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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.
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“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]
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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
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Palaniappan, K. K., & Bertozzi, C. R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00023 · Cited by 280
Bagdonaite, I., Malaker, S. A., Polasky, D. A., Riley, N. M., Schjoldager, K. T.-B. G., Vakhrushev, S. Y., Halim, A., Aoki-Kinoshita, K. F., Nesvizhskii, A. I., Bertozzi, C. R., et al. (2022) · Nature Reviews Methods Primers · doi:10.1038/s43586-022-00128-4 · Cited by 271
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Bagdonaite, I., & Wandall, H. H. (2018) · Glycobiology · doi:10.1093/glycob/cwy021 · Cited by 234
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Riley, N. M., Malaker, S. A., Drießen, M. D., & Bertozzi, C. R. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00218 · Cited by 222
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Riley, N. M., Bertozzi, C. R., & Pitteri, S. J. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r120.002277 · Cited by 237
The glycosylation in SARS-CoV-2 and its receptor ACE2
Gong, Y., Qin, S., Dai, L., & Tian, Z. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00809-8 · Cited by 226
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Riley, N. M., & Coon, J. J. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04810 · Cited by 184
Pagel, O., Loroch, S., Sickmann, A., & Zahedi, R. P. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2015.1042867 · Cited by 163
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Kizuka, Y., & Taniguchi, N. (2016) · Biomolecules · doi:10.3390/biom6020025 · Cited by 163
Characterizing the O-glycosylation landscape of human plasma, platelets, and endothelial cells
King, S. L., Joshi, H. J., Schjoldager, K. T.-B. G., Halim, A., Madsen, T. D., Dziegiel, M. H., Woetmann, A., Vakhrushev, S. Y., & Wandall, H. H. (2017) · Blood Advances · doi:10.1182/bloodadvances.2016002121 · Cited by 150
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Nason, R., Büll, C., Konstantinidi, A., Sun, L., Ye, Z., Halim, A., Du, W., Sørensen, D. M., Durbesson, F., Furukawa, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24366-4 · Cited by 123
Self-citationGoth, C. K., Halim, A., Khetarpal, S. A., Rader, D. J., Clausen, H., & Schjoldager, K. T.-B. G. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1511175112 · Cited by 123
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Steentoft, C., Migliorini, D., King-Peoples, T. R., Mandel, U., June, C. H., & Posey, A. D. (2018) · Glycobiology · doi:10.1093/glycob/cwy008 · Cited by 102
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Ye, Z., Mao, Y., Clausen, H., & Vakhrushev, S. Y. (2019) · Nature Methods · doi:10.1038/s41592-019-0504-x · Cited by 89
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Yang, S., Onigman, P., Wu, W. W., Sjögren, J., Nyhlén, H., Shen, R., & Cipollo, J. F. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b01834 · Cited by 89
Recent advances in mass spectrometric analysis of glycoproteins
Banazadeh, A., Veillon, L. J., Wooding, K. M., Zabet‐Moghaddam, M., & Mechref, Y. S. (2016) · Electrophoresis · doi:10.1002/elps.201600357 · Cited by 88
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Bagdonaite, I., Thompson, A. J., Wang, X., Søgaard, M., Fougeroux, C. E., Frank, M., Diedrich, J. K., Yates, J. R., Salanti, A., Vakhrushev, S. Y., et al. (2021) · Viruses · doi:10.3390/v13040551 · Cited by 77
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Bagdonaite, I., Nordén, R., Joshi, H. J., King, S. L., Vakhrushev, S. Y., Olofsson, S., & Wandall, H. H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.721746 · Cited by 68
Self-citationNarimatsu, H. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2015.1084874 · Cited by 66
Narimatsu, H., Kaji, H., Vakhrushev, S. Y., Clausen, H., Zhang, H., Noro, E., Togayachi, A., Nagai‐Okatani, C., Kuno, A., Zou, X., et al. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00515 · Cited by 67
Self-citationNarimatsu, Y., Joshi, H. J., Schjoldager, K. T.-B. G., Hintze, J., Halim, A., Steentoft, C., Nason, R., Mandel, U., Bennett, E., Clausen, H., et al. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.001121 · Cited by 61
Self-citationAdvancements in mass spectrometry-based glycoproteomics and glycomics
Lu, H., Zhang, Y., & Yang, P. (2016) · National Science Review · doi:10.1093/nsr/nww019 · Cited by 61
Liquid chromatography-tandem mass spectrometry-based fragmentation analysis of glycopeptides
Nilsson, J. (2016) · Glycoconjugate Journal · doi:10.1007/s10719-016-9649-3 · Cited by 58
Bagdonaite, I., Nordén, R., Joshi, H. J., Dabelsteen, S., Nyström, K., Vakhrushev, S. Y., Olofsson, S., & Wandall, H. H. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004784 · Cited by 56
