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Predicting glycan structure from tandem mass spectrometry via deep learning
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Abstract
Glycans constitute the most complicated post-translational modification, modulating protein activity in health and disease. However, structural annotation from tandem mass spectrometry (MS/MS) data is a bottleneck in glycomics, preventing high-throughput endeavors and relegating glycomics to a few experts. Trained on a newly curated set of 500,000 annotated MS/MS spectra, here we present CandyCrunch, a dilated residual neural network predicting glycan structure from raw liquid chromatography–MS/MS data in seconds (top-1 accuracy: 90.3%). We developed an open-access Python-based workflow of raw data conversion and prediction, followed by automated curation and fragment annotation, with predictions recapitulating and extending expert annotation. We demonstrate that this can be used for de novo annotation, diagnostic fragment identification and high-throughput glycomics. For maximum impact, this entire pipeline is tightly interlaced with our glycowork platform and can be easily tested at https://colab.research.google.com/github/BojarLab/CandyCrunch/blob/main/CandyCrunch.ipynb . We envision CandyCrunch to democratize structural glycomics and the elucidation of biological roles of glycans.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
PyTorch: An Imperative Style, High-Performance Deep Learning Library
Paszke, A., Gross, S., Massa, F., Lerer, A., Bradbury, J., Chanan, G., Killeen, T., Lin, Z., Gimelshein, N., Antiga, L., et al. (2019) · arXiv · doi:10.48550/arxiv.1912.01703 · Cited by 31,473
Abraham, M. J., Murtola, T., Schulz, R., Páll, S., Smith, J. C., Hess, B., & Lindahl, E. (2015) · SoftwareX · doi:10.1016/j.softx.2015.06.001 · Cited by 27,190
Development and testing of a general amber force field
Wang, J.-M., Wolf, R., Caldwell, J., Kollman, P., & Case, D. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20035 · Cited by 18,318
Ankerst, M. (1999) · doi:10.1145/304181.304187 · Cited by 3,982
ACPYPE - AnteChamber PYthon Parser interfacE
da Silva, A. S., & Vranken, W. (2012) · BMC Research Notes · doi:10.1186/1756-0500-5-367 · Cited by 3,232
Highly accurate protein structure prediction for the human proteome
Tunyasuvunakool, K., Adler, J., Wu, Z., Green, T., Zielinski, M., Žídek, A., Bridgland, A., Cowie, A., Meyer, C., Laydon, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03828-1 · Cited by 3,025
A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
Domon, B., & Costello, C. E. (1988) · Glycoconjugate Journal · doi:10.1007/bf01049915 · Cited by 2,766
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635 · cited 1×
“The exact structure of complex carbohydrates is often key in mediating their function 3 , such as sialic acid only facilitating influenza infection in a particular linkage orientation 4 .”
GLYCAM06: A generalizable biomolecular force field. Carbohydrates
Kirschner, K. N., Yongye, A. B., Tschampel, S. M., González‐Outeiriño, J., Daniels, C. R., Foley, B. L., & Woods, R. J. (2007) · Journal of Computational Chemistry · doi:10.1002/jcc.20820 · Cited by 2,267
GlycoWorkbench: A Tool for the Computer-Assisted Annotation of Mass Spectra of Glycans
Ceroni, A., Maaß, K., Geyer, H., Geyer, R., Dell, A., & Haslam, S. M. (2008) · Journal of Proteome Research · doi:10.1021/pr7008252 · Cited by 1,055
Data Conversion with ProteoWizard msConvert
Adusumilli, R., & Mallick, P. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6747-6_23 · Cited by 609
Laughlin, S. T., & Bertozzi, C. R. (2007) · Nature Protocols · doi:10.1038/nprot.2007.422 · Cited by 337
