{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T12:40:41Z","timestamp":1770813641953,"version":"3.50.1"},"reference-count":78,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Proteomics"],"published-print":{"date-parts":[[2011,10]]},"DOI":"10.1016\/j.jprot.2011.01.002","type":"journal-article","created":{"date-parts":[[2011,1,22]],"date-time":"2011-01-22T04:46:19Z","timestamp":1295671579000},"page":"2453-2475","source":"Crossref","is-referenced-by-count":50,"title":["Redox proteomics of fat globules unveils broad protein lactosylation and compositional changes in milk samples subjected to various technological procedures"],"prefix":"10.1016","volume":"74","author":[{"given":"Simona","family":"Arena","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Giovanni","family":"Renzone","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gianfranco","family":"Novi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrea","family":"Scaloni","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jprot.2011.01.002_bb0005","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.jprot.2009.09.018","article-title":"OMICS-rooted studies of milk proteins, oligosaccharides and lipids","volume":"73","author":"Casado","year":"2009","journal-title":"J Proteomics"},{"key":"10.1016\/j.jprot.2011.01.002_bb0010","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1097\/00075197-200211000-00007","article-title":"Bioactive components in milk","volume":"5","author":"German","year":"2002","journal-title":"Curr Opin Clin Nutr Metab Care"},{"key":"10.1016\/j.jprot.2011.01.002_bb0015","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1186\/1476-511X-6-25","article-title":"Bovine milk in human nutrition \u2014 a review","volume":"6","author":"Haug","year":"2007","journal-title":"Lipids Health Dis"},{"key":"10.1016\/j.jprot.2011.01.002_bb0020","doi-asserted-by":"crossref","first-page":"1537S","DOI":"10.1093\/ajcn\/77.6.1537S","article-title":"Nutritional and physiologic significance of human milk proteins","volume":"77","author":"L\u00f6nnerdal","year":"2003","journal-title":"Am J Clin Nutr"},{"key":"10.1016\/j.jprot.2011.01.002_bb0025","doi-asserted-by":"crossref","first-page":"3339","DOI":"10.1021\/pr100123f","article-title":"Human milk proteins: an interactomics and updated functional overview","volume":"9","author":"D'Alessandro","year":"2010","journal-title":"J Proteome Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0030","doi-asserted-by":"crossref","unstructured":"D'Alessandro A, Zolla L, Scaloni A. The bovine milk proteome: cherishing, nourishing and fostering molecular complexity. An interactomics and functional overview. Mol Biosyst 2010, in press.","DOI":"10.1039\/C0MB00027B"},{"key":"10.1016\/j.jprot.2011.01.002_bb0035","first-page":"G139","article-title":"Intestinal absorption of undegraded proteins in men: presence of bromelain in plasma after oral intake","volume":"273","author":"Castell","year":"1997","journal-title":"Am J Physiol"},{"key":"10.1016\/j.jprot.2011.01.002_bb0040","doi-asserted-by":"crossref","first-page":"2555","DOI":"10.1271\/bbb.80252","article-title":"Absorption, migration and kinetics in peripheral blood of orally administered ovalbumin in a mouse model","volume":"72","author":"Matsubara","year":"2008","journal-title":"Biosci Biotechnol Biochem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0045","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1016\/j.intimp.2007.05.019","article-title":"Uptake of ingested bovine lactoferrin and its accumulation in adult mouse tissues","volume":"7","author":"Fischer","year":"2007","journal-title":"Int Immunopharmacol"},{"key":"10.1016\/j.jprot.2011.01.002_bb0050","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1016\/0091-6749(94)90259-3","article-title":"Beta-lactoglobulin secretion in human milk varies widely after cow's milk ingestion in mothers of infants with cow's milk allergy","volume":"93","author":"Sorva","year":"1994","journal-title":"J Allergy Clin Immunol"},{"key":"10.1016\/j.jprot.2011.01.002_bb0055","doi-asserted-by":"crossref","first-page":"8631","DOI":"10.1021\/jf061760h","article-title":"Uptake of 2S albumin allergens, Ber e 1 and Ses i 1, across human intestinal epithelial Caco-2 cell