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Most proteins trafficking the secretory pathway of metazoan cells will acquire GalNAc-type O-glycosylation. GalNAc-type O-glycosylation is differentially regulated in cells by the expression of a repertoire of up to twenty genes encoding polypeptide GalNAc-transferase isoforms (GalNAc-Ts) that initi...
ORGANISM(S): Homo sapiens (Human) 
2019-06-24 | PXD009955 | Pride
We report a LC-MS/MS O-glycoproteomics strategy using Data Independent Acquisition (DIA) mode that holds the potential for enabling direct analysis of O-glycoproteins with characterization of sites and structures of O-glycans on a proteome-wide scale with quantification of stoichiometries. To explor...
ORGANISM(S): Homo sapiens (Human) 
2019-11-19 | PXD011063 | Pride
The human genome contains at least 35 genes that encode Golgi sulfotransferases functioning in the secretory pathway, where they are involved in decorating glycosaminoglycans, glycolipids, and glycoproteins with sulfate groups. Our insight into the sulfotransferases that serve glycoproteins and in p...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD028982 | Pride
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
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
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
Small molecule inhibitors of glycosylation enzymes can be valuable tools for dissecting glycan functions and present great potential as drug discovery candidates. Most screening campaigns for inhibitors of glycosyltransferases have been limited to in vitro enzyme assays using recombinant enzymes, wh...
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD029623 | Pride
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
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
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
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