ArticleNature communications2025
Cysteine-enabled cleavability to advance cross-linking mass spectrometry for global analysis of endogenous protein-protein interactions.
Article in Nature communications, 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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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
1 citing paper in PubMed.
- Reprogramming the lipid peroxidation product 4-ONE as a chemoselective cleavable crosslinker.Nature communications · 2026Article
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Authors and funding
7 authors.
Funding
Abstract
Cross-linking mass spectrometry (XL-MS) is a powerful technology for probing protein-protein interactions (PPIs) and elucidating architectures of protein complexes at the systems level. While successful, the proteome coverage remains limited. To expand the scope of global PPI profiling, we introduce an innovative cysteine-based cleavable XL-MS platform using non-cleavable heterobifunctional lysine-cysteine (K-C) cross-linkers. The oxidation-induced transformation of cysteine cleavability enables unambiguous identification of cross-linked peptides. This strategy has been successfully applied to proteome-wide XL-MS analysis of intact cells, and its broad applicability has been demonstrated using three heterobifunctional cross-linkers. A total of 25,401 unique linkages from 2007 proteins have been identified, significantly expanding the existing XL-PPI map and increasing the interconnectivity of the human interactome. The XL-data generated here has been coupled with AlphaFold-based predictions and integrative modeling to reveal the structural characteristics of cellular networks, offering insights into the organization of native protein complexes in cells including the SERBP1-ribosome and eEF1A1-eEF1B complexes. Due to the effectiveness in modulating cysteine cleavability, our work presents an avenue for developing bifunctional/multifunctional cross-linking reagents to further advance XL-MS technologies. Additionally, the same strategy can be easily adapted to facilitate the characterization of cysteine modifications, reactivity and interactions to benefit chemical proteomics.
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