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ProteomicsEThcD-sceHCD-MS/MS-based Clinical N-glycoproteomics
Site-specific N-glycosylation characterization requires intact N-glycopeptide analysis based on suitable tandem mass spectrometry (MS/MS) method. Electron-transfer/higher-energy collisional dissociation (EThcD), stepped collision energy/higher-energy collisional dissociation (sceHCD), and higher-ene...
ORGANISM(S): Homo sapiens (Human) 
2022-04-04 | PXD030288 | Pride
Glycoproteomics Mass spectrometry Ethcd-scehcd Fragmentation mode N-glycosylation Clinical sample 
ProteomicsComprehensive human plasma N-glycoproteome profiling based on EThcD-sceHCD-MS/MS
N-glycoproteins are involved in various biological processes. More than one-third of plasma tumor protein biomarkers approved by the Food and Drug Administration (FDA) are glycoproteins which would enhance the specificity and/or sensitivity of cancer diagnosis. Therefore, the characterization of pla...
ORGANISM(S): Homo sapiens (Human) 
2022-08-12 | PXD030622 | Pride
Mass spectrometry  human plasma  n-glycoproteomics  combinatorial peptide ligands library  ethcd-scehcd 
ProteomicsSite-specific N-glycosylation Characterization of Micro Disease-related Proteins Based on EThcD-sceHCD-MS/MS
Monoclonal immunoglobulin produced by clonal plasma cells is the main cause in multiple myeloma and monoclonal gammopathy of renal significance. Because of the complicated purification method and the low stoichiometry of purified protein and glycans, site-specific N-glycosylation characterization fo...
ORGANISM(S): Homo sapiens (Human) 
2022-09-13 | PXD035757 | Pride
N-glycosylation  microscale  serum  monoclonal immunoglobulin  mass spectrometry  ethcd-scehcd 
UnknownComprehensive Plasma N-Glycoproteome Profiling Based on EThcD-sceHCD-MS/MS.
Not available
S-EPMC9251008 | biostudies-literature
UnknownSite-specific N-glycosylation characterization of micro monoclonal immunoglobulins based on EThcD-sceHCD-MS/MS.
Not available
S-EPMC9520751 | biostudies-literature
UnknownSequential Analysis of the N/O-Glycosylation of Heavily Glycosylated HIV-1 gp120 Using EThcD-sceHCD-MS/MS.
Not available
S-EPMC8567067 | biostudies-literature
ProteomicsOptimal Dissociation Methods Differ for N- and O-glycopeptides
Site-specific characterization of glycosylation requires intact glycopeptide analysis, and recent efforts have focused on how to best interrogate glycopeptides using tandem mass spectrometry (MS/MS). Beam-type collisional activation, i.e., higher-energy collisional dissociation (HCD), has been a val...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2020-07-20 | PXD017646 | Pride
Glycoproteomics N-glycopeptides Scehcd Ethcd O-glycopeptides Etd 
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 
ProteomicsA Combinatorial Enzymatic Approach for Identifying O-glycopeptides
Proteins glycosylation is primarily characterized as N-glycosylation or O-glycosylation. Recognition of the consensus N-glycosylation sequon (N-X-S/T/C) has enabled the mapping of the glycosite occupancy of intact glycopeptides, whereas O-glycosylation consensus sequons do not exit, making the chara...
ORGANISM(S): Homo sapiens (Human) 
2024-04-25 | PXD042701 | Pride
Rax-based enrichment O-glycosites O-glycosylation Impa Scehcd-based ms/ms 
UnknownComparative N-Glycoproteomics Analysis of Clinical Samples Via Different Mass Spectrometry Dissociation Methods.
Not available
S-EPMC8907888 | biostudies-literature
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