{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T11:03:35Z","timestamp":1790247815177,"version":"4.1.0"},"reference-count":63,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,2,1]],"date-time":"2018-02-01T00:00:00Z","timestamp":1517443200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,2,1]],"date-time":"2018-02-01T00:00:00Z","timestamp":1517443200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Acta Biomaterialia"],"published-print":{"date-parts":[[2018,2]]},"DOI":"10.1016\/j.actbio.2017.11.048","type":"journal-article","created":{"date-parts":[[2017,12,6]],"date-time":"2017-12-06T03:22:10Z","timestamp":1512530530000},"page":"147-155","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":84,"special_numbering":"C","title":["Light-triggered dissociation of self-assembled \u03b2-amyloid aggregates into small, nontoxic fragments by ruthenium (II) complex"],"prefix":"10.1016","volume":"67","author":[{"given":"Giyeong","family":"Son","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Byung Il","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"You Jung","family":"Chung","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chan Beum","family":"Park","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.actbio.2017.11.048_b0005","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1038\/537036a","article-title":"Alzheimer's disease: Attack on amyloid-\u03b2 protein","volume":"537","author":"Reiman","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.actbio.2017.11.048_b0010","doi-asserted-by":"crossref","first-page":"8762","DOI":"10.1038\/ncomms9762","article-title":"Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer\u2019s disease","volume":"6","author":"Zhang","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.actbio.2017.11.048_b0015","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1038\/nsmb1345","article-title":"Evidence of fibril-like -sheet structures in a neurotoxic amyloid intermediate of Alzheimer's \u03b2-amyloid","volume":"14","author":"Chimon","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.actbio.2017.11.048_b0020","doi-asserted-by":"crossref","first-page":"7883","DOI":"10.1021\/ja000645z","article-title":"Structure of the \u03b2-amyloid(10\u201335) fibril","volume":"122","author":"Burkoth","year":"2000","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.actbio.2017.11.048_b0025","doi-asserted-by":"crossref","first-page":"10289","DOI":"10.1002\/anie.201203595","article-title":"Hydrogen bonding in Alzheimer\u2019s amyloid-\u03b2 fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy","volume":"51","author":"Antzutkin","year":"2012","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.actbio.2017.11.048_b0030","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1021\/bm501521r","article-title":"Stable, metastable, and kinetically trapped amyloid aggregate phases","volume":"16","author":"Miti","year":"2015","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.actbio.2017.11.048_b0035","doi-asserted-by":"crossref","first-page":"573","DOI":"10.2174\/138920307783018703","article-title":"Molecular mechanisms of polypeptide aggregation in human diseases","volume":"8","author":"Khare","year":"2007","journal-title":"Curr. Protein Pep. Sc."},{"key":"10.1016\/j.actbio.2017.11.048_b0040","doi-asserted-by":"crossref","first-page":"14786","DOI":"10.1074\/jbc.270.24.14786","article-title":"Intracellular A\u03b21-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells","volume":"270","author":"Yang","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.actbio.2017.11.048_b0045","doi-asserted-by":"crossref","first-page":"9543","DOI":"10.1039\/C4CC03791J","article-title":"Photodegradation of amyloid \u03b2 and reduction of its cytotoxicity to PC12 cells using porphyrin derivatives","volume":"50","author":"Hirabayashi","year":"2014","journal-title":"Chem. Commun."},{"key":"10.1016\/j.actbio.2017.11.048_b0050","doi-asserted-by":"crossref","unstructured":"Y. Ishida T. Fujii K. Oka D. Takahashi K. Toshima Inhibition of amyloid \u03b2 aggregation and cytotoxicity by photodegradation using a designed fullerene derivative Chem. Asian J. 6 2011 2312 2315","DOI":"10.1002\/asia.201100421"},{"key":"10.1016\/j.actbio.2017.11.048_b0055","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1039\/c0md00075b","article-title":"Photo-degradation of amyloid \u03b2 by a designed fullerene-sugar hybrid","volume":"1","author":"Ishida","year":"2010","journal-title":"MedChemComm"},{"key":"10.1016\/j.actbio.2017.11.048_b0060","doi-asserted-by":"crossref","first-page":"11394","DOI":"10.1039\/c3cc46772d","article-title":"Photodegradation of \u03b2-sheet amyloid fibrils associated with Alzheimer's disease by using polyoxometalates as photocatalysts","volume":"49","author":"Li","year":"2013","journal-title":"Chem. Commun."