{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T11:20:28Z","timestamp":1792668028912,"version":"4.5.0"},"publisher-location":"New York, NY","reference-count":36,"publisher":"Springer US","isbn-type":[{"value":"9781071612408","type":"print"},{"value":"9781071612415","type":"electronic"}],"license":[{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021]]},"DOI":"10.1007\/978-1-0716-1241-5_8","type":"book-chapter","created":{"date-parts":[[2021,4,28]],"date-time":"2021-04-28T02:19:05Z","timestamp":1619576345000},"page":"107-120","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Enrichment of Intact Glycopeptides Using Strong Anion Exchange and Electrostatic Repulsion Hydrophilic Interaction Chromatography"],"prefix":"10.1007","author":[{"given":"Abel","family":"Bermudez","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sharon J.","family":"Pitteri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,4,29]]},"reference":[{"key":"8_CR1","volume-title":"Essentials of glycobiology","year":"2015","unstructured":"Varki A, Cummings RD et al (eds) (2015) Essentials of glycobiology. Cold Spring Harbor (NY), New York"},{"issue":"6","key":"8_CR2","doi-asserted-by":"publisher","first-page":"346","DOI":"10.1038\/s41581-019-0129-4","volume":"15","author":"C Reily","year":"2019","unstructured":"Reily C, Stewart TJ, Renfrow MB, Novak J (2019) Glycosylation in health and disease. Nat Rev Nephrol 15(6):346\u2013366. https:\/\/doi.org\/10.1038\/s41581-019-0129-4","journal-title":"Nat Rev Nephrol"},{"issue":"3","key":"8_CR3","doi-asserted-by":"publisher","first-page":"1713","DOI":"10.1021\/pr401200h","volume":"13","author":"J Zhu","year":"2014","unstructured":"Zhu J, Sun Z, Cheng K, Chen R, Ye M, Xu B, Sun D, Wang L, Liu J, Wang F, Zou H (2014) Comprehensive mapping of protein N-glycosylation in human liver by combining hydrophilic interaction chromatography and hydrazide chemistry. J Proteome Res 13(3):1713\u20131721. https:\/\/doi.org\/10.1021\/pr401200h","journal-title":"J Proteome Res"},{"issue":"6","key":"8_CR4","doi-asserted-by":"publisher","first-page":"660","DOI":"10.1038\/nbt827","volume":"21","author":"H Zhang","year":"2003","unstructured":"Zhang H, Li XJ, Martin DB, Aebersold R (2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol 21(6):660\u2013666. https:\/\/doi.org\/10.1038\/nbt827","journal-title":"Nat Biotechnol"},{"issue":"6","key":"8_CR5","doi-asserted-by":"publisher","first-page":"2070","DOI":"10.1021\/pr0502065","volume":"4","author":"T Liu","year":"2005","unstructured":"Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD (2005) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res 4(6):2070\u20132080. https:\/\/doi.org\/10.1021\/pr0502065","journal-title":"J Proteome Res"},{"issue":"12","key":"8_CR6","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0081921","volume":"8","author":"X Li","year":"2013","unstructured":"Li X, Jiang J, Zhao X, Wang J, Han H, Zhao Y, Peng B, Zhong R, Ying W, Qian X (2013) N-glycoproteome analysis of the secretome of human metastatic hepatocellular carcinoma cell lines combining hydrazide chemistry, HILIC enrichment and mass spectrometry. PLoS One 8(12):e81921. https:\/\/doi.org\/10.1371\/journal.pone.0081921","journal-title":"PLoS One"},{"issue":"3","key":"8_CR7","doi-asserted-by":"publisher","first-page":"1636","DOI":"10.1021\/pr401122m","volume":"13","author":"S Magdeldin","year":"2014","unstructured":"Magdeldin S, Yamamoto K, Yoshida Y, Xu B, Zhang Y, Fujinaka H, Yaoita E, Yates JR 3rd, Yamamoto