{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,23]],"date-time":"2026-01-23T10:38:22Z","timestamp":1769164702782,"version":"3.49.0"},"reference-count":68,"publisher":"Public Library of Science (PLoS)","issue":"12","license":[{"start":{"date-parts":[[2015,12,7]],"date-time":"2015-12-07T00:00:00Z","timestamp":1449446400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0144025","type":"journal-article","created":{"date-parts":[[2015,12,8]],"date-time":"2015-12-08T19:15:19Z","timestamp":1449602119000},"page":"e0144025","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":35,"title":["Overexpression of Catalase Diminishes Oxidative Cysteine Modifications of Cardiac Proteins"],"prefix":"10.1371","volume":"10","author":[{"given":"Chunxiang","family":"Yao","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jessica B.","family":"Behring","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Di","family":"Shao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aaron L.","family":"Sverdlov","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephen A.","family":"Whelan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aly","family":"Elezaby","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaoyan","family":"Yin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Deborah A.","family":"Siwik","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Francesca","family":"Seta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Catherine E.","family":"Costello","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Richard A.","family":"Cohen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reiko","family":"Matsui","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wilson S.","family":"Colucci","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mark E.","family":"McComb","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Markus M.","family":"Bachschmid","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2015,12,7]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1152\/physrev.1998.78.2.547","article-title":"The free radical theory of aging matures","volume":"78","author":"KB Beckman","year":"1998","journal-title":"Physiol Rev"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1152\/physrev.1979.59.3.527","article-title":"Hydroperoxide metabolism in mammalian organs","volume":"59","author":"B Chance","year":"1979","journal-title":"Physiol Rev"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"2789","DOI":"10.1161\/CIRCULATIONAHA.108.822403","article-title":"Overexpression of catalase targeted to mitochondria attenuates murine cardiac aging","volume":"119","author":"D-F Dai","year":"2009","journal-title":"Circulation"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"e000184","DOI":"10.1161\/JAHA.113.000184","article-title":"Hydrogen peroxide-mediated SERCA cysteine 674 oxidation contributes to impaired cardiac myocyte relaxation in senescent mouse heart","volume":"2","author":"F Qin","year":"2013","journal-title":"J Am Heart Assoc"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1111\/j.1440-1681.2007.04540.x","article-title":"Cardiac-specific overexpression of catalase prolongs lifespan and attenuates ageing-induced cardiomyocyte contractile dysfunction and protein damage","volume":"34","author":"S Wu","journal-title":"Clin Exp Pharmacol Physiol"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"12610","DOI":"10.1074\/jbc.271.21.12610","article-title":"Suppression of doxorubicin cardiotoxicity by overexpression of catalase in the heart of transgenic mice","volume":"271","author":"YJ Kang","year":"1996","journal-title":"J Biol Chem"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.phrs.2006.02.005","article-title":"Role of endogenous hydrogen peroxide in cardiovascular ischaemia\/reperfusion function: studies in mouse hearts with catalase-overexpression in the vascular endothelium","volume":"54","author":"G W\u00f6lkart","year":"2006","journal-title":"Pharmacol Res"},{"key":"ref8","first-page":"H1090","article-title":"Catalase-overexpressing transgenic mouse heart is resistant to ischemia-reperfusion injury","volume":"273","author":"G Li","year":"1997","journal-title":"Am J Physiol"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1016\/j.freeradbiomed.2012.07.084","article-title":"Cardiac-specific overexpression of catalase attenuates lipopolysaccharide-induced myocardial contractile dysfunction: role of autophagy","volume":"53","author":"S Turdi","year":"2012","journal-title":"Free Radic Biol Med"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1161\/CIRCHEARTFAILURE.109.864785","article-title":"Cardiac-specific overexpression of catalase identifies hydrogen peroxide-dependent and -independent phases of myocardial remodeling and prevents the progression to overt heart failure in G(alpha)q-overexpressing transgenic mice","volume":"3","author":"F Qin","year":"2010","journal-title":"Circ Heart Fail"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/j.redox.2014.02.005","article-title":"Hydrogen peroxide signaling in vascular endothelial cells","volume":"2","author":"R