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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 
ProteomicsXL-MS data analysis with MeroX and XlinkX
Comparison of MeroX in different modes and XlinkX upon variation of database size based on DSBU linked BSA as test-dataset
ORGANISM(S): Bos taurus (Bovine) 
2020-11-17 | PXD021648 | Pride
Mass-spectromerty Dsbu Xlinkx Merox Crosslinking 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 
ProteomicsInvestigation of interaction of p97, p37, PPI, SDS22 and Inhibitor-3 using cross-linking mass spectrometry (CL-MS)
In this project we investigated the complexes PPI/SDS22/Inhibitor-3 and p97/p37/PPI/SDS22/Inhibitor-3 by CL-MS using DSBU as crosslinker.
ORGANISM(S): Homo sapiens (Human) 
2024-11-22 | PXD026696 | Pride
Dsbu Ppi Inhibitor-3 Sds22 P97 
ProteomicsPRR of Tau Crosslinking with Tubulin
We used cross-linking mass spectrometry with the cleavable cross-linker, disuccinimidyl dibutyric urea (DSBU) to map sites of interaction between the proline rich domain (PRR, tau amino acids 149-244) and tubulin. For comparison, we also conducted these experiments with PRR constructs containing mul...
ORGANISM(S): Bos taurus (Bovine) Escherichia coli 
2026-03-09 | PXD049384 | Pride
Tubulin Tau Phosphorylation Proline rich region 
ProteomicsCharacterisation of BiP-GRP94-HT2 interaction
Characterization of the interaction of BiP-GRP94 in the presence and absence of HT2 using cross linking with DSBU and subsequent analysis of cross linked peptides by LC-MS/MS
ORGANISM(S): Mus musculus (Mouse) 
2025-07-14 | PXD059917 | Pride
Bip  grp94  cross linking ms  cl-ms  dsbu 
ProteomicsDSSBU: An MS-Cleavable Analogue of the BS3 Cross-Linker
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
Bsa Protein cross-linking Dssbu cross-linker 
ProteomicsReanalysis of a proteome-wide level study with MaxLynx
Reanalysis of the publicly available proteome-wide level dataset with DSBU from Goetze et al., Anal Chem. 2019 (PXD012546).
ORGANISM(S): Homo sapiens (Human) 
2022-01-11 | PXD027188 | Pride
Maxquant Cross-linking Maxlynx 
ProteomicsInteraction mapping of human condensin I and condensin II complexes using DSBU-cross-linking and mass spectrometry
Human condensin I and condensin II complexes play essential roles in chromatin condensation during the cell division process. Both complexes use ATP as the energy source to pack extended chromatin into the short form of chromosome. In order to understand the mechanism of their function, we performed...
ORGANISM(S): Homo sapiens (Human) 
2020-05-25 | PXD017531 | Pride
Condensin Dsbu Q-exactive Cross-linking Human Protein complex Xl-ms Chromatin Chromosome 
ProteomicsImproved peptide backbone fragmentation is the primary advantage of MS-cleavable crosslinkers
Proteome-wide crosslinking mass spectrometry studies have coincided with the advent of MS-cleavable crosslinkers that can reveal the individual masses of the two crosslinked peptides. However, recently such studies have also been published with non-cleavable crosslinkers suggesting that MS-cleavabil...
ORGANISM(S): Mus musculus (Mouse) Escherichia coli Drosophila melanogaster (Fruit fly) 
2022-06-24 | PXD032821 | Pride
Lc-msms Dsbu Ms-cleavable crosslinker Dsso Crosslinking Clms 
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