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
Dystroglycan: from biosynthesis to pathogenesis of human disease
Barresi, R., & Campbell, K. P. (2006) · Journal of Cell Science · doi:10.1242/jcs.02814 · Cited by 608
A Genetic Approach to Mammalian Glycan Function
Lowe, J. B., & Marth, J. D. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161809 · Cited by 602
A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation
Hang, H. C., Yu, C., Kato, D. L., & Bertozzi, C. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2335201100 · Cited by 580
The utility of ETD mass spectrometry in proteomic analysis
Mikesh, L. M., Ueberheide, B. M., Chi, A., Coon, J. J., Syka, J. E. P., Shabanowitz, J., & Hunt, D. F. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.10.003 · Cited by 545
Studies on the Chemical and Enzymatic Modification of Glycoproteins
Lenten, L. V., & Ashwell, G. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62392-0 · Cited by 489
Polypeptide GalNAc-transferase T3 and Familial Tumoral Calcinosis
Kato, K., Jeanneau, C., Tarp, M. A., Benet‐Pagès, A., Lorenz‐Depiereux, B., Bennett, E., Mandel, U., Strom, T. M., & Clausen, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602469200 · Cited by 424
Self-citationWells, L., Vosseller, K., Cole, R. N., Cronshaw, J. M., Matunis, M. J., & Hart, G. W. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200048-mcp200 · Cited by 421
Glycoproteomics based on tandem mass spectrometry of glycopeptides
Wuhrer, M., Catalina, M., Deelder, A. M., & Hokke, C. H. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.09.041 · Cited by 417
Tretter, V. E., Altmann, F., & März, L. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16166.x · Cited by 410
Structures of Sialylated O-Linked Oligosaccharides of Bovine Peripheral Nerve α-Dystroglycan
Chiba, A., Matsumura, K., Yamada, H., Inazu, T., Shimizu, T., Kusunoki, S., Kanazawa, I., Kobata, A., & Endo, T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2156 · Cited by 402
Mirgorodskaya, E. E., Roepstorff, P., & Zubarev, R. A. (1999) · Analytical Chemistry · doi:10.1021/ac990578v · Cited by 382
Kelleher, N. L., Zubarev, R. A., Bush, K. A., Furie, B., Furie, B. C., McLafferty, F. W., & Walsh, C. T. (1999) · Analytical Chemistry · doi:10.1021/ac990684x · Cited by 367
Boyce, M., Carrico, I. S., Ganguli, A. S., Yu, S., Hangauer, M. J., Hubbard, S. C., Kohler, J. J., & Bertozzi, C. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010045108 · Cited by 353
Mining the O-glycoproteome using zinc-finger nuclease–glycoengineered SimpleCell lines
Steentoft, C., Vakhrushev, S. Y., Vester-Christensen, M. B., Schjoldager, K. T.-B. G., Kong, Y., Bennett, E., Mandel, U., Wandall, H. H., Levery, S. B., & Clausen, H. (2011) · Nature Methods · doi:10.1038/nmeth.1731 · Cited by 350
Self-citationVosseller, K., Trinidad, J. C., Chalkley, R. J., Specht, C. G., Thalhammer, A., Lynn, A. J., Snedecor, J., Guan, S., Medzihradszky, K. F., Maltby, D. A., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500040-mcp200 · Cited by 346
Enrichment of glycopeptides for glycan structure and attachment site identification
Nilsson, J., Rüetschi, U., Halim, A., Hesse, C., Carlsohn, E., Brinkmalm, G., & Larson, G. (2009) · Nature Methods · doi:10.1038/nmeth.1392 · Cited by 322
Self-citationDecision tree–driven tandem mass spectrometry for shotgun proteomics
Swaney, D. L., McAlister, G. C., & Coon, J. J. (2008) · Nature Methods · doi:10.1038/nmeth.1260 · Cited by 318
Dystroglycan Function Requires Xylosyl- and Glucuronyltransferase Activities of LARGE
Inamori, K., Yoshida‐Moriguchi, T., Hara, Y., Anderson, M. E., Yu, L. P., & Campbell, K. P. (2012) · Science · doi:10.1126/science.1214115 · Cited by 301
Alfaro, J. F., Gong, C., Monroe, M. E., Aldrich, J. T., Clauss, T. R., Purvine, S. O., Wang, Z., Camp, D., Shabanowitz, J., Stanley, P., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200425109 · Cited by 298
Exploring the Sialiome Using Titanium Dioxide Chromatography and Mass Spectrometry
Larsen, M. R., Jensen, S. S., Jakobsen, L. A., & Heegaard, N. H. H. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700086-mcp200 · Cited by 278
Mucin‐type O‐glycosylation – putting the pieces together
