{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,15]],"date-time":"2025-12-15T19:39:50Z","timestamp":1765827590966,"version":"3.40.3"},"publisher-location":"New York, NY","reference-count":47,"publisher":"Springer New York","isbn-type":[{"type":"print","value":"9781493972005"},{"type":"electronic","value":"9781493972012"}],"license":[{"start":{"date-parts":[[2017,1,1]],"date-time":"2017-01-01T00:00:00Z","timestamp":1483228800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2017]]},"DOI":"10.1007\/978-1-4939-7201-2_7","type":"book-chapter","created":{"date-parts":[[2017,8,14]],"date-time":"2017-08-14T14:43:24Z","timestamp":1502721804000},"page":"109-128","source":"Crossref","is-referenced-by-count":5,"title":["Microfluidics-Mass Spectrometry of Protein-Carbohydrate Interactions: Applications to the Development of Therapeutics and Biomarker Discovery"],"prefix":"10.1007","author":[{"given":"Alina D.","family":"Zamfir","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2017,8,15]]},"reference":[{"key":"7_CR1","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1038\/nrm4073","volume":"16","author":"C Xu","year":"2015","unstructured":"Xu C, Ng DT (2015) Glycosylation-directed quality control of protein folding. Nat Rev Mol Cell Biol 16:742\u2013752","journal-title":"Nat Rev Mol Cell Biol"},{"key":"7_CR2","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1007\/978-1-4939-2205-5_12","volume":"1258","author":"K Swiech","year":"2015","unstructured":"Swiech K, de Freitas MC, Covas DT, Pican\u00e7o-Castro V (2015) Recombinant glycoprotein production in human cell lines. Methods Mol Biol 1258:223\u2013240","journal-title":"Methods Mol Biol"},{"key":"7_CR3","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.bbamem.2015.12.018","volume":"1858","author":"C Zurzolo","year":"2016","unstructured":"Zurzolo C, Simons K (2016) Glycosylphosphatidylinositol-anchored proteins: membrane organization and transport. Biochim Biophys Acta 1858:632\u2013639","journal-title":"Biochim Biophys Acta"},{"key":"7_CR4","first-page":"2056","volume":"5","author":"M Cohen","year":"2015","unstructured":"Cohen M (2015) Notable aspects of glycan-protein interactions. Biomol Ther 5:2056\u20132072","journal-title":"Biomol Ther"},{"key":"7_CR5","doi-asserted-by":"crossref","first-page":"2429","DOI":"10.1002\/anie.200503168","volume":"45","author":"FH Cederkvist","year":"2006","unstructured":"Cederkvist FH, Zamfir AD, Bahrke S et al (2006) Ication of a high-affinity-binding oligosaccharide by (+) nanoelectrospray quadrupole time-of-flight tandem mass spectrometry of a noncovalent enzyme-ligand complex. Agew Chem Int Ed Engl 45:2429\u20132434","journal-title":"Agew Chem Int Ed Engl"},{"key":"7_CR6","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1111\/j.1440-1711.2005.01373.x","volume":"83","author":"J Holgersson","year":"2005","unstructured":"Holgersson J, Gustafsson A, Breimer ME (2005) Characteristics of protein\u2013carbohydrate interactions as a basis for developing novel carbohydrate-based antirejection therapies. Immunol Cell Biol 83:694\u2013708","journal-title":"Immunol Cell Biol"},{"key":"7_CR7","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/j.canlet.2016.02.016","volume":"374","author":"SR Krishn","year":"2016","unstructured":"Krishn SR, Kaur S, Smith LM et al (2016) Mucins and associated glycan signatures in colon adenoma-carcinoma sequence: prospective pathological implication(s) for early diagnosis of colon cancer. Cancer Lett 374:304\u2013314","journal-title":"Cancer Lett"},{"key":"7_CR8","first-page":"6","volume":"17","author":"X Li","year":"2016","unstructured":"Li X, Wang X, Tan Z et al (2016) Role of glycans in cancer cells undergoing