{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T03:34:39Z","timestamp":1772768079784,"version":"3.50.1"},"reference-count":72,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2015,6,1]],"date-time":"2015-06-01T00:00:00Z","timestamp":1433116800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2015,6,1]],"date-time":"2015-06-01T00:00:00Z","timestamp":1433116800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,9,8]],"date-time":"2020-09-08T00:00:00Z","timestamp":1599523200000},"content-version":"vor","delay-in-days":1926,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["mcponline.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular &amp; Cellular Proteomics"],"published-print":{"date-parts":[[2015,6]]},"DOI":"10.1074\/mcp.o114.046748","type":"journal-article","created":{"date-parts":[[2015,3,23]],"date-time":"2015-03-23T23:02:45Z","timestamp":1427151765000},"page":"1645-1656","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":29,"title":["A Microarray-Matrix-assisted Laser Desorption\/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM)*"],"prefix":"10.1016","volume":"14","author":[{"given":"Martin","family":"Pabst","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Simon Karl","family":"K\u00fcster","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fabian","family":"Wahl","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jasmin","family":"Krismer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Petra S.","family":"Dittrich","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Renato","family":"Zenobi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/mcp.O114.046748_bib1","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/S0304-4165(99)00165-8","article-title":"On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database","volume":"1473","author":"Apweiler","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/mcp.O114.046748_bib2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1432-1033.1993.tb18347.x","article-title":"Protein glycosylation. Structural and functional aspects","volume":"218","author":"Lis","year":"1993","journal-title":"Eur. J. Biochem"},{"key":"10.1074\/mcp.O114.046748_bib3","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1038\/nmeth0111-55","article-title":"At last, functional glycomics","volume":"8","author":"Zaia","year":"2011","journal-title":"Nat. Methods"},{"key":"10.1074\/mcp.O114.046748_bib4","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.cbpa.2009.07.022","article-title":"Determination of glycosylation sites and site-specific heterogeneity in glycoproteins","volume":"13","author":"An","year":"2009","journal-title":"Curr. Opin. Chem. Biol"},{"key":"10.1074\/mcp.O114.046748_bib5","doi-asserted-by":"crossref","first-page":"2370","DOI":"10.1126\/science.291.5512.2370","article-title":"Glycosylation and the immune system","volume":"291","author":"Rudd","year":"2001","journal-title":"Science"},{"key":"10.1074\/mcp.O114.046748_bib6","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1074\/mcp.R112.026005","article-title":"Glycoproteomic analysis of antibodies","volume":"12","author":"Zauner","year":"2013","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib7","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1021\/pr900956x","article-title":"GlycoSpectrumScan: fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA","volume":"9","author":"Deshpande","year":"2010","journal-title":"J. Proteome Res"},{"key":"10.1074\/mcp.O114.046748_bib8","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1021\/pr400714w","article-title":"Site-Specific N-Glycosylation Analysis of Human Immunoglobulin E","volume":"13","author":"Plomp","year":"2013","journal-title":"J. Proteome Res"},{"key":"10.1074\/mcp.O114.046748_bib9","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1021\/pr4012393","article-title":"Site-Specific Glycosylation of Secretory Immunoglobulin A from Human Colostrum","volume":"13","author":"Huang","year":"2015","journal-title":"J. Proteome Res"},{"key":"10.1074\/mcp.O114.046748_bib10","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/s10875-010-9409-2","article-title":"Analytical and Functional Aspects of Antibody Sialylation","volume":"30","author":"Stadlmann","year":"2010","journal-title":"J. Clin. Immunol"},{"key":"10.1074\/mcp.O114.046748_bib11","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.jim.2007.07.014","article-title":"Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry","volume":"326","author":"Mimura","year":"2007","journal-title":"J. Immunol. Methods"},{"key":"10.1074\/mcp.O114.046748_bib12","doi-asserted-by":"crossref","first-page":"2338","DOI":"10.1128\/AAC.01142-09","article-title":"Preclinical in vitro and in vivo characterization of the fully human monoclonal IgM antibody KBPA101 specific for Pseudomonas aeruginosa serotype IATS-O11","volume":"54","author":"Horn","year":"2010","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/mcp.O114.046748_bib13","doi-asserted-by":"crossref","first-page":"6263","DOI":"10.1073\/pnas.1320544111","article-title":"Expression