by DNA-binding proteins, which have to deform the DNA.
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