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ProteomicsAn Amphibious Bi-functional Probe For Protein Chemical Cross-linking.
Chemical cross-linking mass spectrometry (CXMS) has emerged as a powerful and well-established method for probing protein structure, conformational dynamics, and protein–protein interactions, particularly in cases where classical high-resolution techniques face intrinsic limitations. The development...
ORGANISM(S): Homo sapiens (Human) Equus caballus (Horse) 
2026-07-13 | PXD074784 | Pride
Togni reagents Radical labeling Chemical cross-linking Mass spectrometry Protein footprinting Fluoroalkylation : protein structure 
ProteomicsOn the reproducibility of label-free quantitative cross-linking/mass spectrometry
Quantitative cross-linking/mass spectrometry (QCLMS) is an emerging approach to study conformational changes of proteins and multi-subunit complexes. Distinguishing protein conformations requires reproducibly identifying and quantifying cross-linked peptides. Here we analyzed the variation between m...
ORGANISM(S): Homo sapiens (Human) 
2018-01-02 | PXD007250 | Pride
Cross-linking Mass-spectrometry Skyline Quatitation 
ProteomicsIn planta chemical crosslinking and mass spectrometry analysis of protein structure and interaction in Arabidopsis
Mass spectrometry analysis in combination with the site-specific chemical cross-linking has emerged as a powerful method in study of three-dimensional structure of protein complex and in mapping of protein-protein interactions (PPIs). Even though in vitro cross-linking experiments have been widely a...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2016-06-28 | PXD003658 | Pride
Arabidopsis Mass spectrometry Disuccinimidyl suberate In planta chemical cross-linking Interactomics Exhaustive cross-linked peptides identification tool 
ProteomicsIdentification of human PKD2 interaction partners from cytosolic protein fractions of HeLa cells by affinity enrichment cross-linking/MS
We investigated the interaction network of human PKD2 in the cytosol as well as in Golgi-enriched subcellular protein fractions, using an affinity enrichment strategy combined with chemical cross-linking/mass spectrometry (MS). Analysis of the subproteomes revealed the presence of distinct proteins ...
ORGANISM(S): Homo sapiens (Human) 
2016-09-27 | PXD003909 | Pride
Human Pkd2 Cross-linking/ms Affinity enrichment Orbitrap fusion 
ProteomicsIdentification of human PKD2 interaction partners from Golgi-enriched protein fractions of HeLa cells by affinity enrichment cross-linking/MS
We investigated the interaction network of human PKD2 in the cytosol as well as in Golgi-enriched subcellular protein fractions, using an affinity enrichment strategy combined with chemical cross-linking/mass spectrometry (MS). Analysis of the subproteomes revealed the presence of distinct proteins ...
ORGANISM(S): Homo sapiens (Human) 
2016-09-27 | PXD003913 | Pride
Human Pkd2 Hela cells Cross-linking/ms Affinity enrichment Golgi apparatus Orbitrap fusion 
ProteomicsAnalysis of bilirubin-induced bovine serum albumin stability using protein denaturation and quantitative cross-linking mass spectrometry
We report the combination of protein-denaturation stability principles with quantitative cross-linking mass spectrometry using isobaric quantitative protein interaction reporter technologies. This method enables the evaluation of ligand-induced protein engagement through analysis of cross-link rela...
ORGANISM(S): Bos taurus (Bovine) 
2024-07-03 | PXD036649 | Pride
Quantitative cross-linking Protein stability Mass spectrometry 
Proteomicscross-linking mass spectrometry of synaptosome
Cross-linking mass spectrometry data of synaptosome and microsome fractions of mouse cerebellum and hippocampus.
ORGANISM(S): Mus musculus (Mouse) 
2020-12-03 | PXD010317 | Pride
Synaptosome Microsome Cross-linking mass spectrometry 
Proteomicsmitochondria cross-linking mass spectrometry
We performed cross-linking mass spectrometry experiments on intact mitochondria isolated from mouse heart in two conditions, native-state and high-salt treatment to disrupt electrostatic interactions. Both conditions were provided in biological replicates.
ORGANISM(S): Mus musculus (Mouse) 
2017-12-11 | PXD006816 | Pride
Mouse Heart Cross-linking mass spectrometry Mitochondria 
ProteomicsInteractions of CDK19 with MED12 and cyclin-C assessed by chemical cross-linking mass spectrometry
Chemical cross-linking coupled to mass spectrometry was used to study binary and ternary complexes involving cyclin-dependent kinase 19 (CDK19), cyclin-C, and an N-terminal fragment of subunit 12 of the Mediator complex (MED12 1-100). Cross-linking was performed using disuccinimidyl suberate (DSS). ...
ORGANISM(S): Homo sapiens (Human) 
2020-05-18 | PXD019251 | Pride
Chemical cross-linking  dss  structural proteomics  mediator complex  kinase 
ProteomicscapsPASEF – Collisional Cross Section Assisted Precursor Selection Applied to Cross-linking Mass Spectrometry
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
Ion mobility Cross-linking mass spectrometry Xl-ms Phox 
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