Jensen, P. H., Kolarich, D., & Packer, N. H. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07429.x · Cited by 252
Halim, A., Brinkmalm, G., Rüetschi, U., Brinkmalm, A., Portelius, E., Zetterberg, H., Blennow, K., Larson, G., & Nilsson, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102664108 · Cited by 250
Self-citationLocation, location, location: new insights into O-GalNAc protein glycosylation
Gill, D. J., Clausen, H., & Bard, F. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.11.004 · Cited by 248
Self-citationPalmisano, G., Lendal, S. E., Engholm‐Keller, K., Leth‐Larsen, R., Parker, B. L., & Larsen, M. R. (2010) · Nature Protocols · doi:10.1038/nprot.2010.167 · Cited by 241
Chalkley, R. J., Thalhammer, A., Schoepfer, R., & Burlingame, A. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900288106 · Cited by 239
Deciphering a global network of functionally associated post‐translational modifications
Mínguez, P., Parca, L., Diella, F., Mende, D. R., Kumar, R. D., Helmer‐Citterich, M., Gavin, A., van Noort, V., & Bork, P. (2012) · Molecular Systems Biology · doi:10.1038/msb.2012.31 · Cited by 238
Zhurov, K. O., Fornelli, L., Wodrich, M. D., Laskay, Ü. A., & Tsybin, Y. O. (2013) · Chemical Society Reviews · doi:10.1039/c3cs35477f · Cited by 231
Wiesner, J., Premsler, T., & Sickmann, A. (2008) · PROTEOMICS · doi:10.1002/pmic.200800329 · Cited by 224
SGK196 Is a Glycosylation-Specific O -Mannose Kinase Required for Dystroglycan Function
Yoshida‐Moriguchi, T., Willer, T., Anderson, M. E., Venzke, D. P., Whyte, T., Francesco Muntoni, A., Lee, H., Nelson, S. F., Yu, L. P., & Campbell, K. P. (2013) · Science · doi:10.1126/science.1239951 · Cited by 216
Thaysen‐Andersen, M., & Packer, N. H. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.05.002 · Cited by 207
Schjoldager, K. T.-B. G., & Clausen, H. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.09.014 · Cited by 193
Self-citationThe heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality
Boskovski, M. T., Yuan, S., Borbye‐Lorenzen, N., Goth, C. K., Makova, S. Z., Clausen, H., Brueckner, M. K., & Khokha, M. K. (2013) · Nature · doi:10.1038/nature12723 · Cited by 174
Self-citationPalmisano, G., Melo‐Braga, M. N., Engholm‐Keller, K., Parker, B. L., & Larsen, M. R. (2012) · Journal of Proteome Research · doi:10.1021/pr2011268 · Cited by 168
N- and O-Glycosylation in the Murine Synaptosome
Trinidad, J. C., Schoepfer, R., Burlingame, A. L., & Medzihradszky, K. F. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030007 · Cited by 164
Iwai, T., Kudo, T., Kawamoto, R., Kubota, T., Togayachi, A., Hiruma, T., Okada, T., Kawamoto, T., Morozumi, K., & Narimatsu, H. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407983102 · Cited by 159
Galactose Oxidase from Polyporus circinatus, Fr
Cooper, J. A. D., Smith, W., Bacila, M., & Medina, H. S. G. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70223-8 · Cited by 158
Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins
Vester-Christensen, M. B., Halim, A., Joshi, H. J., Steentoft, C., Bennett, E., Levery, S. B., Vakhrushev, S. Y., & Clausen, H. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313446110 · Cited by 154
Self-citationHalim, A., Nilsson, J., Rüetschi, U., Hesse, C., & Larson, G. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013649 · Cited by 151
Self-citationIchikawa, S., Sorenson, A. H., Austin, A. M., Mackenzie, D. S., Fritz, T. A., Moh, A., Hui, S. L., & Econs, M. J. (2009) · Endocrinology · doi:10.1210/en.2008-0877 · Cited by 148
Gerken, T. A., Jamison, O., Perrine, C. L., Collette, J. C., Moinova, H., Ravi, L., Markowitz, S. D., Shen, W., Patel, H. V., & Tabak, L. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.218701 · Cited by 145
O-Glycosylation Modulates Proprotein Convertase Activation of Angiopoietin-like Protein 3
Schjoldager, K. T.-B. G., Vester-Christensen, M. B., Bennett, E., Levery, S. B., Schwientek, T., Yin, W., Blixt, O., & Clausen, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.156950 · Cited by 135
Self-citationSchjoldager, K. T.-B. G., Vakhrushev, S. Y., Kong, Y., Steentoft, C., Nudelman, A. S., Pedersen, N. B., Wandall, H. H., Mandel, U., Bennett, E., Levery, S. B., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203563109 · Cited by 132
