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Post-translational modifications (PTMs) regulate protein homeostasis, but how aging impacts PTMs remains unclear. Here, we used mass spectrometry to reveal changes in hundreds of protein ubiquitylation, acetylation, and phosphorylation sites in the mouse aging brain. We show that aging has a major impact on protein ubiquitylation.

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The structural biology of deoxyhypusination complexes.

Structure

February 2025

Małopolska Centre of Biotechnology, Jagiellonian University, Kraków, Poland. Electronic address:

Deoxyhypusination is the first rate-limiting step of the unique post-translational modification-hypusination-that is catalyzed by deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). This modification is essential for the activation of translation factor 5A in eukaryotes (eIF5A) and Archaea (aIF5A). This perspective focuses on the structural biology of deoxyhypusination complexes in eukaryotic and archaeal organisms.

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Quantitative profiling of PTM stoichiometry by DNA mass tags.

Bioorg Med Chem

February 2025

Synthetic and Functional Biomolecules Center, Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China; Peking-Tsinghua Cente

Article Synopsis
  • Protein post-translational modification (PTM) is crucial for regulating protein function, and understanding the proportion of modified proteins, known as PTM stoichiometry, is important for studying these modifications.
  • The researchers developed a new method called "STO-MS+" that improves upon the original "STO-MS" technique by using a better mass tag and a label-free analysis to enhance measurement efficiency and precision.
  • STO-MS+ was successfully applied to measure the stoichiometry of three specific PTMs, showcasing significant advancements in the analysis of post-translational modifications in biological samples.
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Article Synopsis
  • Protein phosphorylation is essential for disease regulation and drug development but poses significant analytical challenges due to its complexity and low detectability.
  • The Chip-DIA strategy combines a phosphoproteomic chip with advanced mass spectrometry to enable highly sensitive analysis of phosphorylation at the single-cell level.
  • This approach successfully identified unique phosphoproteomic profiles in lung cancer, helping to uncover potential targeted therapies for resistant cancer subtypes and supporting precision oncology.
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Ribosomes are an archetypal ribonucleoprotein assembly. Due to ribosomal evolution and function, r-proteins share specific physicochemical similarities, making the riboproteome particularly suited for tailored proteome profiling methods. Moreover, the structural proteome of ribonucleoprotein assemblies reflects context-dependent functional features.

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