epithelial-mesenchymal transition. Front Oncol 17:6\u201333","journal-title":"Front Oncol"},{"key":"7_CR9","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1007\/978-3-319-06068-2_8","volume":"806","author":"AD Zamfir","year":"2014","unstructured":"Zamfir AD (2014) Neurological analyses: focus on gangliosides and mass spectrometry. Adv Exp Med Biol 806:153\u2013204","journal-title":"Adv Exp Med Biol"},{"key":"7_CR10","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1080\/07328303.2015.1085061","volume":"34","author":"F C\u0103pitan","year":"2015","unstructured":"C\u0103pitan F, Robu A, Popescu L et al (2015) B subunit monomers of Cholerae toxin bind G1 ganglioside class as revealed by chip-nanoelectrospray multistage mass spectrometry. J Carbohydr Chem 34:388\u2013408","journal-title":"J Carbohydr Chem"},{"key":"7_CR11","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.bbagen.2014.09.026","volume":"1850","author":"SB Levery","year":"2015","unstructured":"Levery SB, Steentoft C, Halim A et al (2015) Advances in mass spectrometry driven O-glycoproteomics. Biochim Biophys Acta 1850:33\u201342","journal-title":"Biochim Biophys Acta"},{"key":"7_CR12","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.cca.2016.05.027","volume":"459","author":"ME Lassman","year":"2016","unstructured":"Lassman ME, McAvoy T, Chappell DL et al (2016) The clinical utility of mass spectrometry based protein assays. Clin Chim Acta 459:155\u2013161","journal-title":"Clin Chim Acta"},{"key":"7_CR13","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1089\/omi.2009.0146","volume":"14","author":"J Zaia","year":"2010","unstructured":"Zaia J (2010) Mass spectrometry and glycomics. OMICS 14:401\u2013418","journal-title":"OMICS"},{"key":"7_CR14","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1007\/978-1-4939-1292-6_20","volume":"1200","author":"J Hirabayashi","year":"2014","unstructured":"Hirabayashi J (2014) Lectin-based glycomics: how and when was the technology born? Methods Mol Biol 1200:225\u2013242","journal-title":"Methods Mol Biol"},{"key":"7_CR15","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.dmpk.2015.11.008","volume":"31","author":"N Nakayama","year":"2016","unstructured":"Nakayama N, Bando Y, Fukuda T et al (2016) Developments of mass spectrometry-based technologies for effective drug development linked with clinical proteomes. Drug Metab Pharmacokinet 31:3\u201311","journal-title":"Drug Metab Pharmacokinet"},{"key":"7_CR16","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1002\/prca.201500140","volume":"10","author":"R Longuesp\u00e9e","year":"2016","unstructured":"Longuesp\u00e9e R, Casadonte R, Kriegsmann M et al (2016) MALDI mass spectrometry imaging: a cutting-edge tool for fundamental and clinical histopathology. Proteomics Clin Appl 10:701\u2013719","journal-title":"Proteomics Clin Appl"},{"key":"7_CR17","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.aca.2016.06.019","volume":"935","author":"GG Morbioli","year":"2016","unstructured":"Morbioli GG, Mazzu-Nascimento T, Aquino A et al (2016) Recombinant drugs-on-a-chip: the usage of capillary electrophoresis and trends in miniaturized systems \u2013 a review. Anal Chim Acta 935:44\u201357","journal-title":"Anal Chim Acta"},{"key":"7_CR18","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1002\/mas.20197","volume":"28","author":"L B\u00eendil\u0103","year":"2009","unstructured":"B\u00eendil\u0103 L, Peter-Katalini\u0107 J (2009) Chip-mass spectrometry for glycomic studies. Mass Spectrom Rev 28:223\u2013253","journal-title":"Mass Spectrom Rev"},{"key":"7_CR19","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.carres.2014.08.014","volume":"398","author":"M