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ProteomicsConjugation site characterization of antibody–drug conjugates using electron-transfer/higher-energy collision dissociation (EThcD)
Antibody–drug conjugates (ADCs) are formed by binding of cytotoxic drugs to monoclonal antibodies (mAbs) through chemical linkers. A comprehensive evaluation of the critical quality attributes (CQAs) of ADCs is vital for drug development but remains challenging owing to ADC structural heterogeneity ...
ORGANISM(S): Homo Sapiens 
2023-02-14 | PXD040111 |
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 
UnknownIn-Source Collision-Induced Dissociation (CID) Improves Higher-Energy Collisional Dissociation (HCD)-Dependent Fragmentation of ADP-Ribosyl Peptides.
Not available
S-EPMC11617611 | biostudies-literature
UnknownElectron-Transfer/Higher-Energy Collision Dissociation (EThcD)-Enabled Intact Glycopeptide/Glycoproteome Characterization.
Not available
S-EPMC5711575 | biostudies-literature
UnknownEvaluation of front-end higher energy collision-induced dissociation on a benchtop dual-pressure linear ion trap mass spectrometer for shotgun proteomics.
Not available
S-EPMC3277647 | biostudies-literature
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 
ProteomicsExtensive backbone cleavage coverage of intact proteoforms in a mass range of 10-70 kDa by integrating electron, collision, and photon-based fragmentation techniques during an electrophoretic timescale
Capillary zone electrophoresis (CZE) –-tandem mass spectrometry (MS/MS) has been documented as a useful tool for top-down proteomics (TDP). However, CZE-MS/MS-based TDP typically has limited backbone cleavage coverage for identified proteoforms due to the use of traditional collision-based fragmenta...
ORGANISM(S): Homo sapiens (Human) 
2026-02-16 | PXD070486 | Pride
Capillary zone electrophoresis mass spectrometry  top-down proteomics  orbitrap ascend tribrid  ultraviolet photodissociation  higher-energy collisional dissociation  electron transfer dissociation 
ProteomicsCellular ADP-ribosylome characterization with HCD and EThcD
Protein ADP-ribosylation is a post-translational modification involved in important physiological and pathological processes. Here, we present an optimized method using the Orbitrap Fusion Tribrid mass spectrometer, which drastically improves the overall ADP-ribosylation site localization score and ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-07-28 | MSV000080008 | MassIVE
UnknownLarge-Scale Differentiation and Site Specific Discrimination of Hydroxyproline Isomers by Electron Transfer/Higher-Energy Collision Dissociation (EThcD) Mass Spectrometry.
Not available
S-EPMC6481173 | biostudies-literature
UnknownDirect and Detailed Site-Specific Glycopeptide Characterization by Higher-Energy Electron-Activated Dissociation Tandem Mass Spectrometry.
Not available
S-EPMC10885852 | biostudies-literature
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