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. 2021 Nov 26;53(11):1674–1682. doi: 10.1038/s12276-021-00709-5

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© The Author(s) 2021

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. 3 — Key etiological proteins of neurodegenerative diseases, such as tau, α-synuclein, HTT, and neurofilament, can be directly O-GlcNAcylated, and proteins, including amyloid-beta and TDP-43, are indirectly affected by O-GlcNAcylation. In neurodegenerative diseases, altered O-GlcNAcylation is detected, and this abnormal O-GlcNAc status and subsequent excessive phosphorylation can cause pathological protein aggregation, resulting in cellular toxicity in neurons.