Tight junction proteins at the blood–brain barrier: far more than claudin-5
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Cellular and Molecular Neuroscience,Pharmacology,Molecular Biology,Molecular Medicine
Link
http://link.springer.com/article/10.1007/s00018-019-03030-7/fulltext.html
Reference74 articles.
1. Krause G, Winkler L, Mueller SL, Haseloff RF, Piontek J, Blasig IE (2008) Structure and function of claudins. Biochim Biophys Acta 1778(3):631–645. https://doi.org/10.1016/j.bbamem.2007.10.018
2. Haseloff RF, Dithmer S, Winkler L, Wolburg H, Blasig IE (2015) Transmembrane proteins of the tight junctions at the blood–brain barrier: structural and functional aspects. Semin Cell Dev Biol 38:16–25. https://doi.org/10.1016/j.semcdb.2014.11.004
3. Maher GJ, Hilton EN, Urquhart JE, Davidson AE, Spencer HL, Black GC, Manson FD (2011) The cataract-associated protein TMEM114, and TMEM235, are glycosylated transmembrane proteins that are distinct from claudin family members. FEBS Lett 585(14):2187–2192. https://doi.org/10.1016/j.febslet.2011.05.060
4. Mineta K, Yamamoto Y, Yamazaki Y, Tanaka H, Tada Y, Saito K, Tamura A, Igarashi M, Endo T, Takeuchi K, Tsukita S (2011) Predicted expansion of the claudin multigene family. FEBS Lett 585(4):606–612. https://doi.org/10.1016/j.febslet.2011.01.028
5. Cording J, Berg J, Kading N, Bellmann C, Tscheik C, Westphal JK, Milatz S, Gunzel D, Wolburg H, Piontek J, Huber O, Blasig IE (2013) In tight junctions, claudins regulate the interactions between occludin, tricellulin and marvelD3, which, inversely, modulate claudin oligomerization. J Cell Sci 126(Pt 2):554–564. https://doi.org/10.1242/jcs.114306
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