and glycoengineering of functionally active heteromultimeric IgM in plants","volume":"111","author":"Loos","year":"2014","journal-title":"Proc. Natl. Acad. Sci U.S.A"},{"key":"10.1074\/mcp.O114.046748_bib14","doi-asserted-by":"crossref","first-page":"9","DOI":"10.2165\/11530550-000000000-00000","article-title":"Glycosylation of therapeutic proteins: an effective strategy to optimize efficacy","volume":"24","author":"Sola","year":"2010","journal-title":"BioDrugs"},{"key":"10.1074\/mcp.O114.046748_bib15","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1016\/j.carres.2010.02.017","article-title":"IL-1beta and TNF-alpha alter the glycophenotype of primary human chondrocytes in vitro","volume":"345","author":"Pabst","year":"2010","journal-title":"Carbohydr. Res"},{"key":"10.1074\/mcp.O114.046748_bib16","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.joca.2009.09.004","article-title":"Phenotype-related differential alpha-2,6- or alpha-2,3-sialylation of glycoprotein N-glycans in human chondrocytes","volume":"18","author":"Toegel","year":"2010","journal-title":"Osteoarthritis Cartilage"},{"key":"10.1074\/mcp.O114.046748_bib17","doi-asserted-by":"crossref","first-page":"1667","DOI":"10.1021\/pr1009959","article-title":"Plasma protein N-glycan profiles are associated with calendar age, familial longevity and health","volume":"10","author":"Ruhaak","year":"2011","journal-title":"J. Proteome Res"},{"key":"10.1074\/mcp.O114.046748_bib18","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1002\/pmic.201000517","article-title":"Glycan analysis by modern instrumental methods","volume":"11","author":"Pabst","year":"2011","journal-title":"Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib19","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.1016\/j.bbapap.2006.10.007","article-title":"Strategies for analysis of glycoprotein glycosylation","volume":"1764","author":"Geyer","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/mcp.O114.046748_bib20","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1073\/pnas.74.1.134","article-title":"Enzymatic conversion of proteins to glycoproteins","volume":"74","author":"Pless","year":"1977","journal-title":"Proc. Natl. Acad. Sci U.S.A"},{"key":"10.1074\/mcp.O114.046748_bib21","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.febslet.2004.08.061","article-title":"N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin","volume":"576","author":"Satomi","year":"2004","journal-title":"FEBS Letters"},{"key":"10.1074\/mcp.O114.046748_bib22","doi-asserted-by":"crossref","first-page":"4665","DOI":"10.1021\/bi00338a028","article-title":"Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F","volume":"24","author":"Tarentino","year":"1985","journal-title":"Biochemistry"},{"key":"10.1074\/mcp.O114.046748_bib23","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1016\/0006-291X(77)90982-2","article-title":"Demonstration of a new amidase acting on glycopeptides","volume":"76","author":"Takahashi","year":"1977","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/mcp.O114.046748_bib24","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1016\/j.molcel.2012.04.031","article-title":"Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery","volume":"46","author":"Zielinska","year":"2012","journal-title":"Mol. Cell"},{"key":"10.1074\/mcp.O114.046748_bib25","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1002\/j.1460-2075.1987.tb02359.x","article-title":"Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1","volume":"6","author":"Parekh","year":"1987","journal-title":"EMBO J"},{"key":"10.1074\/mcp.O114.046748_bib26","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1016\/0300-9084(88)90280-5","article-title":"Novel fast atom bombardment mass spectrometric procedures for glycoprotein analysis","volume":"70","author":"Dell","year":"1988","journal-title":"Biochimie"},{"key":"10.1074\/mcp.O114.046748_bib27","doi-asserted-by":"crossref","first-page":"8618","DOI":"10.1021\/bi00423a017","article-title":"Site-specific glycosylation of human recombinant erythropoietin: analysis of glycopeptides or peptides at each glycosylation site by fast atom bombardment mass spectrometry","volume":"27","author":"Sasaki","year":"1988","journal-title":"Biochemistry"},{"key":"10.1074\/mcp.O114.046748_bib28","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1093\/glycob\/1.4.393","article-title":"Site-specific N-glycosylation of human chorionic gonadotrophin\u2013structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy","volume":"1","author":"Weisshaar","year":"1991","journal-title":"Glycobiology"},{"key":"10.1074\/mcp.O114.046748_bib29","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1006\/abio.1994.1259","article-title":"Applications of electrospray mass spectrometry to erythropoietin N- and O-linked