{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T16:01:26Z","timestamp":1789142486759,"version":"build-2803163510"},"reference-count":75,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100012310","name":"Alzahra University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100012310","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005317","name":"Kermanshah University of Medical Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005317","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Chemistry"],"published-print":{"date-parts":[[2021,2]]},"DOI":"10.1016\/j.bpc.2020.106522","type":"journal-article","created":{"date-parts":[[2020,12,16]],"date-time":"2020-12-16T03:50:56Z","timestamp":1608090656000},"page":"106522","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"special_numbering":"C","title":["Synthesis and in vitro quantification of amyloid fibrils by barbituric and thiobarbituric acid-based chromene derivatives"],"prefix":"10.1016","volume":"269","author":[{"given":"Seyyed Abolghasem","family":"Ghadami","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Setayesh","family":"Shevidi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leila","family":"Hosseinzadeh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2064-7875","authenticated-orcid":false,"given":"Hadi","family":"Adibi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"5","key":"10.1016\/j.bpc.2020.106522_bb0005","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1242\/dmm.030205","article-title":"Neurodegenerative disease: models, mechanisms, and a new hope","volume":"10","author":"Gitler","year":"2017","journal-title":"Dis. Model. Mech."},{"key":"10.1016\/j.bpc.2020.106522_bb0010","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.bpc.2020.106522_bb0015","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.pneurobio.2015.07.003","article-title":"Protein aggregation and neurodegeneration in prototypical neurodegenerative diseases: examples of amyloidopathies, tauopathies and synucleinopathies","volume":"155","author":"Bourdenx","year":"2017","journal-title":"Prog. Neurobiol."},{"issue":"12","key":"10.1016\/j.bpc.2020.106522_bb0020","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."},{"issue":"5","key":"10.1016\/j.bpc.2020.106522_bb0025","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1016\/j.semcdb.2011.03.011","article-title":"Amyloid in neurodegenerative diseases: friend or foe?","volume":"22","author":"Wolfe","year":"2011","journal-title":"Semin. Cell Dev. Biol."},{"issue":"7","key":"10.1016\/j.bpc.2020.106522_bb0030","doi-asserted-by":"crossref","first-page":"3595","DOI":"10.1021\/acsbiomaterials.9b00086","article-title":"Improving sensitivity and specificity of amyloid-\u03b2 peptides and tau protein detection with Antibiofouling magnetic nanoparticles for liquid biopsy of Alzheimer\u2019s disease","volume":"5","author":"Li","year":"2019","journal-title":"ACS Biomaterials Science & Engineering"},{"issue":"7","key":"10.1016\/j.bpc.2020.106522_bb0035","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1038\/s41569-020-0334-7","article-title":"Diagnostic imaging of cardiac amyloidosis","volume":"17","author":"Martinez-Naharro","year":"2020","journal-title":"Nat. Rev. Cardiol."},{"issue":"1","key":"10.1016\/j.bpc.2020.106522_bb0040","doi-asserted-by":"crossref","first-page":"23668","DOI":"10.1038\/srep23668","article-title":"A high affinity Red fluorescence and colorimetric probe for amyloid \u03b2 aggregates","volume":"6","author":"Rajasekhar","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bpc.2020.106522_bb0045","first-page":"39(1)","article-title":"Congo Red and amyloids: history and relationship","author":"Yakupova","year":"2019","journal-title":"Biosci. Rep."