monolayers","volume":"54","author":"Moreno","year":"2006","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0060","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/S0308-8146(98)00075-2","article-title":"Effect of heating on Maillard reactions in milk","volume":"62","author":"van Boekel","year":"1998","journal-title":"Food Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0065","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.chroma.2007.04.035","article-title":"Direct determination of methionine sulfoxide in milk proteins by enzyme hydrolysis\/high-performance liquid chromatography","volume":"1157","author":"Baxter","year":"2007","journal-title":"J Chromatogr A"},{"key":"10.1016\/j.jprot.2011.01.002_bb0070","doi-asserted-by":"crossref","first-page":"6096","DOI":"10.1021\/jf0705567","article-title":"Site-specific formation of Maillard, oxidation, and condensation products from whey proteins during reaction with lactose","volume":"55","author":"Meltretter","year":"2007","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0075","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.chroma.2004.08.104","article-title":"Quantitative determination of dityrosine in milk powders by liquid chromatography coupled to tandem mass spectrometry using isotope dilution","volume":"1052","author":"Fenaille","year":"2004","journal-title":"J Chromatogr A"},{"key":"10.1016\/j.jprot.2011.01.002_bb0080","doi-asserted-by":"crossref","first-page":"3097","DOI":"10.1002\/pmic.200401139","article-title":"Carbonylation of milk powder proteins as a consequence of processing conditions","volume":"5","author":"Fenaille","year":"2005","journal-title":"Proteomics"},{"key":"10.1016\/j.jprot.2011.01.002_bb0085","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.foodchem.2003.11.019","article-title":"Assessment of protein glycation markers in infant formulas","volume":"87","author":"Birlouez-Aragon","year":"2004","journal-title":"Food Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0090","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/S0308-8146(98)00244-1","article-title":"Determination of N(epsilon)-carboxymethyllysine in milk products by a modified reversed-phase HPLC method","volume":"65","author":"Drusch","year":"1999","journal-title":"Food Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0095","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1007\/s002170050043","article-title":"Detection and quantification of pentosidine in foods","volume":"204","author":"Henle","year":"1997","journal-title":"Z Lebensm Unters Forsch"},{"key":"10.1016\/j.jprot.2011.01.002_bb0100","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1007\/s002170050397","article-title":"Detection of Maillard products of lactose in heated or processed milk by HPLC\/DAD","volume":"208","author":"Pischetsrieder","year":"1999","journal-title":"Z Lebensm Unters Forsch"},{"key":"10.1016\/j.jprot.2011.01.002_bb0105","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1007\/BF01193359","article-title":"Evaluation of the extent of the early Maillard-reaction in milk products by direct measurement of the Amadori-product lactulosyllysine","volume":"193","author":"Henle","year":"1991","journal-title":"Z Lebensm Unters Forsch"},{"key":"10.1016\/j.jprot.2011.01.002_bb0110","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1021\/ac990590n","article-title":"Modern mass spectrometric methodologies in monitoring milk quality","volume":"72","author":"Siciliano","year":"2000","journal-title":"Anal Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0115","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0021-9673(98)00610-4","article-title":"Analysis of the Maillard reaction products of beta-lactoglobulin and lactose in skimmed milk powder by capillary electrophoresis and electrospray mass spectrometry","volume":"822","author":"Jones","year":"1998","journal-title":"J Chromatogr A"},{"key":"10.1016\/j.jprot.2011.01.002_bb0120","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1006\/bbrc.1997.6955","article-title":"Nonenzymic lactosylation of bovine beta-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms","volume":"236","author":"Morgan","year":"1997","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.jprot.2011.01.002_bb0125","doi-asserted-by":"crossref","first-page":"8874","DOI":"10.1021\/jf061646z","article-title":"Investigation of the lactosylation of whey proteins by liquid chromatography-mass