glycans","volume":"219","author":"Linsley","year":"1994","journal-title":"Anal. Biochem"},{"key":"10.1074\/mcp.O114.046748_bib30","first-page":"115","article-title":"Glycoproteomics based on tandem mass spectrometry of glycopeptides","volume":"849","author":"Wuhrer","year":"2007","journal-title":"J. Chromatogr"},{"key":"10.1074\/mcp.O114.046748_bib31","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.R110.003251","article-title":"Mass spectrometry based glycoproteomics\u2013from a proteomics perspective","volume":"10","author":"Pan","year":"2011","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib32","doi-asserted-by":"crossref","first-page":"5791","DOI":"10.1021\/pr400783j","article-title":"Site-specific glycan-Peptide analysis for determination of N-glycoproteome heterogeneity","volume":"12","author":"Parker","year":"2013","journal-title":"J. Proteome Res"},{"key":"10.1074\/mcp.O114.046748_bib33","doi-asserted-by":"crossref","first-page":"3697","DOI":"10.1021\/pr800258k","article-title":"Experimental evaluation of protein identification by an LC\/MALDI\/on-target digestion approach","volume":"7","author":"Getie-Kebtie","year":"2008","journal-title":"J. Proteome Res"},{"key":"10.1074\/mcp.O114.046748_bib34","doi-asserted-by":"crossref","first-page":"3144","DOI":"10.1021\/ac702081a","article-title":"Maximizing coverage of glycosylation heterogeneity in MALDI-MS analysis of glycoproteins with up to 27 glycosylation sites","volume":"80","author":"Zhang","year":"2008","journal-title":"Anal. Chem"},{"key":"10.1074\/mcp.O114.046748_bib35","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1515\/hsz-2012-0148","article-title":"Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140","volume":"393","author":"Pabst","year":"2012","journal-title":"Biol. Chem"},{"key":"10.1074\/mcp.O114.046748_bib36","doi-asserted-by":"crossref","first-page":"2020","DOI":"10.1002\/rcm.1585","article-title":"Site-specific N-glycosylation analysis: matrix-assisted laser desorption\/ionization quadrupole-quadrupole time-of-flight tandem mass spectral signatures for recognition and identification of glycopeptides","volume":"18","author":"Krokhin","year":"2004","journal-title":"Rapid Commun. Mass Spectrom"},{"key":"10.1074\/mcp.O114.046748_bib37","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1038\/nprot.2012.062","article-title":"Determination of site-specific glycan heterogeneity on glycoproteins","volume":"7","author":"Kolarich","year":"2012","journal-title":"Nat. Protocols"},{"key":"10.1074\/mcp.O114.046748_bib38","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1038\/nbt.1532","article-title":"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins","volume":"27","author":"Wollscheid","year":"2009","journal-title":"Nat. Biotechnol"},{"key":"10.1074\/mcp.O114.046748_bib39","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1002\/pmic.200700720","article-title":"Glycoproteomic characterization of butyrylcholinesterase from human plasma","volume":"8","author":"Kolarich","year":"2008","journal-title":"Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib40","doi-asserted-by":"crossref","first-page":"1856","DOI":"10.1021\/bi952354m","article-title":"Cell line and site specific comparative analysis of the N-linked oligosaccharides on human ICAM-1des454\u2013532 by electrospray ionization mass spectrometry","volume":"35","author":"Bloom","year":"1996","journal-title":"Biochemistry"},{"key":"10.1074\/mcp.O114.046748_bib41","doi-asserted-by":"crossref","first-page":"2909","DOI":"10.1021\/ac00024a020","article-title":"Characterization of the tryptic map of recombinant DNA derived tissue plasminogen activator by high-performance liquid chromatography-electrospray ionization mass spectrometry","volume":"63","author":"Ling","year":"1991","journal-title":"Anal. Chem"},{"key":"10.1074\/mcp.O114.046748_bib42","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/1044-0305(94)85050-X","article-title":"Characterization of protein iv-glycosylation by reversed-phase microbore liquid chromatography\/electrospray mass spectrometry, complementary mobile phases, and sequential exoglycosidase digestion","volume":"5","author":"Medzihradszky","year":"1994","journal-title":"J. Am. Soc. Mass Spectrom"},{"key":"10.1074\/mcp.O114.046748_bib43","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1002\/pro.5560040419","article-title":"Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC\/electrospray mass spectrometry and sequential glycosidase digestion","volume":"4","author":"Schindler","year":"1995","journal-title":"Protein Sci"},{"key":"10.1074\/mcp.O114.046748_bib44","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1021\/ac048619x","article-title":"Protein glycosylation analyzed by normal-phase nano-liquid chromatography\u2013mass spectrometry of glycopeptides","volume":"77","author":"Wuhrer","year":"2005","journal-title":"Anal. Chem"},{"key":"10.1074\/mcp.O114.046748_bib45","doi-asserted-by":"crossref","first-page":"i","DOI":"10.1002\/jms.3210","article-title":"Quantitative mapping of glycoprotein