Bret\u00f3n-Romero","year":"2014","journal-title":"Redox Biol"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1089\/ars.2011.4336","article-title":"Regulation of cell physiology and pathology by protein S-glutathionylation: lessons learned from the cardiovascular system","volume":"16","author":"D Pimentel","year":"2012","journal-title":"Antioxid Redox Signal"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"1975","DOI":"10.1096\/fj.13-233445","article-title":"Does reversible cysteine oxidation link the Western diet to cardiac dysfunction?","volume":"28","author":"JB Behring","year":"2014","journal-title":"FASEB J"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1161\/CIRCULATIONAHA.110.003418","article-title":"Mitochondrial transporter ATP binding cassette mitochondrial erythroid is a novel gene required for cardiac recovery after ischemia\/reperfusion","volume":"124","author":"M Liesa","year":"2011","journal-title":"Circulation"},{"key":"ref15","article-title":"High fat, high sucrose diet causes cardiac mitochondrial dysfunction due in part to oxidative post-translational modification of mitochondrial complex II","author":"AL Sverdlov","year":"2014","journal-title":"J Mol Cell Cardiol"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/nature09787","article-title":"Telomere dysfunction induces metabolic and mitochondrial compromise","volume":"470","author":"E Sahin","year":"2011","journal-title":"Nature"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"9819","DOI":"10.1021\/ac901335x","article-title":"Software tool for researching annotations of proteins: open-source protein annotation software with data visualization","volume":"81","author":"VN Bhatia","year":"2009","journal-title":"Anal Chem"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"13.22.1","DOI":"10.1002\/0471250953.bi1322s44","article-title":"STRAP PTM: Software Tool for Rapid Annotation and Differential Comparison of Protein Post-Translational Modifications","volume":"13","author":"JL Spencer","year":"2013","journal-title":"Curr Protoc Bioinformatics"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1093\/oxfordjournals.jbchem.a021883","article-title":"Ascorbic acid and reducing agents regulate the fates and functions of S-nitrosothiols","volume":"122","author":"M Kashiba-Iwatsuki","year":"1997","journal-title":"J Biochem"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"1473","DOI":"10.1074\/mcp.M700065-MCP200","article-title":"Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue","volume":"6","author":"RL Charles","year":"2007","journal-title":"Mol Cell Proteomics"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.1093\/jn\/114.10.1853","article-title":"Tissue glutathione as a cyst(e)ine reservoir during cystine depletion in growing rats","volume":"114","author":"ES Cho","year":"1984","journal-title":"J Nutr"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"5587","DOI":"10.4049\/jimmunol.176.9.5587","article-title":"Nitrotyrosine proteome survey in asthma identifies oxidative mechanism of catalase inactivation","volume":"176","author":"S Ghosh","year":"2006","journal-title":"J Immunol"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"4403","DOI":"10.1074\/jbc.R111.283432","article-title":"Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides","volume":"287","author":"SG Rhee","year":"2012","journal-title":"J Biol Chem"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/S0014-5793(03)00493-9","article-title":"Mitochondrial and cytosolic expression of human peroxiredoxin 5 in Saccharomyces cerevisiae protect yeast cells from oxidative stress induced by paraquat","volume":"544","author":"N Ti\u00ean Nguy\u00ean-nhu","year":"2003","journal-title":"FEBS Lett"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1046\/j.1432-1327.1999.00089.x","article-title":"Identification of the reactive cysteine residue (Cys227) in human carbonyl reductase","volume":"260","author":"JN Tinguely","year":"1999","journal-title":"Eur J Biochem"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"13106","DOI":"10.1021\/bi049136q","article-title":"Human carbonyl reductase catalyzes reduction of 4-oxonon-2-enal","volume":"43","author":"JA Doorn","year":"2004","journal-title":"Biochemistry"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.cbi.2012.12.011","article-title":"S-nitrosoglutathione covalently modifies cysteine residues of human carbonyl reductase 1 and affects its activity","volume":"202","author":"T Hartmanov\u00e1","year":"2013","journal-title":"Chem Biol Interact"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"35756","DOI":"10.1074\/jbc.M807125200","article-title":"Human carbonyl reductase 1 is an S-nitrosoglutathione reductase","volume":"283","author":"RL Bateman","year":"2008","journal-title":"J Biol Chem"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1111\/j.1365-2796.2007.01905.x","article-title":"Mitochondrial dysfunction as a cause of ageing","volume":"263","author":"A Trifunovic","year":"2008","journal-title":"J Intern Med"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.cmet.2006.02.002","article-title":"HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia","volume":"3","author":"J