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. 2018 Oct 1;8(11):1804–1819. doi: 10.1002/2211-5463.12518

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© 2018 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.

This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Phosphorylation at Ser361 and C‐arrestin domain regulates the amount of p27^kip1. HuH‐ 7 cells were transfected with TXNIP or its mutants in the expression plasmids. Whole‐cell lysates (A), cytoplasmic and nuclear fractions (B) of the transfected HuH‐7 cells were prepared for western blots. The antibodies used in Western blots are indicated in the figure. (C) Statistical analysis of western blots for p27^kip1. Amount of p27^kip1 in the transfected cells (TXNIP wild‐type or its mutants) was compared with that of non‐transfected cells for cytoplasm and nuclei. The relative amounts of p27^kip1 are expressed as mean ± SD (*P < 0.05, t test, n = 4). GAPDH, glyceraldehyde 3‐phosphate dehydrogenase; WT, wild‐type.