spectrometry","volume":"54","author":"Czerwenka","year":"2006","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0130","doi-asserted-by":"crossref","first-page":"2065","DOI":"10.1007\/s00216-007-1447-0","article-title":"Evaluation of the thermal history of bovine milk from the lactosylation of whey proteins: an investigation by liquid chromatography-electrospray ionization mass spectrometry","volume":"389","author":"Losito","year":"2007","journal-title":"Anal Bioanal Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0135","doi-asserted-by":"crossref","first-page":"2985","DOI":"10.1021\/jf063083x","article-title":"Effect of heat treatment on the detection of intact bovine beta-lactoglobulins by LC mass spectrometry","volume":"55","author":"Monaci","year":"2007","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0140","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/S0003-2697(03)00357-9","article-title":"Monitoring of beta-lactoglobulin dry-state glycation using various analytical techniques","volume":"320","author":"Fenaille","year":"2003","journal-title":"Anal Biochem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0145","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1002\/mnfr.200900008","article-title":"Assessment of heat treatment of dairy products by MALDI-TOF-MS","volume":"53","author":"Meltretter","year":"2009","journal-title":"Mol Nutr Food Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0150","doi-asserted-by":"crossref","first-page":"1483","DOI":"10.1002\/rcm.1077","article-title":"Solid-state glycation of beta-lactoglobulin monitored by electrospray ionisation mass spectrometry and gel electrophoresis techniques","volume":"17","author":"Fenaille","year":"2003","journal-title":"Rapid Commun Mass Spectrom"},{"key":"10.1016\/j.jprot.2011.01.002_bb0155","doi-asserted-by":"crossref","first-page":"2095","DOI":"10.1021\/jf048688c","article-title":"Kinetics and mechanism of lactosylation of alpha-lactalbumin","volume":"53","author":"Lund","year":"2005","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0160","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/S0167-4838(02)00290-X","article-title":"Characterization of heat-induced lactosylation products in caseins by immunoenzymatic and mass spectrometric methodologies","volume":"1598","author":"Scaloni","year":"2002","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.jprot.2011.01.002_bb0165","doi-asserted-by":"crossref","first-page":"2270","DOI":"10.3168\/jds.S0022-0302(97)76176-9","article-title":"Characterization by ionization mass spectrometry of lactosyl beta-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site","volume":"80","author":"Leonil","year":"1997","journal-title":"J Dairy Sci"},{"key":"10.1016\/j.jprot.2011.01.002_bb0170","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/S0167-4838(98)00177-0","article-title":"Identification of a \u03b2-lactoglobulin lactosylation site","volume":"1388","author":"Fogliano","year":"1998","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.jprot.2011.01.002_bb0175","doi-asserted-by":"crossref","first-page":"5165","DOI":"10.1021\/jf800571j","article-title":"Identification and site-specific relative quantification of beta-lactoglobulin modifications in heated milk and dairy products","volume":"56","author":"Meltretter","year":"2008","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0180","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1002\/jms.539","article-title":"Solid-state glycation of beta-lactoglobulin by lactose and galactose: localization of the modified amino acids using mass spectrometric techniques","volume":"39","author":"Fenaille","year":"2004","journal-title":"J Mass Spectrom"},{"key":"10.1016\/j.jprot.2011.01.002_bb0185","doi-asserted-by":"crossref","first-page":"3414","DOI":"10.1002\/pmic.201000321","article-title":"Modern proteomic methodologies for the characterization of lactosylation protein targets in milk","volume":"10","author":"Arena","year":"2010","journal-title":"Proteomics"},{"key":"10.1016\/j.jprot.2011.01.002_bb0190","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1007\/s00216-010-3465-6","article-title":"Correlation between lactosylation and denaturation of major whey proteins: an investigation by liquid chromatography-electrospray ionization mass spectrometry","volume":"396","author":"Losito","year":"2010","journal-title":"Anal