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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
Reanalysis of a synthetic crosslinked peptide library datasets with DSS (non-cleavable), DSSO and DSBU (MS-cleavable) cross linkers from Beveridge et al., Nat. Commun., 2020 (PXD014337)
ORGANISM(S): Streptococcus pyogenes ABC020006030 
2022-01-11 | PXD027159 | Pride
Protein cross-linking has assumed an irreplaceable role in structural proteomics. Recently, significant efforts have been made to develop novel MS-cleavable reagents. These cross-linkers enhance the reliability of cross-link identification. Presently, only water-insoluble MS-cleavable cross-linkers ...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2025-05-07 | PXD055284 | Pride
In this study, we introduce a new MS-cleavable cross-linker called disulfodisuccinimidyl dibutyric urea (DSSBU), which we developed in-house. DSSBU contains an N-hydroxysulfosuccinimide (sulfo-NHS) reactive group that primarily modifies lysine residues. It therefore serves as a water-soluble counter...
ORGANISM(S): Bos taurus (Bovine) 
2025-12-29 | PXD052450 | Pride
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