{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,23]],"date-time":"2026-03-23T22:06:15Z","timestamp":1774303575179,"version":"3.50.1"},"reference-count":39,"publisher":"Springer Science and Business Media LLC","issue":"2","license":[{"start":{"date-parts":[[2020,10,17]],"date-time":"2020-10-17T00:00:00Z","timestamp":1602892800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2020,10,17]],"date-time":"2020-10-17T00:00:00Z","timestamp":1602892800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/100000009","name":"Foundation for the National Institutes of Health","doi-asserted-by":"publisher","award":["ZIA-000751-02"],"award-info":[{"award-number":["ZIA-000751-02"]}],"id":[{"id":"10.13039\/100000009","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000009","name":"Foundation for the National Institutes of Health","doi-asserted-by":"publisher","award":["Z01-DE-000713"],"award-info":[{"award-number":["Z01-DE-000713"]}],"id":[{"id":"10.13039\/100000009","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000009","name":"Foundation for the National Institutes of Health","doi-asserted-by":"publisher","award":["1-ZIA-DE000739-05"],"award-info":[{"award-number":["1-ZIA-DE000739-05"]}],"id":[{"id":"10.13039\/100000009","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Glycoconj J"],"published-print":{"date-parts":[[2021,4]]},"DOI":"10.1007\/s10719-020-09952-w","type":"journal-article","created":{"date-parts":[[2020,10,17]],"date-time":"2020-10-17T06:02:39Z","timestamp":1602914559000},"page":"145-156","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Improved online LC-MS\/MS identification of O-glycosites by EThcD fragmentation, chemoenzymatic reaction, and SPE enrichment"],"prefix":"10.1007","volume":"38","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7958-0594","authenticated-orcid":false,"given":"Shuang","family":"Yang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yan","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Matthew","family":"Mann","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qiong","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E","family":"Tian","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Liping","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John F.","family":"Cipollo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kelly G.","family":"Ten Hagen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lawrence A.","family":"Tabak","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2020,10,17]]},"reference":[{"issue":"6","key":"9952_CR1","doi-asserted-by":"publisher","first-page":"736","DOI":"10.1093\/glycob\/cwr182","volume":"22","author":"EP Bennett","year":"2012","unstructured":"Bennett, E.P., Mandel, U., Clausen, H., Gerken, T.A., Fritz, T.A., Tabak, L.A.: Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family. Glycobiology. 22(6), 736\u2013756 (2012)","journal-title":"Glycobiology"},{"issue":"49","key":"9952_CR2","doi-asserted-by":"publisher","first-page":"19064","DOI":"10.1074\/jbc.RA118.004516","volume":"293","author":"J Hintze","year":"2018","unstructured":"Hintze, J., Ye, Z., Narimatsu, Y., Madsen, T.D., Joshi, H.J., Goth, C.K., Linstedt, A., Bachert, C., Mandel, U., Bennett, E.P.: Probing the contribution of individual polypeptide GalNAc-transferase isoforms to the O-glycoproteome by inducible expression in isogenic cell lines. J. Biol. Chem. 293(49), 19064\u201319077 (2018)","journal-title":"J. Biol. Chem."},{"key":"9952_CR3","volume-title":"Essentials of Glycobiology","author":"I Brockhausen","year":"2009","unstructured":"Brockhausen, I., Schachter, H., Stanley, P.: O-GalNAc glycans. In: Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., Hart, G.W., Etzler, M.E. (eds.) Essentials of Glycobiology, 2nd edn. Cold Spring Harbor Laboratory Press, New York (2009)","edition":"2"},{"issue":"1","key":"9952_CR4","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41467-017-02088-w","volume":"9","author":"S Ji","year":"2018","unstructured":"Ji, S., Samara, N.L., Revoredo, L., Zhang, L., Tran, D.T., Muirhead, K., Tabak, L.A., Ten Hagen, K.G.: A molecular switch orchestrates enzyme specificity and secretory granule morphology. Nat. Commun. 