Publications by authors named "S Rychnovsky"

Article Synopsis
  • Cross-linking mass spectrometry (XL-MS) allows researchers to study protein-protein interactions (PPIs) by connecting nearby protein residues, providing insights into protein structure and interactions.* -
  • The new trioxane-based cross-linker TSTO targets three lysine residues at once, improving the identification of complex protein interactions by enabling clearer analysis through LC-MS.* -
  • This innovative approach enhances the spatial resolution of PPIs and offers new structural insights for protein complexes, paving the way for advancements in structural systems biology.*
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Sulfuric acid in the atmosphere can participate in acid-catalyzed and acid-driven reactions, including those within secondary organic aerosols (SOA). Previous studies have observed enhanced absorption at visible wavelengths and significant changes in the chemical composition when SOA was exposed to sulfuric acid. However, the specific chromophores responsible for these changes could not be identified.

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The development of MS-cleavable cross-linking mass spectrometry (XL-MS) has enabled the effective capture and identification of endogenous protein-protein interactions (PPIs) and their residue contacts at the global scale without cell engineering. So far, only lysine-reactive cross-linkers have been successfully applied for proteome-wide PPI profiling. However, lysine cross-linkers alone cannot uncover the complete PPI map in cells.

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The tumor suppressor p53 is the most frequently mutated protein in human cancer. The majority of these mutations are missense mutations in the DNA binding domain of p53. Restoring p53 tumor suppressor function could have a major impact on the therapy for a wide range of cancers.

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We report the first total synthesis of (2)-hydroxynorneomajucin, a norsesquiterpene derived from the genus. This natural product displays neurotrophic properties. Small molecule neurotrophins have potential as therapeutics in neurodegenerative diseases.

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