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. 2019 Oct 15;151(12):1347–1356. doi: 10.1085/jgp.201812264

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© 2019 Twomey et al.

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Figure 5. — Sequence alignment for claudins and claudin-fold AMPAR auxiliary subunits. The secondary structure of STZ is shown above the sequence alignment as cylinders (α-helices), arrows (β-strands), or lines (loops). Completely conserved residues are highlighted in yellow. Mostly conserved residues are highlighted in blue (or green for homologous residues). Conserved cysteines forming a disulfide bridge between β3 and β4 are connected by a red bracket. The C-terminal residues are excluded.