},{"issue":"7","key":"10.1016\/j.bpc.2020.106522_bb0050","doi-asserted-by":"crossref","first-page":"1584","DOI":"10.1039\/C6OB02760A","article-title":"A red-NIR emissive probe for the selective detection of albumin in urine samples and live cells","volume":"15","author":"Rajasekhar","year":"2017","journal-title":"Organic & Biomolecular Chemistry"},{"issue":"6","key":"10.1016\/j.bpc.2020.106522_bb0055","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.1007\/s13738-019-01599-1","article-title":"Detection\/quantification of amyloid aggregation in solution using the novel fluorescent benzofuranone-derivative compounds as amyloid fluorescent probes: synthesis and in vitro characterization","volume":"16","author":"Abbasbeigi","year":"2019","journal-title":"J. Iran. Chem. Soc."},{"issue":"2","key":"10.1016\/j.bpc.2020.106522_bb0060","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.bbrc.2006.03.024","article-title":"Mechanism of thioflavin T accumulation inside cells overexpressing P-glycoprotein or multidrug resistance-associated protein: role of lipophilicity and positive charge","volume":"343","author":"Darghal","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"4","key":"10.1016\/j.bpc.2020.106522_bb0065","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1007\/s00232-015-9778-9","article-title":"Permeability of the blood-brain barrier: molecular mechanism of transport of drugs and physiologically important compounds","volume":"248","author":"Fong","year":"2015","journal-title":"J. Membr. Biol."},{"issue":"3","key":"10.1016\/j.bpc.2020.106522_bb0070","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1002\/pro.5560020312","article-title":"Thioflavine T interaction with synthetic Alzheimer\u2019s disease beta-amyloid peptides: detection of amyloid aggregation in solution","volume":"2","author":"LeVine","year":"1993","journal-title":"Protein Sci."},{"issue":"2\u20133","key":"10.1016\/j.bpc.2020.106522_bb0075","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.bpc.2011.08.004","article-title":"Amyloid fibril formation by native and modified bovine beta-lactoglobulins proceeds through unfolded form of proteins: a comparative study","volume":"159","author":"Ghadami","year":"2011","journal-title":"Biophys. Chem."},{"issue":"20","key":"10.1016\/j.bpc.2020.106522_bb0080","doi-asserted-by":"crossref","first-page":"21449","DOI":"10.1074\/jbc.M314141200","article-title":"Mechanism of insulin fibrillation: the structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate","volume":"279","author":"Hua","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.bpc.2020.106522_bb0085","doi-asserted-by":"crossref","first-page":"2411","DOI":"10.1002\/pro.5560041120","article-title":"How to measure and predict the molar absorption coefficient of a protein","volume":"4","author":"Pace","year":"1995","journal-title":"Protein Sci."},{"issue":"4","key":"10.1016\/j.bpc.2020.106522_bb0090","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1007\/BF00124499","article-title":"Distributed automated docking of flexible ligands to proteins: parallel applications of AutoDock 2.4","volume":"10","author":"Morris","year":"1996","journal-title":"J. Comput. Aided Mol. Des."},{"issue":"10","key":"10.1016\/j.bpc.2020.106522_bb0095","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1021\/ed100362d","article-title":"Technology for the Organic Chemist: three exploratory modules","volume":"87","author":"Esteb","year":"2010","journal-title":"J. Chem. Educ."},{"issue":"1","key":"10.1016\/j.bpc.2020.106522_bb0100","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/1758-2946-4-17","article-title":"Avogadro: an advanced semantic chemical editor, visualization, and analysis platform","volume":"4","author":"Hanwell","year":"2012","journal-title":"J Cheminform"},{"issue":"14","key":"10.1016\/j.bpc.2020.106522_bb0105","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.1002\/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B","article-title":"Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function","volume":"19","author":"Morris","year":"1998","journal-title":"J. Comput. Chem."