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The main substrates of PTEN are phosphoinositides, particularly phosphatidylinositol-3,4,5-triphosphate (PIP3) whose intracellular levels are reduced following its dephosphorylation by PTEN to a diphosphate product (PIP2), and consequently AKT kinase activity and signaling are restrained.
The main substrates of PTEN are inositol phospholipids generated by the activation of PI3K [ 33].
Glutamine, instead, though nonessential, represents the most abundant amino acid in the human body and one of the main substrates of anaplerotic reactions fuelling the TCA cycle.
It is known that P-AMPK is also an inhibitory molecule of the mTOR pathway; thus, we analysed the phosporylation state of p70S6K and 4EBP1, the two main substrates of mTOR.
The maturation of flax phloem fibres involves the deposition and later degradation of a large galactan-rich polysaccharide [ 57], which is likely one of the main substrates of these BGAL proteins.
However, SET7/9 exhibits only weak lysine methyltransferase activity towards H3 in nucleosomes in vitro, suggesting that additional factors may affect SET7/9-dependent H3K4 methylation in vivo, or that histone proteins are not the main substrates of SET7/9.
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Phosphatidylinositol 3-phosphate (PtdIns3P) is a main substrate of myotubularin and is produced by PI3-kinases including class II PI3KC2Β.
Experiments were conducted for one year in eight VFPCWs, the main substrate of which consisted of river sand at four of the wetlands, or a mixture of sand and dolomite (10 1 weight ratio) at the other four wetlands.
Because oxygen is the main substrate of the ETC, hypoxic conditions consequently decreases mitochondrial function and initiates expression of a host of genes that are needed for compensatory ATP production by glycolysis.
Most importantly, these treatments were not effective for eliminating very low-molecular-mass DNA fragments (shorter than 200 bp), the main substrate of ancient and often forensic DNA analyses (e.g., [44], [45]).
Since pyruvate is the main substrate of brain mitochondria [31], extramitochondrial Ca2+ is able to adjust the supply of OXPHOS with its main substrates precisely and reversibly, like a physiological "gas pedal", acting in response to distinct, Ca2+-mediated cellular demands.
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