micro-heterogeneity and macro-heterogeneity: an evaluation of mass spectrometry signal strengths using synthetic peptides and glycopeptides","volume":"48","author":"Stavenhagen","year":"2013","journal-title":"J. Mass Spectrom"},{"key":"10.1074\/mcp.O114.046748_bib46","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.ab.2009.08.023","article-title":"Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies","volume":"395","author":"Wohlgemuth","year":"2009","journal-title":"Anal. Biochem"},{"key":"10.1074\/mcp.O114.046748_bib47","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/j.jprot.2008.06.013","article-title":"Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry","volume":"71","author":"Calvano","year":"2008","journal-title":"J. Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib48","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1038\/nbt827","article-title":"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry","volume":"21","author":"Zhang","year":"2003","journal-title":"Nat. Biotechnol"},{"key":"10.1074\/mcp.O114.046748_bib49","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M110.006833","article-title":"Quantitative N-linked glycoproteomics of myocardial ischemia and reperfusion injury reveals early remodeling in the extracellular environment","volume":"10","author":"Parker","year":"2011","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib50","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1002\/pmic.201100498","article-title":"MALDI-TOF-MS analysis of sialylated glycans and glycopeptides using 4-chloro-alpha-cyanocinnamic acid matrix","volume":"12","author":"Selman","year":"2012","journal-title":"Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib51","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1002\/rcm.1521","volume":"18","author":"Demelbauer","year":"2004","journal-title":"Rapid Commun. Mass Spectrom"},{"key":"10.1074\/mcp.O114.046748_bib52","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1021\/ac00055a009","article-title":"Collisional fragmentation of glycopeptides by electrospray ionization LC\/MS and LC\/MS\/MS: methods for selective detection of glycopeptides in protein digests","volume":"65","author":"Huddleston","year":"1993","journal-title":"Anal. Chem"},{"key":"10.1074\/mcp.O114.046748_bib53","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1093\/glycob\/8.8.755","article-title":"Site localization of sialyl Lewis (x) antigen on alpha1-acid glycoprotein by high performance liquid chromatography-electrospray mass spectrometry","volume":"8","author":"Dage","year":"1998","journal-title":"Glycobiology"},{"key":"10.1074\/mcp.O114.046748_bib54","doi-asserted-by":"crossref","first-page":"2251","DOI":"10.1002\/pmic.201300036","article-title":"PTM MarkerFinder, a software tool to detect and validate spectra from peptides carrying post-translational modifications","volume":"13","author":"Nanni","year":"2013","journal-title":"Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib55","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1039\/b713816d","article-title":"Glycopeptide analysis by mass spectrometry","volume":"133","author":"Dalpathado","year":"2008","journal-title":"Analyst"},{"key":"10.1074\/mcp.O114.046748_bib56","doi-asserted-by":"crossref","first-page":"560391","DOI":"10.1155\/2012\/560391","article-title":"Increasing the productivity of glycopeptides analysis by using higher-energy collision dissociation-accurate mass-product-dependent electron transfer dissociation","volume":"2012","author":"Saba","year":"2012","journal-title":"Int. J. Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib57","doi-asserted-by":"crossref","first-page":"137","DOI":"10.2174\/138620709787315436","article-title":"High-energy collision induced dissociation of biomolecules: MALDI-TOF\/RTOF mass spectrometry in comparison to tandem sector mass spectrometry","volume":"12","author":"Pittenauer","year":"2009","journal-title":"Comb. Chem. High Throughput Screen"},{"key":"10.1074\/mcp.O114.046748_bib58","first-page":"252","article-title":"Analysis of glycoproteins in human serum by means of glycospecific magnetic bead separation and LC-MALDI-TOF\/TOF analysis with automated glycopeptide detection","volume":"18","author":"Sparbier","year":"2007","journal-title":"J. Biomol. Tech"},{"key":"10.1074\/mcp.O114.046748_bib59","doi-asserted-by":"crossref","first-page":"4848","DOI":"10.1021\/ac4041982","article-title":"Droplet-Based Fractionation of Nano-LC Separations on Microarrays for Analysis with Sub-Peak Resolution Using MALDI-MS","volume":"86","author":"Kuster","year":"2014","journal-title":"Anal. Chem"},{"key":"10.1074\/mcp.O114.046748_bib60","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1021\/pr7006957","article-title":"Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility","volume":"7","author":"Go","year":"2008","journal-title":"J. Proteome Res"},{"key":"10.1074\/mcp.O114.046748_bib61","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.1002\/anie.201409440","article-title":"Screening