Clinical Epigenetics · 2024 · 15 citations · 65 references
Life SciencesMolecular BiologyNeurobiologyMolecular NeurobiologyPost-translational ModificationProteomicsHistone ModificationsHistone Post-translational ModificationsMass Spectrometry-based ProteomicsNeurodegenerative DiseasesNeurodegenerative DisordersPost-translational RegulationAlzheimer Disease EpigeneticsAlzheimer Disease ProgressionHistone AcetylationHistone ProteomicsMass Spectrometry ProteomicsNeurodegenerative Disease EpigeneticsPeptide Mass SpectrometryPost-translational Histone Modifications
Alzheimer's disease (AD) has a complex pathogenesis, and multiple studies have indicated that histone post-translational modifications, especially acetylation, play a significant role in it. With the development of mass spectrometry and proteomics, an increasing number of novel HPTMs, including lactoylation, crotonylation, β-hydroxybutyrylation, 2-hydroxyisobutyrylation, succinylation, and malonylation, have been identified. These novel HPTMs closely link substance metabolism to gene regulation, and an increasing number of relevant studies on the relationship between novel HPTMs and AD have become available. This review summarizes the current advances and implications of novel HPTMs in AD, providing insight into the deeper pathogenesis of AD and the development of novel drugs.
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