9(1), 1\u201313 (2018)","journal-title":"Nat. Commun."},{"issue":"37","key":"9952_CR5","doi-asserted-by":"publisher","first-page":"32684","DOI":"10.1074\/jbc.M111.273722","volume":"286","author":"JW Pedersen","year":"2011","unstructured":"Pedersen, J.W., Bennett, E.P., Katrine, T.-B.S., Meldal, M., Holm\u00e9r, A.P., Blixt, O., Cl\u00f3, E., Levery, S.B., Clausen, H., Wandall, H.H.: Lectin domains of polypeptide GalNAc transferases exhibit glycopeptide binding specificity. J. Biol. Chem. 286(37), 32684\u201332696 (2011)","journal-title":"J. Biol. Chem."},{"issue":"1","key":"9952_CR6","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1093\/glycob\/cwu089","volume":"25","author":"Y Kong","year":"2015","unstructured":"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.P., Levery, S.B., Vakhrushev, S.Y.: Probing polypeptide GalNAc-transferase isoform substrate specificities by in vitro analysis. Glycobiology. 25(1), 55\u201365 (2015)","journal-title":"Glycobiology"},{"issue":"10","key":"9952_CR7","doi-asserted-by":"publisher","first-page":"791","DOI":"10.1074\/mcp.M200048-MCP200","volume":"1","author":"L Wells","year":"2002","unstructured":"Wells, L., Vosseller, K., Cole, R.N., Cronshaw, J.M., Matunis, M.J., Hart, G.W.: Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cell. Proteomics. 1(10), 791\u2013804 (2002)","journal-title":"Mol. Cell. Proteomics"},{"key":"9952_CR8","volume-title":"Approaches to the O-Glycoproteome","author":"JM Walker","year":"2005","unstructured":"Walker, J.M.: Approaches to the O-Glycoproteome. The proteomics protocols handbook. Humana Press Inc., Totowa (2005)"},{"issue":"13","key":"9952_CR9","doi-asserted-by":"publisher","first-page":"8261","DOI":"10.1021\/acs.analchem.8b01834","volume":"90","author":"S Yang","year":"2018","unstructured":"Yang, S., Onigman, P., Wu, W.W., Sjogren, J., Nyhlen, H., Shen, R.-F., Cipollo, J.: Deciphering protein O-glycosylation: solid-phase chemoenzymatic cleavage and enrichment. Anal. Chem. 90(13), 8261\u20138269 (2018)","journal-title":"Anal. Chem."},{"issue":"15","key":"9952_CR10","doi-asserted-by":"publisher","first-page":"7278","DOI":"10.1073\/pnas.1813020116","volume":"116","author":"SA Malaker","year":"2019","unstructured":"Malaker, S.A., Pedram, K., Ferracane, M.J., Bensing, B.A., Krishnan, V., Pett, C., Yu, J., Woods, E.C., Kramer, J.R., Westerlind, U.: The mucin-selective protease StcE enables molecular and functional analysis of human cancer-associated mucins. Proc. Natl. Acad. Sci. U. S. A. 116(15), 7278\u20137287 (2019)","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"23","key":"9952_CR11","doi-asserted-by":"publisher","first-page":"9654","DOI":"10.1021\/ac101856r","volume":"82","author":"CC Nwosu","year":"2010","unstructured":"Nwosu, C.C., Strum, J.S., An, H.J., Lebrilla, C.B.: Enhanced detection and identification of glycopeptides in negative ion mode mass spectrometry. Anal. Chem. 82(23), 9654\u20139662 (2010)","journal-title":"Anal. Chem."},{"issue":"11","key":"9952_CR12","doi-asserted-by":"publisher","first-page":"5849","DOI":"10.1021\/acs.analchem.6b00479","volume":"88","author":"GS Kammeijer","year":"2016","unstructured":"Kammeijer, G.S., Kohler, I., Jansen, B.C., Hensbergen, P.J., Mayboroda, O.A., Falck, D., Wuhrer, M.: Dopant enriched nitrogen gas combined with sheathless capillary electrophoresis\u2013electrospray ionization-mass spectrometry for improved sensitivity and repeatability in glycopeptide analysis. Anal. Chem. 88(11), 5849\u20135856 (2016)","journal-title":"Anal. Chem."},{"issue":"16","key":"9952_CR13","doi-asserted-by":"publisher","first-page":"2533","DOI":"10.1002\/jssc.200600133","volume":"29","author":"Y Takegawa","year":"2006","unstructured":"Takegawa, Y., Deguchi, K., Ito, H., Keira, T., Nakagawa, H., Nishimura, S.I.: Simple separation of isomeric sialylated N-glycopeptides by a zwitterionic type of hydrophilic interaction chromatography. J. Sep. Sci. 29(16), 2533\u20132540 (2006)","journal-title":"J. Sep. Sci."