{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T19:16:46Z","timestamp":1784747806167,"version":"3.55.0"},"reference-count":55,"publisher":"Springer Science and Business Media LLC","issue":"11","license":[{"start":{"date-parts":[[2016,1,22]],"date-time":"2016-01-22T00:00:00Z","timestamp":1453420800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/100007921","name":"University of Pittsburgh","doi-asserted-by":"publisher","award":["Start Up Funds"],"award-info":[{"award-number":["Start Up Funds"]}],"id":[{"id":"10.13039\/100007921","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Anal Bioanal Chem"],"published-print":{"date-parts":[[2016,4]]},"DOI":"10.1007\/s00216-016-9307-4","type":"journal-article","created":{"date-parts":[[2016,1,22]],"date-time":"2016-01-22T00:43:05Z","timestamp":1453423385000},"page":"2993-3004","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["A simple isotopic labeling method to study cysteine oxidation in Alzheimer\u2019s disease: oxidized cysteine-selective dimethylation (OxcysDML)"],"prefix":"10.1007","volume":"408","author":[{"given":"Liqing","family":"Gu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ren\u00e3 A. S.","family":"Robinson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2016,1,22]]},"reference":[{"issue":"11","key":"9307_CR1","doi-asserted-by":"crossref","first-page":"1638","DOI":"10.1039\/c0ay00375a","volume":"2","author":"U Tornvall","year":"2010","unstructured":"Tornvall U. Pinpointing oxidative modifications in proteins-recent advances in analytical methods. Anal Methods-UK. 2010;2(11):1638\u201350.","journal-title":"Anal Methods-UK"},{"issue":"5","key":"9307_CR2","doi-asserted-by":"crossref","first-page":"494","DOI":"10.3109\/10715762.2015.1009053","volume":"49","author":"S Boronat","year":"2015","unstructured":"Boronat S, Garcia-Santamarina S, Hidalgo E. Gel-free proteomic methodologies to study reversible cysteine oxidation and irreversible protein carbonyl formation. Free Radic Res. 2015;49(5):494\u2013510.","journal-title":"Free Radic Res"},{"issue":"2","key":"9307_CR3","first-page":"378","volume":"5","author":"I Verrastro","year":"2015","unstructured":"Verrastro I, Pasha S, Jensen KT, Pitt AR, Spickett CM. Mass spectrometry-based methods for identifying oxidized proteins in disease: advances and challenges. Biogeosciences. 2015;5(2):378\u2013411.","journal-title":"Biogeosciences"},{"issue":"12","key":"9307_CR4","doi-asserted-by":"crossref","first-page":"2315","DOI":"10.1016\/j.bbapap.2014.09.024","volume":"1844","author":"SM Couvertier","year":"2014","unstructured":"Couvertier SM, Zhou Y, Weerapana E. Chemical-proteomic strategies to investigate cysteine posttranslational modifications. Bba Proteins Proteom. 2014;1844(12):2315\u201330.","journal-title":"Bba Proteins Proteom"},{"issue":"6","key":"9307_CR5","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1089\/ars.2010.3376","volume":"14","author":"C Klomsiri","year":"2011","unstructured":"Klomsiri C, Karplus PA, Poole LB. Cysteine-based redox switches in enzymes. Antioxid Redox Signal. 2011;14(6):1065\u201377.","journal-title":"Antioxid Redox Signal"},{"issue":"16","key":"9307_CR6","doi-asserted-by":"crossref","first-page":"2560","DOI":"10.1021\/bi401700f","volume":"53","author":"S Garcia-Santamarina","year":"2014","unstructured":"Garcia-Santamarina S, Boronat S, Hidalgo E. Reversible cysteine oxidation in hydrogen peroxide sensing and signal transduction. Biochemistry. 2014;53(16):2560\u201380.","journal-title":"Biochemistry"},{"key":"9307_CR7","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.freeradbiomed.2014.09.016","volume":"80","author":"NOD Baez","year":"2015","unstructured":"Baez NOD, Reisz JA, Furdui CM. Mass spectrometry in studies of protein thiol chemistry and signaling: opportunities and caveats. Free Radical Bio Med. 2015;80:191\u2013211.","journal-title":"Free Radical Bio Med"},{"issue":"6961","key":"9307_CR8","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1038\/nature02075","volume":"425","author":"B Biteau","year":"2003","unstructured":"Biteau B, Labarre J, Toledano MB. