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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 
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 
ProteomicsFolding of beta-tubulin by the chaperonin TRiC/CCT studied by chemical cross-linking and mass spectrometry
Chemical cross-linking coupled to mass spectrometry was used to study the folding of the client protein, beta-tubulin, by the chaperonin TRiC/CCT. Different complexes containing TRiC/CCT and/or the chaperone prefoldin were cross-linked in absence or presence of nucleotides with the homobifunctional,...
ORGANISM(S): Homo sapiens (Human) 
2022-12-08 | PXD030590 | Pride
Chemical cross-linking  dss  structural proteomics  protein folding Tric/cct  prefoldin  tubulin 
ProteomicsStructure of Cyanobacterial Phycobilisome Core Revealed by Structural Modeling and Chemical Cross-linking
In cyanobacteria and red algae, the structural basis dictating efficient excitation energy transfer from the phycobilisome (PBS) antenna complex to the reaction centers (RCs) remains unclear. PBS has several peripheral rods and a central core, which binds to the thylakoid membrane, allowing energy c...
ORGANISM(S): Synechocystis sp. PCC 6803 substr. GT-S 
2021-09-09 | PXD017873 | Pride
Phycobilisome core structure I-tasser Mass spectrometry Phycobilisome Protein structure prediction Protein cross-linking Photosynthesis   
ProteomicsCharacterizing the dynamic oligomerization of Hsp90β using photo-cross-linking
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
Hsp90 Cleavable cross-linkers Diazirine Photo-cross-linking 
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 
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 a complex between the chaperonin TRiC/CCT and its cochaperones, prefoldin and phosducin-like protein 2A
Chemical cross-linking coupled to mass spectrometry was used to study the architecture of the co-complex between TRiC/CCT, PFD and PhLP2A. The complex was cross-linked with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).
ORGANISM(S): Homo sapiens (Human) 
2023-12-11 | PXD040144 | Pride
Chemical cross-linking  dss  structural proteomics  protein folding  chaperonin  tric/cct  prefoldin  phosducin-like protein 2a 
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