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ProteomicsElectron Transfer/ Higher Energy Collisional Dissociation of Doubly Charged Peptide Ions: Identification of Labile Protein Phosphorylations
Fragmentation behaviour of labile phosphorylated peptides
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2019-05-27 | PXD012989 | Pride
Labile phosphorylations Ethcd 
ProteomicsOptimization of Higher-Energy Collisional Dissociation Fragmentation Energies for Intact Protein-level Tandem Mass Tag Labeling
Isobaric chemical tag labeling (e.g., iTRAQ and TMT) is a commonly used approach in quantitative proteomics research. Typically, peptides are covalently labeled with isobaric chemical tags, and quantification is enabled through detection of low-mass reporter ions generated after MS2 fragmentation. R...
ORGANISM(S): Homo sapiens (Human) 
2023-01-17 | PXD037491 | Pride
Protein-level tmt labeling  top-down proteomics  quantitative proteomics  hcd 
ProteomicsHigher-energy collisional dissociation mass spectrometry fragmentation in cancer cells
mass spectrometric analysis of monosaccharide in cancer cells
ORGANISM(S): Homo Sapiens 
2025-10-23 | PXD069643 |
ProteomicsSequential N/O-glycosylation analysis of heavily glycosylated HIV-1 gp120 by combination of electron-transfer/higher-energy collisional dissociation and stepped collision energy/higher-energy collisional dissociation (EThcD-sceHCD)
The envelope (Env) glycoprotein on the surface of human immunodeficiency virus type 1 (HIV-1) which decorated with a dense array of glycans is a determinant for viral invasion and host immune response of HIV-1 and a major target for a preventive HIV-1 vaccine. Improved vaccine design requires an und...
ORGANISM(S): Homo sapiens (Human) 
2021-11-03 | PXD025078 | Pride
Envelope glycoprotein Human immunodeficiency virus Ethcd-scehcd-ms/ms N/o-glycosylation 
ProteomicsSystems analysis of plasma IgG intact N-glycopeptides from pa-tients with chronic kidney diseases via combined electron-transfer/higher-energy collisional dissociation and stepped colli-sion energy/higher-energy collisional dissociation mass spectrom-etry within half an hour
Immunoglobulin G (IgG) molecules modulate an immune response. However, site-specific N-glycosylation signatures of plasma IgG in patients with chronic kidney disease (CKD) remain unclear. This study aimed to propose a novel method to explore the N-glycosylation pattern of IgG and to compare it with ...
ORGANISM(S): Homo sapiens (Human) 
2021-11-25 | PXD027174 | Pride
Glycosylation Immunoglobulin g Chronic kidney disease Lc-ms/ms 
UnknownCharacterization of intact N- and O-linked glycopeptides using higher energy collisional dissociation.
Not available
S-EPMC5627992 | biostudies-literature
UnknownIn-Source Collision-Induced Dissociation (CID) Improves Higher-Energy Collisional Dissociation (HCD)-Dependent Fragmentation of ADP-Ribosyl Peptides.
Not available
S-EPMC11617611 | biostudies-literature
UnknownDifferentiating Positional Isomers of Nucleoside Modifications by Higher-Energy Collisional Dissociation Mass Spectrometry (HCD MS).
Not available
S-EPMC6062210 | biostudies-literature
UnknownOptimization of Higher-Energy Collisional Dissociation Fragmentation Energy for Intact Protein-Level Tandem Mass Tag Labeling.
Not available
S-EPMC10164041 | biostudies-literature
UnknownSimply Extending the Mass Range in Electron Transfer Higher Energy Collisional Dissociation Increases Confidence in N-Glycopeptide Identification.
Not available
S-EPMC6706795 | biostudies-literature
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