Year: 2025
Type: article
Abstract: Histone post-translational modifications (PTMs) serve as a crucial mechanism in epigenetic regulation and play a fundamental role in the regulation of biological activities. The complexity of histone modifications is remarkable, with over 30 types of modifications and hundreds of modification sites reported, which makes the development of global histone PTM analysis techniques critical. In recent years, with advancements in mass spectrometry technology, proteomics has emerged as a powerful tool for histone modification identification. By detecting mass shifts induced by PTMs, mass spectrometry enables the unbiased identification of multiple histone modification types, as well as the detection of new PTMs with unknown amino acid mass shifts. In this review, we focus on recent developments in mass spectrometry-based techniques for global histone PTM identification and summarize recently discovered new types of histone modifications.
Source: Scientia Sinica Chimica
Language: English
Subfield: Spectroscopy
Field: Chemistry
Domain: Physical Sciences
Open Access status: bronze
OpenAlex ID: W4408537368