T (2014) Deep proteome mapping of mouse kidney based on OFFGel prefractionation reveals remarkable protein post- translational modifications. J Proteome Res 13(3):1636\u20131646. https:\/\/doi.org\/10.1021\/pr401122m","journal-title":"J Proteome Res"},{"issue":"19","key":"8_CR8","doi-asserted-by":"publisher","first-page":"2745","DOI":"10.1002\/jssc.201100427","volume":"34","author":"B Zhang","year":"2011","unstructured":"Zhang B, Sheng Q, Li X, Liang Q, Yan J, Liang X (2011) Selective enrichment of glycopeptides for mass spectrometry analysis using C18 fractionation and titanium dioxide chromatography. J Sep Sci 34(19):2745\u20132750. https:\/\/doi.org\/10.1002\/jssc.201100427","journal-title":"J Sep Sci"},{"issue":"8","key":"8_CR9","doi-asserted-by":"publisher","first-page":"1306","DOI":"10.1002\/pmic.201200367","volume":"13","author":"J Zhu","year":"2013","unstructured":"Zhu J, Wang F, Cheng K, Dong J, Sun D, Chen R, Wang L, Ye M, Zou H (2013) A simple integrated system for rapid analysis of sialic-acid-containing N-glycopeptides from human serum. Proteomics 13(8):1306\u20131313. https:\/\/doi.org\/10.1002\/pmic.201200367","journal-title":"Proteomics"},{"issue":"11","key":"8_CR10","doi-asserted-by":"publisher","first-page":"1191","DOI":"10.1074\/mcp.M112.017509","volume":"11","author":"G Palmisano","year":"2012","unstructured":"Palmisano G, Parker BL, Engholm-Keller K, Lendal SE, Kulej K, Schulz M, Schwammle V, Graham ME, Saxtorph H, Cordwell SJ, Larsen MR (2012) A novel method for the simultaneous enrichment, identification, and quantification of phosphopeptides and sialylated glycopeptides applied to a temporal profile of mouse brain development. Mol Cell Proteomics 11(11):1191\u20131202. https:\/\/doi.org\/10.1074\/mcp.M112.017509","journal-title":"Mol Cell Proteomics"},{"key":"8_CR11","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1007\/978-1-61779-148-2_21","volume":"753","author":"G Palmisano","year":"2011","unstructured":"Palmisano G, Lendal SE, Larsen MR (2011) Titanium dioxide enrichment of sialic acid-containing glycopeptides. Methods Mol Biol 753:309\u2013322. https:\/\/doi.org\/10.1007\/978-1-61779-148-2_21","journal-title":"Methods Mol Biol"},{"issue":"10","key":"8_CR12","doi-asserted-by":"publisher","first-page":"1778","DOI":"10.1074\/mcp.M700086-MCP200","volume":"6","author":"MR Larsen","year":"2007","unstructured":"Larsen MR, Jensen SS, Jakobsen LA, Heegaard NH (2007) Exploring the sialiome using titanium dioxide chromatography and mass spectrometry. Mol Cell Proteomics 6(10):1778\u20131787. https:\/\/doi.org\/10.1074\/mcp.M700086-MCP200","journal-title":"Mol Cell Proteomics"},{"key":"8_CR13","doi-asserted-by":"publisher","first-page":"490531","DOI":"10.1155\/2015\/490531","volume":"2015","author":"A Kirwan","year":"2015","unstructured":"Kirwan A, Utratna M, O\u2019Dwyer ME, Joshi L, Kilcoyne M (2015) Glycosylation-based serum biomarkers for cancer diagnostics and prognostics. Biomed Res Int 2015:490531. https:\/\/doi.org\/10.1155\/2015\/490531","journal-title":"Biomed Res Int"},{"issue":"1-2","key":"8_CR14","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1016\/j.jchromb.2006.09.041","volume":"849","author":"M Wuhrer","year":"2007","unstructured":"Wuhrer M, Catalina MI, Deelder AM, Hokke CH (2007) Glycoproteomics based on tandem mass spectrometry of glycopeptides. J Chromatogr B Analyt Technol Biomed Life Sci 849(1-2):115\u2013128. https:\/\/doi.org\/10.1016\/j.jchromb.2006.09.041","journal-title":"J Chromatogr B Analyt