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ProteomicsNucleocytoplasmic O-Man glycoproteome
Dynamic cycling of N-Acetylglucosamine (GlcNAc) on serine (Ser) and threonine (Thr) residues (O-GlcNAcylation) is an essential process in all eukaryotic cells except yeast, e.g Saccharomyces cerevisiae. O-GlcNAcylation modulates signaling and cellular processes in an intricate interplay with protein...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) Schizosaccharomyces pombe 
2015-12-08 | PXD002924 | Pride
O-glycoproteomics Saccharomyces cerevisiae 
ProteomicsIdentification of global inhibitors of cellular glycosylation
Small molecule inhibitors of glycosylation enzymes are valuable tools for dissecting glycan functions and potential drug candidates. Screening for inhibitors of glycosyltransferases are mainly performed by in vitro enzyme assays with difficulties moving candidates to cells and animals. Here, we circ...
ORGANISM(S): Homo sapiens (Human) 
2023-05-05 | PXD039334 | Pride
Golgi fragmentation Cell-based glycan array O-glycosylation Sars-cov-2 Compound library screen Glycosylation inhibitor Glycosyltransferases 
ProteomicsFruit fly O-GlcNAc glycoproteomics
The reversible posttranslational O-GlcNAc modification of serine or threonine residues of intracellular proteins is involved in many cellular events from signaling cascades to epigenetic and transcriptional regulation. O-GlcNAcylation is a conserved nutrient-dependent process involving two enzymes,...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2021-04-26 | PXD025344 | Pride
Fusion O-glcnac Drosophila melanogaster 
ProteomicsDeconstruction of protein O-glycosylation
GalNAc-transferase (GalNAc-T) isoforms modify distinct subsets of the O-glycoproteome and GalNAc-type O-glycosylation is found on most proteins trafficking through the secretory pathway in metazoan cells. The O-glycoproteome is regulated by up to 20 polypeptide GalNAc-Ts and the contributions and bi...
ORGANISM(S): Homo sapiens (Human) 
2015-08-21 | PXD002770 | Pride
Galnt/ dimethylation/ apolipoproteins/ mass spectrometry 
ProteomicsAn Atlas of Human Glycosylation Pathways Enables Display of the Human Glycome by Gene Engineered Cells
The structural diversity of glycans on cells – the glycome – is vast and complex to decipher. Glycan arrays have played a pivotal role in exploring the informational content of glycans. Current glycan arrays display oligosaccharides generated by chemical and chemoenzymatic synthesis or isolated from...
ORGANISM(S): Homo sapiens (Human) 
2019-06-24 | PXD013676 | Pride
Lc-ms Cell array Glycoprotein Orbitrap 
ProteomicsMapping the O-mannose glycoproteome in Saccharomyces cerevisiae
O-Mannosylation is a vital protein modification conserved from fungi to humans. In an essential step towards the full understanding of O-mannosylation we mapped the O mannose glycoproteome in baker´s yeast.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-01-18 | PXD003238 | Pride
Saccharomyces cerevisiae Glycoproteome O-mannose 
ProteomicsCHO O-Mannosylation independent of POMT1/2
Protein O-mannosylation is found in yeast and metazoans and a family of conserved orthologous polypeptide O-mannosyltransferases is believed to initiate this important posttranslational modification. We recently discovered that the large families of cadherins and protocadherins carry highly conserve...
ORGANISM(S): Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) 
2017-05-18 | PXD004341 | Pride
Mannose Glycoproteomics O-mannosyltransferase O-glycosylation 
ProteomicsHuman O-Mannosylation independent of POMT1/2
Protein O-mannosylation is found in yeast and metazoans and a family of conserved orthologous polypeptide O-mannosyltransferases is believed to initiate this important posttranslational modification. We recently discovered that the large families of cadherins and protocadherins carry highly conserve...
ORGANISM(S): Homo sapiens (Human) 
2017-05-18 | PXD004358 | Pride
O-glycosylation Glycoproteomics O-mannose Mannosyltransferase 
ProteomicsThe Glycosylation Design Space for Recombinant Lysosomal Replacement Enzymes Produced in CHO Cells
Lysosomal storage diseases are rare life-threatening disorders caused by deficiency of a lysosomal enzyme, and delivery of a recombinant replacement enzyme is the primary therapy for several of these diseases. The structures of N-glycans on recombinant replacement enzymes are important for their the...
ORGANISM(S): Homo sapiens (Human) Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) 
2019-05-31 | PXD013140 | Pride
N-glycoproteomics Enzyme replacement therapy Glycoengineering 
TranscriptomicsPancreatic tumor cell lines
Dr. Clausen's laboratory is interested in the structure, biosynthesis and genetic regulation of glycoconjugates, with a major focus on mucins. This laboratory is studying the glycosylation and secretion process of mucins and biological functions involving mucins. This lab is also interested in recep...
ORGANISM(S): Homo sapiens 
2010-12-11 | E-GEOD-26011 | biostudies-arrayexpress
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