{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T14:51:11Z","timestamp":1791557471396,"version":"4.3.4"},"reference-count":59,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,8,1]],"date-time":"2024-08-01T00:00:00Z","timestamp":1722470400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100004504","name":"Research Council of Lithuania","doi-asserted-by":"publisher","award":["S-MIP-22-34"],"award-info":[{"award-number":["S-MIP-22-34"]}],"id":[{"id":"10.13039\/501100004504","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Archives of Biochemistry and Biophysics"],"published-print":{"date-parts":[[2024,8]]},"DOI":"10.1016\/j.abb.2024.110087","type":"journal-article","created":{"date-parts":[[2024,7,6]],"date-time":"2024-07-06T18:05:41Z","timestamp":1720289141000},"page":"110087","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"special_numbering":"C","title":["S100A9 inhibits and redirects prion protein 89-230 fragment amyloid aggregation"],"prefix":"10.1016","volume":"758","author":[{"given":"Mantas","family":"Ziaunys","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Darius","family":"Sulskis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kamile","family":"Mikalauskaite","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrius","family":"Sakalauskas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruta","family":"Snieckute","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vytautas","family":"Smirnovas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.abb.2024.110087_bib1","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade","volume":"86","author":"Chiti","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.abb.2024.110087_bib2","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1038\/nrm3810","article-title":"The amyloid state and its association with protein misfolding diseases","volume":"15","author":"Knowles","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.abb.2024.110087_bib3","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/s41580-018-0060-8","article-title":"A new era for understanding amyloid structures and disease","volume":"19","author":"Iadanza","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.abb.2024.110087_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7554\/eLife.76494","article-title":"Assembly of recombinant tau into filaments identical to those of Alzheimer's disease and chronic traumatic encephalopathy","volume":"11","author":"L\u00f6vestam","year":"2022","journal-title":"Elife"},{"key":"10.1016\/j.abb.2024.110087_bib5","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1038\/s41586-022-05319-3","article-title":"Structures of \u03b1-synuclein filaments from human brains with Lewy pathology","volume":"610","author":"Yang","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.abb.2024.110087_bib6","article-title":"Alzheimer's disease drug development pipeline: 2023, Alzheimer's Dement","volume":"9","author":"Cummings","year":"2023","journal-title":"Transl. Res. Clin. Interv."},{"key":"10.1016\/j.abb.2024.110087_bib7","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1080\/13543784.2017.1323868","article-title":"Why do trials for Alzheimer's disease drugs keep failing? A discontinued drug perspective for 2010-2015","volume":"26","author":"Mehta","year":"2017","journal-title":"Expert Opin. Investig. Drugs."},{"key":"10.1016\/j.abb.2024.110087_bib8","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms12408","article-title":"Projected increase in amyotrophic lateral sclerosis from 2015 to 2040","volume":"7","author":"Arthur","year":"2016","journal-title":"Nat. Commun."},{"key":"10.1016\/j.abb.2024.110087_bib9","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.2105\/AJPH.88.9.1337","article-title":"Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset","volume":"88","author":"Brookmeyer","year":"1998","journal-title":"Am. J. Public Health."},{"key":"10.1016\/j.abb.2024.110087_bib10","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/nprot.2016.010","article-title":"Molecular mechanisms of protein aggregation from global fitting of kinetic models","volume":"11","author":"Meisl","year":"2016","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.abb.2024.110087_bib11","doi-asserted-by":"crossref","first-page":"9384","DOI":"10.1073\/pnas.1401564111","article-title":"Differences in nucleation behavior underlie the contrasting aggregation kinetics of the A\u03b240 and A\u03b242 peptides","volume":"111","author":"Meisl","year":"2014","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.abb.2024.110087_bib12","doi-asserted-by":"crossref","first-page":"7671","DOI":"10.1073\/pnas.1315346111","article-title":"Solution conditions determine the relative importance of nucleation and growth processes in -synuclein aggregation","volume":"111","author":"Buell","year":"2014","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.abb.2024.110087_bib13","doi-asserted-by":"crossref","first-page":"6981","DOI":"10.1021\/bi500695g","article-title":"Mechanism