Sarbu","year":"2015","unstructured":"Sarbu M, Robu A, Peter-Katalini\u0107 J, Zamfir AD (2015) Automated chip-nanoelectrospray mass spectrometry for glycourinomics in Schindler disease type I. Carbohydr Res 398:90\u2013100","journal-title":"Carbohydr Res"},{"key":"7_CR20","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1007\/978-1-61779-498-8_10","volume":"836","author":"AD Zamfir","year":"2012","unstructured":"Zamfir AD, Flangea C, Serb A et al (2012) Brain chondroitin\/dermatan sulfate, from cerebral tissue to fine structure: extraction, preparation, and fully automated chip-electrospray mass spectrometric analysis. Methods Mol Biol 836:145\u2013159","journal-title":"Methods Mol Biol"},{"key":"7_CR21","doi-asserted-by":"crossref","first-page":"2399","DOI":"10.1007\/s00726-015-2030-1","volume":"47","author":"F C\u0103pitan","year":"2015","unstructured":"C\u0103pitan F, Robu AC, Schiopu C et al (2015) \u03b2-Lactoglobulin detected in human milk forms noncovalent complexes with maltooligosaccharides as revealed by chip-nanoelectrospray high-resolution tandem mass spectrometry. Amino Acids 47:2399\u20132407","journal-title":"Amino Acids"},{"key":"7_CR22","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.ab.2008.03.039","volume":"378","author":"R Almeida","year":"2008","unstructured":"Almeida R, Mosoarca C, Chirita M et al (2008) Coupling of fully automated chip-based electrospray ionization to high capacity ion trap mass spectrometer for ganglioside analysis. Anal Biochem 378:43\u201352","journal-title":"Anal Biochem"},{"key":"7_CR23","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1080\/09540100903452122","volume":"21","author":"G Bu","year":"2010","unstructured":"Bu G, Luo Y, Jing L, Zhang Y (2010) Reduced antigenicity of \u03b2-lactoglobulin by conjugation with glucose through controlled Maillard reaction conditions. Food Agric Immunol 21:143\u2013156","journal-title":"Food Agric Immunol"},{"key":"7_CR24","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1007\/BF01049915","volume":"5","author":"B Domon","year":"1988","unstructured":"Domon B, Costello CE (1988) A systematic nomenclature for carbohydrate fragmentation in FAB-MS\/MS spectra of glycoconjugates. Glycoconj J 5:397\u2013409","journal-title":"Glycoconj J"},{"key":"7_CR25","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0076-6879(06)17015-9","volume":"417","author":"PH Lopez","year":"2006","unstructured":"Lopez PH, Schnaar RL (2006) Determination of glycolipid-protein interaction specificity. Methods Enzymol 417:205\u2013220","journal-title":"Methods Enzymol"},{"key":"7_CR26","doi-asserted-by":"crossref","first-page":"1824","DOI":"10.1007\/s12035-015-9136-z","volume":"53","author":"M Aureli","year":"2016","unstructured":"Aureli M, Mauri L, Ciampa MG et al (2016) GM1 ganglioside: past studies and future potential. Mol Neurobiol 53:1824\u20131842","journal-title":"Mol Neurobiol"},{"key":"7_CR27","doi-asserted-by":"crossref","first-page":"7321","DOI":"10.1007\/s00216-013-7173-x","volume":"405","author":"AD Zamfir","year":"2013","unstructured":"Zamfir AD, Fabris D, Capitan F et al (2013) Profiling and sequence analysis of gangliosides in human astrocytoma by high-resolution mass spectrometry. Anal Bioanal Chem 405:7321\u20137335","journal-title":"Anal Bioanal Chem"},{"key":"7_CR28","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1002\/jnr.23411","volume":"92","author":"T Ariga","year":"2014","unstructured":"Ariga T (2014) Pathogenic role of ganglioside metabolism in neurodegenerative diseases. J Neurosci Res 92:1227\u20131242","journal-title":"J Neurosci Res"},{"key":"7_CR29","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1517\/14728222.2014.986459","volume":"19","author":"M