{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,22]],"date-time":"2026-08-22T07:17:21Z","timestamp":1787383041844,"version":"build-2736575974"},"reference-count":48,"publisher":"Oxford University Press (OUP)","issue":"7","license":[{"start":{"date-parts":[[2020,7,1]],"date-time":"2020-07-01T00:00:00Z","timestamp":1593561600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"},{"start":{"date-parts":[[2021,6,30]],"date-time":"2021-06-30T00:00:00Z","timestamp":1625011200000},"content-version":"am","delay-in-days":364,"URL":"http:\/\/rsc.li\/journals-terms-of-use"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["DK110665"],"award-info":[{"award-number":["DK110665"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["NS105888"],"award-info":[{"award-number":["NS105888"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["DK110665"],"award-info":[{"award-number":["DK110665"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["NS105888"],"award-info":[{"award-number":["NS105888"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["rsc.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2020,7,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Plasma proteins are covalently modified in vivo by the high-glucose conditions in the bloodstreams of people with diabetes, resulting in changes to both structure and function. Human Serum Albumin (HSA) functions as a carrier-protein in the bloodstream, binding various ligands and tightly regulating their bioavailability. HSA is known to react with glucose via the Maillard reaction, causing adverse effects on its ability to bind and deliver certain ligands, such as metals. Here, the binding between in vivo glycated HSA and zinc (Zn2+) was determined using a novel centrifugal ultrafiltration method that was developed using a 3D-printed device. This method is rapid (90 minutes), capable of high-throughput measurements (24 samples), low-cost (&amp;lt;$1.00 USD per device) and requires lower sample volumes (200 \u03bcL) compared to other binding techniques. This device was used to determine an equilibrium dissociation constant between Zn2+ and a commercially obtained normal HSA (nHSA) with a glycation level of 11.5% (Kd = 2.1 (\u00b10.5) \u00d7 10\u22127 M). A glycated fraction of the nHSA sample was enriched (gHSA, 65.5%) and isolated using boronate-affinity chromatography, and found to have a 2.3-fold decrease in Zn2+ binding-affinity (Kd = 4.8 (\u00b10.8) \u00d7 10\u22127 M) when compared to the nHSA sample. The level of glycation of HSA in control plasma (13.0% \u00b1 0.8, n = 3 donors) and plasma from people with diabetes (26.9% \u00b1 6.6, n = 5 donors) was assessed using mass spectrometry. Furthermore, HSA was isolated from plasma obtained in-house from a person with type 1 diabetes and found to have a glycation level of 24.1% and Kd = 3.3 (\u00b1 0.5) \u00d7 10\u22127 M for Zn2+, revealing a 1.5-fold decrease in binding affinity compared to nHSA. These findings suggest that increased levels of glycated HSA result in reduced binding to Zn2+, which may have implications in complications associated with diabetes.<\/jats:p>","DOI":"10.1039\/d0mt00123f","type":"journal-article","created":{"date-parts":[[2020,6,30]],"date-time":"2020-06-30T18:26:45Z","timestamp":1593541605000},"page":"1036-1043","update-policy":"https:\/\/doi.org\/10.1039\/rsc_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["A novel 3D-printed centrifugal ultrafiltration method reveals <i>in vivo<\/i> glycation of human serum albumin decreases its binding affinity for zinc"],"prefix":"10.1093","volume":"12","author":[{"given":"Monica J","family":"Jacobs","sequence":"first","affiliation":[{"name":"Institute for Quantitative Health Science & Engineering, Michigan State University, East Lansing, MI, 48824, USA. Fax: +1 517 353 1116; Tel: +1 517 353 1116"},{"name":"Comparative Medicine and Integrative Biology, Michigan State University, East Lansing, MI, 48824, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cody W","family":"Pinger","sequence":"additional","affiliation":[{"name":"Institute for Quantitative Health Science & Engineering, Michigan State University, East Lansing, MI, 48824, USA. Fax: +1 517 353 1116; Tel: +1 517 353 1116"},{"name":"Department of Biomedical Engineering, Michigan