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MetabolomicsSerum protein N-glycosylation changes in multiple myeloma

BACKGROUND: Multiple myeloma is characterized by clonal proliferation of malignant plasma cells in the bone marrow that produce monoclonal immunoglobulins. N-glycosylation changes of these monoclonal immunoglobulins have been reported in multiple myeloma, but previous studies on...

2022-04-27 | MTBLS676 | MetaboLights
MetabolomicsN-glycosylation Profiling of Colorectal Cancer Cell Lines Reveals Association of Fucosylation with Differentiation and Caudal Type Homebox 1 (CDX1)/Villin mRNA Expression
Various cancers such as colorectal cancer (CRC) are associated with alterations in protein glycosylation. CRC cell lines are frequently used to study these (glyco)biological changes and their mechanisms. However, differences between CRC cell lines with regard to their glycosylation have hitherto bee...
2017-02-03 | MTBLS227 | MetaboLights
TranscriptomicsRole of the polypeptide N-acetylgalactosaminyltransferase 3 in ovarian cancer progression: possible implications in abnormal mucin O-glycosylation
Previously, we have identified the polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) gene as notably hypomethylated in low-malignant potential (LMP) and high-grade (HG) serous epithelial ovarian tumors, compared to normal ovarian tissues. Here we show that GALNT3 is strongly overexpressed in ...
ORGANISM(S): Homo sapiens 
2014-05-22 | E-GEOD-52602 | biostudies-arrayexpress
ProteomicsAlterations in protein expression and site-specific N-glycosylation of prostate cancer tissues
Samples were analyzed using a Maxis II QTOF instrument (Bruker Daltonik GmbH, Bremen, Germany) equipped with CaptiveSpray nanoBooster ion source coupled to a Dionex UltiMate 3000 RSLCnano system (Sunnyvale, CA, USA). Peptides were separated on an Acquity M-Class BEH130 C18 analytical column using gr...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-04-28 | MSV000087329 | MassIVE
ProteomicsLC-MS/MS-based 4D Label-Free N-Glycosylation Proteomics Analysis of Bone Marrow Cells from ADO2 Mouse
This project aims to investigate N-linked glycosylation modifications in bone marrow cells (BMCs) of an autosomal dominant osteopetrosis type 2 (ADO2) mouse model carrying the Clcn7 (r284w) mutation. Using LC-MS/MS-based 4D Label-Free N-Glycosylation Proteomics Analysis, we identified significant al...
ORGANISM(S): Mus Musculus 
2025-02-05 | PXD060501 |
ModelsIrani2015 - Genome-scale metabolic model of P.pastoris N-glycosylation
Irani2015 - Genome-scale metabolic model of P.pastoris N-glycosylation This model is described in the article: Genome-scale metabolic model of Pichia pastoris with native and humanized glycosylation of recombinant proteins. Irani ZA, Kerkhoven E, Shojaosadati SA, Nielsen J. ...
2024-10-15 | BIOMD0000001096 | BioModels
FROG 
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
ProteomicsGlycoPCT: quantitative glycoproteomics based on pressure cycling technology reveals distinctive N-glycosylation in human liver with non-alcoholic fatty liver disease
Protein N-glycosylation plays a crucial role in the human liver, impacting key functions like hepatocyte lipid metabolism hepatocyte apoptosis, and inflammatory response. Despite its significance, the site-specific N-glycosylation patterns and their variations of liver biosy samples between healthy ...
ORGANISM(S): Homo Sapiens 
PXD053626 |
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
ProteomicsSolid-phase extraction of N-linked glycans and glycosite-containing peptides (NGAG) for comprehensive characterization of glycoproteins
A novel chemoenzymatic method termed solid phase extraction of N-linked Glycans And Glycosite-containing peptides (NGAG) for the simultaneous analysis of N-glycans, glycosite-containing peptides, and intact N-glycopeptides with site-specific glycosylation information.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080840 | MassIVE
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