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. 2023 Jun 26;14:1183101. doi: 10.3389/fphys.2023.1183101

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Copyright © 2023 Bez Batti Angulski, Hosny, Cohen, Martin, Hahn, Bauer and Metzger.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Full-length dystrophin and representative truncated dystrophins currently in use in clinical trials. (A) Full-length dystrophin versus (B) the truncated dystrophin constructs: i) mini-dystrophin Δ3990, ii) microdystrophin ΔR4-23/ΔCT (µDysH2) and iii) microdystrophin μDys-5R. Domains are identified as the N-terminal actin-binding domain, 1–24 spectrin-like repeats, four hinges (H1–H4), a cysteine-rich domain, and a C-terminal domain (CTD). The nNOS-binding domain is shown by the red numbers (repeats 16 and 17).