{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T13:48:53Z","timestamp":1791294533235,"version":"4.1.0"},"reference-count":59,"publisher":"Elsevier BV","issue":"26","license":[{"start":{"date-parts":[[2013,6,1]],"date-time":"2013-06-01T00:00:00Z","timestamp":1370044800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,7]],"date-time":"2020-09-07T00:00:00Z","timestamp":1599436800000},"content-version":"vor","delay-in-days":2655,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2013,6]]},"DOI":"10.1074\/jbc.m113.457739","type":"journal-article","created":{"date-parts":[[2013,5,17]],"date-time":"2013-05-17T02:49:54Z","timestamp":1368758994000},"page":"18673-18683","source":"Crossref","is-referenced-by-count":71,"title":["Structural Insights into A\u03b242 Oligomers Using Site-directed Spin Labeling"],"prefix":"10.1016","volume":"288","author":[{"given":"Lei","family":"Gu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cong","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhefeng","family":"Guo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M113.457739_bib1","doi-asserted-by":"crossref","first-page":"a004457","DOI":"10.1101\/cshperspect.a004457","article-title":"Alzheimer's disease","volume":"3","author":"Selkoe","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol"},{"key":"10.1074\/jbc.M113.457739_bib2","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1152\/physrev.00023.2009","article-title":"Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process","volume":"90","author":"De Strooper","year":"2010","journal-title":"Physiol. Rev"},{"key":"10.1074\/jbc.M113.457739_bib3","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/0896-6273(94)90458-8","article-title":"Visualization of A\u03b242(43) and A\u03b240 in senile plaques with end-specific A\u03b2 monoclonals: Evidence that an initially deposited species is A\u03b242(43)","volume":"13","author":"Iwatsubo","year":"1994","journal-title":"Neuron"},{"key":"10.1074\/jbc.M113.457739_bib4","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1126\/science.1072994","article-title":"The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics","volume":"297","author":"Hardy","year":"2002","journal-title":"Science"},{"key":"10.1074\/jbc.M113.457739_bib5","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1002\/1531-8249(199912)46:6<860::AID-ANA8>3.0.CO;2-M","article-title":"Soluble pool of A\u03b2 amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease","volume":"46","author":"McLean","year":"1999","journal-title":"Ann. Neurol"},{"key":"10.1074\/jbc.M113.457739_bib6","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.chembiol.2012.02.003","article-title":"Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships","volume":"19","author":"Bemporad","year":"2012","journal-title":"Chem. Biol"},{"key":"10.1074\/jbc.M113.457739_bib7","doi-asserted-by":"crossref","first-page":"3801","DOI":"10.1523\/JNEUROSCI.5543-03.2004","article-title":"Dimeric amyloid \u03b2 protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated Tau accumulation in the Tg2576 mouse model of Alzheimer's disease","volume":"24","author":"Kawarabayashi","year":"2004","journal-title":"J. Neurosci"},{"key":"10.1074\/jbc.M113.457739_bib8","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1038\/nm1782","article-title":"Amyloid-\u03b2 protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory","volume":"14","author":"Shankar","year":"2008","journal-title":"Nat. Med"},{"key":"10.1074\/jbc.M113.457739_bib9","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1038\/nature04533","article-title":"A specific amyloid-\u03b2 protein assembly in the brain impairs memory","volume":"440","author":"Lesn\u00e9","year":"2006","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.457739_bib10","doi-asserted-by":"crossref","first-page":"4749","DOI":"10.1074\/jbc.R800036200","article-title":"Amyloid \u03b2-protein assembly and Alzheimer disease","volume":"284","author":"Roychaudhuri","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.457739_bib11","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/nn.3028","article-title":"The toxic A\u03b2 oligomer and Alzheimer's disease: an emperor in need of clothes","volume":"15","author":"Benilova","year":"2012","journal-title":"Nat. Neurosci"},{"key":"10.1074\/jbc.M113.457739_bib12","doi-asserted-by":"crossref","first-page":"6448","DOI":"10.1073\/pnas.95.11.6448","article-title":"Diffusible, nonfibrillar ligands derived from A\u03b21\u201342 are potent central nervous system neurotoxins","volume":"95","author":"Lambert","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.457739_bib13","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1111\/j.1471-4159.2005.03407.x","article-title":"Globular amyloid \u03b2-peptide1\u201342 oligomer \u2013 a homogenous and stable neuropathological protein in Alzheimer's