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UnknownSulfoxide-diazirine (SODA) as a Cleavable Photoaffinity Group To Enable the Identification of Photolabeled Modification Sites via LC-MS<sup>3</sup>.
Not available
S-EPMC12416438 | biostudies-literature
ProteomicsSulfoxide-diazirine (SODA) as a cleavable photoaffinity group to enable identification of photolabeled modification sites via LC-MS3
Photoaffinity labeling is a common approach in chemical proteomics for identification of small molecule probe tar-gets. However, the modification site on the target protein remains difficult to identify, because of the probe modifica-tion and potential fragmentation during tandem mass spectrometry. ...
ORGANISM(S): Bos taurus (Bovine) 
2025-08-25 | PXD065837 | Pride
Sulfoxide-diazirine Photolabeleing Lc-ms3 Cleavable photoaffinity group 
UnknownEnabling Photoactivated Cross-Linking Mass Spectrometric Analysis of Protein Complexes by Novel MS-Cleavable Cross-Linkers.
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S-EPMC8214149 | biostudies-literature
ProteomicsEnabling Photoactivated Cross-linking Mass Spectrometric Analysis of Protein Complexes by Novel MS-cleavable Cross-linkers
Cross-linking mass spectrometry (XL-MS) is a powerful tool for studying protein-protein interactions and elucidating architectures of protein complexes. While residue-specific XL-MS studies have been very successful, accessibility of interaction regions non-targetable by specific chemistries remain ...
ORGANISM(S): Bos taurus (Bovine) Saccharomyces cerevisiae (Baker's yeast) 
2021-05-07 | PXD022690 | Pride
26s proteasome Photocross-linking Sdaso Bsa 
ProteomicsU1 snRNP and RNA polymerase II interaction is predominantly mediated by Prp40 rather than U1-70K in yeast
Transcription and splicing are coupled both temporally and physically. A previous cryo-EM structure of the human U1 snRNP and RNA polymerase pol II complex has shown that U1 snRNP uses predominantly the RRM domain of U1-70K to directly interact with the RPB2 subunit of pol II. However, residues on U...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2026-05-20 | PXD078573 | Pride
Yeast Spliceosome Splicing Pol ii Snrnp Prp40 
ProteomicsSUMO-2 activity is inhibited by non-covalent interactions with the Aβ peptide: an exploration of potential pathogenic mechanisms in Alzheimer’s Disease
SUMOylation is a post-translational modification involving the addition of SUMO isoforms to target proteins and plays a role in various biological processes, including neurodegenerative diseases and ocular pathologies. This study investigates the interaction between SUMO-2 and amyloid (Aβ) peptides,...
ORGANISM(S): Homo sapiens (Human) 
2025-08-25 | PXD066055 | Pride
Aβ Protein protein interactions Crosslinking ms Alzheimer’s disease Xl-ms Sumo-2 Cross-linking mass spectrometry 
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