ArticleAnalytical chemistry2025
Stabilizing Proteins by Chemical Cross-Linking: Insights into Conformation, Unfolding, and Aggregation Using Native Ion Mobility Mass Spectrometry.
Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Who cites it
1 citing paper in PubMed.
- Hyphenated Mass Spectrometry-Based Strategies for Characterizing Oligomers of α‑Synuclein in Parkinson's Disease.ACS central science · 2026Article
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Authors and funding
7 authors.
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Abstract
The function and stability of proteins depend on their three-dimensional structure, which includes conformational dynamics and potential self-assembly. Protein structural organization is particularly important in biotechnological applications, where protein integrity is often challenged by nonphysiological conditions, leading to disassembly, aggregation, and eventually the loss of function or activity. The use of chemical cross-linking strategies, such as the in situ cyclization of proteins (INCYPRO), can overcome these challenges, providing proteins and protein complexes with enhanced resistance to thermal and chemical stress. To probe how cross-linking affects protein structure and stability, we combined native ion mobility mass spectrometry (nIM-MS) and collision-induced unfolding (CIU). Here, we compare the wild-type (WT) and chemically cross-linked trimeric complex of
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