Sort   by:  
 Page size 
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 
ProteomicsCross-linking mass spectrometry analyses of three different kinetochore protein complexes (KMN, NDC80C, MIS12C) using an MS-cleavable cross-linker, BuUrBu (DSBU)
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
Dsbu Q-exactive Cross-linking ms Buurbu Merox Human Kinetochore Protein complex Ms-cleavable cross-linker 
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 
ProteomicsA Glycosidic-Bond-Based Mass-Spectrometry-Cleavable Cross-linker Enables In Vivo Cross-linking for Protein Complex Analysis
Chemical cross-linking mass spectrometry (CXMS) has emerged as a powerful technology to analyze protein complex structure and interaction. However, the spectral fragmentation behavior and spectral data retrieval of cross-linked peptides are more complex than single peptides. In this study, we design...
ORGANISM(S): Homo Sapiens Saccharomyces Cerevisiae 
2023-12-06 | PXD047554 |
UnknownDeveloping an Acidic Residue Reactive and Sulfoxide-Containing MS-Cleavable Homobifunctional Cross-Linker for Probing Protein-Protein Interactions.
Not available
S-EPMC4989248 | biostudies-literature
UnknownDevelopment of a Novel Sulfoxide-Containing MS-Cleavable Homobifunctional Cysteine-Reactive Cross-Linker for Studying Protein-Protein Interactions.
Not available
S-EPMC6037416 | biostudies-literature
ProteomicsCross-linking mass spectrometry analysis of human ADAR1 deaminase domain WT using an MS-cleavable cross-linker, DSBU
Cross-linking mass spectrometry analysis of human ADAR1 deaminase domain WT protein (hADAR1d WT) was carried out using an MS-cleavable cross-linker, DSBU, to support the homology model structure of hADAR1d WT.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-08-21 | MSV000085996 | MassIVE
ProteomicsTrioxane-based MS-cleavable Cross-linking Mass Spectrometry for Profiling Multimeric Interactions of Cellular Networks
Here, we present a novel trioxane-based MS-cleavable homotrifunctional cross-linker TSTO, which can target three proximal lysine residues simultaneously. Owing to its unique structure and MS-cleavability, TSTO enables fast and unambiguous identification of cross-linked peptides using LC-MSn analysis...
ORGANISM(S): Homo sapiens (Human) 
2025-05-30 | PXD054551 | Pride
Tsto Xl-ms Cross-linking mass spectrometry 
ProteomicsTrioxane-based MS-cleavable Cross-linking Mass Spectrometry for Profiling Multimeric Interactions of Cellular Networks
Here, we present a novel trioxane-based MS-cleavable homotrifunctional cross-linker TSTO, which can target three proximal lysine residues simultaneously. Owing to its unique structure and MS-cleavability, TSTO enables fast and unambiguous identification of cross-linked peptides using LC-MSn analysis...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-30 | PXD063825 | Pride
Tsto Xl-ms Lc-msn 
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 
Sort   by:  
 Page size