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature. 2003;425(6961):980\u20134.","journal-title":"Nature"},{"issue":"49","key":"9307_CR9","doi-asserted-by":"crossref","first-page":"50994","DOI":"10.1074\/jbc.M409482200","volume":"279","author":"TS Chang","year":"2004","unstructured":"Chang TS, Jeong W, Woo HA, Lee SM, Park S, Rhee SG. Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. J Biol Chem. 2004;279(49):50994\u20131001.","journal-title":"J Biol Chem"},{"issue":"9533","key":"9307_CR10","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/S0140-6736(06)69113-7","volume":"368","author":"K Blennow","year":"2006","unstructured":"Blennow K, de Leon MJ, Zetterberg H. Alzheimer\u2019s disease. Lancet. 2006;368(9533):387\u2013403.","journal-title":"Lancet"},{"key":"9307_CR11","doi-asserted-by":"crossref","first-page":"985845","DOI":"10.1155\/2015\/985845","volume":"2015","author":"S Rosales-Corral","year":"2015","unstructured":"Rosales-Corral S, Tan DX, Manchester L, Reiter RJ. Diabetes and Alzheimer disease, two overlapping pathologies with the same background: oxidative stress. Oxidative Med Cell Longev. 2015;2015:985845.","journal-title":"Oxidative Med Cell Longev"},{"issue":"7","key":"9307_CR12","doi-asserted-by":"crossref","first-page":"1506","DOI":"10.1002\/jnr.21275","volume":"85","author":"SF Newman","year":"2007","unstructured":"Newman SF, Sultana R, Perluigi M, Coccia R, Cai J, Pierce WM, et al. An increase in S-glutathionylated proteins in the Alzheimer\u2019s disease inferior parietal lobule, a proteomics approach. J Neurosci Res. 2007;85(7):1506\u201314.","journal-title":"J Neurosci Res"},{"key":"9307_CR13","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.neuroscience.2013.10.026","volume":"256","author":"S Zahid","year":"2014","unstructured":"Zahid S, Khan R, Oellerich M, Ahmed N, Asif AR. Differential S-nitrosylation of proteins in Alzheimer\u2019s disease. Neuroscience. 2014;256:126\u201336.","journal-title":"Neuroscience"},{"key":"9307_CR14","doi-asserted-by":"crossref","first-page":"2288","DOI":"10.1074\/mcp.M113.036079","volume":"13","author":"M Zareba-Koziol","year":"2014","unstructured":"Zareba-Koziol M, Szwajda A, Dadlez M, Wyslouch-Cieszynska A, Lalowski M. Global analysis of S-nitrosylation sites in the wild type and APP transgenic mouse brain\u2014clues for synaptic pathology. Mol Cell Proteomics MCP. 2014;13:2288\u2013305.","journal-title":"Mol Cell Proteomics MCP"},{"issue":"4\u20135","key":"9307_CR15","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/j.brainresbull.2009.04.018","volume":"80","author":"IM Riederer","year":"2009","unstructured":"Riederer IM, Schiffrin M, Kovari E, Bouras C, Riederer BM. Ubiquitination and cysteine nitrosylation during aging and Alzheimer\u2019s disease. Brain Res Bull. 2009;80(4\u20135):233\u201341.","journal-title":"Brain Res Bull"},{"key":"9307_CR16","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.nbd.2014.12.027","volume":"76","author":"CH Chen","year":"2015","unstructured":"Chen CH, Li W, Sultana R, You MH, Kondo A, Shahpasand K, et al. Pin1 cysteine-113 oxidation inhibits its catalytic activity and cellular function in Alzheimer\u2019s disease. Neurobiol Dis. 2015;76:13\u201323.","journal-title":"Neurobiol Dis"},{"issue":"4","key":"9307_CR17","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1002\/mas.21374","volume":"33","author":"DA Butterfield","year":"2013","unstructured":"Butterfield DA, Gu L, Domenico FD, Robinson RA. Mass spectrometry and redox proteomics: applications in disease. Mass Spectrom Rev. 2013;33(4):277\u2013301.","journal-title":"Mass Spectrom Rev"},{"issue":"5","key":"9307_CR18","doi-asserted-by":"crossref","first-page":"2026","DOI":"10.1021\/acs.jproteome.5b00133","volume":"14","author":"R Li","year":"2015","unstructured":"Li R, Huang JQ, Kast J. Identification of total reversible cysteine oxidation in an atherosclerosis model using a modified biotin switch assay. J Proteome Res. 2015;14(5):2026\u201335.","journal-title":"J Proteome Res"},{"issue":"6","key":"9307_CR19","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1002\/pmic.201300307","volume":"14","author":"P Liu","year":"2014","unstructured":"Liu P, Zhang H, Wang H, Xia Y. Identification of redox-sensitive cysteines in the Arabidopsis proteome using OxiTRAQ, a quantitative redox proteomics method. Proteomics. 