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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 
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 
ProteomicsA model dataset for quantitative cross-linking/mass spectrometry using isotope-labeled cross-linkers
Dynamic proteins and multi-protein complexes govern most biological processes. Cross-linking/mass spectrometry (CLMS) is increasingly successful in providing residue-resolution data on static proteinaceous structures. In order to investigate the technical feasibility of recording dynamic processes u...
ORGANISM(S): Homo sapiens (Human) 
2016-05-06 | PXD004107 | Pride
Model dataset Isotope-labeled cross-linkers Hsa Quantitative cross-linking/mass spectromentry 
ProteomicsA Simple Cross-Linking/Mass Spectrometry Workflow to Study System-Wide Protein Interactions in Drosophila Embryos
We provide a cross-linking/MS workflow that can be applied to complex systems. The software tool MeroX 2.0 can be used to identify cross-linked peptide on a proteome-wide level. We applied the workflow to extracts of Drosophila embryos and identified 5,129 unique cross-linked residue pairs in biolog...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2019-07-09 | PXD012546 | Pride
Cross-linking Mass spectrometry Xlms Cxms Drosophila 
Proteomics"In-gel cross-linking mass spectrometry (IGX-MS) of proteins and protein complexes"
Cross-linking mass spectrometry has developed into an important method to study protein structures and interactions. The in-solution cross-linking workflows involve time and sample consuming steps and do not provide sensible solutions for differentiating cross-links obtained from co-occurring protei...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) Escherichia coli 
2020-12-14 | PXD020014 | Pride
Bn-page/ cross-linking/ protein complexes/ complement/ protein modeling 
ProteomicsOptimized cross-linking mass spectrometry for in situ interaction proteomics
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
Human Cross-linking mass spectrometry Chromatin 
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 
ProteomicsData independent acquisition cross-linking/mass spectrometry
Quantitative cross-linking/mass spectrometry (QCLMS) provides increasing structural detail on altered protein states in solution. Accurate quantitation is a value in itself but may also be central to elucidating small differences between protein states. Hence, QCLMS could benefit from data independe...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) Oryctolagus cuniculus (Rabbit) Gallus gallus (Chicken) Equus caballus (Horse) 
2019-01-25 | PXD011036 | Pride
Xi Reproducibility Spectronaut Data independent acquisition Label-free Mass spectrometry Quantitation Cross-linking 
ProteomicsCross-linking/mass spectrometry analysis of AUGMIN complex
We applied cross-linking/mass spectrometry to characterize in vivo Augmin from Drosophila in absence of any other structural information. The identified cross-links revealed topology of the Augmin complex and allowed us to predict potential interfaces between Augmin and γ-TuRC.
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2017-04-04 | PXD006246 | Pride
Augmin complex Cross-linking/mass spectromentry 
ProteomicsA simplified in vivo cross-linking mass spectrometry strategy for proteome-wide studies.
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
Click-chemistry Mass spectrometry Structural biology In vivo biochemistry Cross-linking 
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