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. 2011 Feb 3;6(2):e16654. doi: 10.1371/journal.pone.0016654

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Lin 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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(A) Examination of Akt activation. NRK-49f cells were incubated with 0 and 12 µM AA for 1, 3 and 6 h. The phosphorylated activation form of Akt was detected by immunoblotting. (B) The levels of phosphorylated PDK1 and PI3K-p85 were evaluated by Western Blot at indicated periods of AA treatment. (C) The interaction of phosph-PDK1 with Akt. After 1 h of 0 and 12 µM AA treatments, cells were immunoprecipitated with anti-Akt antibody. The immunoprecipitated pellets were further immnoblotted with anti-phospho PDK1 or anti-Akt antibody. The input and mouse IgG were served as positive and negative control, respectively.