},{"key":"10.1016\/j.actbio.2017.11.048_b0065","doi-asserted-by":"crossref","first-page":"11472","DOI":"10.1002\/anie.201504310","article-title":"Photoexcited porphyrins as a strong suppressor of \u03b2-amyloid aggregation and synaptic toxicity","volume":"54","author":"Lee","year":"2015","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.actbio.2017.11.048_b0070","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.biomaterials.2014.10.058","article-title":"Photo-induced inhibition of Alzheimer's \u03b2-amyloid aggregation in vitro by rose bengal","volume":"38","author":"Lee","year":"2015","journal-title":"Biomaterials"},{"key":"10.1016\/j.actbio.2017.11.048_b0075","doi-asserted-by":"crossref","first-page":"4386","DOI":"10.1002\/smll.201401121","article-title":"Reduced aggregation and cytotoxicity of amyloid peptides by graphene oxide\/gold nanocomposites prepared by pulsed laser ablation in water","volume":"10","author":"Li","year":"2014","journal-title":"Small"},{"key":"10.1016\/j.actbio.2017.11.048_b0080","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1038\/nmeth.f.324","article-title":"Optogenetics","volume":"8","author":"Deisseroth","year":"2011","journal-title":"Nat. Methods"},{"key":"10.1016\/j.actbio.2017.11.048_b0085","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1126\/science.1232437","article-title":"Injectable, cellular-scale optoelectronics with applications for wireless optogenetics","volume":"340","author":"Kim","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.actbio.2017.11.048_b0090","doi-asserted-by":"crossref","first-page":"3631","DOI":"10.1002\/smll.201201068","article-title":"Negatively charged gold nanoparticles inhibit Alzheimer's amyloid-\u03b2 fibrillization, induce fibril dissociation, and mitigate neurotoxicity","volume":"8","author":"Liao","year":"2012","journal-title":"Small"},{"key":"10.1016\/j.actbio.2017.11.048_b0095","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1038\/nchem.2550","article-title":"Switchable photooxygenation catalysts that sense higher-order amyloid structures","volume":"8","author":"Taniguchi","year":"2016","journal-title":"Nat. Chem."},{"key":"10.1016\/j.actbio.2017.11.048_b0100","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1021\/cn100057j","article-title":"Oral treatment with the d-enantiomeric peptide D3 improves the pathology and behavior of Alzheimer\u2019s disease transgenic mice","volume":"1","author":"Aileen Funke","year":"2010","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.actbio.2017.11.048_b0105","doi-asserted-by":"crossref","first-page":"11589","DOI":"10.1002\/anie.201205018","article-title":"Water oxidation by single-site ruthenium complexes: using ligands as redox and proton transfer mediators","volume":"51","author":"K\u00e4rk\u00e4s","year":"2012","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.actbio.2017.11.048_b0110","doi-asserted-by":"crossref","first-page":"11813","DOI":"10.1002\/anie.201406553","article-title":"Selective generation of formamides through photocatalytic CO2 reduction catalyzed by ruthenium carbonyl compounds","volume":"53","author":"Kobayashi","year":"2014","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.actbio.2017.11.048_b0115","doi-asserted-by":"crossref","first-page":"5322","DOI":"10.1021\/cr300503r","article-title":"Visible light photoredox catalysis with transition metal complexes: applications in organic synthesis","volume":"113","author":"Prier","year":"2013","journal-title":"Chem. Rev."