ReviewMolecular & cellular proteomics : MCP2021
Meta-heterogeneity: Evaluating and Describing the Diversity in Glycosylation Between Sites on the Same Glycoprotein.
Review in Molecular & cellular proteomics : MCP, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
63 citing papers in PubMed.
- Article
- Micro- and Macro-Heterogeneity of N-Glycoproteome Remodeling in Endoplasmic Reticulum Stress.Molecular & cellular proteomics : MCP · 2026Article
- GlycoDiveR: A Modular R Framework to Analyze and Visualize Highly Dimensional Glycoproteomics Data.ACS measurement science au · 2026Article
- Site-Specific Glycosylation Profiling of Protein Subunit and Inactivated Virus Vaccines.Vaccines · 2026Article
- Characterizing the Effects of Protein Glycosylation Perturbation on Phosphorylation Signaling.Analytical chemistry · 2026Article
- Mapping ST3GAL transferase specificities in the glycosylation landscape of N/TERT-1 keratinocytes using Glycogenomics and mass spectrometry.Glycobiology · 2026Article
- Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein O-Glycosylation in Complex Biological Samples.Journal of the American Society for Mass Spectrometry · 2026Review
- Enzymatically controlled release of proteins and peptides: A promising, alternative secretion approach.iScience · 2026Article
- GlycoDiveR: a modular R framework to analyze and visualize highly dimensional glycoproteomics data.bioRxiv : the preprint server for biology · 2026Article
- Blood proteomics: insights from public data.Genome biology · 2026Review
- Structural-activity relationship ofFrontiers in immunology · 2026Review
- Characterizing the Effects of Protein Glycosylation Perturbation on Phosphorylation Signaling.bioRxiv : the preprint server for biology · 2025Article
- Elucidating the dynamics of integrin αIIbβ3 from native platelet membranes by cryo-EM with build-and-retrieve method.Blood advances · 2025Article
- Analytical dissection of minor glycoforms and glycoprotein associations in rAAV preparations by multimodal glycoproteomics.Analytical and bioanalytical chemistry · 2025Article
- Altered glycosylation of EVs in cancers: galectin-3-binding protein (LGALS3BP).Discover oncology · 2025Review
- Ultradeep N-glycoproteome atlas of mouse reveals spatiotemporal signatures of brain aging and neurodegenerative diseases.Nature communications · 2025Article
- Uncovering protein glycosylation dynamics and heterogeneity using deep quantitative glycoprofiling (DQGlyco).Nature structural & molecular biology · 2025Article
- Plasma N-Glycoproteomics in monozygotic twin pairs discordant for body mass index reveals an obesity signature related to inflammation and iron metabolism.Biology direct · 2025Article
- Changes in the dynamic characteristics of G-protein can alter the immune-protection efficacy of rabies virus vaccine.Journal of virology · 2025Article
- Intact glycopeptide analysis of human prostate tissue reveals site-specific heterogeneity of protein glycosylation in prostate cancer.Glycobiology · 2025Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mass spectrometry-based glycoproteomics has gone through some incredible developments over the last few years. Technological advances in glycopeptide enrichment, fragmentation methods, and data analysis workflows have enabled the transition of glycoproteomics from a niche application, mainly focused on the characterization of isolated glycoproteins, to a mature technology capable of profiling thousands of intact glycopeptides at once. In addition to numerous biological discoveries catalyzed by the technology, we are also observing an increase in studies focusing on global protein glycosylation and the relationship between multiple glycosylation sites on the same protein. It has become apparent that just describing protein glycosylation in terms of micro- and macro-heterogeneity, respectively, the variation and occupancy of glycans at a given site, is not sufficient to describe the observed interactions between sites. In this perspective we propose a new term, meta-heterogeneity, to describe a higher level of glycan regulation: the variation in glycosylation across multiple sites of a given protein. We provide literature examples of extensive meta-heterogeneity on relevant proteins such as antibodies, erythropoietin, myeloperoxidase, and a number of serum and plasma proteins. Furthermore, we postulate on the possible biological reasons and causes behind the intriguing meta-heterogeneity observed in glycoproteins.
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