Negative-Ion Electrospray Mass Spectrometry of Neutral Underivatized Oligosaccharides
Chai, W., Piskarev, V. E., & Lawson, A. M. (2001) · Analytical Chemistry · doi:10.1021/ac0010126 · Cited by 221
MS2DeepScore: a novel deep learning similarity measure to compare tandem mass spectra
Huber, F., van der Burg, S., van der Hooft, J. J. J., & Ridder, L. (2021) · Journal of Cheminformatics · doi:10.1186/s13321-021-00558-4 · Cited by 219
GlycoPOST realizes FAIR principles for glycomics mass spectrometry data
Watanabe, Y., Aoki-Kinoshita, K. F., Ishihama, Y., & Okuda, S. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1012 · Cited by 194
Pyteomics 4.0: Five Years of Development of a Python Proteomics Framework
Levitsky, L. I., Klein, J., Ivanov, M. V., & Gorshkov, M. V. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00717 · Cited by 174
Characterization of isomeric glycan structures by LC‐MS/MS
Veillon, L. J., Huang, Y., Peng, W., Dong, X., Cho, B. G., & Mechref, Y. S. (2017) · Electrophoresis · doi:10.1002/elps.201700042 · Cited by 163
GlyTouCan: an accessible glycan structure repository
Tiemeyer, M., Aoki, K., Paulson, J. C., Cummings, R. D., York, W. S., Karlsson, N. G., Lisacek, F., Packer, N. H., Campbell, M. P., Aoki, N. P., et al. (2017) · Glycobiology · doi:10.1093/glycob/cwx066 · Cited by 158
Self-citationKawahara, R., Chernykh, A., Alagesan, K., Bern, M. W., Cao, W., Chalkley, R. J., Cheng, K., Choo, M. S., Edwards, N. J., Goldman, R., et al. (2021) · Nature Methods · doi:10.1038/s41592-021-01309-x · Cited by 148
Structural Diversity of Human Gastric Mucin Glycans
Jin, C., Kenny, D. T., Skoog, E. C., Padra, M., Adamczyk, B., Vitizeva, V., Thorell, A., Venkatakrishnan, V., Lindén, S. K., & Karlsson, N. G. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.067983 · Cited by 148
Self-citationA Faster Algorithm for Detecting Network Motifs
Wernicke, S. (2005) · Lecture notes in computer science · doi:10.1007/11557067_14 · Cited by 144
UniCarb-DB: a database resource for glycomic discovery
Hayes, C. A., Karlsson, N. G., Struwe, W. B., Lisacek, F., Rudd, P. M., Packer, N. H., & Campbell, M. P. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr137 · Cited by 142
Self-citationASAM: Adaptive Sharpness-Aware Minimization for Scale-Invariant Learning of Deep Neural NetworksPreprint
Kwon, J., Kim, J.-S., Park, H., & Choi, I. K. (2021) · arXiv (Cornell University) · doi:10.48550/arxiv.2102.11600 · Cited by 136
Structural Feature Ions for Distinguishing N- and O-Linked Glycan Isomers by LC-ESI-IT MS/MS
Everest‐Dass, A., Abrahams, J. L., Kolarich, D., Packer, N. H., & Campbell, M. P. (2013) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-013-0610-4 · Cited by 132
Sequence-to-sequence translation from mass spectra to peptides with a transformer model
Yilmaz, M., Fondrie, W. E., Bittremieux, W., Melendez, C., Nelson, R., Ananth, V., Oh, S., & Noble, W. S. (2024) · Nature Communications · doi:10.1038/s41467-024-49731-x · Cited by 125
Influence of Host Sialic Acid Receptors Structure on the Host Specificity of Influenza Viruses
Zhao, C., & Pu, J. (2022) · Viruses · doi:10.3390/v14102141 · Cited by 120
High-Throughput Glycomic Methods
Trbojević‐Akmačić, I., Lageveen‐Kammeijer, G. S. M., Heijs, B., Pribić, T., Deriš, H., Wuhrer, M., & Lauc, G. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01031 · Cited by 109
PolyLoss: A Polynomial Expansion Perspective of Classification Loss FunctionsPreprint
Leng, Z., Tan, M., Liu, C., Cubuk, E. D., Shi, X., Cheng, S., & Anguelov, D. (2022) · arXiv (Cornell University) · doi:10.48550/arxiv.2204.12511 · Cited by 109