Suzuki","year":"2015","unstructured":"Suzuki M, Cheung NK (2015) Disialoganglioside GD2 as a therapeutic target for human diseases. Expert Opin Ther Targets 19:349\u2013362","journal-title":"Expert Opin Ther Targets"},{"key":"7_CR30","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1007\/s10495-015-1103-7","volume":"20","author":"I Horwacik","year":"2015","unstructured":"Horwacik I, Rokita H (2015) Targeting of tumor-associated gangliosides with antibodies affects signaling pathways and leads to cell death including apoptosis. Apoptosis 20:679\u2013688","journal-title":"Apoptosis"},{"key":"7_CR31","doi-asserted-by":"crossref","first-page":"1925","DOI":"10.1073\/pnas.0709619104","volume":"105","author":"AR Todeschini","year":"2008","unstructured":"Todeschini AR, Dos Santos JN, Handa K, Hakomori SI (2008) Ganglioside GM2\/GM3 complex affixed on silica nanospheres strongly inhibits cell motility through CD82\/cMet-mediated pathway. Proc Natl Acad Sci U S A 105:1925\u20131930","journal-title":"Proc Natl Acad Sci U S A"},{"key":"7_CR32","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1038\/nchembio.2059","volume":"12","author":"N Komura","year":"2016","unstructured":"Komura N, Suzuki KG, Ando H et al (2016) Raft-based interactions of gangliosides with a GPI-anchored receptor. Nat Chem Biol 12:402\u2013410","journal-title":"Nat Chem Biol"},{"key":"7_CR33","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1007\/s10719-015-9579-5","volume":"32","author":"K Yanagisawa","year":"2015","unstructured":"Yanagisawa K (2015) GM1 ganglioside and Alzheimer\u2019s disease. Glycoconj J 32:87\u201391","journal-title":"Glycoconj J"},{"key":"7_CR34","doi-asserted-by":"crossref","unstructured":"Ohkawa Y, Momota H, Kato A et al (2015) Ganglioside GD3 enhances invasiveness of gliomas by forming a complex with platelet-derived growth factor receptor \u03b1 and Yes kinase. J Biol Chem (26):16043\u201316058","DOI":"10.1074\/jbc.M114.635755"},{"key":"7_CR35","doi-asserted-by":"crossref","first-page":"1779","DOI":"10.1002\/eji.201242867","volume":"43","author":"T Gustafsson","year":"2013","unstructured":"Gustafsson T, Hua YJ, Dahlgren MW et al (2013) Direct interaction between cholera toxin and dendritic cells is required for oral adjuvant activity. Eur J Immunol 43:1779\u20131788","journal-title":"Eur J Immunol"},{"key":"7_CR36","doi-asserted-by":"crossref","first-page":"6884","DOI":"10.1021\/ac301511t","volume":"84","author":"CS Kim","year":"2012","unstructured":"Kim CS, Seo JH, Cha HJ (2012) Functional interaction analysis of GM1-related carbohydrates and vibrio cholerae toxins using carbohydrate microarray. Anal Chem 84:6884\u20136890","journal-title":"Anal Chem"},{"key":"7_CR37","doi-asserted-by":"crossref","first-page":"4640","DOI":"10.1039\/c3cs00001j","volume":"42","author":"N Jayaraman","year":"2013","unstructured":"Jayaraman N, Maiti K, Naresh K (2013) Multivalent glycoliposomes and micelles to study carbohydrate-protein and carbohydrate-carbohydrate interactions. Chem Soc Rev 42:4640\u20134656","journal-title":"Chem Soc Rev"},{"key":"7_CR38","doi-asserted-by":"crossref","first-page":"4742","DOI":"10.1021\/acs.analchem.6b00043","volume":"88","author":"J Li","year":"2016","unstructured":"Li J, Fan X, Kitova EN et al (2016) Screening glycolipids against proteins in vitro using picodiscs and catch-and-release electrospray ionization-mass spectrometry. Anal Chem 88:4742\u20134750","journal-title":"Anal Chem"},{"key":"7_CR39","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1007\/s13361-013-0751-5","volume":"25","author":"H Lin","year":"2014","unstructured":"Lin H, Kitova EN, Klassen JS (2014) Measuring positive cooperativity