Self-citationPalmisano, G., Parker, B. L., Engholm‐Keller, K., Lendal, S. E., Kulej, K., Schulz, M., Schwämmle, V., Graham, M. E., Saxtorph, H., Cordwell, S. J., et al. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.017509 · Cited by 125
Probing Glycosyltransferase Activities with the Staudinger Ligation
Hang, H. C., Yu, C., Pratt, M. R., & Bertozzi, C. R. (2003) · Journal of the American Chemical Society · doi:10.1021/ja037692m · Cited by 120
Hara, Y., Kanagawa, M., Kunz, S., Yoshida‐Moriguchi, T., Satz, J. S., Kobayashi, Y. M., Zhu, Z., Burden, S. J., Oldstone, M. B. A., & Campbell, K. P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114836108 · Cited by 113
Finne, J., Krusius, T., Margolis, R. K., & Margolis, R. U. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86708-x · Cited by 113
Mass spectrometric analysis of N- and O-glycosylation of tissues and cells
HASLAM, S., NORTH, S., & DELL, A. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.08.006 · Cited by 111
Mass Spectrometric Determination of the Sites of O-Glycan Attachment with Low Picomolar Sensitivity
Rademaker, G. J., Pergantis, S. A., Blok‐Tip, L., Langridge, J., Kleen, A., & THOMAS‐OATES, J. E. (1998) · Analytical Biochemistry · doi:10.1006/abio.1997.2548 · Cited by 108
Use of CID/ETD Mass Spectrometry to Analyze Glycopeptides
Mechref, Y. S. (2012) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1211s68 · Cited by 107
González, L. J., Takao, T., Hori, H., Besada, V., Rodríguez, R., Padrón, G., & Shimonishi, Y. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90592-u · Cited by 104
Protein O-glycosylation analysis
Zauner, G., Kozak, R. P., Gardner, R. A., Fernandes, D. L., Deelder, A. M., & Wuhrer, M. (2012) · Biological Chemistry · doi:10.1515/hsz-2012-0144 · Cited by 103
O’Neill, R. A. (1996) · Journal of Chromatography A · doi:10.1016/0021-9673(95)00502-1 · Cited by 102
Enhanced Mass Spectrometric Mapping of the Human GalNAc-type O-Glycoproteome with SimpleCells
Vakhrushev, S. Y., Steentoft, C., Vester-Christensen, M. B., Bennett, E., Clausen, H., & Levery, S. B. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o112.021972 · Cited by 102
Self-citationProbing polypeptide GalNAc-transferase isoform substrate specificities by in vitro analysis
Kong, Y., Joshi, H. J., Schjoldager, K. T.-B. G., Madsen, T. D., Gerken, T. A., Vester-Christensen, M. B., Wandall, H. H., Bennett, E., Levery, S. B., Vakhrushev, S. Y., et al. (2014) · Glycobiology · doi:10.1093/glycob/cwu089 · Cited by 101
Self-citationSchjoldager, K. T.-B. G., Vester-Christensen, M. B., Goth, C. K., Petersen, T. N., Brunak, S., Bennett, E., Levery, S. B., & Clausen, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.287912 · Cited by 100
Self-citationDetection and Analysis of Proteins Modified by O‐Linked N‐Acetylglucosamine
Zachara, N. E., Vosseller, K., & Hart, G. W. (2011) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1208s66 · Cited by 100
Stalnaker, S. H., Hashmi, S., Lim, J.-M., Aoki, K., Porterfield, M., Gutiérrez‐Sánchez, G., WHEELER, J. L., Ervasti, J. M., Bergmann, C., Tiemeyer, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.126474 · Cited by 99
Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans
Ramya, T. N. C., Weerapana, E., Cravatt, B. F., & Paulson, J. C. (2012) · Glycobiology · doi:10.1093/glycob/cws144 · Cited by 99
O-glycosylation pattern of CD24 from mouse brain
Bleckmann, C., Geyer, H., Lieberoth, A., Splittstoesser, F., Liu, Y., Feizi, T., Schachner, M., KLEENE, R. B., Reinhold, V. N., & Geyer, R. (2009) · Biological Chemistry · doi:10.1515/bc.2009.044 · Cited by 90
Affinity Enrichment and Characterization of Mucin Core-1 Type Glycopeptides from Bovine Serum
Darula, Z., & Medzihradszky, K. F. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900211-mcp200 · Cited by 89
Wells, L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.438978 · Cited by 88
The GalNAc-type O-Glycoproteome of CHO Cells Characterized by the SimpleCell Strategy
Yang, Z., Halim, A., Narimatsu, Y., Joshi, H. J., Steentoft, C., Schjoldager, K. T.-B. G., Schulz, M. A., Sealover, N. R., Kayser, K. J., Bennett, E., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.041541 · Cited by 85
Self-citationHanisch, F., Jovanović, M., & Peter‐Katalinić, J. (2001) · Analytical Biochemistry · doi:10.1006/abio.2000.4955 · Cited by 84