of amyloid-\u03b2 fibril elongation","volume":"53","author":"Gurry","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.abb.2024.110087_bib14","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1021\/acschemneuro.7b00409","article-title":"Thermodynamics of amyloid-\u03b2 fibril elongation: atomistic details of the transition state","volume":"9","author":"Rodriguez","year":"2018","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.abb.2024.110087_bib15","doi-asserted-by":"crossref","first-page":"4644","DOI":"10.1021\/acs.jpcb.5b01160","article-title":"Fragmentation of amyloid fibrils occurs in preferential positions depending on the environmental conditions","volume":"119","author":"Nicoud","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.abb.2024.110087_bib16","doi-asserted-by":"crossref","first-page":"8667","DOI":"10.1039\/C8CC02204F","article-title":"Secondary nucleation in amyloid formation","volume":"54","author":"T\u00f6rnquist","year":"2018","journal-title":"Chem. Commun."},{"key":"10.1016\/j.abb.2024.110087_bib17","doi-asserted-by":"crossref","DOI":"10.1017\/S0033583516000172","article-title":"Secondary nucleation of monomers on fibril surface dominates \u03b1-synuclein aggregation and provides autocatalytic amyloid amplification","volume":"50","author":"Gaspar","year":"2017","journal-title":"Q. Rev. Biophys."},{"key":"10.1016\/j.abb.2024.110087_bib18","doi-asserted-by":"crossref","first-page":"3497","DOI":"10.1074\/mcp.M113.037309","article-title":"A \u201cproteomic ruler\u201d for protein copy number and concentration estimation without spike-in standards","volume":"13","author":"Wi\u015bniewski","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.abb.2024.110087_bib19","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1111\/j.1471-4159.2012.07847.x","article-title":"Cross-seeding effects of amyloid \u03b2-protein and \u03b1-synuclein","volume":"122","author":"Ono","year":"2012","journal-title":"J. Neurochem."},{"key":"10.1016\/j.abb.2024.110087_bib20","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1007\/s00401-015-1525-x","article-title":"Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo","volume":"131","author":"Vasconcelos","year":"2016","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.abb.2024.110087_bib21","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1007\/s00401-014-1371-2","article-title":"Tau aggregation and its interplay with amyloid-\u03b2","volume":"129","author":"Nisbet","year":"2015","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.abb.2024.110087_bib22","doi-asserted-by":"crossref","first-page":"6086","DOI":"10.1002\/anie.201800197","article-title":"Amyloid-\u03b2 peptide induces prion protein amyloid formation: evidence for its widespread amyloidogenic effect","volume":"57","author":"Honda","year":"2018","journal-title":"Angew. Chemie - Int. Ed."},{"key":"10.1016\/j.abb.2024.110087_bib23","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.cell.2013.05.057","article-title":"Distinct \u03b1-synuclein strains differentially promote tau inclusions in neurons","volume":"154","author":"Guo","year":"2013","journal-title":"Cell"},{"key":"10.1016\/j.abb.2024.110087_bib24","doi-asserted-by":"crossref","first-page":"7470","DOI":"10.1074\/jbc.RA119.012284","article-title":"Structural basis of the interplay between \u03b1-synuclein and Tau in regulating pathological amyloid aggregation","volume":"295","author":"Lu","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2024.110087_bib25","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.ppat.1006563","article-title":"Cross-seeding of prions by aggregated \u03b1-synuclein leads to transmissible spongiform encephalopathy","volume":"13","author":"Katorcha","year":"2017","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.abb.2024.110087_bib26","doi-asserted-by":"crossref","first-page":"D352","DOI":"10.1093\/nar\/gkac882","article-title":"AmyloGraph: a comprehensive database of amyloid\u2013amyloid interactions","volume":"51","author":"Burdukiewicz","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.abb.2024.110087_bib27","doi-asserted-by":"crossref","first-page":"2893","DOI":"10.3390\/ijms13032893","article-title":"Pro-inflammatory S100A8 and S100A9 proteins: self-assembly into multifunctional native and amyloid complexes","volume":"13","author":"Vogl","year":"2012","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2024.110087_bib28","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1007\/s00401-013-1208-4","article-title":"The role of pro-inflammatory S100A9 in Alzheimer's disease amyloid-neuroinflammatory cascade","volume":"127","author":"Wang","year":"2014","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.abb.2024.110087_bib29","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1186\/s12974-018-1210-9","article-title":"Co-aggregation of pro-inflammatory S100A9 with \u03b1-synuclein in Parkinson's disease: ex vivo and in vitro studies","volume":"15","author":"Horvath","year":"2018","journal-title":"J. Neuroinflammation"},{"key":"10.1016\/j.abb.2024.110087_bib30","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1111\/j.1582-4934.2008.00159.x","article-title":"S100B induces tau protein hyperphosphorylation via Dickopff-1 up-regulation and disrupts the Wnt pathway in human neural stem cells","volume":"12","author":"Esposito","year":"2008","journal-title":"J. Cell Mol. Med."