State University, East Lansing, MI, 48824, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andre D","family":"Castiaux","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Saint Louis University, East Lansing, MI, 48824, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Konnor J","family":"Maloney","sequence":"additional","affiliation":[{"name":"Department of Biomedical Engineering, Michigan State University, East Lansing, MI, 48824, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4754-6671","authenticated-orcid":false,"given":"Dana M","family":"Spence","sequence":"additional","affiliation":[{"name":"Institute for Quantitative Health Science & Engineering, Michigan State University, East Lansing, MI, 48824, USA. Fax: +1 517 353 1116; Tel: +1 517 353 1116"},{"name":"Department of Biomedical Engineering, Michigan State University, East Lansing, MI, 48824, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2020,7,6]]},"reference":[{"key":"2021121004461044100_cit1","volume-title":"National Diabetes Statistics Report 2020"},{"key":"2021121004461044100_cit2","volume-title":"What is Diabetes"},{"key":"2021121004461044100_cit3","volume-title":"Types of Diabetes Mellitus"},{"key":"2021121004461044100_cit4","article-title":"Diabetes micro-vascular complications","volume-title":"Prim. Care Rep.","author":"Dugan","year":"2017"},{"issue":"1","key":"2021121004461044100_cit5","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.diabres.2004.09.004","article-title":"Advanced glycation endproducts--role in pathology of diabetic complications","volume":"67","author":"Ahmed","year":"2005","journal-title":"Diabetes Res. Clin. Pract."},{"issue":"3","key":"2021121004461044100_cit6","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1681\/ASN.2006070772","article-title":"Glycated Albumin Is a Better Glycemic Indicator than Glycated Hemoglobin Values in Hemodialysis Patients with Diabetes: Effect of Anemia and Erythropoietin Injection","volume":"18","author":"Inaba","year":"2007","journal-title":"J. Am. Soc. Nephrol."},{"key":"2021121004461044100_cit7","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.cca.2013.07.013","article-title":"Review: Glycation of human serum albumin","volume":"425","author":"Anguizola","year":"2013","journal-title":"Clin. Chim. Acta"},{"issue":"14","key":"2021121004461044100_cit8","doi-asserted-by":"crossref","first-page":"1862","DOI":"10.2174\/1381612821666150302115025","article-title":"Review: Modifications of Human Serum Albumin and Their Binding Effect","volume":"21","author":"Lee","year":"2015","journal-title":"Curr. Pharm. Des."},{"key":"2021121004461044100_cit9","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.freeradbiomed.2019.06.023","article-title":"Pro-oxidant and pro-inflammatory effects of glycated albumin on cardiomyocytes","volume":"144","author":"Martinez Fernandez","year":"2019","journal-title":"Free Radicals Biol. Med."},{"key":"2021121004461044100_cit10","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1186\/2251-6581-13-49","article-title":"Glycated albumin: an overview of the In Vitro models of an In Vivo potential disease marker","volume":"13","author":"Arasteh","year":"2014","journal-title":"J. Diabetes Metab. Disord."},{"issue":"3","key":"2021121004461044100_cit11","doi-asserted-by":"crossref","first-page":"239","DOI":"10.2174\/2213235X1130100005","article-title":"Effects of Fatty Acids and Glycation on Drug Interactions with Human Serum Albumin","volume":"1","author":"Anguizola","year":"2013","journal-title":"Curr. Metabolomics"},{"key":"2021121004461044100_cit12","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/j.saa.2015.01.120","article-title":"Effects of non-enzymatic glycation in human serum albumin. Spectroscopic analysis","volume":"152","author":"Szkudlarek","year":"2016","journal-title":"Spectrochim. Acta, Part A"},{"issue":"2","key":"2021121004461044100_cit13","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.diabet.2011.11.002","article-title":"Structural modifications of human albumin in diabetes","volume":"38","author":"Guerin-Dubourg","year":"2012","journal-title":"Diabetes Metab."