Articles with "serine 408" as a keyword



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Serine 408 phosphorylation is a molecular switch that regulates structure and function of the occludin α-helical bundle

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Published in 2022 at "Proceedings of the National Academy of Sciences of the United States of America"

DOI: 10.1073/pnas.2204618119

Abstract: Significance Tight junctions form selectively permeable seals that limit paracellular flux. Increased tight junction permeability has been associated with intestinal disease. Previous studies indicate that casein kinase 2 (CK2) phosphorylates S408 within an unstructured region… read more here.

Keywords: tight junction; phosphorylation; helical bundle; serine 408 ... See more keywords