Kim","year":"2006","journal-title":"Cell Metab"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"H1327","DOI":"10.1152\/ajpheart.00997.2010","article-title":"Characterization of potential S-nitrosylation sites in the myocardium","volume":"300","author":"MJ Kohr","year":"2011","journal-title":"Am J Physiol Heart Circ Physiol"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"24588","DOI":"10.1074\/jbc.M114.572701","article-title":"Structural and spectroscopic insights into BolA-glutaredoxin complexes","volume":"289","author":"T Roret","year":"2014","journal-title":"J Biol Chem"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/j.febslet.2004.11.111","article-title":"Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin","volume":"579","author":"MA Huynen","year":"2005","journal-title":"FEBS Lett"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1016\/j.ajhg.2011.08.011","article-title":"Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes","volume":"89","author":"JM Cameron","year":"2011","journal-title":"Am J Hum Genet"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"3128","DOI":"10.1038\/ncomms4128","article-title":"Metabolic enzyme expression highlights a key role for MTHFD2 and the mitochondrial folate pathway in cancer","volume":"5","author":"R Nilsson","year":"2014","journal-title":"Nat Commun"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1007\/s002329900540","article-title":"Mouse VDAC isoforms expressed in yeast: channel properties and their roles in mitochondrial outer membrane permeability","volume":"170","author":"X Xu","year":"1999","journal-title":"J Membr Biol"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1186\/1471-2148-7-31","article-title":"The evolutionary history of mitochondrial porins","volume":"7","author":"MJ Young","year":"2007","journal-title":"BMC Evol Biol"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.2174\/138161206777585111","article-title":"The voltage-dependent anion channel (VDAC): function in intracellular signalling, cell life and cell death","volume":"12","author":"V Shoshan-Barmatz","year":"2006","journal-title":"Curr Pharm Des"},{"issue":"Suppl 1","key":"ref39","doi-asserted-by":"crossref","first-page":"S31","DOI":"10.1111\/j.1440-1746.2006.04643.x","article-title":"Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism","volume":"22","author":"JJ Lemasters","year":"2007","journal-title":"J Gastroenterol Hepatol"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1083\/jcb.200105057","article-title":"VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release","volume":"155","author":"M Madesh","year":"2001","journal-title":"J Cell Biol"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"2202","DOI":"10.1096\/fj.03-0012com","article-title":"Role of reactive oxygen species and cardiolipin in the release of cytochrome c from mitochondria","volume":"17","author":"G Petrosillo","year":"2003","journal-title":"FASEB J"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"2179","DOI":"10.1074\/jbc.M111.268920","article-title":"Structure-based analysis of VDAC1 protein: defining oligomer contact sites","volume":"287","author":"S Geula","year":"2012","journal-title":"J Biol Chem"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"25584","DOI":"10.1074\/jbc.M113.493692","article-title":"Modulation of human mitochondrial voltage-dependent anion channel 2 (hVDAC-2) structural stability by cysteine-assisted barrel-lipid interactions","volume":"288","author":"SR Maurya","year":"2013","journal-title":"J Biol Chem"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"7127","DOI":"10.1021\/bi973055v","article-title":"Structure and intramodular dynamics of the amino-terminal LIM domain from quail cysteine- and glycine-rich protein CRP2","volume":"37","author":"G Kontaxis","year":"1998","journal-title":"Biochemistry"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/0092-8674(94)90191-0","article-title":"The LIM domain is a modular protein-binding interface","volume":"79","author":"KL Schmeichel","year":"1994","journal-title":"Cell"},{"issue":"Pt 3","key":"ref46","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1042\/bj3520601","article-title":"The latent transforming growth factor beta binding protein (LTBP) family","volume":"352","author":"R Okl\u00fc","year":"2000","journal-title":"Biochem J"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.cell.2009.04.037","article-title":"Blinded by the Light: The Growing Complexity of p53","volume":"137","author":"KH Vousden","year":"2009","journal-title":"Cell"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1038\/sj.onc.1210263","article-title":"Coping with stress: multiple ways to activate p53","volume":"26","author":"HF Horn","year":"2007","journal-title":"Oncogene"},{"key":"ref49","article-title":"p53 as an intervention target for cancer and aging","volume":"3","author":"P Hasty","year":"2013","journal-title":"Pathobiol Aging Age Relat Dis"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"2358","DOI":"10.1016\/j.biocel.2007.08.010","article-title":"Protein