Self-citationA Biologist's Field Guide to Multiplexed Quantitative Proteomics
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Self-citationHoffmann, M., Pioch, M., Pralow, A., Hennig, R., Kottler, R., Reichl, U., & Rapp, E. (2018) · PROTEOMICS · doi:10.1002/pmic.201800282 · Cited by 55
SweetNET: A Bioinformatics Workflow for Glycopeptide MS/MS Spectral Analysis
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Zhang, T., Miller, M. C., Zheng, Y., Zhang, Z., Xue, H., Zhao, D., Su, J., Mayo, K. H., Zhou, Y., & Tai, G. (2017) · Biochemical Journal · doi:10.1042/bcj20170143 · Cited by 50
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You, X. Y., Qin, H., & Ye, M. (2017) · Journal of Separation Science · doi:10.1002/jssc.201700834 · Cited by 45
Goth, C. K., Tuhkanen, H. E., Khan, H., Lackman, J. J., Wang, S., Narimatsu, Y., Hansen, L. H., Overall, C. M., Clausen, H., Schjoldager, K. T.-B. G., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.730614 · Cited by 49
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Self-citationNoborn, F., Toledo, A. G., Green, A., Nasir, W., Sihlbom, C., Nilsson, J., & Larson, G. (2016) · Scientific Reports · doi:10.1038/srep34537 · Cited by 40
Yamamoto, S., Kinoshita, M., & Suzuki, S. (2016) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2016.07.015 · Cited by 37
Xu, G., Goonatilleke, E., Wongkham, S., & Lebrilla, C. B. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05103 · Cited by 35
van Tol, W., Wessels, H. J. C. T., & Lefeber, D. J. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.12.006 · Cited by 34
Park, M., Reddy, G. R., Wallukat, G., Xiang, Y. K., & Steinberg, S. F. (2017) · Scientific Reports · doi:10.1038/s41598-017-06607-z · Cited by 33
Novel methods in glycomics: a 2019 update
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Vos, G. M., Weber, J., Sweet, I. R., Hooijschuur, K. C., Toraño, J. S., & Boons, G. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c00127 · Cited by 29
Nilsson, J., Brinkmalm, G., Ramadan, S., Gilborne, L., Noborn, F., Blennow, K., Wallin, A., Svensson, J., Abo-Riya, M. A., Huang, X., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-41897-5 · Cited by 29
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Joshi, H. J., Jørgensen, A., Schjoldager, K. T.-B. G., Halim, A., Dworkin, L. A., Steentoft, C., Wandall, H. H., Clausen, H., & Vakhrushev, S. Y. (2017) · Glycobiology · doi:10.1093/glycob/cwx104 · Cited by 28
Self-citationZhao, X., Zheng, S., Li, Y., Huang, J., Zhang, W., Xie, Y., Qin, W., & Qian, X. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b02228 · Cited by 29
Chen, Z., Wang, D., Yu, Q., Johnson, J., Shipman, R. D., Zhong, X., Huang, J., Yu, Q., Zetterberg, H., Asthana, S., et al. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00932 · Cited by 27
Yue, X., Qin, H., Chen, Y., Fang, Z., Liu, L., Zhu, H., Liu, X., Zhou, J., Tian, K., Qiao, X., et al. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c05236 · Cited by 26
Lackman, J. J., Goth, C. K., Halim, A., Vakhrushev, S. Y., Clausen, H., & Petäjä‐Repo, U. E. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.10.016 · Cited by 26
Self-citationValošková, K., Biebl, J., Roblek, M., Emtenani, S., Gyoergy, A., Mišová, M., Ratheesh, A., Reis-Rodrigues, P., Shkarina, K., Larsen, I. S. B., et al. (2019) · eLife · doi:10.7554/elife.41801 · Cited by 23
Self-citationNilsson, J., Noborn, F., Toledo, A. G., Nasir, W., Sihlbom, C., & Larson, G. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1539-1 · Cited by 23
Contessotto, P., Spelat, R., Ferro, F., Vysockas, V., Krivickienė, A., Jin, C., Chantepie, S., Chinello, C., Pauža, A. G., Valente, C., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36350-1 · Cited by 24
Miller, M. C., Zheng, Y., Zhou, Y., Tai, G., & Mayo, K. H. (2018) · Glycobiology · doi:10.1093/glycob/cwy085 · Cited by 21
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Self-citationBarroso, A., Giménez, E., Benavente, F., Barbosa, J., & Sanz‐Nebot, V. (2016) · Talanta · doi:10.1016/j.talanta.2016.07.055 · Cited by 18
Napoletano, C., Steentoff, C., Battisti, F., Ye, Z., Rahimi, H., Zizzari, I. G., Dionisi, M., Cerbelli, B., Tomao, F., French, D., et al. (2020) · Cancers · doi:10.3390/cancers12102841 · Cited by 18
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Kolli, V. S. K., Roth, H. A., Cruz, G. D. L., Fernando, G. S., & Dodds, E. D. (2015) · Analytica Chimica Acta · doi:10.1016/j.aca.2015.09.013 · Cited by 15
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Gashash, E. A., Aloor, A., Li, D., Zhu, H., Xu, X., Xiao, C., Zhang, J., Parameswaran, A., Song, J. K., Ma, C., et al. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00359 · Cited by 15
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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
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