},{"issue":"58","key":"10.1016\/j.bpc.2020.106522_bb0110","doi-asserted-by":"crossref","first-page":"11665","DOI":"10.1039\/C5CC03662C","article-title":"The synthesis and evaluation of near-infrared probes with barbituric acid acceptors for in vivo detection of amyloid plaques","volume":"51","author":"Zhou","year":"2015","journal-title":"Chem Commun (Camb)"},{"key":"10.1016\/j.bpc.2020.106522_bb0115","first-page":"25(1)","article-title":"Barbituric Acid Based Fluorogens: Synthesis, Aggregation-Induced Emission, and Protein Fibril Detection","author":"Ding","year":"2019","journal-title":"Molecules"},{"issue":"10","key":"10.1016\/j.bpc.2020.106522_bb0120","doi-asserted-by":"crossref","first-page":"1801","DOI":"10.1039\/c3tc32161d","article-title":"Twisted intramolecular charge transfer, aggregation-induced emission, supramolecular self-assembly and the optical waveguide of barbituric acid-functionalized tetraphenylethene","volume":"2","author":"Wang","year":"2014","journal-title":"J. Mater. Chem. C"},{"issue":"48","key":"10.1016\/j.bpc.2020.106522_bb0125","doi-asserted-by":"crossref","first-page":"30229","DOI":"10.1039\/C7RA03956E","article-title":"Facile fabrication of AIE\/AIEE-active fluorescent nanoparticles based on barbituric for cell imaging applications","volume":"7","author":"Li","year":"2017","journal-title":"RSC Adv."},{"key":"10.1016\/j.bpc.2020.106522_bb0130","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.btre.2016.01.002","article-title":"Role of pH-induced structural change in protein aggregation in foam fractionation of bovine serum albumin","volume":"9","author":"Li","year":"2016","journal-title":"Biotechnology Reports"},{"issue":"2","key":"10.1016\/j.bpc.2020.106522_bb0135","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.bpc.2003.09.004","article-title":"Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering","volume":"107","author":"Militello","year":"2004","journal-title":"Biophys. Chem."},{"issue":"12","key":"10.1016\/j.bpc.2020.106522_bb0140","doi-asserted-by":"crossref","first-page":"2349","DOI":"10.1002\/bip.360251212","article-title":"Helix \u2192 \u03b2 conformational transition of poly(L-lysine) on dye binding","volume":"25","author":"Scaria","year":"1986","journal-title":"Biopolymers"},{"issue":"1","key":"10.1016\/j.bpc.2020.106522_bb0145","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.jsb.2004.08.002","article-title":"The binding of thioflavin-T to amyloid fibrils: localisation and implications","volume":"149","author":"Krebs","year":"2005","journal-title":"J. Struct. Biol."},{"issue":"1","key":"10.1016\/j.bpc.2020.106522_bb0150","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/s00044-012-0012-3","article-title":"Synthesis and in vitro characterization of some benzothiazole- and benzofuranone-derivatives for quantification of fibrillar aggregates and inhibition of amyloid-mediated peroxidase activity","volume":"22","author":"Ghadami","year":"2013","journal-title":"Med. Chem. Res."},{"issue":"13","key":"10.1016\/j.bpc.2020.106522_bb0155","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.1016\/S0024-3205(01)01232-2","article-title":"Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain","volume":"69","author":"Klunk","year":"2001","journal-title":"Life Sci."},{"issue":"4","key":"10.1016\/j.bpc.2020.106522_bb0160","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1016\/j.jmb.2008.11.006","article-title":"Molecular mechanism of thioflavin-T binding to the surface of beta-rich peptide self-assemblies","volume":"385","author":"Biancalana","year":"2009","journal-title":"J. Mol. Biol."