Technol Biomed Life Sci"},{"issue":"15","key":"8_CR15","doi-asserted-by":"publisher","first-page":"2091","DOI":"10.1002\/elps.201400034","volume":"35","author":"BY Huang","year":"2014","unstructured":"Huang BY, Yang CK, Liu CP, Liu CY (2014) Stationary phases for the enrichment of glycoproteins and glycopeptides. Electrophoresis 35(15):2091\u20132107. https:\/\/doi.org\/10.1002\/elps.201400034","journal-title":"Electrophoresis"},{"issue":"4","key":"8_CR16","doi-asserted-by":"publisher","first-page":"688","DOI":"10.1039\/c3an01813j","volume":"139","author":"CC Chen","year":"2014","unstructured":"Chen CC, Su WC, Huang BY, Chen YJ, Tai HC, Obena RP (2014) Interaction modes and approaches to glycopeptide and glycoprotein enrichment. Analyst 139(4):688\u2013704. https:\/\/doi.org\/10.1039\/c3an01813j","journal-title":"Analyst"},{"issue":"18","key":"8_CR17","doi-asserted-by":"publisher","first-page":"2341","DOI":"10.1002\/jssc.201200434","volume":"35","author":"S Ongay","year":"2012","unstructured":"Ongay S, Boichenko A, Govorukhina N, Bischoff R (2012) Glycopeptide enrichment and separation for protein glycosylation analysis. J Sep Sci 35(18):2341\u20132372. https:\/\/doi.org\/10.1002\/jssc.201200434","journal-title":"J Sep Sci"},{"issue":"1","key":"8_CR18","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1111\/j.1432-1033.1993.tb18347.x","volume":"218","author":"H Lis","year":"1993","unstructured":"Lis H, Sharon N (1993) Protein glycosylation. Structural and functional aspects. Eur J Biochem 218(1):1\u201327","journal-title":"Eur J Biochem"},{"key":"8_CR19","volume-title":"Essentials of glycobiology. Essentials of glycobiology","author":"A Varki","year":"2009","unstructured":"Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME (2009) Essentials of glycobiology. Essentials of glycobiology, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor (NY), New York","edition":"2"},{"issue":"45","key":"8_CR20","doi-asserted-by":"publisher","first-page":"42530","DOI":"10.1074\/jbc.M206114200","volume":"277","author":"NM Young","year":"2002","unstructured":"Young NM, Brisson JR, Kelly J, Watson DC, Tessier L, Lanthier PH, Jarrell HC, Cadotte N, St Michael F, Aberg E, Szymanski CM (2002) Structure of the N-linked glycan present on multiple glycoproteins in the gram-negative bacterium, campylobacter jejuni. J Biol Chem 277(45):42530\u201342539. https:\/\/doi.org\/10.1074\/jbc.M206114200","journal-title":"J Biol Chem"},{"issue":"9","key":"8_CR21","doi-asserted-by":"publisher","first-page":"2802","DOI":"10.1021\/ac048751x","volume":"77","author":"R Qiu","year":"2005","unstructured":"Qiu R, Regnier FE (2005) Use of multidimensional lectin affinity chromatography in differential glycoproteomics. Anal Chem 77(9):2802\u20132809. https:\/\/doi.org\/10.1021\/ac048751x","journal-title":"Anal Chem"},{"issue":"2","key":"8_CR22","doi-asserted-by":"publisher","first-page":"293","DOI":"10.1016\/S0378-4347(00)00550-8","volume":"752","author":"M Geng","year":"2001","unstructured":"Geng M, Zhang X, Bina M, Regnier F (2001) Proteomics of glycoproteins based on affinity selection of glycopeptides from tryptic digests. J Chromatogr B Biomed Sci Appl 752(2):293\u2013306","journal-title":"J Chromatogr B Biomed Sci Appl"},{"issue":"5","key":"8_CR23","doi-asserted-by":"publisher","first-page":"2062","DOI":"10.1021\/pr8007489","volume":"9","author":"G Alvarez-Manilla","year":"2010","unstructured":"Alvarez-Manilla G, Warren NL, Atwood J 3rd, Orlando R, Dalton S, Pierce M (2010) Glycoproteomic