2014;14(6):750\u201362.","journal-title":"Proteomics"},{"issue":"10","key":"9307_CR20","doi-asserted-by":"crossref","first-page":"994","DOI":"10.1038\/13690","volume":"17","author":"SP Gygi","year":"1999","unstructured":"Gygi SP, Rist B, Gerber SA, Turecek F, Gelb MH, Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol. 1999;17(10):994\u20139.","journal-title":"Nat Biotechnol"},{"issue":"11","key":"9307_CR21","doi-asserted-by":"crossref","first-page":"2476","DOI":"10.1016\/j.jprot.2011.05.030","volume":"74","author":"S Garcia-Santamarina","year":"2011","unstructured":"Garcia-Santamarina S, Boronat S, Espadas G, Ayte J, Molina H, Hidalgo E. The oxidized thiol proteome in fission yeast\u2014optimization of an ICAT-based method to identify H2O2-oxidized proteins. J Proteome. 2011;74(11):2476\u201386.","journal-title":"J Proteome"},{"issue":"5","key":"9307_CR22","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1038\/nprot.2014.065","volume":"9","author":"S Garcia-Santamarina","year":"2014","unstructured":"Garcia-Santamarina S, Boronat S, Domenech A, Ayte J, Molina H, Hidalgo E. Monitoring in vivo reversible cysteine oxidation in proteins using ICAT and mass spectrometry. Nat Protoc. 2014;9(5):1131\u201345.","journal-title":"Nat Protoc"},{"issue":"1","key":"9307_CR23","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1038\/nprot.2013.161","volume":"9","author":"J Guo","year":"2014","unstructured":"Guo J, Gaffrey MJ, Su D, Liu T, Camp 2nd DG, Smith RD, et al. Resin-assisted enrichment of thiols as a general strategy for proteomic profiling of cysteine-based reversible modifications. Nat Protoc. 2014;9(1):64\u201375.","journal-title":"Nat Protoc"},{"issue":"6","key":"9307_CR24","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1038\/nbt.1545","volume":"27","author":"MT Forrester","year":"2009","unstructured":"Forrester MT, Thompson JW, Foster MW, Nogueira L, Moseley MA, Stamler JS. Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture. Nat Biotechnol. 2009;27(6):557\u20139.","journal-title":"Nat Biotechnol"},{"issue":"2","key":"9307_CR25","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1194\/jlr.D011106","volume":"52","author":"MT Forrester","year":"2011","unstructured":"Forrester MT, Hess DT, Thompson JW, Hultman R, Moseley MA, Stamler JS, et al. Site-specific analysis of protein S-acylation by resin-assisted capture. J Lipid Res. 2011;52(2):393\u20138.","journal-title":"J Lipid Res"},{"issue":"9","key":"9307_CR26","doi-asserted-by":"crossref","first-page":"1365","DOI":"10.1089\/ars.2013.5326","volume":"20","author":"KT Pan","year":"2014","unstructured":"Pan KT, Chen YY, Pu TH, Chao YS, Yang CY, Bomgarden RD, et al. Mass spectrometry-based quantitative proteomics for dissecting multiplexed redox cysteine modifications in nitric oxide-protected cardiomyocyte under hypoxia. Antioxid Redox Signal. 2014;20(9):1365\u201381.","journal-title":"Antioxid Redox Signal"},{"issue":"7","key":"9307_CR27","doi-asserted-by":"crossref","first-page":"2817","DOI":"10.1021\/ac902778d","volume":"82","author":"F Xiang","year":"2010","unstructured":"Xiang F, Ye H, Chen R, Fu Q, Li L. N, N-dimethyl leucines as novel isobaric tandem mass tags for quantitative proteomics and peptidomics. Anal Chem. 2010;82(7):2817\u201325.","journal-title":"Anal Chem"},{"issue":"4","key":"9307_CR28","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1007\/s13361-014-1059-9","volume":"26","author":"L Gu","year":"2015","unstructured":"Gu L, Evans AR, Robinson RA. Sample multiplexing with cysteine-selective approaches: cysDML and cPILOT. J Am Soc Mass Spectrom. 