Quantitative profiling of posttranslational modifications of pathological tau via sarkosyl fractionation and mass spectrometry
Author:
Funder
Foundation for the National Institutes of Health
Publisher
Springer Science and Business Media LLC
Subject
General Biochemistry, Genetics and Molecular Biology
Link
https://www.nature.com/articles/s41596-023-00939-z.pdf
Reference9 articles.
1. Arakhamia, T. et al. Posttranslational modifications mediate the structural diversity of tauopathy strains. Cell 184, 6207–6210 (2021).
2. Mair, W. et al. FLEXITau: quantifying post-translational modifications of Tau protein in vitro and in human disease. Anal. Chem. 88, 3704–3714 (2016).
3. Naseri, N. N., Wang, H., Guo, J., Sharma, M. & Luo, W. The complexity of tau in Alzheimer’s disease. Neurosci. Lett. 705, 183–194 (2019).
4. Schaffert, L. N. & Carter, W. G. Do post-translational modifications influence protein aggregation in neurodegenerative diseases: a systematic review. Brain Sci. https://doi.org/10.3390/brainsci10040232 (2020).
5. Wenger, K. et al. Common mouse models of tauopathy reflect early but not late human disease. Mol. Neurodegener. 18, 10 (2023).
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