},{"key":"10.1016\/j.actbio.2017.11.048_b0120","doi-asserted-by":"crossref","first-page":"3137","DOI":"10.1039\/b002884n","article-title":"Photosensitized generation of singlet oxygen from ruthenium(II)-substituted benzoaza-crown-bipyridine complexes","volume":"2","author":"Abdel-Shafi","year":"2000","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.actbio.2017.11.048_b0125","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/j.biomaterials.2015.04.002","article-title":"Ruthenium(II) polypyridyl complexes as mitochondria-targeted two-photon photodynamic anticancer agents","volume":"56","author":"Liu","year":"2015","journal-title":"Biomaterials"},{"key":"10.1016\/j.actbio.2017.11.048_b0130","doi-asserted-by":"crossref","first-page":"e105865","DOI":"10.1371\/journal.pone.0105865","article-title":"Silveira-Lacerda, Cytoxicity and apoptotic mechanism of ruthenium(II) amino acid complexes in sarcoma-180 tumor cells","volume":"9","author":"Lima","year":"2014","journal-title":"PLoS ONE"},{"key":"10.1016\/j.actbio.2017.11.048_b0135","doi-asserted-by":"crossref","first-page":"4720","DOI":"10.1021\/ic902593e","article-title":"fac-{Ru(CO)3}2+ selectively targets the histidine residues of the \u03b2-amyloid peptide 1-28. Implications for new Alzheimer's disease treatments based on ruthenium complexes","volume":"49","author":"Valensin","year":"2010","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.actbio.2017.11.048_b0140","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.ejmech.2014.01.052","article-title":"Ruthenium(II) polypyridyl complex as inhibitor of acetylcholinesterase and A\u03b2 aggregation","volume":"75","author":"Vyas","year":"2014","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.actbio.2017.11.048_b0145","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1021\/cn100046m","article-title":"Rangachari, Inhibition of A\u03b242 peptide aggregation by a binuclear ruthenium(II)\u2212platinum(II) complex: potential for multimetal organometallics as anti-amyloid agents","volume":"1","author":"Kumar","year":"2010","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.actbio.2017.11.048_b0150","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/S0009-8981(03)00003-2","article-title":"Protein carbonyl groups as biomarkers of oxidative stress","volume":"329","author":"Dalle-Donne","year":"2003","journal-title":"Clinica Chimica Acta"},{"key":"10.1016\/j.actbio.2017.11.048_b0155","doi-asserted-by":"crossref","first-page":"5960","DOI":"10.1111\/j.1742-4658.2009.07307.x","article-title":"The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds","volume":"276","author":"Hudson","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.actbio.2017.11.048_b0160","doi-asserted-by":"crossref","first-page":"e96082","DOI":"10.1371\/journal.pone.0096082","article-title":"Synthesis, characterization, in vitro cytotoxicity, and apoptosis-inducing properties of ruthenium(II) complexes","volume":"9","author":"Xu","year":"2014","journal-title":"PLoS ONE"},{"key":"10.1016\/j.actbio.2017.11.048_b0165","doi-asserted-by":"crossref","first-page":"9298","DOI":"10.1021\/jp503282m","article-title":"Disaggregation ability of different chelating molecules on copper ion-triggered amyloid fibers","volume":"118","author":"Zhu","year":"2014","journal-title":"J. Phys. Chem. B."},{"key":"10.1016\/j.actbio.2017.11.048_b0170","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1126\/science.1853202","article-title":"Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition","volume":"253","author":"Barrow","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.actbio.2017.11.048_b0175","doi-asserted-by":"crossref","first-page":"12588","DOI":"10.1021\/la302626d","article-title":"Light-triggered disassembly of amyloid fibrils","volume":"28","author":"Measey","year":"2012","journal-title":"Langmuir"},{"key":"10.1016\/j.actbio.2017.11.048_b0180","doi-asserted-by":"crossref","first-page":"2788","DOI":"10.1073\/pnas.69.10.2788","article-title":"Intermolecular interaction effects in the amide I vibrations of \u03b2 polypeptides","volume":"69","author":"Krimm","year":"1972","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.actbio.2017.11.048_b0185","doi-asserted-by":"crossref","first-page":"20313","DOI":"10.1074\/jbc.272.33.20313","article-title":"Protein oxidation in aging, disease, and oxidative stress","volume":"272","author":"Berlett","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.actbio.2017.11.048_b0190","doi-asserted-by":"crossref","first-page":"2280","DOI":"10.1021\/acs.accounts.5b00227","article-title":"New Ru(II) complexes for dual photoreactivity: ligand exchange and 1O2 generation","volume":"48","author":"Knoll","year":"2015","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.actbio.2017.11.048_b0195","doi-asserted-by":"crossref","first-page":"1798","DOI":"10.1073\/pnas.0709501105","article-title":"Plasmonic engineering of singlet oxygen generation","volume":"105","author":"Zhang","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.actbio.2017.11.048_b0200","doi-asserted-by":"crossref","first-page":"2031","DOI":"10.1021\/ac061743r","article-title":"Oxidation artifacts in the electrospray mass spectrometry of A\u03b2 peptide","volume":"79","author":"Chen","year":"2007","journal-title":"Anal. Chem."