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Title XMAP215 is a microtubule nucleation factor that functions synergistically with the γ-tubulin ring complex.
XMAP215 is a microtubule nucleation factor that functions synergistically with the γ-tubulin ring complex.
MEC-6 increases amiloride-sensitive Na+ currents produced by MEC-4(d)/MEC-10(d) by approximately 30-fold, and functions synergistically with MEC-2 (a stomatin-like protein that regulates MEC-4(d)/MEC-10(d) channel activity) to increase the currents by 200-fold.
The crystallographic structure of the complex with DNA suggests that the tetrameric repressor functions synergistically with catabolite gene activator protein (CAP) and participates in the quaternary formation of repression loops in which one tetrameric repressor interacts simultaneously with two sites on the genomic DNA.
C/EBPα also functions synergistically with PPARγ to promote the expression of genes found in both BAT and WAT [11] as well as PGC-1α and UCP1, which are preferentially or exclusively expressed in brown adipocytes.
The downregulation of miR-17 may represent an explanation for the effectiveness of these drugs in specific hematologic malignancies that are dependent on Myc pathway deregulation for their pathogenesis (e.g. chronic lymphocytic leukemia and aggressive lymphomas), since miR-17 functions synergistically with Myc to promote aggressive tumor growth in lymphoma[14].
Similar(41)
Overall, our results indicate the PUF60 and U2AF65/35 function synergistically in splicing, but are also able to functionally replace each other in the splicing of some, but not all substrates.
Proteins function synergistically in development, metabolism and signaling.
In contrast, a different study argues that it is still needs to be determined whether the constituents of a SE function synergistically or additively63.
Specifically, using next-generation RNA sequencing (RNA-Seq), we found that Set5 and Set1 function synergistically to regulate specific transcriptional programs at subtelomeres and transposable elements.
When incubated in combination with Xyn10D-Fae1A, Xyl3A improved the release of xylose monomers from a hemicellulosic xylan substrate, suggesting that these two enzymes function synergistically to depolymerize xylan.
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