ArticleiScience2026
RAGE phosphorylation by CK2 in human epithelial cell model: Modulation of connexin 43 expression.
Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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9 authors.
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Abstract
The receptor for advanced glycation end products (RAGE) is a membrane protein involved in many diseases linked to epithelial dysfunction. Its activation mechanism remains unclear because RAGE lacks intrinsic kinase activity depending on other kinases for phosphorylation. Using an epithelial amniotic cell model (FL cells), researchers combined mass spectrometry, phosphorylation assays, microscale thermophoresis to show that RAGE intracellular domain binds to the α subunit of protein kinase CK2, leading to the phosphorylation of RAGE at serine 400. Ser400Ala mutation preserves CK2α binding but disrupts downstream signaling, altering phosphorylation of the transcription factors CREB (Ser133) and c-Jun (Ser63) after AGE ligands stimulation.
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