Bioanal Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0195","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/S0924-2244(02)00133-4","article-title":"Recent advances in the characterisation of heat induced aggregates and intermediates of whey proteins","volume":"13","author":"de la Fuente","year":"2002","journal-title":"Trends Food Sci Technol"},{"key":"10.1016\/j.jprot.2011.01.002_bb0200","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1002\/mnfr.200600112","article-title":"Proteolysis of milk proteins lactosylated in model systems","volume":"51","author":"Dalsgaard","year":"2007","journal-title":"Mol Nutr Food Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0205","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1080\/09540100400003444","article-title":"Immunoprobes for thermally-induced alteration in whey protein structure and their application to the analysis of thermally-treated milks","volume":"15","author":"Karamanova","year":"2003","journal-title":"Food Agric Immunol"},{"key":"10.1016\/j.jprot.2011.01.002_bb0210","doi-asserted-by":"crossref","first-page":"4002","DOI":"10.1021\/jf035458+","article-title":"Maillard reaction and enzymatic browning affect the allergenicity of Pru av 1, the major allergen from cherry (Prunus avium)","volume":"52","author":"Gruber","year":"2004","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0215","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1002\/mnfr.200700035","article-title":"Dietary advanced glycation endproducts (AGEs) and their health effects","volume":"51","author":"Sebekova","year":"2007","journal-title":"Mol Nutr Food Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0220","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1002\/mnfr.200700067","article-title":"Dietary advanced glycation end products \u2014 a risk to human health? A call for an interdisciplinary debate","volume":"51","author":"Henle","year":"2007","journal-title":"Mol Nutr Food Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0225","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s003940200000","article-title":"Nutritional and metabolic consequences of the early Maillard reaction of heat treated milk in the pig. Significance for man","volume":"41","author":"R\u00e9rat","year":"2002","journal-title":"Eur J Nutr"},{"key":"10.1016\/j.jprot.2011.01.002_bb0230","doi-asserted-by":"crossref","first-page":"2289","DOI":"10.3168\/jds.S0022-0302(05)72906-4","article-title":"Bovine milk fat globule membrane as a potential nutraceutical","volume":"88","author":"Spitsberg","year":"2005","journal-title":"J Dairy Sci"},{"key":"10.1016\/j.jprot.2011.01.002_bb0235","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1017\/S0022029900030594","article-title":"Changes in structure of the bovine milk fat globule membrane on heating whole milk","volume":"59","author":"Houlihan","year":"1992","journal-title":"J Dairy Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0240","doi-asserted-by":"crossref","first-page":"24","DOI":"10.3168\/jds.S0022-0302(95)76612-7","article-title":"Heat-induced interactions between the proteins of milk fat globule membrane and skim milk","volume":"78","author":"Kim","year":"1995","journal-title":"J Dairy Sci"},{"key":"10.1016\/j.jprot.2011.01.002_bb0245","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1017\/S002202990200571X","article-title":"Chemical changes in bovine milk fat globule membrane caused by heat treatment and homogenization of whole milk","volume":"69","author":"Lee","year":"2002","journal-title":"J Dairy Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0250","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1017\/S0022029904000512","article-title":"Interactions of fat globule surface proteins during concentration of whole milk in a pilot-scale multiple-effect evaporator","volume":"71","author":"Ye","year":"2004","journal-title":"J Dairy Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0255","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1016\/j.idairyj.2006.04.007","article-title":"Behaviour of homogenized fat globules during the spray drying of whole milk","volume":"17","author":"Ye","year":"2007","journal-title":"Int Dairy J"},{"key":"10.1016\/j.jprot.2011.01.002_bb0260","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1017\/S0022029908003464","article-title":"Changes