Sort   by:  
 Page size 
Proteomics1. Site-specific O-glycosylation analysis of SARS-CoV-2 spike protein produced in insect and human cells
2. Enveloped viruses hijack not only host translation processes, but also its glycosylation machinery and to a variable extent cover viral surface proteins with tolerogenic host-like structures. SARS-CoV-2 surface protein S presents as a trimer on the viral surface and is covered by a dense shield o...
ORGANISM(S): Homo sapiens (Human) Drosophila melanogaster (Fruit fly) 
2021-04-07 | PXD024767 | Pride
Sars-cov-2 O-glycosylation Lc-ms N-glycosylation Etd 
ProteomicsMolecular Regulation and Physiological Role of GOLPH3-mediated Golgi retention
The Golgi complex serves as the central hub of the biosynthetic pathway, where anterograde and retrograde trafficking fluxes converge. The mechanism by which cargo and Golgi-resident proteins traverse this organelle has long been debated. Recent discoveries have identified a molecular machinery that...
ORGANISM(S): Homo sapiens (Human) 
2026-09-07 | PXD064301 | Pride
Human Glycoproteomics Liver Golph3 
ProteomicsO-glycan initiation directs distinct biological pathways and controls epithelial differentiation
Glycosylation is an abundant post-translational modification of both intracellular and extracellular proteins [1]. The majority of glycans are classified as N-linked chains, where the carbohydrate moiety is attached to asparagine residues, or O-linked chains, most commonly linked to a serine or thre...
ORGANISM(S): Homo sapiens (Human) 
2020-05-22 | PXD016618 | Pride
Differential glycoproteomics Polyomics Polypeptide galnac-transferase Tissue development 3d skin 
ProteomicsProbing the ovarian cancer O-glycoproteome by the Macrophage Galactose like C-type Lectin (MGL): dissecting novel patterns of immune recognition
Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type O-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface which prof...
ORGANISM(S): Homo sapiens (Human) 
2020-10-19 | PXD017510 | Pride
Ovarian cancer O-glycosylation Cancer immunotherapy Tn antigen Dcs Tumor biomarker 
ProteomicsProbing the contribution of individual polypeptide GalNAc-transferase isoforms to the O-glycoproteome by inducible expression in isogenic cell lines
The GalNAc-type O-glycoproteome is orchestrated by a large family of polypeptide GalNAc-transferase isoenzymes (GalNAc-Ts) with partially overlapping contributions to the O-glycoproteome as well as distinct non-redundant functions. Increasing evidence indicate that individual GalNAc-Ts co-regulate a...
ORGANISM(S): Homo sapiens (Human) 
2018-10-16 | PXD010155 | Pride
Inducible expression Galnac-transferase O-glycosylation Glycoproteomics Mass spectrometry 
ProteomicsGALNT11 Controlled O-glycans Modulate Ligand Interactions of the Endocytic Receptor LRP1
Low-density lipoprotein receptor (LDLR) and LDLR-related proteins (LRPs) are essential endocytic receptors and regulators of multiple physiological processes including protein reabsorption, cholesterol clearance, and neuronal protein trafficking. Previously, we identified O-GalNAc glycans within lig...
ORGANISM(S): Homo sapiens (Human) 
2026-03-02 | PXD058370 | Pride
Glycosylation Lrp1 Tmt Mass spectrometry Galnt11 
ProteomicsExploring glycosylation of mucins with O-glycodomain reporters expressed in glycoengineered HEK293 cells
Mucins and glycoproteins with mucin-like regions contain densely O-glycosylated domains often found in tandem repeat (TR) sequences. These O-glycodomains have traditionally been difficult to characterize because of resistance to proteolytic digestion, and knowledge of positions of O-glycans is parti...
ORGANISM(S): Homo sapiens (Human) 
2022-05-20 | PXD029885 | Pride
Glycosylation Cell-based glycan array Intact mass Mucins Glycomucinases Glycosyltransferases O-glycodomains Glycoengineering 
ProteomicsEssential functions of glycans in human epithelia dissected by a CRISPR/Cas9-engineered human organotypic skin model
The glycome undergoes characteristic changes during histogenesis and organogenesis, but our understanding of the importance of select glycan structures for tissue formation and homeostasis is incomplete. Here, we present a human organotypic platform that allows genetic dissection of cellular glycosy...
ORGANISM(S): Homo sapiens (Human) 
2021-09-09 | PXD018418 | Pride
Skin Glycoproteomics Glycosylation 
ProteomicsMammalian Cell-Based Production of Glycans, Glycopeptides and Glycomodules
Access to defined glycans and glycoconjugates is pivotal for discovery, dissection, and harnessing of a range of biological functions orchestrated by cellular glycosylation processes and the glycome. We previously employed genetic glycoengineering by nuclease-based gene editing to develop sustainabl...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD056690 | Pride
Glycosylation Carbohydrate synthesis Mass photometry Microarray Glycoengineering 
ProteomicsDisplay of the Human Mucinome with Defined O-Glycans by Gene Engineered Cells
Mucins are a large family of heavily O-glycosylated proteins that cover all mucosal surfaces and constitute the major macromolecules in most body fluids. Mucins can form aggregated networks and bundles that serve as a barrier, but also assist in containing, feeding, clearing and replenishing microor...
ORGANISM(S): Homo sapiens (Human) 
2021-05-11 | PXD024851 | Pride
Glycosylation Orbitrap Intact mass Mucin 
Sort   by:  
 Page size