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Cross-linking mass spectrometry (XL-MS) is becoming a more popular tool for researchers to turn towards for studying proteins and their complexes of interest especially in complex samples such as lysates or whole-cells. Studying a targeted proteins in a complex mixture can be difficult as data on ot...
ORGANISM(S): Neisseria meningitidis serogroup C (strain 8013) Bacteria 
2024-02-07 | PXD045792 | Pride
Protein-protein interactions (PPIs) underpin nearly all cellular processes; therefore, mapping PPI and protein-protein association networks is critical for understanding how biological systems function in health and disease. However, many functionally relevant PPIs are transient and mediated by weak...
ORGANISM(S): Homo sapiens (Human) 
2026-05-27 | PXD064228 | Pride
ecent development of mass spectrometer cleavable protein cross-linkers and algorithms for their spectral identification now permits large-scale cross-linking mass spectrometry (XL-MS). Here, we optimized the use of cleavable disuccinimidyl sulfoxide (DSSO) cross-linker for labeling native protein co...
ORGANISM(S): Homo sapiens (Human) 
2019-04-03 | PXD010796 | Pride
Ion mobility separates molecules in the gas-phase on their physico-chemical properties, providing information about their size as collisional cross-sections. The timsTOF Pro combines trapped ion mobility with a quadrupole, HCD cell and a time-of-flight mass spectrometer, to interrogate ions at high ...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2020-07-22 | PXD018189 | Pride
Chemical cross-linking (XL) coupled to mass spectrometry (MS) has become a powerful approach to probe the structure of protein assemblies. Although most of the applications concerned purified complexes, latest developments focus on large-scale in vivo studies. Pushing in this direction, we describe ...
ORGANISM(S): Neisseria meningitidis Bacteria 
2021-02-25 | PXD021553 | Pride
Cross-linking Mass Spectrometry (XL-MS) is a powerful tool for examining protein structures and interactions. Nevertheless, anal-ysis of low-abundance cross-linked peptides is often limited in data-dependent acquisition (DDA) mode due to its semistochastic nature. To address this issue, we introduce...
ORGANISM(S): Homo Sapiens Saccharomyces Cerevisiae 
2023-06-26 | PXD043282 |
The analysis of proteins and protein complexes by cross-linking mass spectrometry (XL-MS) has expanded in the last dec-ade. However, mostly used approaches suffer important limitations in term of efficiency and sensitivity. We describe here a new workflow based on the advanced use of the trifunction...
ORGANISM(S): Oryctolagus cuniculus (Rabbit) 
2021-08-11 | PXD010422 | Pride
The combination of cross-linking/mass spectrometry (XL-MS) and ion mobility is still underexplored for conducting protein conformational and protein-protein interaction studies. We present a method for analyzing cross-linking mixtures on a timsTOF Pro mass spectrometer that allows separating ions ba...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) Escherichia coli 
2022-03-17 | PXD027234 | Pride
We developed an in situ cross-linking coupled reversed-phase liquid chromatography-based co-fractionation mass spectrometry (XL-CoFrac-MS) platform to analyze drug-induced protein complex changes. A software tool, ChromaQuant, was built to automate chromatographic peak quantification. Using RS4;11 l...
ORGANISM(S): Homo Sapiens 
2025-08-23 | PXD067673 |
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
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