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ProteomicsA Combinatorial Enzymatic Approach for Identifying O-glycopeptides
Proteins glycosylation is primarily characterized as N-glycosylation or O-glycosylation. Recognition of the consensus N-glycosylation sequon (N-X-S/T/C) has enabled the mapping of the glycosite occupancy of intact glycopeptides, whereas O-glycosylation consensus sequons do not exit, making the chara...
ORGANISM(S): Homo sapiens (Human) 
2024-04-25 | PXD042701 | Pride
Rax-based enrichment O-glycosites O-glycosylation Impa Scehcd-based ms/ms 
ProteomicsQuantitative Phosphoproteomics Reveals Crosstalk Between Phosphorylation and O-GlcNAc in the DNA Damage Response Pathway
The modification of intracellular proteins by monosaccharides of O-linked linked β-N-acetylglucosamine (O-GlcNAc) is thought to mediate proteins by regulating protein phosphorylation, either by modifying and modulating protein kinases or by competing with phosphorylation for hydroxyl residues. To pr...
ORGANISM(S): Mus musculus (Mouse) 
2015-01-28 | PXD001153 | Pride
Mouse embryonic fibroblast Atm Ogt knockout 
ProteomicsExtensive hypoglycosylation of serum N-glycoproteins in SRD5A3 deficiency
Polyprenol reductase is an enzyme encoded by the SRD5A3 gene, which catalyzes the synthesis of dolichol from polyprenols. Dolichol serves as a carrier for glycan precursors in N-linked glycosylation or monosaccharides in O-glycosylation, C-mannosylation, and GPI anchor biosynthesis. Pathogenic varia...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD053534 | Pride
Srd5a3-cdg Glycosylation Rare diseases Orbitrap eclipse tribrid Polyprenol reductase Type 1 cdg Complex glycans 
ProteomicsDiscovery of non-canonical translation initiation sites through mass spectrometric analysis of protein N-termini
Translation initiation generally occurs at AUG codons in eukaryotes although it has been shown that non-AUG or non-canonical translation initiation can also occur. However, the evidence for non-canonical translation initiation sites (TISs) is largely indirect and based on ribosome profiling studies....
ORGANISM(S): Homo sapiens (Human) 
2017-11-23 | PXD006633 | Pride
Human Non-canonical Tails 
UnknownQuantitative phosphoproteomics reveals crosstalk between phosphorylation and O-GlcNAc in the DNA damage response pathway.
Not available
S-EPMC4564869 | biostudies-literature
ProteomicsProteome and glycoproteome analysis of fibroblasts from patients with congenital disorders of glycosylation
In the biological systems, several genes are involved in protein glycosylation pathway. Congenital Disorders of Glycosylation (CDG) is known to be a multisystem disorder. Pathogenic variants in the glycosylation genes lead to abnormal N- or O-linked glycosylation that causes cellular stress. We used...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD044327 | Pride
Glycosylation Proteomics Glycoproteomics Cdg Fibroblasts 
UnknownPurification, Cloning and Immuno-Biochemical Characterization of a Fungal Aspartic Protease Allergen Rhi o 1 from the Airborne Mold Rhizopus oryzae.
Not available
S-EPMC4682942 | biostudies-literature
UnknownGlobal O-glycoproteome enrichment and analysis enabled by a combinatorial enzymatic workflow.
Not available
S-EPMC11046030 | biostudies-literature
ProteomicsA transcriptomic and proteomic map of primary human cell types
Molecular profiling of human primary cell types is essential for a comprehensive understanding of human biology. Here, we describe the transcriptome and proteome map of 28 primary human cell types. Three major clusters of epithelial, endothelial, and mesenchymal cell types were observed at both the ...
ORGANISM(S): Homo sapiens (Human) 
2026-01-23 | PXD062642 | Pride
Primary cells Post-translational modifications Transcriptomics Lc-ms/ms 
UnknownComplement activating ABO anti-A IgM/IgG act synergistically to cause erythrophagocytosis: implications among minor ABO incompatible transfusions.
Not available
S-EPMC7257204 | biostudies-literature
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