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We predicted that FOG-1 and FOG-3, as terminal regulators of the sperm fate, might regulate a battery of gamete-specific differentiation genes.
We predicted that the FOG-1 and FOG-3 proteins, as terminal regulators of the sperm fate, might regulate a battery of gamete-specific differentiation genes.
Except for 30 known LIPUS-regulated genes, our study demonstrated for the first time that over 100 genes were related to the underlying molecular mechanism of LIPUS and suggested that LIPUS might regulate a transient expression of numerous critical genes in osteoblastic cells.
Such a mechanism could explain how inducible activation of GATA factors might regulate a more restrictive set of transcriptional targets.
It is possible that CTIP2 might regulate a subset of epithelial stem cell population in skin as well as in HNSCC.
Knocking-down basonuclin in mouse oocytes eliminated approximately one quarter of RNA polymerase I (Pol I) transcription foci, without affecting the BrU incorporation of the remaining ones, suggesting that basonuclin might regulate a subset of rDNA.
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It is currently unknown how calpain cleavage affects SMN function, however, it is tempting to speculate that calpain cleavage could lead to altered protein interactions or might regulate an activity of the SMN complex through incorporation of the cleavage products.
Notably, miR-2941 and miR-2952 share the first nine 5' nucleotides and thus, have the same seed (Table 2), suggesting these two miRNAs might regulate an overlapping set of target mRNAs.
Considering this, recent investigations suggested that miRNAs in collaboration with defined cardiac transcription factors might regulate directly a reprogramming process of a somatic cell type into another, adding a new exciting level for therapeutic intervention [ 121].
As a result of the architecture and the properties of the combined structure elements a functional macromolecule is obtained that might regulate accessibility to a central shape persistent macrocycle via reversible brush-coil transitions.
PKM2Q393K (Q393 is located on helix α14) is a SAICAR-insensitive mutant, suggesting that the compound might regulate PKM2 through both A-A′ and C-C′ interfaces.
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