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The phrase "a significant decrease in autophosphorylation of" is correct and usable in written English.
It can be used in scientific or technical contexts when discussing changes in the process of autophosphorylation, often in relation to proteins or enzymes.
Example: "The study revealed a significant decrease in autophosphorylation of the enzyme, indicating a potential alteration in its activity."
Alternatives: "a notable reduction in autophosphorylation of" or "a marked decline in autophosphorylation of".
Exact(1)
They demonstrated that treatment with mAb 806 resulted in a significant decrease in autophosphorylation of EGFRvIII and downstream molecule Bcl-XL, whereas the receptor level was only slightly decreased.
Similar(59)
A significant decrease in the DSL further contribute to the decrease of the E2E.
However, we also found a significant decrease of white-matter volumes and no significant decrease in total gray-matter volumes.
Single-agent trastuzumab at 1 μg/ml resulted in a moderate decrease in total levels of HER2, and, as expected, a more significant decrease in HER2 activity as reflected by the level of HER2 autophosphorylation.
However, it did result in a significant increase in the autophosphorylation of the catalytic subunit in oncogenic forms of p110α and elevation of autophosphorylation of all wt (wild-type) isoforms.
Also the exposure to PS caused a slight decrease in the autophosphorylation of FAK indicating for the deactivation of FAK and lowered adhesion to the extracellular matrix.
Ser does not therefore appear to be a significant site of autophosphorylation in eEF2K.
Compared with the wild type receptor, Ron∆1039 1047 exhibited a significant increase in receptor autophosphorylation, induced Erk phosphorylation and AP-1 transcriptional activity both in the presence and absence of MSP.
IGF-1-induced receptor activation results in autophosphorylation of cytoplasmic kinase domains and enhances their capability to phosphorylate downstream substrates.
RET protein dimerization results in autophosphorylation of several intracellular RET tyrosine residues, and these autophosphorylation sites serve as binding sites for a variety of docking proteins.
The S26D mutation mimicking the phosphorylated state of CaMKII causes a dramatic decrease in Thr autophosphorylation levels and greatly reduces the catalytic activity towards an exogenous substrate (autocamtide-3), whereas the S26A mutation has no effect.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com