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ProteomicsA systematic evaluation of fragmentation methods for unlabeled and isobaric mass tag-labeled O-glycopeptides
Dissecting site-specific functions of O-glycosylation requires simultaneous identification and quantification of differentially ex-pressed O-glycopeptides by mass spectrometry. However, different dissociation methods have not been systematically compared in their performance in terms of identificati...
ORGANISM(S): Homo sapiens (Human) 
2021-11-25 | PXD025407 | Pride
Glycoproteomics Hcd Etd Lc-ms/ms 
ProteomicsAn optimised fragmentation regime for cross-linking/mass spectrometry
In this study we compared three different fragmentation techniques and two combined fragmentation schemes available on a novel tribrid mass spectrometer (Orbitrap Fusion Lumos, Themro Fisher Scientific) CID, HCD, ETD, ETD with supplemental CID (ETciD) and ETD with supplemental HCD (EThcD) on cross-l...
ORGANISM(S): Homo sapiens (Human) 
2016-08-02 | PXD003737 | Pride
Etcid Cid Cross-linking Ethcd Hcd Etd 
ProteomicsBenchmarking multiple fragmentation methods on an Orbitrap Fusion for top-down phospho-proteoform characterization
Top-down analysis of intact proteins by mass spectrometry provides an ideal platform for comprehensive proteoform characterization, in particular, for the identification and localization of post-translational modifications (PTM) co-occurring on a protein. One of the main bottlenecks in top-down prot...
ORGANISM(S): Homo sapiens (Human) 
2015-07-16 | PXD001845 | Pride
Fragmentation Bora Ethcd Top down proteomics Phosphorylation Proteoform Orbitrap fusion 
ProteomicsA Bacterial Mannose Binding Lectin as a Tool for the Enrichment of C-and O- Mannosylated Peptides
C-mannosylated peptides are easily detected by mass spectrometry (MS) from purified proteins but not from complex biological samples. Enrichment of specific glycopeptides by lectin affinity prior to MS analysis has been widely applied to support glycopeptide identification, but was up till now not a...
ORGANISM(S): Homo sapiens (Human) 
2022-05-13 | PXD031355 | Pride
Etcid Bc2l-a lectin Glycoproteomics O-mannosylation C-mannosylation 
ProteomicsOptimizing the parameters governing the fragmentation of cross-linked peptides in a tribrid mass spectrometer
We compared the five different ways of fragmentation available on a tribrid mass spectrometer and optimized their collision energies with regard to optimal sequence coverage of cross-linked peptides. We created a library of bis(sulfosuccinimidyl)suberate (BS3/DSS) cross-linked precursors, derived fr...
ORGANISM(S): Homo sapiens (Human) 
2017-04-19 | PXD006131 | Pride
Lc-ms Fusion lumos Fragmentation Cross-linking 
ProteomicsA bespoke analytical workflow for the identification of sulfopep-tides and confident discrimination from phosphopeptides_C4PR_LIV
Protein tyrosine sulfation (sY) is a post-translational modification (PTM) catalysed by Golgi-resident Tyrosyl Protein Sul-foTransferases (TPSTs). Information on protein tyrosine sulfation is currently limited to ~50 human proteins with only a handful of those having verified sites of sulfation. The...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD043713 | Pride
Tyrosine-o-sulfation Sulfotyrosine Sulfation 
UnknownPreparing to read the ubiquitin code: top-down analysis of unanchored ubiquitin tetramers.
Not available
S-EPMC5618806 | biostudies-literature
UnknownCustom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides.
Not available
S-EPMC10696596 | biostudies-literature
UnknownThe Key Role of Metal Adducts in the Differentiation of Phosphopeptide from Sulfopeptide Sequences by High-Resolution Mass Spectrometry.
Not available
S-EPMC9260711 | biostudies-literature
UnknownOptimizing the Parameters Governing the Fragmentation of Cross-Linked Peptides in a Tribrid Mass Spectrometer.
Not available
S-EPMC5436099 | biostudies-literature
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