Deep-Learning Resources for Studying Glycan-Mediated Host-Microbe Interactions
Bojar, D., Powers, R. K., Camacho, D. M., & Collins, J. J. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.10.004 · Cited by 80
Self-citationpymzML v2.0: introducing a highly compressed and seekable gzip format
Kösters, M., Leufken, J., Schulze, S., Sugimoto, K., Klein, J., Zahedi, R. P., Hippler, M., Leidel, S. A., & Fufezan, C. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty046 · Cited by 76
Classification of Tandem Mass Spectra for Identification of N- and O-linked Glycopeptides
Eshghi, S. T., Yang, W., Hu, Y., Shah, P., Sun, S., Li, X. D., & Zhang, H. (2016) · Scientific Reports · doi:10.1038/srep37189 · Cited by 66
Glycowork: A Python package for glycan data science and machine learning
Thomès, L., Burkholz, R., & Bojar, D. (2021) · Glycobiology · doi:10.1093/glycob/cwab067 · Cited by 58
Self-citationYu, J., Schorlemer, M., Toledo, A. G., Pett, C., Sihlbom, C., Larson, G., Westerlind, U., & Nilsson, J. (2015) · Chemistry - A European Journal · doi:10.1002/chem.201503659 · Cited by 53
Software Platform for High-Throughput Glycomics
Vakhrushev, S. Y., Dadimov, D., & Peter‐Katalinić, J. (2009) · Analytical Chemistry · doi:10.1021/ac802408f · Cited by 48
RNASeqGUI: a GUI for analysing RNA-Seq data
Russo, F., & Angelini, C. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu308 · Cited by 46
Correcting for sparsity and interdependence in glycomics by accounting for glycan biosynthesis
Bao, B., Kellman, B. P., Chiang, A. W. T., Zhang, Y., Sorrentino, J. T., York, A. K., Mohammad, M. A., Haymond, M. W., Bode, L., & Lewis, N. E. (2021) · Nature Communications · doi:10.1038/s41467-021-25183-5 · Cited by 45
The influence of sialylation on glycan negative ion dissociation and energetics
Seymour, J. L., Costello, C. E., & Zaia, J. (2006) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2006.02.022 · Cited by 44
glypy: An Open Source Glycoinformatics Library
Klein, J., & Zaia, J. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00367 · Cited by 43
Cancer glycomics offers potential biomarkers and therapeutic targets in the framework of 3P medicine
Guo, Y., Jia, W., Yang, J., & Zhan, X. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.970489 · Cited by 35
Harvey, D. J. (2022) · Mass Spectrometry Reviews · doi:10.1002/mas.21806 · Cited by 32
Plasma N-glycome shows continuous deterioration as the diagnosis of insulin resistance approaches
Cvetko, A., Mangino, M., Tijardović, M., Kifer, D., Falchi, M., Keser, T., Perola, M., Spector, T. D., Lauc, G., Menni, C., et al. (2021) · BMJ Open Diabetes Research & Care · doi:10.1136/bmjdrc-2021-002263 · Cited by 31
Horlacher, O., Jin, C., Alocci, D., Mariethoz, J. A., Müller, M., Karlsson, N. G., & Lisacek, F. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b02754 · Cited by 30
Self-citationGlycoDraw: a python implementation for generating high-quality glycan figures
Lundstrøm, J., Urban, J., Thomès, L., & Bojar, D. (2023) · Glycobiology · doi:10.1093/glycob/cwad063 · Cited by 24
Self-citationIntegrated N- and O-Glycomics of Acute Myeloid Leukemia (AML) Cell Lines
Blöchl, C., Wang, D., Madunić, K., Lageveen‐Kammeijer, G. S. M., Huber, C. G., Wuhrer, M., & Zhang, T. (2021) · Cells · doi:10.3390/cells10113058 · Cited by 23
Thomès, L., Karlsson, V., Lundstrøm, J., & Bojar, D. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112710 · Cited by 23
Self-citationBreast Milk Oligosaccharides Contain Immunomodulatory Glucuronic Acid and LacdiNAc
Jin, C., Lundstrøm, J., Korhonen, E., Luis, A. S., & Bojar, D. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100635 · Cited by 22
