ArticleMethods in molecular biology (Clifton, N.J.)2017
Mass Spectrometry Analysis of Lysine Posttranslational Modifications of Tau Protein from Alzheimer's Disease Brain.
Article in Methods in molecular biology (Clifton, N.J.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Disease-specific tau polymorphs are associated with unique protein networks across proteinopathies.The EMBO journal · 2026Article
- Lysine methylation is an endogenous post-translational modifications of tau protein in human brain and a modulator of aggregation propensity.Methods in enzymology · 2026Article
- HDAC9-mediated calmodulin deacetylation induces memory impairment in Alzheimer's disease.CNS neuroscience & therapeutics · 2024Article
- Quantification of Methylation and Phosphorylation Stoichiometry.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Targeting amyloid proteins for clinical diagnosis of neurodegenerative diseases.Fundamental research · 2023Review
- Article
- DNA damage response and repair pathway modulation by non-histone protein methylation: implications in neurodegeneration.Journal of cell communication and signaling · 2020Review
- Quantification of Tau Protein Lysine Methylation in Aging and Alzheimer's Disease.Journal of Alzheimer's disease : JAD · 2019Article
- Review
- Protein SUMOylation modification and its associations with disease.Open biology · 2017Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Recent advances in mass spectrometry (MS)-based proteomics have greatly facilitated the robust identification and quantification of posttranslational modifications (PTMs), including those that are present at substoichiometric site occupancies. The abnormal posttranslational modification and accumulation of the microtubule-associated protein tau has been implicated in the pathogenesis of Alzheimer's disease (AD), and it is thought that the primary mode of regulation of tau occurs through PTMs. Several studies have been published regarding tau phosphorylation; however, other tau PTMs such as ubiquitylation, acetylation, methylation, oxidation, sumoylation, nitration, and glycosylation have not been analyzed as extensively. The comprehensive detection and delineation of these PTMs is critical for drug target discovery and validation. Lysine-directed PTMs including ubiquitylation, acetylation, and methylation play key regulatory roles with respect to the rates of tau turnover and aggregation. MS-based analytical approaches have been used to gain insight into the tau lysine-directed PTM signature that is most closely associated with neurofibrillary lesion formation. This chapter provides details pertaining to the liquid chromatography tandem mass spectrometry (LC-MS/MS)-based analysis of the lysine-directed posttranslational modification of tau.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.