{"doi":"10.1016/j.mcpro.2021.100086","title":"Glycoproteomics: Making the Study of the Most Structurally Diverse and Most Abundant Post-Translational Modifications More Accessible to the Scientific Community","abstract":"In 2013, we served as guest editors for the Glycomics special issue where the Athens guidelines for glycomic analyses were first revealed that have since been adopted by multiple journals (1Wells L. Hart G.W. Athens Guidelines for the Publication of Glycomics DataGlycomics: Building upon proteomics to advance glycosciences.Mol. Cell. Proteomics. 2013; 12: 833-835Abstract Full Text Full Text PDF PubMed Scopus (22) Google Scholar). At that moment in time, we could not have easily conceived of a special issue dedicated to glycoproteomics. However, just 8 years later, we find ourselves presenting a special issue of Molecular & Cellular Proteomics on Glycoproteomics that introduces the reader to the recent explosion in front-end enrichment methods, analytical approaches, and back-end software solutions dedicated to glycoproteomics. This special issue includes nine review articles and nine research articles that introduce the reader to the exciting, challenging, and rapidly evolving field of glycoproteomics, which is so highly dependent on MS. Glycoproteomics has been front and center this past year as scientists tackled the COVID-19 pandemic, given that the spike glycoprotein of SARS-CoV-2, which is often the basis for antibody and vaccine therapeutics, is a trimer glycoprotein consisting of 66 occupied N-linked glycosylation sites, and that the host receptor, ACE2, is also heavily glycosylated (2Watanabe Y. Allen J.D. Wrapp D. McLellan J.S. Crispin M. Site-specific glycan analysis of the SARS-CoV-2 spike.Science. 2020; 369: 330-333Crossref PubMed Scopus (522) Google Scholar, 3Zhao P. Praissman J.L. Grant O.C. Cai Y. Xiao T. Rosenbalm K.E. Aoki K. Kellman B.P. Bridger R. Barouch D.H. Brindley M.A. Lewis N.E. Tiemeyer M. Chen B. Woods R.J. et al.Virus-receptor interactions of glycosylated SARS-CoV-2 spike and human ACE2 receptor.Cell Host Microbe. 2020; 28: 586-601.e586Abstract Full Text Full Text PDF PubMed Scopus (122) Google Scholar). Thus, an issue devoted to understanding this heterogenous class of post-translational modifications seems very timely. The number of various glycan moieties that can modify proteins easily surpasses the sum of all other post-translational modifications combined, and the majority of all expressed mammalian proteins (secreted, membrane bound, and intracellular) are glycosylated (4Varki A. Cummings R.D. Esko J.D. Stanley P. Hart G.W. Aebi M. Darvill A.G. Kinoshita T. Packer N.H. Prestegard J.H. Schnaar R.L. Seeberger P.H. Essentials of Glycobiology. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY2015Google Scholar). Thus, it is essential to be able to characterize these challenging biomolecules to better understand the fundamental roles that glycoconjugates play in nearly all aspects of physiology and pathophysiology. A review by West et al. (5West C.M. Malzl D. Hykollari A. Wilson I.B.H. Glycomics, glycoproteomics, and glycogenomics: An inter-taxa evolutionary perspective.Mol. Cell. Proteomics. 2021; 20: 100024Abstract Full Text Full Text PDF PubMed Google Scholar) gives us an intertaxa evolutionary perspective on glycomics, glycoproteomics, and glycogenomics. Riley et al. (6Riley N.M. Bertozzi C.R. Pitteri S.J. A pragmatic guide to enrichment strategies for mass spectrometry-based glycoproteomics.Mol. Cell. Proteomics. 2021; 20: 100029Abstract Full Text Full Text PDF Google Scholar) provide a pragmatic guide to the plethora of enrichment strategies that exist for glycoproteins, while a review by Maynard and Chalkley (7Maynard J.C. Chalkley R.J. Methods for enrichment and assignment of N-acetylglucosamine modification sites.Mol. Cell. Proteomics. 2021; 20: 100031Abstract Full Text Full Text PDF PubMed Google Scholar) focuses specifically on enrichment and assignment of O-GlcNAc sites on proteins. Research articles by Kurz et al. (8Kurz S. Sheikh M.O. Lu S. Wells L. Tiemeyer M. Separation and identification of permethylated glycan isomers by reversed phase NanoLC-NSI-MS(n).Mol. Cell. Proteo","journal":"Molecular & Cellular Proteomics","year":2021,"id":194802,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":9,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9352,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2021-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":227815,"name":"Lance Wells","orcid":"0000-0003-4956-5363","position":1,"is_corresponding":false},{"id":299280,"name":"Gerald W. Hart","orcid":"0000-0001-7812-4351","position":0,"is_corresponding":true}],"reference_count":20,"raw_metadata":null,"created_at":"2026-07-18T23:49:59.476757Z","pmid":"34091217","pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}