disease","volume":"95","author":"Barghorn","year":"2005","journal-title":"J. Neurochem"},{"key":"10.1074\/jbc.M113.457739_bib14","doi-asserted-by":"crossref","first-page":"29639","DOI":"10.1074\/jbc.R800016200","article-title":"Structural classification of toxic amyloid oligomers","volume":"283","author":"Glabe","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.457739_bib15","doi-asserted-by":"crossref","first-page":"6370","DOI":"10.1073\/pnas.1237107100","article-title":"Spherical aggregates of \u03b2-amyloid (amylospheroid) show high neurotoxicity and activate Tau protein kinase I\/glycogen synthase kinase-3\u03b2","volume":"100","author":"Hoshi","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.457739_bib16","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1042\/BJ20090379","article-title":"Antiparallel \u03b2-sheet: a signature structure of the oligomeric amyloid \u03b2-peptide","volume":"421","author":"Cerf","year":"2009","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M113.457739_bib17","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1007\/s00109-008-0391-6","article-title":"Oligomeric and fibrillar species of \u03b2-amyloid (A\u03b242) both impair mitochondrial function in P301L Tau transgenic mice","volume":"86","author":"Eckert","year":"2008","journal-title":"J. Mol. Med"},{"key":"10.1074\/jbc.M113.457739_bib18","doi-asserted-by":"crossref","first-page":"12503","DOI":"10.1073\/pnas.1206433109","article-title":"Molecular basis of \u03b2-amyloid oligomer recognition with a conformational antibody fragment","volume":"109","author":"Morgado","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.457739_bib19","doi-asserted-by":"crossref","first-page":"19232","DOI":"10.1073\/pnas.0703793104","article-title":"Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing A\u03b2 protofibrils","volume":"104","author":"Habicht","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.457739_bib20","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1038\/nsmb.1799","article-title":"Structural conversion of neurotoxic amyloid-\u03b2(1\u201342) oligomers to fibrils","volume":"17","author":"Ahmed","year":"2010","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M113.457739_bib21","doi-asserted-by":"crossref","first-page":"7717","DOI":"10.1073\/pnas.1203193109","article-title":"Toxic fibrillar oligomers of amyloid-\u03b2 have cross-\u03b2 structure","volume":"109","author":"Stroud","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.457739_bib22","doi-asserted-by":"crossref","first-page":"15595","DOI":"10.1073\/pnas.1001740107","article-title":"Stabilization of neurotoxic Alzheimer amyloid-\u03b2 oligomers by protein engineering","volume":"107","author":"Sandberg","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.457739_bib23","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1007\/s00018-010-0529-x","article-title":"Transformation of amyloid \u03b2(1\u201340) oligomers into fibrils is characterized by a major change in secondary structure","volume":"68","author":"Sarroukh","year":"2011","journal-title":"Cell. Mol. Life Sci"},{"key":"10.1074\/jbc.M113.457739_bib24","doi-asserted-by":"crossref","first-page":"4088","DOI":"10.1016\/j.febslet.2012.10.022","article-title":"A comparative analysis of the aggregation behavior of amyloid-\u03b2 peptide variants","volume":"586","author":"Vandersteen","year":"2012","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M113.457739_bib25","doi-asserted-by":"crossref","first-page":"6736","DOI":"10.1021\/ja200222n","article-title":"Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic \u03b2-sheet mimics","volume":"133","author":"Liu","year":"2011","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M113.457739_bib26","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1126\/science.1213151","article-title":"Atomic view of a toxic amyloid small oligomer","volume":"335","author":"Laganowsky","year":"2012","journal-title":"Science"},{"key":"10.1074\/jbc.M113.457739_bib27","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1017\/S0033583508004733","article-title":"Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy","volume":"41","author":"Margittai","year":"2008","journal-title":"Q. Rev. Biophys"},{"key":"10.1074\/jbc.M113.457739_bib28","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1042\/BJ20120034","article-title":"Structural origin of polymorphism for Alzheimer's amyloid-\u03b2 fibrils","volume":"447","author":"Agopian","year":"2012","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M113.457739_bib29","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1038\/78956","article-title":"Identifying conformational changes with site-directed spin labeling","volume":"7","author":"Hubbell","year":"2000","journal-title":"Nat. Struct. Biol"},{"key":"10.1074\/jbc.M113.457739_bib30","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1016\/j.sbi.2006.08.008","article-title":"Recent