GRP78 translocation to the cell surface and O-GlcNAcylation of VE-Cadherin contribute to ER stress-mediated endothelial permeability
Author:
Funder
International Retinal Research Foundation
U.S. Department of Health & Human Services | NIH | National Eye Institute
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-019-47246-w.pdf
Reference51 articles.
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3. Kimata, Y., Ishiwata-Kimata, Y., Yamada, S. & Kohno, K. Yeast unfolded protein response pathway regulates expression of genes for anti-oxidative stress and for cell surface proteins. Genes Cells 11, 59–69, https://doi.org/10.1111/j.1365-2443.2005.00921.x (2006).
4. Chatham, J. C., Not, L. G., Fulop, N. & Marchase, R. B. Hexosamine biosynthesis and protein O-glycosylation: the first line of defense against stress, ischemia, and trauma. Shock 29, 431–440, https://doi.org/10.1097/shk.0b013e3181598bad (2008).
5. Steentoft, C. et al. Mining the O-glycoproteome using zinc-finger nuclease-glycoengineered SimpleCell lines. Nat Methods 8, 977–982, https://doi.org/10.1038/nmeth.1731 (2011).
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