},{"key":"10.1016\/j.actbio.2017.11.048_b0205","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1002\/rcm.1290050412","article-title":"Metastable decay of peptides and proteins in matrix-assisted laser-desorption mass spectrometry","volume":"5","author":"Spengler","year":"1991","journal-title":"Rapid Commun. Mass. Spectrom."},{"key":"10.1016\/j.actbio.2017.11.048_b0210","doi-asserted-by":"crossref","first-page":"604658","DOI":"10.1155\/2015\/604658","article-title":"The role of oxidative stress-induced epigenetic alterations in amyloid-\u03b2 production in Alzheimer's disease","volume":"2015","author":"Zuo","year":"2015","journal-title":"Oxid. Med. Cell. Longev."},{"key":"10.1016\/j.actbio.2017.11.048_b0215","doi-asserted-by":"crossref","first-page":"2411","DOI":"10.1007\/s12274-016-1127-5","article-title":"Platinum-coordinated graphitic carbon nitride nanosheet used for targeted inhibition of amyloid \u03b2-peptide aggregation","volume":"9","author":"Li","year":"2016","journal-title":"Nano Res."},{"key":"10.1016\/j.actbio.2017.11.048_b0220","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1002\/adma.201104864","article-title":"Using graphene oxide high near-infrared absorbance for photothermal treatment of Alzheimer's disease","volume":"24","author":"Li","year":"2012","journal-title":"Adv. Mater."},{"key":"10.1016\/j.actbio.2017.11.048_b0225","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1039\/c0md00075b","article-title":"Photo-degradation of amyloid \u03b2 by a designed fullerene\u2013sugar hybrid","volume":"1","author":"Ishida","year":"2010","journal-title":"Med. Chem. Commun."},{"key":"10.1016\/j.actbio.2017.11.048_b0230","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1042\/BJ20151227","article-title":"Davies, Protein oxidation and peroxidation","volume":"473","author":"Michael","year":"2016","journal-title":"Biochem. J."},{"key":"10.1016\/j.actbio.2017.11.048_b0235","doi-asserted-by":"crossref","first-page":"1992","DOI":"10.1021\/ja036813f","article-title":"Solution NMR studies of the A\u03b2(1\u201340) and A\u03b2(1\u201342) peptides establish that the met35 oxidation state affects the mechanism of amyloid formation","volume":"126","author":"Hou","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.actbio.2017.11.048_b0240","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1042\/BJ20120653","article-title":"Arancio, Is the amyloid hypothesis of Alzheimer's disease therapeutically relevant?","volume":"446","author":"Andrew","year":"2012","journal-title":"Biochem. J."},{"key":"10.1016\/j.actbio.2017.11.048_b0245","doi-asserted-by":"crossref","first-page":"1060","DOI":"10.1038\/nm.2460","article-title":"Resolving controversies on the path to Alzheimer's therapeutics","volume":"17","author":"Selkoe","year":"2011","journal-title":"Nat. Med."},{"key":"10.1016\/j.actbio.2017.11.048_b0250","doi-asserted-by":"crossref","first-page":"9146","DOI":"10.1021\/jm3003813","article-title":"Liberation of copper from amyloid plaques: making a risk factor useful for Alzheimer\u2019s disease treatment","volume":"55","author":"Geng","year":"2012","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.actbio.2017.11.048_b0255","doi-asserted-by":"crossref","first-page":"5110","DOI":"10.1002\/anie.201007824","article-title":"Inhibition of amyloid peptide fibrillation by inorganic nanoparticles: functional similarities with proteins","volume":"50","author":"Yoo","year":"2011","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.actbio.2017.11.048_b0260","doi-asserted-by":"crossref","first-page":"3231","DOI":"10.2174\/138161208786404137","article-title":"Amyloid \u03b2-protein assembly as a therapeutic target of Alzheimers disease","volume":"14","author":"Ghiam","year":"2008","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.actbio.2017.11.048_b0265","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nrm2101","article-title":"Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid \u03b2-peptide","volume":"8","author":"Haass","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.actbio.2017.11.048_b0270","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1021\/acschemneuro.6b00349","article-title":"Inhibition and degradation of amyloid beta (A\u03b240) fibrillation by designed small peptide: a combined spectroscopy, microscopy, and cell toxicity study","volume":"8","author":"Ghosh","year":"2017","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.actbio.2017.11.048_b0275","doi-asserted-by":"crossref","first-page":"1577","DOI":"10.1021\/acschemneuro.7b00080","article-title":"N-terminus binding preference for either tanshinone or analogue in both inhibition of amyloid aggregation and disaggregation of preformed amyloid fibrils\u2014toward introducing a kind of novel anti-Alzheimer compounds","volume":"8","author":"Dong","year":"2017","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.actbio.2017.11.048_b0280","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1039\/C6CC07803F","article-title":"The synergistic effect between KLVFF and self-assembly chaperones on both disaggregation of beta-amyloid fibrils and reducing consequent toxicity","volume":"53","author":"Qu","year":"2017","journal-title":"Chem. Commun."},{"key":"10.1016\/j.actbio.2017.11.048_b0285","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1111\/j.1748-1716.2007.01805.x","article-title":"The PC12 cell as model for neurosecretion","volume":"192","author":"Westerink","year":"2008","journal-title":"Acta Physiol."},{"key":"10.1016\/j.actbio.2017.11.048_b0290","doi-asserted-by":"crossref","first-page":"4184","DOI":"10.1002\/anie.201007067","article-title":"Polyoxometalates as inhibitors of the aggregation of amyloid \u03b2 peptides associated with Alzheimer\u2019s disease","volume":"50","author":"Geng","year":"2011","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.actbio.2017.11.048_b0295","doi-asserted-by":"crossref","first-page":"3422","DOI":"10.1038\/ncomms4422","article-title":"Transition-metal-substituted polyoxometalate derivatives as functional anti-amyloid agents for Alzheimer\u2019s disease","volume":"5","author":"Gao","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.actbio.2017.11.048_b0300","doi-asserted-by":"crossref","first-page":"3348","DOI":"10.1073\/pnas.0813355106","article-title":"Small molecule blockers of the Alzheimer A\u03b2 calcium channel potently protect neurons from A\u03b2 cytotoxicity","volume":"106","author":"Diaz","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.actbio.2017.11.048_b0305","doi-asserted-by":"crossref","first-page":"1820","DOI":"10.1038\/nprot.2008.182","article-title":"Methods for isolation, purification and structural elucidation of bioactive secondary metabolites from marine invertebrates","volume":"3","author":"Ebada","year":"2008","journal-title":"Nat. Protocols"},{"key":"10.1016\/j.actbio.2017.11.048_b0310","doi-asserted-by":"crossref","first-page":"7461","DOI":"10.1002\/anie.201402496","article-title":"Supramolecular inhibition of amyloid fibrillation by cucurbit[7]uril","volume":"53","author":"Lee","year":"2014","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.actbio.2017.11.048_b0315","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1038\/nrc2981","article-title":"Regulation of cancer cell metabolism","volume":"11","author":"Cairns","year":"2011","journal-title":"Nat. Rev. Cancer"}],"container-title":["Acta Biomaterialia"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1742706117307456?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1742706117307456?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T17:02:38Z","timestamp":1761670958000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1742706117307456"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,2]]},"references-count":63,"alternative-id":["S1742706117307456"],"URL":"https:\/\/doi.org\/10.1016\/j.actbio.2017.11.048","relation":{},"ISSN":["1742-7061"],"issn-type":[{"value":"1742-7061","type":"print"}],"subject":[],"published":{"date-parts":[[2018,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Light-triggered dissociation of self-assembled \u03b2-amyloid aggregates into small, nontoxic fragments by ruthenium (II) complex","name":"articletitle","label":"Article Title"},{"value":"Acta Biomaterialia","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.actbio.2017.11.048","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}