},{"issue":"1","key":"9952_CR14","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1021\/ac070997p","volume":"80","author":"AJ Alpert","year":"2008","unstructured":"Alpert, A.J.: Electrostatic repulsion hydrophilic interaction chromatography for isocratic separation of charged solutes and selective isolation of phosphopeptides. Anal. Chem. 80(1), 62\u201376 (2008)","journal-title":"Anal. Chem."},{"issue":"9","key":"9952_CR15","doi-asserted-by":"publisher","first-page":"4704","DOI":"10.1021\/ac504420c","volume":"87","author":"AJ Alpert","year":"2015","unstructured":"Alpert, A.J., Hudecz, O., Mechtler, K.: Anion-exchange chromatography of phosphopeptides: weak anion exchange versus strong anion exchange and anion-exchange chromatography versus electrostatic repulsion\u2013hydrophilic interaction chromatography. Anal. Chem. 87(9), 4704\u20134711 (2015)","journal-title":"Anal. Chem."},{"issue":"3","key":"9952_CR16","doi-asserted-by":"publisher","first-page":"1249","DOI":"10.1021\/acs.jproteome.6b00849","volume":"16","author":"SM Totten","year":"2017","unstructured":"Totten, S.M., Feasley, C.L., Bermudez, A., Pitteri, S.J.: Parallel comparison of N-linked glycopeptide enrichment techniques reveals extensive glycoproteomic analysis of plasma enabled by SAX-ERLIC. J. Proteome Res. 16(3), 1249\u20131260 (2017)","journal-title":"J. Proteome Res."},{"issue":"10","key":"9952_CR17","doi-asserted-by":"publisher","first-page":"3904","DOI":"10.1021\/acs.jproteome.6b00438","volume":"15","author":"LY Lee","year":"2016","unstructured":"Lee, L.Y., Moh, E.S., Parker, B.L., Bern, M., Packer, N.H., Thaysen-Andersen, M.: Toward automated N-glycopeptide identification in glycoproteomics. J. Proteome Res. 15(10), 3904\u20133915 (2016)","journal-title":"J. Proteome Res."},{"issue":"1","key":"9952_CR18","doi-asserted-by":"publisher","first-page":"12.11. 11","DOI":"10.1002\/0471140864.ps1211s68","volume":"68","author":"Y Mechref","year":"2012","unstructured":"Mechref, Y.: Use of CID\/ETD mass spectrometry to analyze glycopeptides. Curr. Protoc. Protein Sci. 68(1), 12.11. 11\u201312.11. 11 (2012)","journal-title":"Curr. Protoc. Protein Sci."},{"issue":"1","key":"9952_CR19","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41467-019-09222-w","volume":"10","author":"NM Riley","year":"2019","unstructured":"Riley, N.M., Hebert, A.S., Westphall, M.S., Coon, J.J.: Capturing site-specific heterogeneity with large-scale N-glycoproteome analysis. Nat. Commun. 10(1), 1\u201313 (2019)","journal-title":"Nat. Commun."},{"issue":"6","key":"9952_CR20","doi-asserted-by":"publisher","first-page":"1210","DOI":"10.1007\/s13361-018-1945-7","volume":"29","author":"A Pap","year":"2018","unstructured":"Pap, A., Klement, E., Hunyadi-Gulyas, E., Darula, Z., Medzihradszky, K.F.: Status report on the high-throughput characterization of complex intact O-glycopeptide mixtures. J. Am. Soc. Mass Spectrom. 29(6), 1210\u20131220 (2018)","journal-title":"J. Am. Soc. Mass Spectrom."},{"issue":"9","key":"9952_CR21","doi-asserted-by":"publisher","first-page":"1751","DOI":"10.1007\/s13361-017-1701-4","volume":"28","author":"Q Yu","year":"2017","unstructured":"Yu, Q., Wang, B., Chen, Z., Urabe, G., Glover, M.S., Shi, X., Guo, L.-W., Kent, K.C., Li, L.: Electron-transfer\/higher-energy collision dissociation (EThcD)-enabled intact glycopeptide\/glycoproteome characterization. J. Am. Soc. Mass Spectrom. 28(9), 1751\u20131764 (2017)","journal-title":"J. Am. Soc. Mass Spectrom."},{"issue":"5","key":"9952_CR22","doi-asserted-by":"publisher","first-page":"1867","DOI":"10.1021\/pr700671z","volume":"7","author":"NJ Hauser","year":"2008","unstructured":"Hauser, N.J., Han, H., McLuckey, S.A., Basile, F.: Electron transfer dissociation of peptides generated by microwave D-cleavage digestion of proteins. J. Proteome Res. 7(5), 1867\u20131872 (2008)","journal-title":"J. Proteome Res."},{"issue":"5","key":"9952_CR23","doi-asserted-by":"publisher","first-page":"993","DOI":"10.1038\/nprot.2016.057","volume":"11","author":"P Giansanti","year":"2016","unstructured":"Giansanti, P., Tsiatsiani, L., Low, T.Y., Heck, A.J.: Six alternative proteases for mass spectrometry\u2013based proteomics beyond trypsin. Nat. Protoc. 11(5), 993\u20131006 (2016)","journal-title":"Nat. Protoc."