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The VEGF pathway is inhibited by soluble VEGF receptors (soluble fetal liver kinase-1 [sFlk-1]) that bind VEGF and block its interaction with endothelial cells.
Proteins in the Grb and SCOS families bind directly to IR and block its interaction with downstream factors.
Specifically, mTORC1 and S6K can phosphorylate IRS-1 to block its interaction with the p85 regulatory subunit of PI3K to negatively regulate the insulin-signaling pathway (Gual et al., 2005).
Other RBPs recruit factors that bind to eIF4E and block its interaction with eIF4G.
sTNFRII binds directly to TNF to block its interaction with cell-surface TNF receptors and modulate the biological responses induced or regulated by TNF.
The inhibitor actions which target the VEGF/VEGFR pathway are divided into 2 categories at present: (1) combining with VEGF to block its interaction with the receptor.
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Indeed, it has been shown that Brm interacts with Cyclin E, that Mel-18, a human homologue of Posterior Sex Combs, interacts with Cyclin D2 possibly blocking its interaction with Cdks [56], [57] and we show here that the ETP Corto interacts with CycG.
PAQR3 has been found to inhibit p110α activity by blocking its interaction with p85.
Interestingly, Δ300 460 mutant retained the ability to bind SPOP, analogous to TRIM28, which inhibits TRIM24 ubiquitination without blocking its interaction with SPOP (Fig. 3h).
In this study, we describe the discovery of a novel series of inhibitors that targets HIV-1 NC protein by blocking its interaction with nucleic acids.
The current finding suggests that Irigenin binds to the C-C loop of EDA, thereby blocking its interaction with integrins on the cell surface and thus abrogating subsequent Epithelial-Mesenchymal transition.
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CEO of Professional Science Editing for Scientists @ prosciediting.com