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. 2025 Feb 18;32:29. doi: 10.1186/s12929-025-01118-w

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© The Author(s) 2025

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. 6 — Quantitative analysis of autophagy and mitophagy proteins in VEH and NAC treated IM muscle. A Representative immunoblots of whole muscle lysates. GAPDH shown as a loading control for whole muscle lysates. B Quantitative analysis of SQSTM1, LC3B-I, LC3B-II, LC3B-II:I, and 4HNE from whole muscle lysates. C Quantitative analysis of PPARGC1A, TFAM, BNIP3, and BNIP3L from whole muscle lysates. D Quantitative analysis of OPA1, MFN2, DNM1L, VDAC1, ANT1, CYCS, SOD1, and SOD2 from whole muscle lysates. E Representative immunoblots of mitochondrial fractions. GAPDH (cytosolic) and SOD2 (mitochondrial) shown to confirm purity of mitochondrial fraction. F Quantitative analysis of LC3B-II and BNIP3 from mitochondrial-enriched fractions. * p < 0.05 compared to VEH group. n = 5–10 per group