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. 2008 Feb 6;3(2):e1554. doi: 10.1371/journal.pone.0001554

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Wang et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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An alanine scan of the FLNA_2561–2565 pentapeptide (VAKGL) shows that residue of FLNA_2561–2565 is critical for NLX binding. All other individual alanine substitutions only mildly attenuated [³H]NLX binding to FLNA in A7 membranes. n = 6. * p<0.01 compared to vehicle.