in the surface protein of the fat globules during homogenization and heat treatment of concentrated milk","volume":"75","author":"Ye","year":"2008","journal-title":"J Dairy Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0265","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/0003-2697(84)90782-6","article-title":"A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids","volume":"138","author":"Wessel","year":"1984","journal-title":"Anal Biochem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0270","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal Biochem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0275","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.jprot.2011.01.002_bb0280","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1002\/elps.200305844","article-title":"Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis","volume":"25","author":"Candiano","year":"2004","journal-title":"Electrophoresis"},{"key":"10.1016\/j.jprot.2011.01.002_bb0285","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1002\/pmic.200601030","article-title":"A widespread picture of the Streptococcus thermophilus proteome by cell lysate fractionation and gel-based\/gel-free approaches","volume":"7","author":"Salzano","year":"2007","journal-title":"Proteomics"},{"key":"10.1016\/j.jprot.2011.01.002_bb0290","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1002\/elps.200900459","article-title":"The proteome of lentil (Lens culinaris Medik.) seeds: discriminating between landraces","volume":"31","author":"Scippa","year":"2010","journal-title":"Electrophoresis"},{"key":"10.1016\/j.jprot.2011.01.002_bb0295","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1074\/mcp.M500226-MCP200","article-title":"Hyperphosphorylation of JNK-interacting protein 1, a protein associated with Alzheimer disease","volume":"5","author":"D'Ambrosio","year":"2006","journal-title":"Mol Cell Proteomics"},{"key":"10.1016\/j.jprot.2011.01.002_bb0300","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1051\/lait:2002004","article-title":"Appearance and submicromic particles in themilk fat globule size distribution uponmechanical treatments","volume":"82","author":"Michalski","year":"2002","journal-title":"Lait"},{"key":"10.1016\/j.jprot.2011.01.002_bb0305","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1051\/lait:2004012","article-title":"The size of native milk fat globules affects physico-chemical and functional properties of Emmental cheese","volume":"84","author":"Michalski","year":"2004","journal-title":"Lait"},{"key":"10.1016\/j.jprot.2011.01.002_bb0310","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1017\/S0022029906001889","article-title":"Bovine milk fat globule membrane proteome","volume":"73","author":"Reinhardt","year":"2006","journal-title":"J Dairy Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0315","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1016\/j.jprot.2009.11.008","article-title":"Qualitative and quantitative profiling of the bovine milk fat globule membrane proteome","volume":"73","author":"Affolter","year":"2010","journal-title":"J Proteomics"},{"key":"10.1016\/j.jprot.2011.01.002_bb0320","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/j.tifs.2006.02.004","article-title":"Does homogenization affect the human health properties of cow'smilk?","volume":"17","author":"Michalski","year":"2006","journal-title":"Trends Food Sci Tech"},{"key":"10.1016\/j.jprot.2011.01.002_bb0325","doi-asserted-by":"crossref","first-page":"1456","DOI":"10.1016\/j.jasms.2005.04.005","article-title":"Immobilization of aminophenylboronic acid on magnetic beads for the direct determination of glycoproteins by matrix assisted laser desorption ionization mass spectrometry","volume":"16","author":"Lee","year":"2005","journal-title":"J Am Soc Mass Spectrom"},{"key":"10.1016\/j.jprot.2011.01.002_bb0330","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/rcm.2793","article-title":"Application of phenylboronic acid modified hydrogel affinity chips for high-throughput mass spectrometric analysis of glycated proteins","volume":"21","author":"Gontarev","year":"2007","journal-title":"Rapid Commun Mass Spectrom"},{"key":"10.1016\/j.jprot.2011.01.002_bb0335","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1196\/annals.1433.060","article-title":"Analysis