},{"key":"9952_CR24","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.jprot.2017.09.014","volume":"170","author":"Y Zhang","year":"2018","unstructured":"Zhang, Y., Xie, X., Zhao, X., Tian, F., Lv, J., Ying, W., Qian, X.: Systems analysis of singly and multiply O-glycosylated peptides in the human serum glycoproteome via EThcD and HCD mass spectrometry. J. Proteome. 170, 14\u201327 (2018)","journal-title":"J. Proteome"},{"issue":"14","key":"9952_CR25","doi-asserted-by":"publisher","first-page":"2612","DOI":"10.1111\/febs.13287","volume":"282","author":"L Tsiatsiani","year":"2015","unstructured":"Tsiatsiani, L., Heck, A.J.: Proteomics beyond trypsin. FEBS J. 282(14), 2612\u20132626 (2015)","journal-title":"FEBS J."},{"issue":"10","key":"9952_CR26","doi-asserted-by":"publisher","first-page":"2644","DOI":"10.1074\/mcp.M115.049726","volume":"14","author":"NM Riley","year":"2015","unstructured":"Riley, N.M., Rush, M.J., Rose, C.M., Richards, A.L., Kwiecien, N.W., Bailey, D.J., Hebert, A.S., Westphall, M.S., Coon, J.J.: The negative mode proteome with activated ion negative electron transfer dissociation (AI-NETD). Mol. Cell. Proteomics. 14(10), 2644\u20132660 (2015)","journal-title":"Mol. Cell. Proteomics"},{"issue":"6","key":"9952_CR27","doi-asserted-by":"publisher","first-page":"1273","DOI":"10.1007\/s13361-018-1931-0","volume":"29","author":"S Yang","year":"2018","unstructured":"Yang, S., Wu, W.W., Shen, R.-F., Bern, M., Cipollo, J.: Identification of sialic acid linkages on intact glycopeptides via differential chemical modification using IntactGIG-HILIC. J. Am. Soc. Mass Spectrom. 29(6), 1273\u20131283 (2018)","journal-title":"J. Am. Soc. Mass Spectrom."},{"issue":"11","key":"9952_CR28","doi-asserted-by":"publisher","first-page":"959","DOI":"10.1038\/nmeth.1260","volume":"5","author":"DL Swaney","year":"2008","unstructured":"Swaney, D.L., McAlister, G.C., Coon, J.J.: Decision tree\u2013driven tandem mass spectrometry for shotgun proteomics. Nat. Methods. 5(11), 959\u2013964 (2008)","journal-title":"Nat. Methods"},{"issue":"2","key":"9952_CR29","doi-asserted-by":"publisher","first-page":"702","DOI":"10.1021\/pr400802z","volume":"13","author":"PD Gershon","year":"2014","unstructured":"Gershon, P.D.: Cleaved and missed sites for trypsin, lys-C, and lys-N can be predicted with high confidence on the basis of sequence context. J. Proteome Res. 13(2), 702\u2013709 (2014)","journal-title":"J. Proteome Res."},{"issue":"7","key":"9952_CR30","doi-asserted-by":"publisher","first-page":"2199","DOI":"10.1073\/pnas.0611217104","volume":"104","author":"H Molina","year":"2007","unstructured":"Molina, H., Horn, D.M., Tang, N., Mathivanan, S., Pandey, A.: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 104(7), 2199\u20132204 (2007)","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"38","key":"9952_CR31","doi-asserted-by":"publisher","first-page":"23503","DOI":"10.1074\/jbc.272.38.23503","volume":"272","author":"HH Wandall","year":"1997","unstructured":"Wandall, H.H., Hassan, H., Mirgorodskaya, E., Kristensen, A.K., Roepstorff, P., Bennett, E.P., Nielsen, P.A., Hollingsworth, M.A., Burchell, J., Taylor-Papadimitriou, J.: Substrate specificities of three members of the human UDP-N-acetyl-\u03b1-d-galactosamine: polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1,-T2, and-T3. J. Biol. Chem. 272(38), 23503\u201323514 (1997)","journal-title":"J. Biol. Chem."},{"issue":"16","key":"9952_CR32","doi-asserted-by":"publisher","first-page":"14493","DOI":"10.1074\/jbc.M111.218701","volume":"286","author":"TA Gerken","year":"2011","unstructured":"Gerken, T.A., Jamison, O., Perrine, C.L., Collette, J.C., Moinova, H., Ravi, L., Markowitz, S.D., Shen, W., Patel, H., Tabak, L.A.: Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases. J. Biol. Chem. 286(16), 14493\u201314507 (2011)","journal-title":"J. Biol. Chem."},{"issue":"43","key":"9952_CR33","doi-asserted-by":"publisher","first-page":"32403","DOI":"10.1074\/jbc.M605149200","volume":"281","author":"TA Gerken","year":"2006","unstructured":"Gerken, T.A., Raman, J., Fritz, T.A., Jamison, O.: Identification of common and unique peptide substrate preferences for the UDP-GalNAc: polypeptide \u03b1-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates. J. Biol. Chem. 281(43), 32403\u201332416 (2006)","journal-title":"J. Biol. Chem."