Glycosylation and Glycoproteins Research

SugarPy enables glycoproteome analysis without glycan databases, validated on human breast milk and other organisms with uncommon glycans.

O-Pair Search identifies O-glycopeptides and localizes O-glycosites using collision- and electron-based dissociation spectra, improving speed and identification rates.

MSFragger-Glyco improves glycopeptide identification in N- and O-glycoproteomics data, increasing glycoPSMs and revealing new glycan trends.

The paper presents an integrated structural analysis of intestinal mucin MUC2, revealing the shared mechanism of polymer formation for mucosal barriers and blood clotting.

This paper introduces GalNAzMe, a monosaccharide probe that selectively labels O-GalNAc glycosylation in living cells, enabling detailed study of this cancer-relevant modification.

The paper presents two high-resolution structures of human ST6Gal I, one unliganded and one with CMP-Neu5Ac bound, revealing structural flexibility and substrate binding details.

This paper identifies two novel O-glycosylation modifications on bacterial flagellins catalyzed by Maf glycosyltransferases in Geobacillus kaustophilus and Clostridium botulinum.

GlypNirO automates quantitative glycoproteomic analysis by integrating Byonic and Proteome Discoverer outputs, identifying glycosylation changes in hepatocellular carcinoma as potential biomarkers.

The paper uses mass spectrometry to analyze post-translational modifications and glycans of SARS-CoV-2 spike protein and hACE2, revealing structural details relevant to virus-host interactions and vaccine development.

The paper identifies sialylation changes in mouse sperm during capacitation, showing that sialylation of ACO2 inhibits its activity, potentially driving the metabolic switch from oxidative phosphorylation to glycolysis.

The paper introduces GlyConnect Compozitor, a tool for visualizing and comparing glycan compositions to aid in selecting appropriate compositions for glycoproteomics analysis.

The paper evaluates normalization methods for glycomics data by assessing how well they enable accurate reconstruction of known glycosylation pathway reactions using Gaussian Graphical Models.

The paper resolves the paradox of glycan microheterogeneity by developing algorithmic compartments that convert inputs to unique outputs, and applies this to real glycan datasets.

This study investigates the role of ST3GAL4 in the interaction between Lassa virus GP-C and human LAMP1, identifying sialylated glycans as mediators of viral entry.

This study identifies site-specific changes in sialylation of N-linked glycoproteins in rat nerve terminals following brief depolarization.

The paper identifies off-target glycans formed during the engineering of Pichia pastoris to produce humanized N-glycans, highlighting challenges in achieving precise glycosylation control.

The paper introduces a method to chemically tag glycans in living cells using engineered glycosyltransferases to study glycan structure and biosynthesis.

The paper analyzes N-linked glycosylation sites in human glycoproteins and finds they are more prevalent in ordered regions than disordered regions, suggesting a functional trade-off between protein stability and flexibility.

The paper uses evolutionary analysis of GT-A fold sequences to identify core components and hypervariable loops contributing to catalytic diversity, and develops a machine learning classifier for donor specificity prediction.

The paper predicts O-glycosylation and phosphorylation sites on SARS-CoV-2 S1 protein to identify potential targets for inhibiting initial host cell binding.

This study investigates N-glycan biosynthesis in the dinoflagellate Breviolum minutum and shows that inhibiting Golgi processing reduces its colonization of the sea anemone Aiptasia.

The paper introduces a chemoenzymatic method to quantitatively analyze N-glycan types on glycoproteins, demonstrating its application in characterizing glycan heterogeneity in IgG1 and MCF7 cells.

The paper introduces a cell-free platform for assembling protein glycosylation pathways and demonstrates its use in creating vaccine proteins and antibody constant regions with specific glycan motifs.

This study uses multilayered N-glycoproteomics to show impaired N-glycosylation in Alzheimer's disease mouse models, affecting protein function and neuronal health.

This study captures site-specific N-glycoproteome heterogeneity using AI-ETD, identifying 1,545 N-glycosites from mouse brain tissue and developing new visualizations for glycopeptide analysis.

This study identifies twelve genetic loci associated with human blood plasma N-glycome composition through genome-wide association analysis, revealing both direct and indirect genetic influences on glycosylation.

The paper introduces EXoO, a method for site-specific extraction of O-linked glycopeptides, enabling the mapping of over 3,000 O-linked glycosylation sites across human tissues and revealing significant differences between tumor and normal kidney tissues.

The paper reanalyzes proteomic and phosphoproteomic data to identify a large number of previously unknown N-linked glycopeptides using GPQuest 2.0.

The paper shows that N-glycosylation of Sog in Drosophila affects BMP signaling by controlling extracellular Sog levels and distribution, adding complexity to BMP regulation.