for protein phosphorylation using nanoscale reactions on microdroplet arrays","volume":"54","author":"Kuster","year":"2015","journal-title":"Angewandte Chemie"},{"key":"10.1074\/mcp.O114.046748_bib62","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1016\/S0021-9258(17)37878-X","article-title":"Structure of the high mannose oligosaccharides of a human IgM myeloma protein. I. The major oligosaccharides of the two high mannose glycopeptides","volume":"254","author":"Chapman","year":"1979","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.O114.046748_bib63","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1016\/S0021-9258(17)37879-1","article-title":"Structure of the high mannose oligosaccharides of a human IgM myeloma protein. II. The minor oligosaccharides of high mannose glycopeptide","volume":"254","author":"Chapman","year":"1979","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.O114.046748_bib64","doi-asserted-by":"crossref","first-page":"29080","DOI":"10.1074\/jbc.M504528200","article-title":"Human serum IgM glycosylation: identification of glycoforms that can bind to mannan-binding lectin","volume":"280","author":"Arnold","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.O114.046748_bib65","doi-asserted-by":"crossref","first-page":"3206","DOI":"10.1039\/c0lc00211a","article-title":"High-density micro-arrays for mass spectrometry","volume":"10","author":"Urban","year":"2010","journal-title":"Lab Chip"},{"key":"10.1074\/mcp.O114.046748_bib66","doi-asserted-by":"crossref","first-page":"9771","DOI":"10.1021\/ac4021775","article-title":"Self-aliquoting microarray plates for accurate quantitative matrix-assisted laser desorption\/ionization mass spectrometry","volume":"85","author":"Pabst","year":"2013","journal-title":"Anal. Chem"},{"key":"10.1074\/mcp.O114.046748_bib67","doi-asserted-by":"crossref","first-page":"2427","DOI":"10.1007\/s00216-011-4923-5","article-title":"Analysis of recombinant human follicle-stimulating hormone (FSH) by mass spectrometric approaches","volume":"400","author":"Grass","year":"2011","journal-title":"Anal. Bioanal. Chem"},{"key":"10.1074\/mcp.O114.046748_bib68","doi-asserted-by":"crossref","first-page":"2932","DOI":"10.1073\/pnas.76.6.2932","article-title":"Amino acid sequence of a mouse immunoglobulin mu chain","volume":"76","author":"Kehry","year":"1979","journal-title":"Proc. Natl. Acad. Sci U.S.A"},{"key":"10.1074\/mcp.O114.046748_bib69","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1002\/1615-9861(200102)1:2<340::AID-PROT340>3.0.CO;2-B","article-title":"GlycoMod\u2013a software tool for determining glycosylation compositions from mass spectrometric data","volume":"1","author":"Cooper","year":"2001","journal-title":"Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib70","doi-asserted-by":"crossref","first-page":"2858","DOI":"10.1002\/pmic.200700968","article-title":"Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides","volume":"8","author":"Stadlmann","year":"2008","journal-title":"Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib71","doi-asserted-by":"crossref","first-page":"2935","DOI":"10.1074\/mcp.M113.030643","article-title":"Interlaboratory study on differential analysis of protein glycosylation by mass spectrometry: the ABRF glycoprotein research multi-institutional study 2012","volume":"12","author":"Leymarie","year":"2013","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/mcp.O114.046748_bib72","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.1089\/088922202320886352","article-title":"High mannose glycans and sialic acid on gp120 regulate binding of mannose-binding lectin (MBL) to HIV type 1","volume":"18","author":"Hart","year":"2002","journal-title":"AIDS Res. Hum. Retroviruses"}],"container-title":["Molecular &amp; Cellular Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1535947620331741?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1535947620331741?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/mcp.O114.046748","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T00:46:06Z","timestamp":1761525966000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1535947620331741"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,6]]},"references-count":72,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2015,6]]}},"alternative-id":["S1535947620331741"],"URL":"https:\/\/doi.org\/10.1074\/mcp.o114.046748","relation":{},"ISSN":["1535-9476"],"issn-type":[{"value":"1535-9476","type":"print"}],"subject":[],"published":{"date-parts":[[2015,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"A Microarray-Matrix-assisted Laser Desorption\/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM)*","name":"articletitle","label":"Article Title"},{"value":"Molecular & Cellular Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/mcp.O114.046748","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2015 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}