},{"key":"10.1016\/j.abb.2024.110087_bib31","doi-asserted-by":"crossref","first-page":"2152","DOI":"10.1021\/acschemneuro.7b00251","article-title":"Finke\u2013watzky two-step nucleation\u2013autocatalysis model of S100A9 amyloid formation: protein misfolding as \u201cnucleation\u201d event","volume":"8","author":"Iashchishyn","year":"2017","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.abb.2024.110087_bib32","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fnmol.2017.00077","article-title":"The biological function of the prion protein: a cell surface scaffold of signaling modules","volume":"10","author":"Linden","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.abb.2024.110087_bib33","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/S0140-6736(99)05128-4","article-title":"Variant creutzfeldt-jakob disease","volume":"354","author":"Collinge","year":"1999","journal-title":"Lancet"},{"key":"10.1016\/j.abb.2024.110087_bib34","first-page":"428","article-title":"Prion disease, semin","volume":"39","author":"Baldwin","year":"2019","journal-title":"Neurol."},{"key":"10.1016\/j.abb.2024.110087_bib35","doi-asserted-by":"crossref","DOI":"10.1016\/S0065-3527(01)56031-5","article-title":"Transmissible spongiform encephalopathies and prion protein interconversions","volume":"56","author":"Caughey","year":"2001","journal-title":"Adv. Virus Res."},{"key":"10.1016\/j.abb.2024.110087_bib36","doi-asserted-by":"crossref","first-page":"2575","DOI":"10.1038\/ncomms3575","article-title":"Structural and functional characterization of two alpha-synuclein strains","volume":"4","author":"Bousset","year":"2013","journal-title":"Nat. Commun."},{"key":"10.1016\/j.abb.2024.110087_bib37","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/372491","article-title":"Polymorphisms at amino acid residues 141 and 154 influence conformational variation in ovine PrP","volume":"2014","author":"Yang","year":"2014","journal-title":"BioMed Res. Int."},{"key":"10.1016\/j.abb.2024.110087_bib38","doi-asserted-by":"crossref","first-page":"89","DOI":"10.4161\/pri.3.2.8859","article-title":"Structural polymorphism of Alzheimer A\u03b2 and other amyloid fibrils","volume":"3","author":"F\u00e4ndrich","year":"2009","journal-title":"Prion"},{"key":"10.1016\/j.abb.2024.110087_bib39","doi-asserted-by":"crossref","first-page":"3163","DOI":"10.1002\/pmic.201400441","article-title":"Version 4.0 of PaxDb: protein abundance data, integrated across model organisms, tissues, and cell-lines","volume":"15","author":"Wang","year":"2015","journal-title":"Proteomics"},{"key":"10.1016\/j.abb.2024.110087_bib40","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1038\/nature13302","article-title":"A draft map of the human proteome","volume":"509","author":"Kim","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.abb.2024.110087_bib41","doi-asserted-by":"crossref","first-page":"2043","DOI":"10.1002\/cne.23777","article-title":"High spatial resolution proteomic comparison of the brain in humans and chimpanzees","volume":"523","author":"Bauernfeind","year":"2015","journal-title":"J. Comp. Neurol."},{"key":"10.1016\/j.abb.2024.110087_bib42","doi-asserted-by":"crossref","first-page":"3152","DOI":"10.1074\/mcp.M114.038554","article-title":"In-depth characterization of the cerebrospinal fluid (CSF) proteome displayed through the CSF proteome resource (CSF-PR)","volume":"13","author":"Guldbrandsen","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.abb.2024.110087_bib43","doi-asserted-by":"crossref","first-page":"2196","DOI":"10.3390\/ijms22042196","article-title":"Neuroinflammation in prion disease","volume":"22","author":"Li","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2024.110087_bib44","doi-asserted-by":"crossref","DOI":"10.3390\/ijms241713200","article-title":"The stabilization of S100A9 structure by calcium inhibits the formation of amyloid fibrils","volume":"24","author":"Sanders","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2024.110087_bib45","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0038314","article-title":"Calcium binding promotes prion protein fragment 90\u2013231 conformational change toward a membrane destabilizing and cytotoxic structure","volume":"7","author":"Sorrentino","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.abb.2024.110087_bib46","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2021.109096","article-title":"Superoxide dismutase-1 alters the rate of prion protein aggregation and resulting fibril