of amadori peptides enriched by boronic acid affinity chromatography","volume":"1126","author":"Frolov","year":"2008","journal-title":"Ann NY Acad Sci"},{"key":"10.1016\/j.jprot.2011.01.002_bb0340","doi-asserted-by":"crossref","first-page":"2323","DOI":"10.1021\/pr070112q","article-title":"Enrichment and analysis of nonenzymatically glycated peptides: boronate affinity chromatography coupled with electron-transfer dissociation mass spectrometry","volume":"6","author":"Zhang","year":"2007","journal-title":"J Proteome Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0345","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1021\/pr700763r","article-title":"Proteomic profiling of nonenzymatically glycated proteins in human plasma and erythrocyte membranes","volume":"7","author":"Zhang","year":"2008","journal-title":"J Proteome Res"},{"key":"10.1016\/j.jprot.2011.01.002_bb0350","doi-asserted-by":"crossref","first-page":"9822","DOI":"10.1021\/ac801704j","article-title":"Improved methods for the enrichment and analysis of glycated peptides","volume":"80","author":"Zhang","year":"2008","journal-title":"Anal Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0355","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1002\/rcm.2884","article-title":"Application of electron transfer dissociation mass spectrometry in analyses of non-enzymatically glycated peptides","volume":"21","author":"Zhang","year":"2007","journal-title":"Rapid Commun Mass Spectrom"},{"key":"10.1016\/j.jprot.2011.01.002_bb0360","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1006\/abio.1998.2636","article-title":"Selective detection of lactolated peptides in hydrolysates by liquid chromatography\/electrospray tandem mass spectrometry","volume":"259","author":"Moll\u00e9","year":"1998","journal-title":"Anal Biochem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0365","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1016\/S0963-9969(00)00112-5","article-title":"Thermal denaturation of mixtures of \u03b2-lactalbumin and \u03b1-lactoglobulin: a differential scanning calorimetric study","volume":"33","author":"Boye","year":"2000","journal-title":"Food Res Int"},{"key":"10.1016\/j.jprot.2011.01.002_bb0370","doi-asserted-by":"crossref","first-page":"1915","DOI":"10.2174\/0929867054546618","article-title":"Biochemical properties of peptides encrypted in bovine milk proteins","volume":"12","author":"Meisel","year":"2005","journal-title":"Curr Med Chem"},{"key":"10.1016\/j.jprot.2011.01.002_bb0375","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1007\/s00217-007-0689-6","article-title":"Antihypertensive and antimicrobial bioactive peptides from milk proteins","volume":"227","author":"Haque","year":"2008","journal-title":"Eur Food Res Technol"},{"key":"10.1016\/j.jprot.2011.01.002_bb0380","doi-asserted-by":"crossref","first-page":"1187","DOI":"10.3168\/jds.S0022-0302(00)74983-6","article-title":"Bioactive milk peptides: a prospectus","volume":"83","author":"Clare","year":"2000","journal-title":"J Dairy Sci"},{"key":"10.1016\/j.jprot.2011.01.002_bb0385","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1038\/nbt1096-1269","article-title":"Stability of food allergens to digestion in vitro","volume":"14","author":"Astwood","year":"1996","journal-title":"Nat Biotechnol"},{"issue":"Suppl 67","key":"10.1016\/j.jprot.2011.01.002_bb0390","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1111\/j.1398-9995.2001.00911.x","article-title":"Structure and function of milk allergens","volume":"56","author":"Wal","year":"2001","journal-title":"Allergy"}],"container-title":["Journal of Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391911000194?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391911000194?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,6,7]],"date-time":"2019-06-07T22:05:38Z","timestamp":1559945138000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874391911000194"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,10]]},"references-count":78,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2011,10]]}},"alternative-id":["S1874391911000194"],"URL":"https:\/\/doi.org\/10.1016\/j.jprot.2011.01.002","relation":{},"ISSN":["1874-3919"],"issn-type":[{"value":"1874-3919","type":"print"}],"subject":[],"published":{"date-parts":[[2011,10]]}}}