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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
A tetrameric CID-cleavable cross-linker was synthesized and applied to BSA and isolated mitochondria from mouse hearts. A real-time instrument method was developed to dynamically target released peptides from cross-linked species, enabling their characterization through a series of ms3 scans.
ORGANISM(S): Bos taurus (Bovine) Mus musculus (Mouse) 
2023-11-27 | PXD032222 | Pride
Even though the amine reactive BS2G and DSG cross-linkers have the same length of spacer and are based on N-hydroxysuccinimidic group, our data showed that each of them formed preferentially different cross-links. We demonstrated that the choice of cross-linker can have a significant impact on the o...
ORGANISM(S): Bos taurus (Bovine) 
2020-02-28 | PXD017299 | Pride
Cross-linking of BSA with a novel cross-linker. Modification of the cross-linker containing peptides with CuAAC-chemistry to attach a cleavable biotin-derivative. Enrichment with streptavidin-beads.
ORGANISM(S): Bos taurus (Bovine) 
2019-10-14 | PXD015080 | Pride
In order to develop a simplified cross-linking mass spectrometry protocol, we applied one-step size-exclusion chromatography (SEC) for peptide purification after proteolysis with Lys-C and trypsin. Three benchmark protein complexes (KMN, NDC80C, MIS12C) from human kinetochore were cross-linked with ...
ORGANISM(S): Homo sapiens (Human) 
2019-04-01 | PXD010070 | Pride
Cross-linking mass spectrometry (XL-MS) has made significant progress in understanding the structure of protein and elucidating architectures of larger protein complexes. Current XL-MS applications are limited to targeting lysine, glutamic acid, aspartic acid, and cysteine residues. There remains a ...
ORGANISM(S): Homo Sapiens 
2020-10-22 | PXD022121 |
A novel cross-linking strategy based on this cross-linker has been developed and demostrated, which provides a complementary XL-MS tool analyzing protein structure
ORGANISM(S): Homo Sapiens 
2022-12-03 | PXD036600 |
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
We introduce a complimentary, heterobifunctional, photoactivatable, benzophenone containing cross-linker and show its successful application to cross-linking/mass spectrometry, by increasing data density, when used alongside a previously developed diazirine-based heterobifunctional cross-linker.
ORGANISM(S): Homo sapiens (Human) 
2017-04-26 | PXD004920 | Pride
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