Self-citationEfficiently predicting high resolution mass spectra with graph neural networksPreprint
Murphy, M. A., Jegelka, S., Fraenkel, E., Kind, T., Healey, D., & Butler, T. (2023) · arXiv (Cornell University) · doi:10.48550/arxiv.2301.11419 · Cited by 22
Malm, E., Srivastava, V., Sundqvist, G., & Bulone, V. (2014) · BMC Bioinformatics · doi:10.1186/s12859-014-0441-8 · Cited by 21
Leoz, M. L. A. D., Simón‐Manso, Y., Woods, R. J., & Stein, S. E. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-2106-8 · Cited by 21
Kumozaki, S., Sato, K., & Sakakibara, Y. (2015) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2015.2430317 · Cited by 19
Altenburg, T., Giese, S. H., Wang, S., Muth, T., & Renard, B. Y. (2022) · Nature Machine Intelligence · doi:10.1038/s42256-022-00467-7 · Cited by 16
HexNAcQuest: A Tool to Distinguish O-GlcNAc and O-GalNAc
Li, W., Hou, C., Li, Y., Wu, C., & Ma, J. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00172 · Cited by 14
Computational Modeling of O-Linked Glycan Biosynthesis in CHO Cells
Kouka, T., Akase, S., Sogabe, I., Jin, C., Karlsson, N. G., & Aoki-Kinoshita, K. F. (2022) · Molecules · doi:10.3390/molecules27061766 · Cited by 12
Self-citationMadunić, K., Luijkx, Y. M. C. A., Mayboroda, O. A., Janssen, G. M. C., van Veelen, P. A., Strijbis, K., Wennekes, T., Lageveen‐Kammeijer, G. S. M., & Wuhrer, M. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100501 · Cited by 9
GlycoDeNovo2: An Improved MS/MS-Based De Novo Glycan Topology Reconstruction Algorithm
Chen, Z., Wei, J., Tang, Y., Lin, C., Costello, C., & Hong, P.-Y. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00288 · Cited by 8
Profiling the glycome of Cardicola forsteri, a blood fluke parasitic to bluefin tuna
Coff, L., Abrahams, J. L., Collett, S., Power, C., Nowak, B. F., Kolarich, D., Bott, N. J., & Ramsland, P. A. (2021) · International Journal for Parasitology · doi:10.1016/j.ijpara.2021.06.004 · Cited by 6
Predicting glycan structure from tandem mass spectrometry via deep learning
Urban, J., Chunsheng, J., Thomsson, K. A., Karlsson, N. G., Ives, C. M., Fadda, E., & Bojar, D. (2023) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.7940046 · Cited by 1
Self-citation
Flagged first, then by citations
Research works printed but not linked: 2
- Rudd, P. M. et al. in Essentials of Glycobiology (eds Varki, A. et al.) Ch. 51 (Cold Spring Harbor Laboratory Press, 2022).
- Guo, C., Pleiss, G., Sun, Y. & Weinberger, K. Q. On calibration of modern neural networks. Preprint at http://arxiv.org/abs/1706.04599 (2017). · arXiv
Cited by
Sorted by citations
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Bechtella, L., Jin, C., Fentker, K., Ertürk, G. R., Safferthal, M., Polewski, Ł., Götze, M., Graeber, S. Y., Vos, G. M., Struwe, W. B., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46825-4 · Cited by 59
Self-citationSignificance of Artificial Intelligence in the Study of Virus–Host Cell Interactions
Elste, J., Saini, A., Mejía-Alvarez, R., Mejía, A., Millán‐Pacheco, C., Swanson-Mungerson, M. A., & Tiwari, V. (2024) · Biomolecules · doi:10.3390/biom14080911 · Cited by 38
Sugar symphony: glycosylation in cancer metabolism and stemness
Varadharaj, V., Petersen, W., Batra, S. K., & Ponnusamy, M. P. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.09.006 · Cited by 33
Glycomics in Human Diseases and Its Emerging Role in Biomarker Discovery
Onigbinde, S. B., Adeniyi, M., Daramola, O. E., Chukwubueze, F. M., Bhuiyan, M. M. A. A., Nwaiwu, J. I., Bhattacharjee, T., & Mechref, Y. S. (2025) · Biomedicines · doi:10.3390/biomedicines13082034 · Cited by 36
GlycoDraw: a python implementation for generating high-quality glycan figures