},{"issue":"19","key":"2021121004461044100_cit14","doi-asserted-by":"crossref","first-page":"3051","DOI":"10.1021\/acs.biochem.5b00273","article-title":"Glycation Alters Ligand Binding, Enzymatic, and Pharmacological Properties of Human Albumin","volume":"54","author":"Baraka-Vidot","year":"2015","journal-title":"Biochemistry"},{"issue":"1","key":"2021121004461044100_cit15","doi-asserted-by":"crossref","first-page":"40","DOI":"10.4103\/0974-7753.114714","article-title":"Zinc deficiency associated with hypothyroidism: An overlooked cause of severe alopecia","volume":"5","author":"Betsy","year":"2013","journal-title":"Int. J. Trichology"},{"issue":"2","key":"2021121004461044100_cit16","doi-asserted-by":"crossref","first-page":"447S","DOI":"10.1093\/ajcn\/68.2.447S","article-title":"Zinc and immune function: the biological basis of altered resistance to infection","volume":"68","author":"Shankar","year":"1998","journal-title":"Am. J. Clin. Nutr."},{"issue":"4","key":"2021121004461044100_cit17","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.3390\/ijerph7041342","article-title":"The Essential Toxin: Impact of Zinc on Human Health","volume":"7","author":"Plum","year":"2010","journal-title":"Int. J. Environ. Res. Public Health"},{"issue":"1","key":"2021121004461044100_cit18","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1039\/B817203J","article-title":"A perspective on the role of metals in diabetes: past findings and possible future directions","volume":"1","author":"Meyer","year":"2009","journal-title":"Metallomics"},{"issue":"11","key":"2021121004461044100_cit19","doi-asserted-by":"crossref","first-page":"1805","DOI":"10.1039\/C9MT00177H","article-title":"A metalloproteomic analysis of interactions between plasma proteins and zinc: elevated fatty acid levels affect zinc distribution","volume":"11","author":"Coverdale","year":"2019","journal-title":"Metallomics"},{"issue":"11","key":"2021121004461044100_cit20","doi-asserted-by":"crossref","first-page":"6635","DOI":"10.1039\/C6SC02267G","article-title":"Circulatory zinc transport is controlled by distinct interdomain sites on mammalian albumins","volume":"7","author":"Handing","year":"2016","journal-title":"Chem. Sci."},{"issue":"5","key":"2021121004461044100_cit21","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1039\/c4ib00243a","article-title":"C-peptide and zinc delivery to erythrocytes requires the presence of albumin: implications in diabetes explored with a 3D-printed fluidic device","volume":"7","author":"Liu","year":"2015","journal-title":"Integr. Biol."},{"issue":"3","key":"2021121004461044100_cit22","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1385\/BTER:81:3:215","article-title":"Zinc and diabetes mellitus","volume":"81","author":"Salgueiro","year":"2001","journal-title":"Biol. Trace Elem. Res."},{"issue":"3","key":"2021121004461044100_cit23","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1007\/s00775-018-1554-8","article-title":"Effect of glycation on human serum albumin-zinc interaction: a biophysical study","volume":"23","author":"Iqbal","year":"2018","journal-title":"J. Biol. Inorg. Chem."},{"issue":"17\u201318","key":"2021121004461044100_cit24","doi-asserted-by":"crossref","first-page":"1606","DOI":"10.1016\/j.cca.2011.05.012","article-title":"Quantitative analysis of glycation patterns in human serum albumin using 16O\/18O-labeling and MALDI-TOF MS","volume":"412","author":"Barnaby","year":"2011","journal-title":"Clin. Chim. Acta"},{"issue":"6","key":"2021121004461044100_cit25","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1002\/jps.2600740625","article-title":"Comparison of Equilibrium Dialysis, Ultrafiltration, and Gel Permeation Chromatography for the Determination of Free Fractions of Phenobarbital and Phenytoin","volume":"74","author":"Melten","year":"1985","journal-title":"J. Pharm. Sci."},{"issue":"9","key":"2021121004461044100_cit26","doi-asserted-by":"crossref","first-page":"4453","DOI":"10.1021\/ac303734c","article-title":"Development of Affinity Microcolumns for Drug\u2013Protein Binding Studies in Personalized Medicine: Interactions of Sulfonylurea Drugs with in vivo Glycated Human Serum Albumin","volume":"85","author":"Anguizola","year":"2013","journal-title":"Anal. Chem."},{"issue":"29","key":"2021121004461044100_cit27","doi-asserted-by":"crossref","first-page":"7565","DOI":"10.1007\/s00216-018-1373-3","article-title":"Ultrafiltration binding analyses of glycated albumin with a 3D-printed syringe attachment","volume":"410","author":"Castiaux","year":"2018","journal-title":"Anal. Bioanal. Chem."