phosphatase 5","volume":"40","author":"TD Hinds","year":"2008","journal-title":"Int J Biochem Cell Biol"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1042\/bj3530417","article-title":"Protein phosphatase 2A: a highly regulated family of serine\/threonine phosphatases implicated in cell growth and signalling","volume":"353","author":"V Janssens","year":"2001","journal-title":"Biochem J"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/sj.onc.1207005","article-title":"Phosphorylation of p53 at serine 37 is important for transcriptional activity and regulation in response to DNA damage","volume":"23","author":"KM Dohoney","year":"2004","journal-title":"Oncogene"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"5977","DOI":"10.1038\/onc.2010.371","article-title":"Serine\/threonine phosphatases in the DNA damage response and cancer","volume":"29","author":"A Peng","year":"2010","journal-title":"Oncogene"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1007\/s00441-005-0137-5","article-title":"Expression analysis of the NDRG2 gene in mouse embryonic and adult tissues","volume":"325","author":"X-L Hu","year":"2006","journal-title":"Cell Tissue Res"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"5335","DOI":"10.1093\/nar\/gkn504","article-title":"N-Myc downstream-regulated gene 2 is involved in p53-mediated apoptosis","volume":"36","author":"N Liu","year":"2008","journal-title":"Nucleic Acids Res"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1186\/1756-9966-29-103","article-title":"NDRG2 suppresses the proliferation of clear cell renal cell carcinoma cell A-498","volume":"29","author":"J-J Ma","year":"2010","journal-title":"J Exp Clin Cancer Res"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.neulet.2005.06.055","article-title":"Ndrg2 promotes neurite outgrowth of NGF-differentiated PC12 cells","volume":"388","author":"K Takahashi","year":"2005","journal-title":"Neurosci Lett"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.nbd.2004.01.003","article-title":"NDRG2: a novel Alzheimer\u2019s disease associated protein","volume":"16","author":"C Mitchelmore","year":"2004","journal-title":"Neurobiol Dis"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1159\/000113765","article-title":"NDRG2 is a new HIF-1 target gene necessary for hypoxia-induced apoptosis in A549 cells","volume":"21","author":"L Wang","year":"2008","journal-title":"Cell Physiol Biochem"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.yjmcc.2013.12.015","article-title":"Proteotoxicity: an underappreciated pathology in cardiac disease","volume":"71","author":"M Sandri","year":"2014","journal-title":"J Mol Cell Cardiol"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.yjmcc.2013.11.006","article-title":"Proteasomal and lysosomal protein degradation and heart disease","volume":"71","author":"X Wang","year":"2014","journal-title":"J Mol Cell Cardiol"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1038\/nature02265","article-title":"Therapeutic approaches to protein-misfolding diseases","volume":"426","author":"FE Cohen","year":"2003","journal-title":"Nature"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.yjmcc.2013.10.008","article-title":"Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond","volume":"71","author":"Z Cui","year":"2014","journal-title":"J Mol Cell Cardiol"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1038\/nbt.1654","article-title":"Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling","volume":"28","author":"G Xu","year":"2010","journal-title":"Nat Biotechnol"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1248\/bpb.21.905","article-title":"Characteristic expression of 105-kDa heat shock protein (HSP105) in various tissues of nonstressed and heat-stressed rats","volume":"21","author":"T Wakatsuki","year":"1998","journal-title":"Biol Pharm Bull"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1172\/JCI109642","article-title":"Enzymatic defenses of the mouse heart against reactive oxygen metabolites: alterations produced by doxorubicin","volume":"65","author":"JH Doroshow","year":"1980","journal-title":"J Clin Invest"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/0891-5849(94)90092-2","article-title":"Weak antioxidant defenses make the heart a target for damage in copper-deficient rats","volume":"17","author":"Y Chen","year":"1994","journal-title":"Free Radic Biol Med"},{"key":"ref68","article-title":"Target Organ Toxicity, Volume 1","author":"T Ishikawa","year":"1986"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0144025","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,5,28]],"date-time":"2022-05-28T14:55:09Z","timestamp":1653749709000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0144025"}},"subtitle":[],"editor":[{"given":"Rodrigo","family":"Franco","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2015,12,7]]},"references-count":68,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2015,12,7]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0144025","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,12,7]]}}}