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. 2020 Apr 17;11(4):238. doi: 10.1038/s41419-020-2421-4

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits 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. 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/4.0/.

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Fig. 5 — Schematic illustrations of the normal folding and functions of wild-type (WT) WRAP53β and molecular defects and functional consequences of the HHS mutations. WRAP53 mutations results in misfolding and destabilization of the WRAP53β protein and impair the binding to and trafficking of partner proteins and RNAs to correct cellular sites. Consequently, this perturbs maintenance of Cajal bodies, shortens telomeres and impairs DNA repair, thereby causing HHS.