The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.
Advances in mass spectrometry driven O-glycoproteomics
Abstract
Background Global analyses of proteins and their modifications by mass spectrometry are essential tools in cell biology and biomedical research. Analyses of glycoproteins represent particular challenges and we are only at the beginnings of the glycoproteomic era. Some of the challenges have been overcome with N-glycoproteins and proteome-wide analysis of N-glycosylation sites is accomplishable today but only by sacrificing information of structures at individual glycosites. More recently advances in analysis of O-glycoproteins have been made and proteome-wide analysis of O-glycosylation sites is becoming available as well. Scope of review Here we discuss the challenges of analysis of O-glycans and new O-glycoproteomics strategies focusing on O-GalNAc and O-Man glycoproteomes. Major conclusions A variety of strategies are now available for proteome-wide analysis of O-glycosylation sites enabling functional studies. However, further developments are still needed for complete analysis of glycan structures at individual sites for both N- and O-glycoproteomics strategies. General significance The advances in O-glycoproteomics have led to identification of new biological functions of O-glycosylation and a new understanding of the importance of where O-glycans are positioned on proteins.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“It is clear that the glycome of an organism is far, far more complex than that of its genome, transcriptome or proteome, and it is only recently that ' glycomics ' has become practically feasible (1065, 1081 -1089).”
From Biological roles of glycans (2017) · cites this paper as [1089]
In the citing paper
“It is clear that the glycome of an organism is far, far more complex than that of its genome, transcriptome or proteome, and it is only recently that ' glycomics ' has become practically feasible (1065, 1081 -1089).”
From Biological roles of glycans (2017) · cites this paper as [1089]
Citations
Cites
ASSEMBLY OF ASPARAGINE-LINKED OLIGOSACCHARIDES
Kornfeld, R., & Kornfeld, S. A. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.003215 · Cited by 4,863
Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J., & Hunt, D. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402700101 · Cited by 2,370
Newly identified loci that influence lipid concentrations and risk of coronary artery disease
Willer, C. J., Sanna, S., Jackson, A. U., Scuteri, A., Bonnycastle, L. L., Clarke, R., Heath, S. C., Timpson, N. J., Najjar, S. S., Stringham, H. M., et al. (2008) · Nature Genetics · doi:10.1038/ng.76 · Cited by 1,585
Prescher, J. A., & Bertozzi, C. R. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0605-13 · Cited by 1,473
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Hart, G. W., Housley, M. P., & Slawson, C. (2007) · Nature · doi:10.1038/nature05815 · Cited by 1,418
Precision mapping of the human O‐GalNAc glycoproteome through SimpleCell technology
Steentoft, C., Vakhrushev, S. Y., Joshi, H. J., Kong, Y., Vester‐Christensen, M. B., Schjoldager, K. T. G., Lavrsen, K., Dabelsteen, S., Pedersen, N. B., Marcos‐Silva, L., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.79 · Cited by 1,408
Self-citationZhang, H., Li, X., Martin, D. B., & Aebersold, R. H. (2003) · Nature Biotechnology · doi:10.1038/nbt827 · Cited by 1,390
Precision Mapping of an In Vivo N-Glycoproteome Reveals Rigid Topological and Sequence Constraints
Zielinska, D. F., Gnad, F., Wiśniewski, J. R., & Mann, M. (2010) · Cell · doi:10.1016/j.cell.2010.04.012 · Cited by 905
Bennett, E. P., Mandel, U., Clausen, H., Gerken, T. A., Fritz, T. A., & Tabak, L. A. (2012) · Glycobiology · doi:10.1093/glycob/cwr182 · Cited by 876
Self-citationGahmberg, C. G., & Hakomori, S. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43774-5 · Cited by 698
Cited by
Sorted by citations
Items 101–111 of 111
Vorobyev, A., Zhurov, K. O., Laskay, Ü. A., & Tsybin, Y. O. (2015) · European Journal of Mass Spectrometry · doi:10.1255/ejms.1370 · Cited by 3
Kip, Ç., Demir, M. C., Hacıefendioğlu, D., Hamaloğlu, K. Ö., Çelikbıçak, Ö., & Tuncel, A. (2021) · Journal of Inorganic and Organometallic Polymers and Materials · doi:10.1007/s10904-021-01890-w · Cited by 3
Unveiling the presence of O-glycosylation in different glycoproteins present in chicken egg white
Landoni, M., Rodríguez, M., & Couto, A. S. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.103938 · Cited by 2
O-Glycoproteomics: Methods, Challenges, and New Opportunities
Riley, N. M., & Malaker, S. A. (2024) · Royal Society of Chemistry eBooks · doi:10.1039/9781839166433-00118 · Cited by 4
Progress of O-glycoprotein and O-glycoproteome analysis in secretion systems
Qian, X., Ying, W., Zhao, Y. K., & Zhang, Y. (2017) · Scientia Sinica Vitae · doi:10.1360/n052017-00170 · Cited by 1
Advances in O-GalNAc glycosylation research based on biological mass spectrometry
Zhao, X., Shen, B., Qian, X., & Qin, W. (2017) · Scientia Sinica Vitae · doi:10.1360/n052017-00137
Sun, X. J., Cheng, J., Tian, W., Gao, S., Guo, J., Hu, F., Zhang, H., Huang, X., Chen, D. D. Y., Chen, Y., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.15.204511
Analysis of O-Glycans by Oxidative Release Combined with 3-Nitrophenylhydrazine Derivatization
Min, Z., Wang, X., Xiaoqiu, Y., Zhang, Q., & Zheng, Q. (2025) · ACS Omega · doi:10.1021/acsomega.5c00652
Mass spectrometry-based O-GalNAc glycoproteomics analysis in complex biological samples
Zou, X., Deng, Y., Zhang, H., Hou, J., Xu, Z., & Zhang, Y. N. (2026) · Glycoscience & Therapy · doi:10.1016/j.glycos.2026.100060
Sweet code on plant proteins: The O-GlcNAc and O-fucose modification
Jia, X., Zheng, J., & Yin, H. (2026) · Glycoscience & Therapy · doi:10.1016/j.glycos.2026.100062
Kaynert, J. T., Hopf, C., Brand, S., Garbers, C., Pich, A., & Buettner, F. F. R. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.21.753134
Metadata
- Authors
- Levery, S. B., Steentoft, C., Halim, A., Narimatsu, Y., Clausen, H., & Vakhrushev, S. Y.
- Affiliations
- University of Copenhagen (DK)
- Corresponding author
- Vakhrushev, Sergey Y.
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 2015-01
- Volume
- 1850
- Issue
- 1
- Pages
- 33-42
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W2004160810
- Cited by
- 111
- References
- 93
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 5 · 2023: 3 · 2022: 7 · 2021: 14 · 2020: 11 · 2019: 9 · 2018: 11 · 2017: 18 · 2016: 16 · 2015: 12
- FWCI
- 1.44
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - General Subjects (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Funders
- The Danish National Research Foundation (DNRF107)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- O-glycosylation sites, O-glycans, glycan structure analysis, N-glycoproteomics
- MeSH terms
- Cell Line, Glycoproteins, Glycosylation, Humans, Polysaccharides, Mass Spectrometry, Proteome, Proteomics, Cell Line, Tumor
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