},{"issue":"2","key":"9952_CR34","doi-asserted-by":"publisher","first-page":"241","DOI":"10.1002\/pmic.201500266","volume":"16","author":"S Yang","year":"2016","unstructured":"Yang, S., Rubin, A., Eshghi, S.T., Zhang, H.: Chemoenzymatic method for glycomics: isolation, identification, and quantitation. Proteomics. 16(2), 241\u2013256 (2016)","journal-title":"Proteomics"},{"issue":"8","key":"9952_CR35","doi-asserted-by":"publisher","first-page":"2208","DOI":"10.1046\/j.1432-1327.2000.01225.x","volume":"267","author":"W Jiang","year":"2000","unstructured":"Jiang, W., Gupta, D., Gallagher, D., Davis, S., Bhavanandan, V.P.: The central domain of bovine submaxillary mucin consists of over 50 tandem repeats of 329 amino acids: chromosomal localization of the BSM1 gene and relations to ovine and porcine counterparts. Euro. J Biochem. 267(8), 2208\u20132217 (2000)","journal-title":"Euro. J Biochem."},{"issue":"12","key":"9952_CR36","doi-asserted-by":"publisher","first-page":"5913","DOI":"10.1016\/S0021-9258(18)45661-X","volume":"262","author":"V Bhavanandan","year":"1987","unstructured":"Bhavanandan, V., Hegarty, J.: Identification of the mucin core protein by cell-free translation of messenger RNA from bovine submaxillary glands. J. Biol. Chem. 262(12), 5913\u20135917 (1987)","journal-title":"J. Biol. Chem."},{"issue":"1","key":"9952_CR37","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1021\/acs.analchem.7b04810","volume":"90","author":"NM Riley","year":"2018","unstructured":"Riley, N.M., Coon, J.J.: The role of electron transfer dissociation in modern proteomics. Anal. Chem. 90(1), 40\u201364 (2018)","journal-title":"Anal. Chem."},{"issue":"2","key":"9952_CR38","doi-asserted-by":"publisher","first-page":"156","DOI":"10.1039\/C9MO00160C","volume":"16","author":"A Pap","year":"2020","unstructured":"Pap, A., Tasnadi, E., Medzihradszky, K.F., Darula, Z.: Novel O-linked sialoglycan structures in human urinary glycoproteins. Mol. Omics. 16(2), 156\u2013164 (2020)","journal-title":"Mol. Omics"},{"key":"9952_CR39","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1016\/j.ijms.2017.09.002","volume":"427","author":"MS Glover","year":"2018","unstructured":"Glover, M.S., Yu, Q., Chen, Z., Shi, X., Kent, K.C., Li, L.: Characterization of intact sialylated glycopeptides and phosphorylated glycopeptides from IMAC enriched samples by EThcD fragmentation: toward combining phosphoproteomics and glycoproteomics. Int. J. Mass Spectrom. 427, 35\u201342 (2018)","journal-title":"Int. J. Mass Spectrom."}],"container-title":["Glycoconjugate Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10719-020-09952-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s10719-020-09952-w\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10719-020-09952-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,10,17]],"date-time":"2021-10-17T01:26:58Z","timestamp":1634434018000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s10719-020-09952-w"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,10,17]]},"references-count":39,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2021,4]]}},"alternative-id":["9952"],"URL":"https:\/\/doi.org\/10.1007\/s10719-020-09952-w","relation":{},"ISSN":["0282-0080","1573-4986"],"issn-type":[{"value":"0282-0080","type":"print"},{"value":"1573-4986","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,10,17]]},"assertion":[{"value":"12 July 2020","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"16 September 2020","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 October 2020","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 October 2020","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Compliance with ethical standards"}},{"value":"The authors declare no conflicts of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}},{"value":"This work didn't use animal model, clinical specimens. All samples are commercially purchased. This study is comply with etheical standards.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical approval"}}]}}