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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 
ProteomicsDSSBU: novel cross-linker tested on bovine serum albumin and human hemoglobin
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
Dssbu Hemoglobin Xl-ms Ms-cleavable cross-linker Bsa 
ProteomicsNHS Carbamate Cross-Linkers Provide Complementary XL-MS Restraints via Preferential N-Terminal Targeting
Cross-linking mass spectrometry (XL-MS) has become a valuable tool for investigating the structural morphology and plasticity of proteins. Traditional cross-linkers contain two N-hydroxy succinimide (NHS) esters that mainly react with lysine residues. In this work, we optimized the in-solution react...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2026-03-30 | PXD069252 | Pride
Crosslinking ms Cross-linking ms Dsso carbamate Nhs carbamate cross-linkers N-terminal reactivity Xl-ms Cross-linking mass spectrometry Ms-cleavable cross-linkers 
ProteomicsReanalysis of a synthetic cross-linked peptide library with MaxLynx
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
Crosslinking 
ProteomicsCharacterizing the dynamic oligomerization of Hsp90β using photo-cross-linking
Cross-linking mass spectrometry (XL-MS) is a powerful tool for probing protein structures. While conventional chemical cross-linkers react with specific residues with defined chemistry, photo-cross-linkers, despite their superior reactivity, have been hindered by incomplete mechanistic understanding...
ORGANISM(S): Homo sapiens (Human) 
2026-04-09 | PXD072009 | Pride
Hsp90 Cleavable cross-linkers Diazirine Photo-cross-linking 
UnknownExploring Spacer Arm Structures for Designs of Asymmetric Sulfoxide-Containing MS-Cleavable Cross-Linkers.
Not available
S-EPMC7363200 | biostudies-literature
UnknownEvaluating Imide-Based Mass Spectrometry-Cleavable Cross-Linkers for Structural Proteomics Studies.
Not available
S-EPMC11350583 | biostudies-literature
UnknownDeveloping new isotope-coded mass spectrometry-cleavable cross-linkers for elucidating protein structures.
Not available
S-EPMC3985771 | biostudies-literature
Proteomics2) Twisting Urea- to Imide-Based Mass Spectrometry-Cleavable Cross-Linkers to Embed Affinity Tags
Disuccinimidyl dibutyric urea (DSBU) is a mass spectrometry (MS)-cleavable cross-linker that has been applied to multiple applications in structural biology, ranging from isolated protein complexes to comprehensive system-wide interactomics. DSBU facilitates a rapid and reliable identification of cr...
ORGANISM(S): Homo sapiens (Human) 
2024-09-03 | PXD050960 | Pride
Protein-protein interactions  structural proteomics Dsbu Cross-linking mass spectrometry  xlms Idp Intrinsically disordered protein 
UnknownDesign of CID-cleavable protein cross-linkers: identical mass modifications for simpler sequence analysis.
Not available
S-EPMC4581996 | biostudies-literature
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