2015;26(4):615\u201330.","journal-title":"J Am Soc Mass Spectrom"},{"issue":"7","key":"9307_CR29","doi-asserted-by":"crossref","first-page":"3200","DOI":"10.1021\/pr401179v","volume":"13","author":"Z Qu","year":"2014","unstructured":"Qu Z, Meng F, Bomgarden RD, Viner RI, Li J, Rogers JC, et al. Proteomic quantification and site-mapping of S-nitrosylated proteins using isobaric iodoTMT reagents. J Proteome Res. 2014;13(7):3200\u201311.","journal-title":"J Proteome Res"},{"issue":"4","key":"9307_CR30","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1007\/s00216-012-6203-4","volume":"404","author":"M Bantscheff","year":"2012","unstructured":"Bantscheff M, Lemeer S, Savitski MM, Kuster B. Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present. Anal Bioanal Chem. 2012;404(4):939\u201365.","journal-title":"Anal Bioanal Chem"},{"issue":"8","key":"9307_CR31","doi-asserted-by":"crossref","first-page":"M111 009654","DOI":"10.1074\/mcp.M111.009654","volume":"10","author":"R Wu","year":"2011","unstructured":"Wu R, Dephoure N, Haas W, Huttlin EL, Zhai B, Sowa ME, et al. Correct interpretation of comprehensive phosphorylation dynamics requires normalization by protein expression changes. Mol Cell Proteomics MCP. 2011;10(8):M111 009654.","journal-title":"Mol Cell Proteomics MCP"},{"key":"9307_CR32","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.freeradbiomed.2013.01.021","volume":"58","author":"V Kumar","year":"2013","unstructured":"Kumar V, Kleffmann T, Hampton MB, Cannell MB, Winterbourn CC. Redox proteomics of thiol proteins in mouse heart during ischemia\/reperfusion using ICAT reagents and mass spectrometry. Free Radical Bio Med. 2013;58:109\u201317.","journal-title":"Free Radical Bio Med"},{"issue":"10","key":"9307_CR33","doi-asserted-by":"crossref","first-page":"5081","DOI":"10.1021\/pr300519c","volume":"11","author":"L Dayon","year":"2012","unstructured":"Dayon L, Sonderegger B, Kussmann M. Combination of gas-phase fractionation and MS(3) acquisition modes for relative protein quantification with isobaric tagging. J Proteome Res. 2012;11(10):5081\u20139.","journal-title":"J Proteome Res"},{"issue":"14","key":"9307_CR34","doi-asserted-by":"crossref","first-page":"1708","DOI":"10.1039\/c3cc47998f","volume":"50","author":"Y Wu","year":"2014","unstructured":"Wu Y, Wang F, Liu Z, Qin H, Song C, Huang J, et al. Five-plex isotope dimethyl labeling for quantitative proteomics. Chem Commun. 2014;50(14):1708\u201310.","journal-title":"Chem Commun"},{"key":"9307_CR35","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/j.jprot.2014.10.015","volume":"113","author":"K Wojdyla","year":"2015","unstructured":"Wojdyla K, Williamson J, Roepstorff P, Rogowska-Wrzesinska A. The SNO\/SOH TMT strategy for combinatorial analysis of reversible cysteine oxidations. J Proteome. 2015;113:415\u201334.","journal-title":"J Proteome"},{"key":"9307_CR36","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.freeradbiomed.2012.12.010","volume":"57","author":"D Su","year":"2013","unstructured":"Su D, Shukla AK, Chen B, Kim JS, Nakayasu E, Qu Y, et al. Quantitative site-specific reactivity profiling of S-nitrosylation in mouse skeletal muscle using cysteinyl peptide enrichment coupled with mass spectrometry. Free Radic Biol Med. 2013;57:68\u201378.","journal-title":"Free Radic Biol Med"},{"issue":"9\u201310","key":"9307_CR37","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1002\/prca.201400149","volume":"9","author":"AR Evans","year":"2015","unstructured":"Evans AR, Gu L, Guerrero Jr R, Robinson RA. Global cPILOT analysis of the APP\/PS-1 mouse liver proteome. Proteomics Clin Appl. 2015;9(9\u201310):872\u201384.","journal-title":"Proteomics Clin Appl"},{"issue":"9","key":"9307_CR38","doi-asserted-by":"crossref","first-page":"4184","DOI":"10.1021\/pr500525e","volume":"13","author":"D