analysis of embryonic stem cells: identification of potential glycobiomarkers using lectin affinity chromatography of glycopeptides. J Proteome Res 9(5):2062\u20132075. https:\/\/doi.org\/10.1021\/pr8007489","journal-title":"J Proteome Res"},{"issue":"18","key":"8_CR24","doi-asserted-by":"publisher","first-page":"3833","DOI":"10.1002\/pmic.200701057","volume":"8","author":"G Picariello","year":"2008","unstructured":"Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F (2008) Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics 8(18):3833\u20133847. https:\/\/doi.org\/10.1002\/pmic.200701057","journal-title":"Proteomics"},{"issue":"5","key":"8_CR25","doi-asserted-by":"publisher","first-page":"2248","DOI":"10.1021\/pr101082c","volume":"10","author":"K Neue","year":"2011","unstructured":"Neue K, Mormann M, Peter-Katalinic J, Pohlentz G (2011) Elucidation of glycoprotein structures by unspecific proteolysis and direct nanoESI mass spectrometric analysis of ZIC-HILIC-enriched glycopeptides. J Proteome Res 10(5):2248\u20132260. https:\/\/doi.org\/10.1021\/pr101082c","journal-title":"J Proteome Res"},{"issue":"13","key":"8_CR26","doi-asserted-by":"publisher","first-page":"5598","DOI":"10.1021\/ac100530w","volume":"82","author":"S Mysling","year":"2010","unstructured":"Mysling S, Palmisano G, Hojrup P, Thaysen-Andersen M (2010) Utilizing ion-pairing hydrophilic interaction chromatography solid phase extraction for efficient glycopeptide enrichment in glycoproteomics. Anal Chem 82(13):5598\u20135609. https:\/\/doi.org\/10.1021\/ac100530w","journal-title":"Anal Chem"},{"issue":"6-7","key":"8_CR27","doi-asserted-by":"publisher","first-page":"891","DOI":"10.1002\/jssc.200900802","volume":"33","author":"A Kondo","year":"2010","unstructured":"Kondo A, Thaysen-Andersen M, Hjerno K, Jensen ON (2010) Characterization of sialylated and fucosylated glycopeptides of beta2-glycoprotein I by a combination of HILIC LC and MALDI MS\/MS. J Sep Sci 33(6-7):891\u2013902. https:\/\/doi.org\/10.1002\/jssc.200900802","journal-title":"J Sep Sci"},{"issue":"1","key":"8_CR28","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1021\/ac070997p","volume":"80","author":"AJ Alpert","year":"2008","unstructured":"Alpert AJ (2008) Electrostatic repulsion hydrophilic interaction chromatography for isocratic separation of charged solutes and selective isolation of phosphopeptides. Anal Chem 80(1):62\u201376. https:\/\/doi.org\/10.1021\/ac070997p","journal-title":"Anal Chem"},{"issue":"3","key":"8_CR29","doi-asserted-by":"publisher","first-page":"1249","DOI":"10.1021\/acs.jproteome.6b00849","volume":"16","author":"SM Totten","year":"2017","unstructured":"Totten SM, Feasley CL, Bermudez A, Pitteri SJ (2017) 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. https:\/\/doi.org\/10.1021\/acs.jproteome.6b00849","journal-title":"J Proteome Res"},{"issue":"6","key":"8_CR30","doi-asserted-by":"publisher","first-page":"1657","DOI":"10.1074\/mcp.O114.046391","volume":"14","author":"E Sok Hwee Cheow","year":"2015","unstructured":"Sok Hwee Cheow E, Hwan Sim K, de Kleijn D, Neng Lee C, Sorokin V, Sze SK (2015) Simultaneous enrichment of plasma soluble and extracellular vesicular glycoproteins using prolonged ultracentrifugation-electrostatic repulsion-hydrophilic interaction chromatography (PUC-ERLIC) approach. Mol Cell Proteomics 14(6):1657\u20131671. https:\/\/doi.org\/10.1074\/mcp.O114.046391","journal-title":"Mol Cell