Abbott, K. L., Matthews, R. T., & Pierce, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803646200 · Cited by 83
Nilsson, J., Nilsson, J., Larson, G., & Grahn, A. (2010) · Glycobiology · doi:10.1093/glycob/cwq082 · Cited by 82
Glycomic Analyses of Mouse Models of Congenital Muscular Dystrophy
Stalnaker, S. H., Aoki, K., Lim, J., Porterfield, M., Liu, M., Satz, J. S., Buskirk, S. W., Xiong, Y., Zhang, P., Campbell, K. P., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.203281 · Cited by 80
Mammalian O-Mannosylation Pathway: Glycan Structures, Enzymes, and Protein Substrates
Praissman, J. L., & Wells, L. (2014) · Biochemistry · doi:10.1021/bi500153y · Cited by 79
The role of mucin-type O-glycans in eukaryotic development
Tabak, L. A. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.02.001 · Cited by 76
How to Dig Deeper? Improved Enrichment Methods for Mucin Core-1 Type Glycopeptides
Darula, Z., Sherman, J., & Medzihradszky, K. F. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o111.016774 · Cited by 69
N-Glycoproteomics – An automated workflow approach
Joenväärä, S., Ritamo, I., Peltoniemi, H., & Renkonen, R. (2008) · Glycobiology · doi:10.1093/glycob/cwn013 · Cited by 63
Precision genome editing: A small revolution for glycobiology
Steentoft, C., Bennett, E., Schjoldager, K. T.-B. G., Vakhrushev, S. Y., Wandall, H. H., & Clausen, H. (2014) · Glycobiology · doi:10.1093/glycob/cwu046 · Cited by 62
Self-citationShimaoka, H., Kuramoto, H., Furukawa, J., Miura, Y., Kurogochi, M., Kita, Y., Hinou, H., Shinohara, Y., & Nishimura, S. (2007) · Chemistry - A European Journal · doi:10.1002/chem.200601613 · Cited by 61
A potential pitfall in 18 O‐based N‐linked glycosylation site mapping
Angel, P. M., Lim, J., Wells, L., Bergmann, C., & Orlando, R. (2007) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.2874 · Cited by 59
Glycoproteomic characterization of recombinant mouse α-dystroglycan
Harrison, R., Hitchen, P. G., Panico, M., Morris, H. R., Mekhaiel, D., Pleass, R. J., Dell, A., Hewitt, J., & Haslam, S. M. (2012) · Glycobiology · doi:10.1093/glycob/cws002 · Cited by 58
Characterization of a novel modification on IgG2 light chain
Martinez, T., Pace, D. L., Brady, L. J., GERHART, M. J., & Balland, A. (2007) · Journal of Chromatography A · doi:10.1016/j.chroma.2007.04.050 · Cited by 53
Du, Y., Wang, F., May, K. M. L., Xu, W., & Liu, H. (2012) · Analytical Chemistry · doi:10.1021/ac3013362 · Cited by 51
Neurofascin 186 Is O-Mannosylated within and Outside of the Mucin Domain
Pacharra, S., Hanisch, F., & Breloy, I. (2012) · Journal of Proteome Research · doi:10.1021/pr200996y · Cited by 45
The Lecticans of Mammalian Brain Perineural Net Are O-Mannosylated
Pacharra, S., Hanisch, F., Mühlenhoff, M., Faissner, A., Rauch, U., & Breloy, I. (2013) · Journal of Proteome Research · doi:10.1021/pr3011028 · Cited by 39
Esapa, C. T., Head, R. A., Jeyabalan, J., Evans, H., Hough, T., Cheeseman, M. T., McNally, E. G., Carr, A. J., Thomas, G. P., Brown, M. A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043205 · Cited by 36
Graham, M. E., Thaysen‐Andersen, M., Bache, N., Craft, G. E., Larsen, M. R., Packer, N. H., & Robinson, P. J. (2011) · Journal of Proteome Research · doi:10.1021/pr1011153 · Cited by 30
Steentoft, C., Bennett, E., & Clausen, H. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-465-4_29 · Cited by 30
Self-citationDiscovery of O-GlcNAc-6-phosphate Modified Proteins in Large-scale Phosphoproteomics Data
Hahne, H., & Küster, B. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.019760 · Cited by 22
Removal of sialic acid from serum gonadotropin by acidic and enzymic hydrolysis
Rafelson, M. E., Clauser, H., & Legault-Demare, J. (1961) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(61)90306-7 · Cited by 17
Cited by
Sorted by citations
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
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
Self-citationGlobal aspects of viral glycosylation
Bagdonaite, I., & Wandall, H. H. (2018) · Glycobiology · doi:10.1093/glycob/cwy021 · Cited by 234
Optimal Dissociation Methods Differ for N - and O -Glycopeptides
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
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