Chen","year":"2014","unstructured":"Chen D, Shah A, Nguyen H, Loo D, Inder KL, Hill MM. Online quantitative proteomics p-value calculator for permutation-based statistical testing of peptide ratios. J Proteome Res. 2014;13(9):4184\u201391.","journal-title":"J Proteome Res"},{"issue":"9","key":"9307_CR39","doi-asserted-by":"crossref","first-page":"4164","DOI":"10.1021\/pr500630a","volume":"13","author":"HT Lau","year":"2014","unstructured":"Lau HT, Suh HW, Golkowski M, Ong SE. Comparing SILAC- and stable isotope dimethyl-labeling approaches for quantitative proteomics. J Proteome Res. 2014;13(9):4164\u201374.","journal-title":"J Proteome Res"},{"issue":"8","key":"9307_CR40","doi-asserted-by":"crossref","first-page":"2963","DOI":"10.1021\/pr0605668","volume":"6","author":"R Shi","year":"2007","unstructured":"Shi R, Kumar C, Zougman A, Zhang Y, Podtelejnikov A, Cox J, et al. Analysis of the mouse liver proteome using advanced mass spectrometry. J Proteome Res. 2007;6(8):2963\u201372.","journal-title":"J Proteome Res"},{"issue":"1","key":"9307_CR41","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1093\/toxsci\/kfu018","volume":"139","author":"YM Go","year":"2014","unstructured":"Go YM, Roede JR, Orr M, Liang Y, Jones DP. Integrated redox proteomics and metabolomics of mitochondria to identify mechanisms of cd toxicity. Toxicol Sci Off J Soc Toxicol. 2014;139(1):59\u201373.","journal-title":"Toxicol Sci Off J Soc Toxicol"},{"issue":"Database issue","key":"9307_CR42","doi-asserted-by":"crossref","first-page":"D154","DOI":"10.1093\/nar\/gki070","volume":"33","author":"A Bairoch","year":"2005","unstructured":"Bairoch A, Apweiler R, Wu CH, Barker WC, Boeckmann B, Ferro S, et al. The Universal Protein Resource (UniProt). Nucleic Acids Res. 2005;33(Database issue):D154\u20139.","journal-title":"Nucleic Acids Res"},{"issue":"2","key":"9307_CR43","first-page":"419","volume":"4","author":"NJ Pace","year":"2014","unstructured":"Pace NJ, Weerapana E. Zinc-binding cysteines: diverse functions and structural motifs. Biogeosciences. 2014;4(2):419\u201334.","journal-title":"Biogeosciences"},{"issue":"9","key":"9307_CR44","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.1016\/j.bbadis.2014.04.012","volume":"1842","author":"JK Morris","year":"2014","unstructured":"Morris JK, Honea RA, Vidoni ED, Swerdlow RH, Burns JM. Is Alzheimer\u2019s disease a systemic disease? Bba Mol Basis Dis. 2014;1842(9):1340\u20139.","journal-title":"Bba Mol Basis Dis"},{"issue":"4","key":"9307_CR45","doi-asserted-by":"crossref","first-page":"661","DOI":"10.3233\/JAD-130665","volume":"37","author":"RA Robinson","year":"2013","unstructured":"Robinson RA, Cao Z, Williams C. Oxidative stress in CD90+ T-cells of AbetaPP\/PS-1 transgenic mice. J Alzheimer\u2019s Dis JAD. 2013;37(4):661\u20136.","journal-title":"J Alzheimer\u2019s Dis JAD"},{"issue":"8","key":"9307_CR46","doi-asserted-by":"crossref","first-page":"1248","DOI":"10.1016\/j.bbadis.2013.09.015","volume":"1842","author":"AM Swomley","year":"2014","unstructured":"Swomley AM, Forster S, Keeney JT, Triplett J, Zhang Z, Sultana R, et al. Abeta, oxidative stress in Alzheimer disease: evidence based on proteomics studies. Bba Mol Basis Dis. 2014;1842(8):1248\u201357.","journal-title":"Bba Mol Basis Dis"},{"issue":"11","key":"9307_CR47","doi-asserted-by":"crossref","first-page":"1610","DOI":"10.1089\/ars.2011.4109","volume":"17","author":"DA Butterfield","year":"2012","unstructured":"Butterfield DA, Perluigi M, Reed T, Muharib T, Hughes CP, Robinson RA, et al. Redox proteomics in selected neurodegenerative disorders: from its infancy to future applications. Antioxid Redox Signal. 