Advances in mass spectrometry driven O-glycoproteomics

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 · see citing works

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 · see citing works

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 · see citing works

Chemistry in living systems

Prescher, J. A., & Bertozzi, C. R. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0605-13 · Cited by 1,473 · see citing works

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 · see citing works

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.-B. 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 1,410 · see citing works

Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry

Zhang, H., Li, X., Martin, D. B., & Aebersold, R. H. (2003) · Nature Biotechnology · doi:10.1038/nbt827 · Cited by 1,389 · see citing works

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 895 · see citing works

Control of mucin-type O-glycosylation: A classification of the polypeptide GalNAc-transferase gene family

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 · see citing works

External Labeling of Cell Surface Galactose and Galactosamine in Glycolipid and Glycoprotein of Human Erythrocytes

Gahmberg, C. G., & Hakomori, S. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43774-5 · Cited by 698 · see citing works

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 598 · see citing works

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 592 · see citing works

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 · see citing works

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 535 · see citing works

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 · see citing works

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 · see citing works

Mapping Sites of O-GlcNAc Modification Using Affinity Tags for Serine and Threonine Post-translational Modifications

Wells, 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 · see citing works

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 · see citing works

Peptide‐ N 4 ‐( N ‐acetyl‐β‐glucosaminyl)asparagine amidase F cannot release glycans with fucose attached α1 → 3 to the asparagine‐linked N ‐acetylglucosamine residue

Tretter, V. E., Altmann, F., & März, L. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16166.x · Cited by 410 · see citing works

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 · see citing works

Localization of O-Glycosylation Sites in Peptides by Electron Capture Dissociation in a Fourier Transform Mass Spectrometer

Mirgorodskaya, E. E., Roepstorff, P., & Zubarev, R. A. (1999) · Analytical Chemistry · doi:10.1021/ac990578v · Cited by 382 · see citing works

Localization of Labile Posttranslational Modifications by Electron Capture Dissociation: The Case of γ-Carboxyglutamic Acid

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 369 · see citing works

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 · see citing works

O-Linked N-Acetylglucosamine Proteomics of Postsynaptic Density Preparations Using Lectin Weak Affinity Chromatography and Mass Spectrometry

Vosseller, 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 · see citing works

Metabolic cross-talk allows labeling of O-linked β- N -acetylglucosamine-modified proteins via the N -acetylgalactosamine salvage pathway

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 345 · see citing works

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 · see citing works

Decision 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 312 · see citing works

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 · see citing works

Tandem mass spectrometry identifies many mouse brain O -GlcNAcylated proteins including EGF domain-specific O -GlcNAc transferase targets

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 · see citing works

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 282 · see citing works

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 · see citing works

Location, 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 · see citing works

Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid β-peptides in human cerebrospinal fluid

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 247 · see citing works

Selective enrichment of sialic acid–containing glycopeptides using titanium dioxide chromatography with analysis by HILIC and mass spectrometry

Palmisano, 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 · see citing works

Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides

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 237 · see citing works

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., & Peer Bork, B. (2012) · Molecular Systems Biology · doi:10.1038/msb.2012.31 · Cited by 233 · see citing works

Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis

Zhurov, K. O., Fornelli, L., Wodrich, M. D., Laskay, Ü. A., & Tsybin, Y. O. (2013) · Chemical Society Reviews · doi:10.1039/c3cs35477f · Cited by 226 · see citing works

Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications

Wiesner, J., Premsler, T., & Sickmann, A. (2008) · PROTEOMICS · doi:10.1002/pmic.200800329 · Cited by 219 · see citing works

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 · see citing works

Advances in LC–MS/MS-based glycoproteomics: Getting closer to system-wide site-specific mapping of the N- and O-glycoproteome

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 209 · see citing works

Site-specific protein O-glycosylation modulates proprotein processing — Deciphering specific functions of the large polypeptide GalNAc-transferase gene family

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 · see citing works

The 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 171 · see citing works

Chemical Deamidation: A Common Pitfall in Large-Scale N-Linked Glycoproteomic Mass Spectrometry-Based Analyses

Palmisano, 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 · see citing works

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 · see citing works

Core 3 synthase is down-regulated in colon carcinoma and profoundly suppresses the metastatic potential of carcinoma cells

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 · see citing works

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 · see citing works

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 · see citing works

Human Urinary Glycoproteomics; Attachment Site Specific Analysis of N- and O-Linked Glycosylations by CID and ECD