conformation","volume":"715","author":"Ziaunys","year":"2022","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.abb.2024.110087_bib47","doi-asserted-by":"crossref","first-page":"7972","DOI":"10.3390\/ijms22157972","article-title":"S100A9 alters the pathway of alpha-synuclein amyloid aggregation","volume":"22","author":"Toleikis","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2024.110087_bib48","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/nsmb.2035","article-title":"Structural organizaton of brain-derived mammalian prions as probed by hydrogen excange","volume":"18","author":"Smirnovas","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.abb.2024.110087_bib49","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0094469","article-title":"Elongation of mouse prion protein amyloid-like fibrils: effect of temperature and denaturant concentration","volume":"9","author":"Milto","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.abb.2024.110087_bib50","doi-asserted-by":"crossref","first-page":"8916","DOI":"10.3390\/ijms21238916","article-title":"Effect of ionic strength on thioflavin-T Affinity to amyloid fibrils and its fluorescence intensity","volume":"21","author":"Mikalauskaite","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2024.110087_bib51","doi-asserted-by":"crossref","first-page":"15174","DOI":"10.1021\/jp805560c","article-title":"Thioflavin T hydroxylation at basic pH and its effect on amyloid fibril detection","volume":"112","author":"Foder\u00e0","year":"2008","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.abb.2024.110087_bib52","doi-asserted-by":"crossref","first-page":"5421","DOI":"10.3390\/ijms23105421","article-title":"Lysozyme amyloid fibril structural variability dependence on initial protein folding state","volume":"23","author":"Mikalauskaite","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2024.110087_bib53","first-page":"181","article-title":"Gwyddion: an open-source software for SPM data analysis","volume":"10","author":"Ne\u010das","year":"2012","journal-title":"Cent. Eur. J. Phys."},{"key":"10.1016\/j.abb.2024.110087_bib54","doi-asserted-by":"crossref","DOI":"10.3390\/antiox11091711","article-title":"Exploring the formation of polymers with anti-amyloid properties within the 2\u20323\u2032-Dihydroxyflavone autoxidation process","volume":"11","author":"Sakalauskas","year":"2022","journal-title":"Antioxidants"},{"key":"10.1016\/j.abb.2024.110087_bib55","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1016\/j.bbabio.2007.06.004","article-title":"Infrared spectroscopy of proteins","volume":"1767","author":"Barth","year":"2007","journal-title":"Biochim. Biophys. Acta - Bioenerg."},{"key":"10.1016\/j.abb.2024.110087_bib56","doi-asserted-by":"crossref","first-page":"7031","DOI":"10.1039\/C9SC05905A","article-title":"Templating S100A9 amyloids on A\u03b2 fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses","volume":"11","author":"Pansieri","year":"2020","journal-title":"Chem. Sci."},{"key":"10.1016\/j.abb.2024.110087_bib57","doi-asserted-by":"crossref","first-page":"4572","DOI":"10.1038\/s41598-020-61663-2","article-title":"Formation of distinct prion protein amyloid fibrils under identical experimental conditions","volume":"10","author":"Ziaunys","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.abb.2024.110087_bib58","doi-asserted-by":"crossref","first-page":"6575","DOI":"10.1021\/acsnano.2c12009","article-title":"Direct observation of competing prion protein fibril populations with distinct structures and kinetics","volume":"17","author":"Sun","year":"2023","journal-title":"ACS Nano"},{"key":"10.1016\/j.abb.2024.110087_bib59","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1073\/pnas.2104148118","article-title":"Amyloid particles facilitate surface-catalyzed cross-seeding by acting as promiscuous nanoparticles","volume":"118","author":"Koloteva-Levine","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."}],"container-title":["Archives of Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986124002091?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986124002091?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,10,8]],"date-time":"2024-10-08T01:44:23Z","timestamp":1728351863000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003986124002091"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,8]]},"references-count":59,"alternative-id":["S0003986124002091"],"URL":"https:\/\/doi.org\/10.1016\/j.abb.2024.110087","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2024.02.06.579161","asserted-by":"object"}]},"ISSN":["0003-9861"],"issn-type":[{"value":"0003-9861","type":"print"}],"subject":[],"published":{"date-parts":[[2024,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"S100A9 inhibits and redirects prion protein 89-230 fragment amyloid aggregation","name":"articletitle","label":"Article Title"},{"value":"Archives of Biochemistry and Biophysics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.abb.2024.110087","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"110087"}}