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. 2024 Jul 30;19:449. doi: 10.1186/s13018-024-04928-0

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — Analysis of polydactyly related to GLI3 reported in other studies. (A) Variants of the GLI3 protein have been reported. (B) Types of GLI3 variants involved in polydactyly. (C) Polydactyly types caused by GLI3 variants. (D) Polydactyly types caused by GLI3 truncation variants. (E) Types of GLI3 variants involved in isolated polydactyly. RD = repressor domain; SUFU = SUFU site; ZFN = zinc finger domain; CS = cleavage site; CBD = CREB-binding protein (CBP) domain; TAD = transactivation domain; TA1 = transactivation domain 1; TA2 = transactivation domain 2