2012;17(11):1610\u201355.","journal-title":"Antioxid Redox Signal"},{"issue":"4","key":"9307_CR48","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1007\/s11064-009-9924-9","volume":"34","author":"F Domenico Di","year":"2009","unstructured":"Di Domenico F, Cenini G, Sultana R, Perluigi M, Uberti D, Memo M, et al. Glutathionylation of the pro-apoptotic protein p53 in Alzheimer\u2019s disease brain: implications for AD pathogenesis. Neurochem Res. 2009;34(4):727\u201333.","journal-title":"Neurochem Res"},{"issue":"1","key":"9307_CR49","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.nbd.2007.06.007","volume":"28","author":"CR Hooijmans","year":"2007","unstructured":"Hooijmans CR, Rutters F, Dederen PJ, Gambarota G, Veltien A, van Groen T, et al. Changes in cerebral blood volume and amyloid pathology in aged Alzheimer APP\/PS1 mice on a docosahexaenoic acid (DHA) diet or cholesterol enriched typical western diet (TWD). Neurobiol Dis. 2007;28(1):16\u201329.","journal-title":"Neurobiol Dis"},{"issue":"9","key":"9307_CR50","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1038\/nm1635","volume":"13","author":"A Sagare","year":"2007","unstructured":"Sagare A, Deane R, Bell RD, Johnson B, Hamm K, Pendu R, et al. Clearance of amyloid-beta by circulating lipoprotein receptors. Nat Med. 2007;13(9):1029\u201331.","journal-title":"Nat Med"},{"issue":"10","key":"9307_CR51","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1016\/j.freeradbiomed.2008.08.012","volume":"45","author":"HM Abdul","year":"2008","unstructured":"Abdul HM, Sultana R, Clair DKS, Markesbery WR, Butterfield DA. Oxidative damage in brain from human mutant APP\/PS-1 double knock-in mice as a function of age. Free Radical Bio Med. 2008;45(10):1420\u20135.","journal-title":"Free Radical Bio Med"},{"issue":"12","key":"9307_CR52","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1002\/(SICI)1099-1166(1998120)13:12<840::AID-GPS877>3.0.CO;2-R","volume":"13","author":"AJ Sinclair","year":"1998","unstructured":"Sinclair AJ, Bayer AJ, Johnston J, Warner C, Maxwell SRJ. Altered plasma antioxidant status in subjects with Alzheimer\u2019s disease and vascular dementia. Int J Geriatr Psych. 1998;13(12):840\u20135.","journal-title":"Int J Geriatr Psych"},{"issue":"1","key":"9307_CR53","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0925-4439(00)00040-5","volume":"1502","author":"MA Smith","year":"2000","unstructured":"Smith MA, Rottkamp CA, Nunomura A, Raina AK, Perry G. Oxidative stress in Alzheimer\u2019s disease. Biochim Biophys Acta. 2000;1502(1):139\u201344.","journal-title":"Biochim Biophys Acta"},{"issue":"25","key":"9307_CR54","doi-asserted-by":"crossref","first-page":"8082","DOI":"10.3748\/wjg.v20.i25.8082","volume":"20","author":"H Cichoz-Lach","year":"2014","unstructured":"Cichoz-Lach H, Michalak A. Oxidative stress as a crucial factor in liver diseases. World J Gastroenterol. 2014;20(25):8082\u201391.","journal-title":"World J Gastroenterol"},{"issue":"9","key":"9307_CR55","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1016\/j.bbadis.2011.12.001","volume":"1822","author":"M Fransen","year":"2012","unstructured":"Fransen M, Nordgren M, Wang B, Apanasets O. Role of peroxisomes in ROS\/RNS-metabolism: implications for human disease. Biochim Biophys Acta. 2012;1822(9):1363\u201373.","journal-title":"Biochim Biophys Acta"}],"container-title":["Analytical and Bioanalytical Chemistry"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00216-016-9307-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s00216-016-9307-4\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00216-016-9307-4","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,9,3]],"date-time":"2019-09-03T18:34:25Z","timestamp":1567535665000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s00216-016-9307-4"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,1,22]]},"references-count":55,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2016,4]]}},"alternative-id":["9307"],"URL":"https:\/\/doi.org\/10.1007\/s00216-016-9307-4","relation":{},"ISSN":["1618-2642","1618-2650"],"issn-type":[{"value":"1618-2642","type":"print"},{"value":"1618-2650","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,1,22]]}}}