Lundstrøm, J., Urban, J., Thomès, L., & Bojar, D. (2023) · Glycobiology · doi:10.1093/glycob/cwad063 · Cited by 24
Self-citationGenerating 3D Models of Carbohydrates with GLYCAM-WebPreprint
Grant, O. C., Wentworth, D., Holmes, S. G., Kandel, R., Sehnal, D., Wang, X., Xiao, Y., Sheppard, P., Grelsson, T., Coulter, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.08.652828 · Cited by 24
Wang, Z., Zhang, J., & Li, L. (2024) · PROTEOMICS · doi:10.1002/pmic.202400057 · Cited by 22
Compositional data analysis enables statistical rigor in comparative glycomics
Bennett, A., Lundstrøm, J., Chatterjee, S., Thaysen‐Andersen, M., & Bojar, D. (2025) · Nature Communications · doi:10.1038/s41467-025-56249-3 · Cited by 19
Self-citationZhang, J., Xu, Z., Zhong, C. Y., Liu, H., Zhu, Q., Sun, Z., Guo, Q. M., & Cui, S. W. (2025) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.70379 · Cited by 18
Geue, N., Safferthal, M., & Pagel, K. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202511591 · Cited by 16
Decoding glycomics with a suite of methods for differential expression analysis
Lundstrøm, J., Urban, J., & Bojar, D. (2023) · Cell Reports Methods · doi:10.1016/j.crmeth.2023.100652 · Cited by 15
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Wang, T., Huang, W., Xu, K., Sun, Y., Zhang, Q. C., Yan, C., Li, Z., & Yan, N. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2423943122 · Cited by 11
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Xiao, Y., Zhang, S., Gao, X., Li, T., Zhang, H., Zhang, P., & Huang, S. (2026) · Science Advances · doi:10.1126/sciadv.aea8462 · Cited by 10
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Loponte, H. F. B. R., Zheng, J., Ding, Y., Oliveira, I. D. A., Basse, K., Todeschini, A. R., Horvatovich, P. L., & Lageveen‐Kammeijer, G. S. M. (2025) · Nature Communications · doi:10.1038/s41467-025-65265-2 · Cited by 12
Zhu, K., Wang, W., Ye, X., & Chen, S. (2024) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2024.117721 · Cited by 10
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Xia, B., Yao, G., Fan, J., Wei, F., Tan, J., Li, P., Wen, L., & Gao, Z. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c22760 · Cited by 3
Yang, M., Yao, Y., Qin, X., Wang, Z., Du, Y., & Dai, Y. (2026) · Food Bioscience · doi:10.1016/j.fbio.2026.108708 · Cited by 3
Kong, X., Zhang, J., Tang, H., Liu, H., Jia, X., Yin, L., Zhu, Q., & Guo, Q. M. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112751 · Cited by 3
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Joo, J., Koid, A., Kim, H., Ghosh, A., Lee, S., Sheshova, M., & Lupoli, T. J. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00338 · Cited by 3
Urban, J., Joeres, R., Thomès, L., Thomsson, K. A., & Bojar, D. (2024) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-024-05500-9 · Cited by 3
Self-citationUrban, J., Joeres, R., & Bojar, D. (2024) · Bioinformatics Advances · doi:10.1093/bioadv/vbaf310 · Cited by 3
Self-citationLiu, Q., Chen, P., Bu, Q., Sun, Y., Chen, Z., Xu, X., & Wang, D. (2025) · Environmental Chemistry and Ecotoxicology · doi:10.1016/j.enceco.2025.07.022 · Cited by 3
Nath, D., Ghosh, S., Bhattacharya, S., Hiremath, P., & Deb, D. (2025) · Progress in optical science and photonics · doi:10.1007/978-981-95-1561-5_6 · Cited by 2
Recent advances in glyco-nanoparticles for probing the glyco-codes of cancer
Ullah, A. K. M. A., & Huang, X. (2025) · Carbohydrate Research · doi:10.1016/j.carres.2025.109757 · Cited by 2
Song, K., Wu, J., Zhen, X., Zhu, R., Li, J., & Han, P. (2026) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2026.105701 · Cited by 2
Artificial intelligence empowering polysaccharide research in drug development