advances and applications of site-directed spin labeling","volume":"16","author":"Fanucci","year":"2006","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.M113.457739_bib31","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1016\/j.str.2011.10.009","article-title":"Toward the fourth dimension of membrane protein structure: insight into dynamics from spin-labeling EPR spectroscopy","volume":"19","author":"McHaourab","year":"2011","journal-title":"Structure"},{"key":"10.1074\/jbc.M113.457739_bib32","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.nbd.2008.01.010","article-title":"A\u03b2-globulomers are formed independently of the fibril pathway","volume":"30","author":"Gellermann","year":"2008","journal-title":"Neurobiol Dis"},{"key":"10.1074\/jbc.M113.457739_bib33","doi-asserted-by":"crossref","first-page":"10369","DOI":"10.1523\/JNEUROSCI.5721-09.2010","article-title":"Generation and therapeutic efficacy of highly oligomer-specific \u03b2-amyloid antibodies","volume":"30","author":"Hillen","year":"2010","journal-title":"J. Neurosci"},{"key":"10.1074\/jbc.M113.457739_bib34","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1523\/JNEUROSCI.4771-07.2008","article-title":"Amyloid \u03b2 oligomers (A\u03b2(1\u201342) globulomer) suppress spontaneous synaptic activity by inhibition of P\/Q-type calcium currents","volume":"28","author":"Nimmrich","year":"2008","journal-title":"J. Neurosci"},{"key":"10.1074\/jbc.M113.457739_bib35","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1021\/bi802046n","article-title":"Structural characterization of a soluble amyloid \u03b2-peptide oligomer","volume":"48","author":"Yu","year":"2009","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.457739_bib36","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1016\/j.bbrc.2007.05.186","article-title":"Stable activity of a deubiquitylating enzyme (Usp2-cc) in the presence of high concentrations of urea and its application to purify aggregation-prone peptides","volume":"359","author":"Shahnawaz","year":"2007","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M113.457739_bib37","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/S0076-6879(05)98044-0","article-title":"Using deubiquitylating enzymes as research tools","volume":"398","author":"Baker","year":"2005","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.M113.457739_bib38","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1016\/j.bbrc.2011.09.097","article-title":"Key residues for the oligomerization of A\u03b242 protein in Alzheimer's disease","volume":"414","author":"Ngo","year":"2011","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M113.457739_bib39","series-title":"Spin Labeling: Theory and Applications","first-page":"1","article-title":"Calculating slow motional magnetic resonance specta","author":"Schneider","year":"1989"},{"key":"10.1074\/jbc.M113.457739_bib40","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1006\/jmra.1996.0113","article-title":"Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm","volume":"120","author":"Budil","year":"1996","journal-title":"J. Magn. Reson"},{"key":"10.1074\/jbc.M113.457739_bib41","doi-asserted-by":"crossref","first-page":"15471","DOI":"10.1021\/bi011544w","article-title":"Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations","volume":"40","author":"Altenbach","year":"2001","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.457739_bib42","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1111\/j.1471-4159.2004.02459.x","article-title":"Environment- and mutation-dependent aggregation behavior of Alzheimer amyloid \u03b2-protein","volume":"90","author":"Yamamoto","year":"2004","journal-title":"J. Neurochem"},{"key":"10.1074\/jbc.M113.457739_bib43","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1016\/j.bbrc.2011.02.092","article-title":"Structural investigation of porcine stomach mucin by X-ray fiber diffraction and homology modeling","volume":"406","author":"Veluraja","year":"2011","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M113.457739_bib44","doi-asserted-by":"crossref","first-page":"6568","DOI":"10.1021\/bi3005686","article-title":"Mapping molecular flexibility of proteins with site-directed spin labeling: a case study of myoglobin","volume":"51","author":"L\u00f3pez","year":"2012","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.457739_bib45","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1016\/S0968-0004(02)02095-9","article-title":"A new spin on protein dynamics","volume":"27","author":"Columbus","year":"2002","journal-title":"Trends Biochem. Sci"},{"key":"10.1074\/jbc.M113.457739_bib46","doi-asserted-by":"crossref","first-page":"e47248","DOI":"10.1371\/journal.pone.0047248","article-title":"Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study","volume":"7","author":"Ngo","year":"2012","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M113.457739_bib47","doi-asserted-by":"crossref","first-page":"9081","DOI":"10.1074\/jbc.M111.292086","article-title":"Solid-support