},{"issue":"38","key":"10.1016\/j.bpc.2020.106522_bb0165","doi-asserted-by":"crossref","first-page":"11220","DOI":"10.1021\/jp506258g","article-title":"Interactions between amyloid-\u03b2 and tau fragments promote aberrant aggregates: implications for amyloid toxicity","volume":"118","author":"Do","year":"2014","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bpc.2020.106522_bb0170","doi-asserted-by":"crossref","first-page":"106421","DOI":"10.1016\/j.bpc.2020.106421","article-title":"Structures of the intrinsically disordered A\u03b2, tau and \u03b1-synuclein proteins in aqueous solution from computer simulations","volume":"264","author":"Nguyen","year":"2020","journal-title":"Biophys. Chem."},{"issue":"7","key":"10.1016\/j.bpc.2020.106522_bb0175","first-page":"1405","article-title":"Molecular mechanism of Thioflavin-T binding to amyloid fibrils. Biochimica et Biophysica Acta (BBA)-proteins and","volume":"1804","author":"Biancalana","year":"2010","journal-title":"Proteomics"},{"key":"10.1016\/j.bpc.2020.106522_bb0180","first-page":"106507","article-title":"Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology","author":"Ivanova","year":"2020","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2020.106522_bb0185","first-page":"19(9)","article-title":"Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms","author":"Giorgetti","year":"2018","journal-title":"Int. J. Mol. Sci."},{"issue":"3","key":"10.1016\/j.bpc.2020.106522_bb0190","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1007\/s13311-013-0192-7","article-title":"Natural compounds may open new routes to treatment of amyloid diseases","volume":"10","author":"Bieschke","year":"2013","journal-title":"Neurotherapeutics"},{"issue":"2\u20133","key":"10.1016\/j.bpc.2020.106522_bb0195","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1006\/jsbi.2000.4221","article-title":"History of the amyloid fibril","volume":"130","author":"Sipe","year":"2000","journal-title":"J. Struct. Biol."},{"issue":"3","key":"10.1016\/j.bpc.2020.106522_bb0200","doi-asserted-by":"crossref","first-page":"241","DOI":"10.31887\/DCNS.2000.2.3\/gsmall","article-title":"Early diagnosis of Alzheimer\u2019s disease: update on combining genetic and brain-imaging measures","volume":"2","author":"Small","year":"2000","journal-title":"Dialogues Clin. Neurosci."},{"issue":"Suppl. 1","key":"10.1016\/j.bpc.2020.106522_bb0205","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1007\/s40120-017-0074-8","article-title":"Amyloid Beta and tau as Alzheimer\u2019s disease blood biomarkers: promise from new technologies","volume":"6","author":"Lue","year":"2017","journal-title":"Neurology and therapy"},{"key":"10.1016\/j.bpc.2020.106522_bb0210","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1016\/j.dadm.2019.05.007","article-title":"Plasma amyloid beta levels are associated with cerebral amyloid and tau deposition","volume":"11","author":"Risacher","year":"2019","journal-title":"Alzheimer's & dementia Amsterdam, Netherlands"},{"issue":"35","key":"10.1016\/j.bpc.2020.106522_bb0215","doi-asserted-by":"crossref","first-page":"11560","DOI":"10.1021\/acs.jpcb.5b05964","article-title":"Investigation of the binding profiles of AZD2184 and Thioflavin T with amyloid-\u03b2(1\u201342) fibril by molecular docking and molecular dynamics methods","volume":"119","author":"Kuang","year":"2015","journal-title":"J. Phys. Chem. B"},{"issue":"3","key":"10.1016\/j.bpc.2020.106522_bb0220","first-page":"232","article-title":"Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods","volume":"31","author":"Cooper","year":"1974","journal-title":"Lab. Investig."},{"issue":"26","key":"10.1016\/j.bpc.2020.106522_bb0225","doi-asserted-by":"crossref","first-page":"15294","DOI":"10.1073\/pnas.2534647100","article-title":"Imaging linear birefringence and dichroism in cerebral amyloid pathologies","volume":"100","author":"Jin","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"5","key":"10.1016\/j.bpc.2020.106522_bb0230","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.jbbm.2007.03.008","article-title":"Cyanine dye-protein interactions: looking for fluorescent probes for amyloid structures","volume":"70","author":"Volkova","year":"2007","journal-title":"J. Biochem. Biophys. Methods"},{"key":"10.1016\/j.bpc.2020.106522_bb0235","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.bios.2017.06.030","article-title":"A\u03b2 plaque-selective NIR fluorescence probe to differentiate Alzheimer\u2019s disease from tauopathies","volume":"98","author":"Rajasekhar","year":"2017","journal-title":"Biosens. Bioelectron."