},{"issue":"10","key":"2021121004461044100_cit28","doi-asserted-by":"crossref","first-page":"6910","DOI":"10.1021\/acs.analchem.9b01302","article-title":"PolyJet 3D-Printed Enclosed Microfluidic Channels without Photocurable Supports","volume":"91","author":"Castiaux","year":"2019","journal-title":"Anal. Chem."},{"issue":"9","key":"2021121004461044100_cit29","doi-asserted-by":"crossref","first-page":"3274","DOI":"10.1039\/D0AN00240B","article-title":"Direct embedding and versatile placement of electrodes in 3D printed microfluidic-devices","volume":"145","author":"Castiaux","year":"2020","journal-title":"Analyst"},{"issue":"14","key":"2021121004461044100_cit30","doi-asserted-by":"crossref","first-page":"7302","DOI":"10.1021\/acs.analchem.7b01848","article-title":"A Printed Equilibrium Dialysis Device with Integrated Membranes for Improved Binding Affinity Measurements","volume":"89","author":"Pinger","year":"2017","journal-title":"Anal. Chem."},{"issue":"12","key":"2021121004461044100_cit31","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1139\/o91-121","article-title":"Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study","volume":"69","author":"Goumakos","year":"1991","journal-title":"Biochem. Cell Biol."},{"issue":"6","key":"2021121004461044100_cit32","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1177\/193229680800200620","article-title":"A Review of Glycated Albumin as an Intermediate Glycation Index for Controlling Diabetes","volume":"2","author":"Roohk","year":"2008","journal-title":"J. Diabetes Sci. Technol."},{"issue":"43","key":"2021121004461044100_cit33","doi-asserted-by":"crossref","first-page":"17125","DOI":"10.1021\/jacs.9b04664","article-title":"Engineering the hCRBPII Domain-Swapped Dimer into a New Class of Protein Switches","volume":"141","author":"Ghanbarpour","year":"2019","journal-title":"J. Am. Chem. Soc."},{"issue":"24","key":"2021121004461044100_cit34","doi-asserted-by":"crossref","first-page":"9398","DOI":"10.1021\/ac701701k","article-title":"Screening for Ligands of Human Retinoid X Receptor-a Using Ultrafiltration Mass Spectrometry","volume":"79","author":"Liu","year":"2007","journal-title":"Anal. Chem."},{"issue":"16","key":"2021121004461044100_cit35","doi-asserted-by":"crossref","first-page":"5992","DOI":"10.1073\/pnas.0711446105","article-title":"Mechanism of Cu+-transporting ATPases: Soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites","volume":"105","author":"Gonz\u00e1lez-Guerrero","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"7","key":"2021121004461044100_cit36","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1016\/S0735-1097(03)00088-3","article-title":"Atherothrombosis, inflammation, and diabetes","volume":"41","author":"Biondi-Zoccai","year":"2003","journal-title":"J. Am. Coll. Cardiol."},{"issue":"4","key":"2021121004461044100_cit37","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1016\/j.bbalip.2018.09.007","article-title":"Crosstalk between zinc and free fatty acids in plasma","volume":"1864","author":"Coverdale","year":"2019","journal-title":"Biochim. Biophys. Acta, Mol. Cell Biol. Lipids"},{"issue":"1","key":"2021121004461044100_cit38","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1111\/jth.12771","article-title":"Plasma free fatty acid levels influence Zn2+-dependent histidinerich glycoprotein\u2013heparin interactions via an allosteric switch on serum albumin","volume":"13","author":"Kassaar","year":"2015","journal-title":"J. Thromb. Haemostasis"},{"issue":"3","key":"2021121004461044100_cit39","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1046\/j.1525-1373.2000.22418.x","article-title":"Albumin facilitates zinc acquisition by endothelial cells","volume":"224","author":"Rowe","year":"2000","journal-title":"Proc. Soc. Exp. Biol. Med."},{"issue":"3","key":"2021121004461044100_cit40","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1002\/(SICI)1097-4652(199606)167:3<539::AID-JCP17>3.0.CO;2-Z","article-title":"Zinc transport across an endothelium includes vesicular cotransport with albumin","volume":"167","author":"Tibaduiza","year":"1996","journal-title":"J. Cell. Physiol."