EPR studies of A\u03b240 monomers reveal a structured state with three ordered segments","volume":"287","author":"Gu","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.457739_bib48","doi-asserted-by":"crossref","first-page":"6350","DOI":"10.1021\/bi300328w","article-title":"High-resolution structure of a protein spin-label in a solvent-exposed \u03b2-sheet and comparison with DEER spectroscopy","volume":"51","author":"Cunningham","year":"2012","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.457739_bib49","doi-asserted-by":"crossref","first-page":"3137","DOI":"10.1021\/bi0360962","article-title":"Motion of spin label side chains in cellular retinol-binding protein: correlation with structure and nearest-neighbor interactions in an antiparallel \u03b2-sheet","volume":"43","author":"Lietzow","year":"2004","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.457739_bib50","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1110\/ps.062739107","article-title":"Structural determinants of nitroxide motion in spin-labeled proteins: Tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme","volume":"16","author":"Guo","year":"2007","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M113.457739_bib51","doi-asserted-by":"crossref","first-page":"3314","DOI":"10.1110\/ps.041024904","article-title":"FTIR reveals structural differences between native \u03b2-sheet proteins and amyloid fibrils","volume":"13","author":"Zandomeneghi","year":"2004","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M113.457739_bib52","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1017\/S0033583502003815","article-title":"What vibrations tell us about proteins","volume":"35","author":"Barth","year":"2002","journal-title":"Q. Rev. Biophys"},{"key":"10.1074\/jbc.M113.457739_bib53","doi-asserted-by":"crossref","first-page":"3458","DOI":"10.1002\/prot.22832","article-title":"\u03b2-Barrel models of soluble amyloid \u03b2 oligomers and annular protofibrils","volume":"78","author":"Shafrir","year":"2010","journal-title":"Proteins"},{"key":"10.1074\/jbc.M113.457739_bib54","doi-asserted-by":"crossref","first-page":"37102","DOI":"10.1074\/jbc.M110.133488","article-title":"Polymorphic C-terminal \u03b2-sheet interactions determine the formation of fibril or amyloid \u03b2-derived diffusible ligand-like globulomer for the Alzheimer A\u03b242 dodecamer","volume":"285","author":"Ma","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.457739_bib55","doi-asserted-by":"crossref","first-page":"34244","DOI":"10.1074\/jbc.M111.241141","article-title":"Polymorphic triple \u03b2-sheet structures contribute to amide hydrogen\/deuterium (H\/D) exchange protection in the Alzheimer amyloid \u03b242 peptide","volume":"286","author":"Ma","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.457739_bib56","doi-asserted-by":"crossref","first-page":"1419","DOI":"10.1523\/JNEUROSCI.4259-10.2011","article-title":"Crystal structure of the amyloid-\u03b2 p3 fragment provides a model for oligomer formation in Alzheimer's disease","volume":"31","author":"Streltsov","year":"2011","journal-title":"J. Neurosci"},{"key":"10.1074\/jbc.M113.457739_bib57","doi-asserted-by":"crossref","first-page":"5099","DOI":"10.1073\/pnas.0711731105","article-title":"Stabilization of a \u03b2-hairpin in monomeric Alzheimer's amyloid-\u03b2 peptide inhibits amyloid formation","volume":"105","author":"Hoyer","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.457739_bib58","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1146\/annurev-physchem-032210-103539","article-title":"Solid-state NMR studies of amyloid fibril structure","volume":"62","author":"Tycko","year":"2011","journal-title":"Annu. Rev. Phys. Chem"},{"key":"10.1074\/jbc.M113.457739_bib59","doi-asserted-by":"crossref","first-page":"3828","DOI":"10.1021\/bi002645h","article-title":"Molecular motion of spin labeled side chains in \u03b1-helices: analysis by variation of side chain structure","volume":"40","author":"Columbus","year":"2001","journal-title":"Biochemistry"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820457230?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820457230?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M113.457739","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T14:43:45Z","timestamp":1641307425000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820457230"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,6]]},"references-count":59,"journal-issue":{"issue":"26","published-print":{"date-parts":[[2013,6]]}},"alternative-id":["S0021925820457230"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m113.457739","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2013,6]]}}}