},{"issue":"1","key":"10.1016\/j.bpc.2020.106522_bb0240","first-page":"1","article-title":"Design, synthesis and biological evaluation of a series of CNS penetrant HDAC inhibitors structurally derived from amyloid-\u03b2 probes","volume":"9","author":"Choi","year":"2019","journal-title":"Sci. Rep."},{"issue":"12","key":"10.1016\/j.bpc.2020.106522_bb0245","doi-asserted-by":"crossref","first-page":"4847","DOI":"10.1021\/acschemneuro.9b00554","article-title":"Unambiguous detection of elevated levels of Hypochlorous acid in double transgenic AD mouse brain","volume":"10","author":"Samanta","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.bpc.2020.106522_bb0250","doi-asserted-by":"crossref","first-page":"106391","DOI":"10.1016\/j.bpc.2020.106391","article-title":"Avenanthramide-C prevents amyloid formation of bovine serum albumin","author":"Vazquez","year":"2020","journal-title":"Biophys. Chem."},{"issue":"1","key":"10.1016\/j.bpc.2020.106522_bb0255","doi-asserted-by":"crossref","first-page":"13324","DOI":"10.1038\/s41598-020-70208-6","article-title":"Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein","volume":"10","author":"Majewski","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bpc.2020.106522_bb0260","first-page":"106505","article-title":"Visualizing and trapping transient oligomers in amyloid assembly pathways","author":"Cawood","year":"2020","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2020.106522_bb0265","doi-asserted-by":"crossref","first-page":"106272","DOI":"10.1016\/j.bpc.2019.106272","article-title":"GM1 Ganglioside role in the interaction of alpha-synuclein with lipid membranes: morphology and structure","volume":"255","author":"Perissinotto","year":"2019","journal-title":"Biophys. Chem."},{"issue":"19","key":"10.1016\/j.bpc.2020.106522_bb0270","doi-asserted-by":"crossref","first-page":"6692","DOI":"10.1039\/C3CS60431D","article-title":"Differences between amyloid-\u03b2 aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer\u2019s disease","volume":"43","author":"Kotler","year":"2014","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.bpc.2020.106522_bb0275","doi-asserted-by":"crossref","first-page":"110615","DOI":"10.1016\/j.colsurfb.2019.110615","article-title":"Kinetic study of Abeta(1-42) amyloidosis in the presence of ganglioside-containing vesicles","volume":"185","author":"Dai","year":"2020","journal-title":"Colloids Surf B Biointerfaces"},{"issue":"28","key":"10.1016\/j.bpc.2020.106522_bb0280","doi-asserted-by":"crossref","first-page":"5837","DOI":"10.1021\/acs.jpcb.0c03796","article-title":"Nanoscale interplay of membrane composition and amyloid self-assembly","volume":"124","author":"Menon","year":"2020","journal-title":"J. Phys. Chem. B"},{"issue":"3","key":"10.1016\/j.bpc.2020.106522_bb0285","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."},{"issue":"6880","key":"10.1016\/j.bpc.2020.106522_bb0290","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/416507a","article-title":"Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases","volume":"416","author":"Bucciantini","year":"2002","journal-title":"nature"},{"key":"10.1016\/j.bpc.2020.106522_bb0295","doi-asserted-by":"crossref","first-page":"106434","DOI":"10.1016\/j.bpc.2020.106434","article-title":"Modulating A\u03b2 aggregation by tyrosol-based ligands: the crucial role of the catechol moiety","volume":"265","author":"Romanucci","year":"2020","journal-title":"Biophys. Chem."},{"issue":"31","key":"10.1016\/j.bpc.2020.106522_bb0300","doi-asserted-by":"crossref","first-page":"12479","DOI":"10.1073\/pnas.1117799109","article-title":"Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers","volume":"109","author":"Mannini","year":"2012","journal-title":"Proc. Natl. Acad. Sci."