},{"issue":"4","key":"2021121004461044100_cit41","doi-asserted-by":"crossref","first-page":"229","DOI":"10.7762\/cnr.2018.7.4.229","article-title":"Diabetes and Alzheimer\u2019s Disease: Mechanisms and Nutritional Aspects","volume":"7","author":"Lee","year":"2018","journal-title":"Clin. Nutr. Res."},{"issue":"6","key":"2021121004461044100_cit42","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1177\/193229680800200619","article-title":"Alzheimer\u2019s Disease Is Type 3 Diabetes\u2013Evidence Reviewed","volume":"2","author":"de la Monte","year":"2008","journal-title":"J. Diabetes Sci. Technol."},{"issue":"5177","key":"2021121004461044100_cit43","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1126\/science.8073293","article-title":"Rapid induction of Alzheimer A beta amyloid formation by zinc","volume":"265","author":"Bush","year":"1994","journal-title":"Science"},{"issue":"45","key":"2021121004461044100_cit44","doi-asserted-by":"crossref","first-page":"16076","DOI":"10.1523\/JNEUROSCI.3454-11.2011","article-title":"The neurophysiology and pathology of brain zinc","volume":"31","author":"Sensi","year":"2011","journal-title":"J. Neurosci."},{"key":"2021121004461044100_cit45","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1023\/A:1012993017026","article-title":"The role of zinc in caspase activation and apoptotic cell death","volume":"14","author":"Truong-Tran","year":"2001","journal-title":"Biometals"},{"key":"2021121004461044100_cit46","doi-asserted-by":"crossref","first-page":"229","DOI":"10.3181\/00379727-215-44132","article-title":"A reappraisal of the role of zinc in life and death decisions of cells","volume":"215","author":"Fraker","year":"1997","journal-title":"Proc. Soc. Exp. Biol. Med."},{"issue":"3","key":"2021121004461044100_cit47","doi-asserted-by":"crossref","first-page":"443","DOI":"10.3233\/JAD-2008-15310","article-title":"Serum Zinc in the Progression of Alzheimer\u2019s Disease","volume":"15","author":"Dong","year":"2008","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"2021121004461044100_cit48","first-page":"1","article-title":"The Role of Zinc in Alzheimer\u2019s Disease","volume":"2011","author":"Watt","year":"2011","journal-title":"J. Alzheimer\u2019s Dis."}],"container-title":["Metallomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/metallomics\/article-pdf\/12\/7\/1036\/41702285\/d0mt00123f.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/metallomics\/article-pdf\/12\/7\/1036\/41702285\/d0mt00123f.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,10]],"date-time":"2021-12-10T05:00:22Z","timestamp":1639112422000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/metallomics\/article\/12\/7\/1036\/5961474"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,7,1]]},"references-count":48,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2020,7,1]]}},"URL":"https:\/\/doi.org\/10.1039\/d0mt00123f","relation":{},"ISSN":["1756-5901","1756-591X"],"issn-type":[{"value":"1756-5901","type":"print"},{"value":"1756-591X","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2020,7]]},"published":{"date-parts":[[2020,7,1]]},"assertion":[{"value":"This document is Similarity Check deposited","name":"similarity_check","explanation":{"URL":"https:\/\/www.crossref.org\/services\/similarity-check\/"},"group":{"name":"similarity_check","label":"SIMILARITY CHECK"}},{"value":"Supplementary Information","URL":"https:\/\/doi.org\/10.1039\/D0MT00123F","name":"related_data","group":{"name":"related_data","label":"RELATED DATA"}},{"value":"Cody W. Pinger (ResearcherID)","URL":"http:\/\/www.researcherid.com\/rid\/G-7852-2017","name":"identifier","group":{"name":"author_identifiers","label":"IDENTIFIERS"}},{"value":"Dana M. Spence (ORCID)","URL":"http:\/\/orcid.org\/0000-0002-4754-6671","name":"identifier","group":{"name":"author_identifiers","label":"IDENTIFIERS"}},{"value":"Single-blind","order":2,"name":"peer_review_method","group":{"name":"peer_review_method","label":"PEER REVIEW METHOD"}},{"value":"Received 13 May 2020; Accepted 30 June 2020;  Accepted Manuscript published 30 June 2020;  Advance Article published 6 July 2020;  Version of Record published 22 July 2020","order":1,"name":"history","group":{"name":"publication_history","label":"PUBLICATION HISTORY"}}]}}