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MetabolomicsDiagnostic Potential of Plasma IgG N-glycans in Discriminating Thyroid Cancer from Benign Thyroid Nodules and Healthy Controls

BACKGROUND: Novel biomarkers are urgently needed to distinguish between benign and malignant thyroid nodules and detect thyroid cancer in the early stage. The associations between serum IgG N-glycosylation and thyroid cancer risk have been revealed. We aimed to explore the potent...

2021-09-01 | MTBLS2935 | MetaboLights
ProteomicsHuman IgG subclasses differ in structural elements of their N-glycosylation
We tested tryptic plasma samples using HILIC-LC-MS/MS, which included mixed human plasma as well as plasma from two healthy individuals collected at three different time points, approximately one month apart. Our focus was on the glycan structure of the Fc domain of IGG subclasses. The results indic...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-06-13 | MSV000095017 | MassIVE
ProteomicsMiddle-up analysis of polyclonal IgG-Fc
Middle-up strategy for the analysis of the fragment crystallizable (Fc) region of human plasma immunoglobulins G (IgGs). The use of hydrophilic interaction liquid chromatography (HILIC) and capillary electrophoresis (CE) coupled to mass spectrometry (MS) allowed to get a comprenhesive view of the N-...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-05-08 | MSV000085388 | MassIVE
ProteomicsAnalysis of N-Glycosylation for SARS-CoV-2 expressed receptor-binding domain VOCs and membrane protein with LC-MS.
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can infect human cells by first attaching to the ACE-2 receptor via its receptor-binding domain (RBD) in the spike protein. We investigated the influence of N-glycosylation sites of the RBD and the membrane (M) protein on IgG antibody bind...
ORGANISM(S): Severe Acute Respiratory Syndrome Coronavirus 2 
2024-04-29 | PXD048930 | panorama
ProteomicsChemical labeling for fine mapping of IgG N-glycosylation by ETD-MS
Immunoglobulin G (IgG), which contains four subclasses (IgG1-4), is one of the most important class of glycoproteins in immune system. Because of its importance in immune system, a steady increase of interest in developing IgG as biomarker or biotherapeutic agents for the treatment of diseases has b...
ORGANISM(S): Homo sapiens (Human) 
2019-08-26 | PXD014713 | Pride
Chemical labeling Igg Glycosylation Glycopeptides Electron transfer dissociation (etd) mass spectrometry 
ProteomicsRole of N-glycosylation in FcRIIIa interaction with IgG
Immunoglobulins G (IgG) and their Fc gamma receptors (FcγRs) play important roles in our immune system. The conserved N-glycan in the Fc region of IgG1 impacts interaction of IgG with FcγRs and the resulting effector functions, which has led to design of antibody therapeutics with greatly improved a...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2022-08-30 | PXD035846 | Pride
Mabs Cd16a Igg N-glycosylation Fc gamma receptors Glycosyltransferases Surface plasmon resonance Glycoengineering 
ProteomicsSite-specific analysis of CD16a and CD32a N-glycosylation from monocytes display donor variability which modulate affinity to IgG1 Fc
Glycopeptide mass spectra of CD16a and CD32a from isolated monocytes display donor and site variability. CD16a N-glycosylation composition affects the affinity of IgG1 Fc. Peptide coverage of CD16a was ~85% while CD32a was ~61%.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-06-26 | MSV000084012 | MassIVE
TranscriptomicsElevated N-linked glycosylation of IgG variable regions in myasthenia gravis disease subtypes
Elevated N-linked glycosylation of immunoglobulin G variable regions (IgG-VN-Glyc) is an emerging molecular phenotype associated with autoimmune disorders. To test the broader specificity of elevated IgG-VN-Glyc, we studied patients with distinct subtypes of myasthenia gravis (MG), a B cell-mediated...
ORGANISM(S): Homo sapiens 
2021-08-13 | GSE182038 | GEO
ProteomicsN-glycosylation patterns of plasma immunoglobulin G in anti-synthetase syndrome disease
Anti-synthetase syndrome (ASS), a subtype of idiopathic inflammatory myopathy (IMM), is characterized by distinctive skin rashes, proximal muscle weakness, and interstitial lung disease (ILD). The etiology of ASS remains largely unknown, and patients endure a poor quality of life and are prone to pu...
ORGANISM(S): Homo Sapiens 
2024-11-20 | PXD058077 |
ProteomicsEndoglycosidases- treated N-glycosylation site identification
Glycoproteins, representing over 50% of human proteins and most biopharmaceuticals, are crucial for regulating various biological processes. The complexity of multiple glycosylation sites often leads to incomplete sequence coverage and ambiguous glycan modification profiles. Here, we developed an in...
ORGANISM(S): Homo Sapiens 
2024-12-30 | PXD059329 |
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