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Ion mobility spectrometry shows great promise to tackle analytically challenging research questions by adding another separation dimension to liquid chromatography-mass spectrometry. The understanding of how analyte properties influence ion mobility has increased through recent studies but no clear ...
ORGANISM(S): Homo Sapiens (human) Cellular Organisms 
Ion mobility spectrometry shows great promise to tackle analytically challenging research questions by adding another separation dimension to liquid chromatography-mass spectrometry. The understanding of how analyte properties influence ion mobility has increased through recent studies but no clear ...
ORGANISM(S): Homo Sapiens (human) 
Crosslink mass spectrometry datasets on sulfo-SDA-crosslinked affinity-purified RNA polymerase binders from SPA-pulldowns in E. coli K12, on rpoB-SPA / nusG-SPA / yacL-SPA. Cleared E. coli lysate was added to anti-FLAG M2 beads to isolate binders to rpoB (RNA polymerase), nusG or yacL (RNA polymer...
ORGANISM(S): Escherichia Coli 
Quantitative proteomics dataset on soluble, affinity-enriched proteins from SPA-pulldowns in E. coli K12, on rpoB-SPA / nusG-SPA / yacL-SPA. This data was used to identify proteins for enrichment analysis and subsequent crosslinking mass spectrometry search (DB creation). Cleared E. coli lysate was ...
ORGANISM(S): Escherichia Coli 
Crosslink mass spectrometry dataset on soluble, SEC-fractionated high-molecular weight proteome of E. coli, crosslinked with BS3 or DSSO. This data was used to identify protein-protein interactions and to obtain information on protein (complex) topologies. In the end, the data was used for finding ...
ORGANISM(S): Escherichia Coli 
Quantitative proteomics dataset on soluble, SEC-fractionated high-molecular weight proteome of E. coli for protein coelution analysis. This data was used to identify proteins for a subsequent crosslinking mass spectrometry search (DB creation) and to correlate protein elution behaviour to validate/...
ORGANISM(S): Escherichia Coli 
Protein glycosylation, a complex and heterogeneous post-translational modification that is frequently dysregulated in disease, has been difficult to analyse at scale. Here we report a data-independent acquisition technique for the large-scale mass-spectrometric quantification of glycopeptides in pla...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-05-29 | MSV000089567 | MassIVE
The role of plasma and serum proteomics in characterizing human disease, identifying biomarkers, and advancing diagnostic technologies is rapidly increasing. However, there is an ongoing need to improve proteomic workflows in terms of accuracy, reproducibility, platform transferability, and cost-eff...
ORGANISM(S): Homo sapiens (Human) 
2025-12-29 | PXD070765 | Pride
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