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. 2018 Apr 27;50(4):53. doi: 10.1038/s12276-018-0079-0

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License, which permits any non-commercial use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. If you remix, transform, or build upon this article or a part thereof, you must distribute your contributions under the same license as the original. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/4.0/.

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Fig. 2 — a Schematic representation of the mutation in IPO13 (ENST00000372343, NM_014652) and functional domains. b Conservation analyses of the mutated residues 111 in IPO13 across different species. c Crystal structure modeling of IPO13 (Phyre2: template c2x19B_). The mutant protein containing R111C (red) shows an increase in the number of hydrogen bonds. d RT-PCR in mouse tissues shows high expression of Ipo13 in the cornea, sclera, lens, and retina. e Comparison of the IPO13 expression in the patient and normal control. The results from real-time quantitative PCR show that the IPO13 mRNA level (normalized to GAPDH) was approximately 43% lower in the patient than in the normal control (***P < 0.0001)