Yu, J., Ningyun, L., Xu, H., & Luo, C. (2026) · Targetome · doi:10.48130/targetome-0026-0026 · Cited by 2
Chen, S., Tao, L., Li, Q., Duan, L., Chen, C., Huang, Z., Cui, Y.-L., Fu, Z.-F., Chen, X., Deng, X.-B., et al. (2026) · Food & medicine homology. · doi:10.26599/fmh.2026.9420165 · Cited by 2
Qin, S., & Tian, Z. (2024) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-024-05505-4 · Cited by 2
Fritsche, S., & Möckl, L. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1519831 · Cited by 2
Dziekonski, E. T. (2025) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2025.117524 · Cited by 1
Wang, Y., Zhang, X., Sui, B., Ma, S., Zhang, J., Yu, A., Xi, H., & Zhao, W. (2026) · Microchemical Journal · doi:10.1016/j.microc.2026.116825 · Cited by 1
An, Z., Chen, L., Bu, C., Shi, D., Zhang, B., Jin, L., & Chi, L. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c00995 · Cited by 1
Understanding glycan structure and function through artificial intelligence
Coff, L., Bashir, U., & Bojar, D. (2026) · BBA Advances · doi:10.1016/j.bbadva.2026.100196 · Cited by 1
Self-citationFang, Z., Ma, M., Yu, G., & Shang, Q. (2026) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2026.125596 · Cited by 1
Ratios in Disguise, Truths Arise: Glycomics Meets Compositional Data AnalysisPreprint
Bennett, A., Lundstrøm, J., Chatterjee, S., Thaysen‐Andersen, M., & Bojar, D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.09.598163 · Cited by 1
Self-citationA Glycan-Aware Diffusion Model for Carbohydrate and Glycoprotein Structure PredictionPreprint
Sundar, K., & Yang, H. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.16.738959 · Cited by 1
Decoding Glycomics: Differential Expression ReimaginedPreprint
Lundstrøm, J., Urban, J., & Bojar, D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.04.551938
Self-citationIonization Characteristics of Glycan Homologues in Various Modes of Electrospray
Allen, N. R., Jeet, K., Ogunsanya, T. I., Ferraro, I., Fernandes, N., Li, H., Webster, T. A., Mason, C., & Li, A. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00425
Geue, N., Safferthal, M., & Pagel, K. (2025) · Angewandte Chemie · doi:10.1002/ange.202511591
Yang, J., Rong, Y., Liu, Z., Gao, L.-J., Liu, Y., Liu, W.-Y., Zhou, J., & Chen, M. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c00791
Advances in MS-based glycomics for biomedical research
Solomon, J., Sanni, A., Purba, W. T., Oluokun, O., Sahioun, S., Fowowe, M., Oluokun, A., Hussein, A., & Mechref, Y. S. (2025) · Analytical Methods · doi:10.1039/d5ay01169h · Cited by 1
Glycomics in the Clinic:A Brief Introduction toGlycosylation-Informed Medicine
Link‐Lenczowski, P. (2025) · Bio-Algorithms and Med-Systems · doi:10.5604/01.3001.0055.5391
Optimization of LC-ExD methods for glycopeptides on an Omnitrap-Orbitrap platform
Downs, M. J., Xia, C., Lin, C., & Zaia, J. (2026) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-026-06400-w
Lin, Y., Lee, Y., Tzeng, H.-E., Wu, W.-H., & Hsiao, K. (2026) · Journal of physiological investigation. · doi:10.4103/ejpi.ejpi-d-25-00065 · Cited by 1
The non-scaffold effects of natural polysaccharides in promoting organ regeneration: a review
Lei, S., Chang, P., Li, L., Niu, Y., Yu, J. M., & Gao, J.-L. (2026) · Journal of Biological Engineering · doi:10.1186/s13036-026-00655-8
Pushing Frontiers for Proteoglycans
Maciej-Hulme, M. L. (2026) · Proteoglycan Research · doi:10.1002/pgr2.70046
Yan, Y., Zhu, Y., Wang, Y., Dai, L., Zou, L., & Wang, Z. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-026-04475-2
Cheng, Y., Liu, J., Gong, B., 裴建元, Zhuang, X., Zeng, C., Zhang, H., Agu, E., Wang, Y., Duan, Z., et al. (2026) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2026.118863