Proteomics"},{"issue":"3","key":"8_CR31","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1586\/14789450.2015.1042867","volume":"12","author":"O Pagel","year":"2015","unstructured":"Pagel O, Loroch S, Sickmann A, Zahedi RP (2015) Current strategies and findings in clinically relevant post-translational modification-specific proteomics. Expert Rev Proteomics 12(3):235\u2013253. https:\/\/doi.org\/10.1586\/14789450.2015.1042867","journal-title":"Expert Rev Proteomics"},{"issue":"9","key":"8_CR32","doi-asserted-by":"publisher","first-page":"2765","DOI":"10.1007\/s00216-012-5724-1","volume":"402","author":"CW Kuo","year":"2012","unstructured":"Kuo CW, Wu IL, Hsiao HH, Khoo KH (2012) Rapid glycopeptide enrichment and N-glycosylation site mapping strategies based on amine-functionalized magnetic nanoparticles. Anal Bioanal Chem 402(9):2765\u20132776. https:\/\/doi.org\/10.1007\/s00216-012-5724-1","journal-title":"Anal Bioanal Chem"},{"key":"8_CR33","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1007\/978-1-61779-319-6_23","volume":"790","author":"P Hao","year":"2011","unstructured":"Hao P, Zhang H, Sze SK (2011) Application of electrostatic repulsion hydrophilic interaction chromatography to the characterization of proteome, glycoproteome, and phosphoproteome using nano LC-MS\/MS. Methods Mol Biol 790:305\u2013318. https:\/\/doi.org\/10.1007\/978-1-61779-319-6_23","journal-title":"Methods Mol Biol"},{"issue":"3","key":"8_CR34","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1007\/s10719-015-9630-6","volume":"33","author":"Z Darula","year":"2016","unstructured":"Darula Z, Sarnyai F, Medzihradszky KF (2016) O-glycosylation sites identified from mucin core-1 type glycopeptides from human serum. Glycoconj J 33(3):435\u2013445. https:\/\/doi.org\/10.1007\/s10719-015-9630-6","journal-title":"Glycoconj J"},{"key":"8_CR35","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/j.chroma.2013.05.037","volume":"1299","author":"L Cao","year":"2013","unstructured":"Cao L, Yu L, Guo Z, Li X, Xue X, Liang X (2013) Application of a strong anion exchange material in electrostatic repulsion-hydrophilic interaction chromatography for selective enrichment of glycopeptides. J Chromatogr A 1299:18\u201324. https:\/\/doi.org\/10.1016\/j.chroma.2013.05.037","journal-title":"J Chromatogr A"},{"key":"8_CR36","doi-asserted-by":"publisher","first-page":"560391","DOI":"10.1155\/2012\/560391","volume":"2012","author":"J Saba","year":"2012","unstructured":"Saba J, Dutta S, Hemenway E, Viner R (2012) Increasing the productivity of glycopeptides analysis by using higher-energy collision dissociation-accurate mass-product-dependent electron transfer dissociation. Int J Proteomics 2012:560391. https:\/\/doi.org\/10.1155\/2012\/560391","journal-title":"Int J Proteomics"}],"container-title":["Methods in Molecular Biology","Mass Spectrometry of Glycoproteins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-0716-1241-5_8","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,4,28]],"date-time":"2021-04-28T02:20:20Z","timestamp":1619576420000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/978-1-0716-1241-5_8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021]]},"ISBN":["9781071612408","9781071612415"],"references-count":36,"URL":"https:\/\/doi.org\/10.1007\/978-1-0716-1241-5_8","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"value":"1064-3745","type":"print"},{"value":"1940-6029","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021]]},"assertion":[{"value":"29 April 2021","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}