Halim, A., Nilsson, J., Rüetschi, U., Hesse, C., & Larson, G. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013649 · Cited by 151 · see citing works

Ablation of the Galnt3 Gene Leads to Low-Circulating Intact Fibroblast Growth Factor 23 (Fgf23) Concentrations and Hyperphosphatemia Despite Increased Fgf23 Expression

Ichikawa, 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 · see citing works

Emerging Paradigms for the Initiation of Mucin-type Protein O-Glycosylation by the Polypeptide GalNAc Transferase Family of Glycosyltransferases

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 · see citing works

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 · see citing works

Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells

Schjoldager, 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 130 · see citing works

A Novel Method for the Simultaneous Enrichment, Identification, and Quantification of Phosphopeptides and Sialylated Glycopeptides Applied to a Temporal Profile of Mouse Brain Development

Palmisano, 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 · see citing works

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 · see citing works

Like-acetylglucosaminyltransferase (LARGE)-dependent modification of dystroglycan at Thr-317/319 is required for laminin binding and arenavirus infection

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 · see citing works

Novel mannitol-containing oligosaccharides obtained by mild alkaline borohydride treatment of a chondroitin sulfate proteoglycan from brain.

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast atom bombardment mass spectrometry: Identification of the positions of carbohydrate-linked asparagine in recombinant α-amylase by treatment with peptide-N-glycosidase F in 18O-labeled water

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 · see citing works

Enzymatic release of oligosaccharides from glycoproteins for chromatographic and electrophoretic analysis

O’Neill, R. A. (1996) · Journal of Chromatography A · doi:10.1016/0021-9673(95)00502-1 · Cited by 102 · see citing works

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 · see citing works

Probing 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 · see citing works

A Systematic Study of Site-specific GalNAc-type O-Glycosylation Modulating Proprotein Convertase Processing

Schjoldager, 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 · see citing works

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 · see citing works

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 98 · see citing works

Detection 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 96 · see citing works

Site Mapping and Characterization of O-Glycan Structures on α-Dystroglycan Isolated from Rabbit Skeletal Muscle

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 94 · see citing works

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 · see citing works

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 88 · see citing works

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 · see citing works

The O-Mannosylation Pathway: Glycosyltransferases and Proteins Implicated in Congenital Muscular Dystrophy

Wells, L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.438978 · Cited by 84 · see citing works

Glycoprotein Identification and Localization of O-Glycosylation Sites by Mass Spectrometric Analysis of Deglycosylated/Alkylaminylated Peptide Fragments

Hanisch, F., Jovanović, M., & Peter‐Katalinić, J. (2001) · Analytical Biochemistry · doi:10.1006/abio.2000.4955 · Cited by 84 · see citing works

Receptor Tyrosine Phosphatase β (RPTPβ) Activity and Signaling Are Attenuated by Glycosylation and Subsequent Cell Surface Galectin-1 Binding

Abbott, K. L., Matthews, R. T., & Pierce, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803646200 · Cited by 83 · see citing works

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 · see citing works

Characterization of site-specific O-glycan structures within the mucin-like domain of α-dystroglycan from human skeletal muscle

Nilsson, J., Nilsson, J., Larson, G., & Grahn, A. (2010) · Glycobiology · doi:10.1093/glycob/cwq082 · Cited by 77 · see citing works

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 74 · see citing works

Mammalian O-Mannosylation Pathway: Glycan Structures, Enzymes, and Protein Substrates

Praissman, J. L., & Wells, L. (2014) · Biochemistry · doi:10.1021/bi500153y · Cited by 73 · see citing works

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 · see citing works

N-Glycoproteomics – An automated workflow approach

Joenväärä, S., Ritamo, I., Peltoniemi, H., & Renkonen, R. (2008) · Glycobiology · doi:10.1093/glycob/cwn013 · Cited by 64 · see citing works

One‐Pot Solid‐Phase Glycoblotting and Probing by Transoximization for High‐Throughput Glycomics and Glycoproteomics

Shimaoka, 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 · see citing works

Precision genome editing: A small revolution for glycobiology

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A potential pitfall in 18 O‐based N‐linked glycosylation site mapping

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Advances toward mapping the full extent of protein site-specific O-GalNAc glycosylation that better reflects underlying glycomic complexity

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