Li, X., Tian, H., Wang, Y., & Yu, Y. (2026) · Applied and Environmental Microbiology · doi:10.1128/aem.02282-25
Li, C., Li, S., Sheng, A., Wang, R., & Sun, X. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.7043795
Biological Functions of Glycosylation and Their Application in Glycoengineered Therapeutics
Kubalek, C., Gardiner, S., Heaps, W. P., McCammon, K. M., Talcott, S., Argyle, M., Bundy, B. C., & Corte, D. D. (2026) · ChemEngineering · doi:10.3390/chemengineering10070085
Wang, Z., Zhang, R., Ling, N., Gao, M., Wang, Q., Gao, X., Guo, C., Tian, H., Wq, L., Xing, Z., et al. (2026) · Phytomedicine · doi:10.1016/j.phymed.2026.158638
GlycoMsHelper: a simple and traceable workflow for Glycomic mass spectrometry data interpretation
Kong, W.-Z., Guérardel, Y., & Fujita, M. (2026) · Glycobiology · doi:10.1093/glycob/cwag057
Sabbor, F., Hussain, S., Lu, P., & Wang, C. (2026) · doi:10.1021/bk-2026-1528.ch001
Cheong, K., Pan, T., Yao, W., Wang, M., Zhong, S., & Sathuvan, M. (2026) · Microchemical Journal · doi:10.1016/j.microc.2026.119477
An engineered nanopore identifies saccharides, amino acids, peptides and ribonucleotides
Yao, L., Wang, Z., Chen, J., Wen, S. U. N., Wang, K., Xiao, Y., Zhang, H., Li, W., Wang, Y., Zhao, L., et al. (2026) · Nature Biotechnology · doi:10.1038/s41587-026-03308-9
Single-monosaccharide resolution glycan profiling enabled by the nanopipette
Ma, H., Li, Y. F., Xu, Z., Ma, W., Xia, B., Gao, Z., Li, T., & Ying, Y. (2026) · Chemical Science · doi:10.1039/d6sc02337a
Harvey, D. J. (2026) · Mass Spectrometry Reviews · doi:10.1002/mas.70029
Li, C., Li, S., Sheng, A., Wang, R., & Sun, X. (2026) · Journal of Chromatography B · doi:10.1016/j.jchromb.2026.125305
O'Connor, P., Murphy, G., & Walsh, N. (2025) · International Journal of Pharmaceutical and Phytopharmacological Research · doi:10.51847/dcbijoo69g
Zhu, J., Huang, S., & Zhang, N. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27209032
Zhang, S., 郝少龙, Dong, X., Deng, Q., Liu, J., Wen, T., & Han, W. (2026) · Cancer Pathogenesis and Therapy · doi:10.1016/j.cpt.2026.10.001
Deng, F., Yang, Y., Hu, Y., Gao, L., Gong, W., Cheng, J., Yang, B., Feng, L., & Jia, X. (2026) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2026.101822
Metadata
- Authors
- Urban, J., Jin, C., Thomsson, K. A., Karlsson, N. G., Ives, C. M., Fadda, E., & Bojar, D.
- Affiliations
- Wallenberg Centre for Molecular and Translational Medicine (SE)
- University of Gothenburg (SE)
- OsloMet – Oslo Metropolitan University (NO)
- National University of Ireland, Maynooth (IE)
- University of Southampton (GB)
- Corresponding author
- Bojar, Daniel
- Venue
- Nature Methods
- Published
- 2024-07
- Volume
- 21
- Issue
- 7
- Pages
- 1206-1215
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- PMC
- PMC11239490
- OpenAlex
- W4400208210
- Cited by
- 79
- References
- 58
- Citations by year
- 2026: 36 · 2025: 26 · 2024: 14
- FWCI
- 10.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Nature Methods (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (acceptedVersion, other-oa)
- Funders
- Knut och Alice Wallenbergs Stiftelse
- Vetenskapsrådet (BioMS)
- Science Foundation Ireland (20/FFP-P/8809)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- glycan structure prediction, tandem mass spectrometry, deep learning, glycomics, fragment identification, post-translational modification
- MeSH terms
- Deep Learning, Chromatography, Liquid, Humans, Polysaccharides, Software, Neural Networks, Computer, Tandem Mass Spectrometry, Glycomics, Workflow
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