using the direct ESI-MS assay. Cholera toxin B subunit homopentamer binding to GM1 pentasaccharide. J Am Soc Mass Spectrom 25:104\u2013110","journal-title":"J Am Soc Mass Spectrom"},{"key":"7_CR40","doi-asserted-by":"crossref","first-page":"1334","DOI":"10.1002\/pmic.201200410","volume":"13","author":"R Tian","year":"2013","unstructured":"Tian R, Jin J, Taylor L et al (2013) Rapid and sensitive MRM-based mass spectrometry approach for systematically exploring ganglioside-protein interactions. Proteomics 13:1334\u20131338","journal-title":"Proteomics"},{"key":"7_CR41","doi-asserted-by":"crossref","first-page":"4888","DOI":"10.1021\/acs.analchem.5b00678","volume":"87","author":"L Han","year":"2015","unstructured":"Han L, Kitova EN, Li J et al (2015) Protein-glycolipid interactions studied in vitro using ESI-MS and nanodiscs: insights into the mechanisms and energetics of binding. Anal Chem 87:4888\u20134896","journal-title":"Anal Chem"},{"key":"7_CR42","doi-asserted-by":"crossref","first-page":"9528","DOI":"10.1073\/pnas.0402700101","volume":"101","author":"JE Syka","year":"2004","unstructured":"Syka JE, Coon JJ, Schroeder MJ et al (2004) Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc Natl Acad Sci U S A 101:9528\u20139533","journal-title":"Proc Natl Acad Sci U S A"},{"key":"7_CR43","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1007\/978-1-61779-513-8_10","volume":"842","author":"FG Hanisch","year":"2012","unstructured":"Hanisch FG (2012) O-glycoproteomics: site-specific O-glycoprotein analysis by CID\/ETD electrospray ionization tandem mass spectrometry and top-down glycoprotein sequencing by in-source decay MALDI mass spectrometry. Methods Mol Biol 842:179\u2013189","journal-title":"Methods Mol Biol"},{"key":"7_CR44","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1007\/s00726-014-1726-y","volume":"46","author":"M Sarbu","year":"2014","unstructured":"Sarbu M, Ghiulai RM, Zamfir AD (2014) Recent developments and applications of electron transfer dissociation mass spectrometry in proteomics. Amino Acids 46:1625\u20131634","journal-title":"Amino Acids"},{"key":"7_CR45","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1002\/bms.1200111109","volume":"11","author":"P Roepstorff","year":"1984","unstructured":"Roepstorff P, Fohlman J (1984) Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed Mass Spectrom 11:601","journal-title":"Biomed Mass Spectrom"},{"key":"7_CR46","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S0079-6123(08)61939-1","volume":"101","author":"CE Costello","year":"1994","unstructured":"Costello CE, Juhasz P, Perreault H (1994) New mass spectral approaches to ganglioside structure determination. Prog Brain Res 101:45\u201361","journal-title":"Prog Brain Res"},{"key":"7_CR47","volume":"7","author":"KM Gallegos","year":"2012","unstructured":"Gallegos KM, Conrady DG, Karve SS et al (2012) Shiga toxin binding to glycolipids and glycans. PLoS One 7:e30368","journal-title":"PLoS One"}],"container-title":["Methods in Molecular Biology","Proteomics for Drug Discovery"],"original-title":[],"link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-4939-7201-2_7","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,3,5]],"date-time":"2018-03-05T07:10:19Z","timestamp":1520233819000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/978-1-4939-7201-2_7"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017]]},"ISBN":["9781493972005","9781493972012"],"references-count":47,"URL":"https:\/\/doi.org\/10.1007\/978-1-4939-7201-2_7","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"type":"print","value":"1064-3745"},{"type":"electronic","value":"1940-6029"}],"subject":[],"published":{"date-parts":[[2017]]}}}