},{"issue":"15","key":"10.1016\/j.bpc.2020.106522_bb0305","doi-asserted-by":"crossref","first-page":"3146","DOI":"10.1128\/MCB.01187-10","article-title":"Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism","volume":"31","author":"Ojha","year":"2011","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bpc.2020.106522_bb0310","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.bpc.2018.02.002","article-title":"Ac-LVFFARK-NH2 conjugation to \u03b2-cyclodextrin exhibits significantly enhanced performance on inhibiting amyloid \u03b2-protein fibrillogenesis and cytotoxicity","volume":"235","author":"Zhang","year":"2018","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2020.106522_bb0315","series-title":"Proteins Membrane Binding and Pore Formation","first-page":"150","article-title":"Amyloid peptide pores and the beta sheet conformation","author":"Kagan","year":"2010"},{"issue":"18","key":"10.1016\/j.bpc.2020.106522_bb0320","doi-asserted-by":"crossref","first-page":"7226","DOI":"10.1523\/JNEUROSCI.21-18-07226.2001","article-title":"A novel action of Alzheimer\u2019s amyloid \u03b2-protein (A\u03b2): oligomeric A\u03b2 promotes lipid release","volume":"21","author":"Michikawa","year":"2001","journal-title":"J. Neurosci."},{"issue":"3","key":"10.1016\/j.bpc.2020.106522_bb0325","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1016\/S0006-3495(01)76109-7","article-title":"Amyloid-\u03b2 peptide assembly: a critical step in fibrillogenesis and membrane disruption","volume":"80","author":"Yip","year":"2001","journal-title":"Biophys. J."},{"issue":"45","key":"10.1016\/j.bpc.2020.106522_bb0330","doi-asserted-by":"crossref","first-page":"10293","DOI":"10.1021\/acs.jpcb.7b07002","article-title":"Membrane binding and pore formation by a cytotoxic fragment of amyloid \u03b2 peptide","volume":"121","author":"Kandel","year":"2017","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bpc.2020.106522_bb0335","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.bpc.2013.07.002","article-title":"A micro-environmental study of the Zn+ 2\u2013A\u03b21\u201316 structural properties","volume":"182","author":"Maiorana","year":"2013","journal-title":"Biophys. Chem."},{"issue":"4","key":"10.1016\/j.bpc.2020.106522_bb0340","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1246\/bcsj.20190356","article-title":"Molecular tools to detect Alloforms of A\u03b2 and tau: implications for multiplexing and multimodal diagnosis of Alzheimer\u2019s disease","volume":"93","author":"Arora","year":"2020","journal-title":"Bull. Chem. Soc. Jpn."},{"issue":"70","key":"10.1016\/j.bpc.2020.106522_bb0345","doi-asserted-by":"crossref","first-page":"13434","DOI":"10.1039\/C5CC05264E","article-title":"Function and toxicity of amyloid beta and recent therapeutic interventions targeting amyloid beta in Alzheimer\u2019s disease","volume":"51","author":"Rajasekhar","year":"2015","journal-title":"Chem. Commun."},{"issue":"42","key":"10.1016\/j.bpc.2020.106522_bb0350","doi-asserted-by":"crossref","first-page":"23780","DOI":"10.1039\/C8RA03620A","article-title":"Current progress, challenges and future prospects of diagnostic and therapeutic interventions in Alzheimer\u2019s disease","volume":"8","author":"Rajasekhar","year":"2018","journal-title":"RSC Adv."},{"issue":"2","key":"10.1016\/j.bpc.2020.106522_bb0355","doi-asserted-by":"crossref","first-page":"135","DOI":"10.31887\/DCNS.2009.11.2\/bdubois","article-title":"Early detection of Alzheimer\u2019s disease: new diagnostic criteria","volume":"11","author":"Dubois","year":"2009","journal-title":"Dialogues Clin. Neurosci."},{"issue":"1","key":"10.1016\/j.bpc.2020.106522_bb0360","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0301-4622(01)00155-7","article-title":"Effects of intermediates on aggregation of native bovine serum albumin","volume":"91","author":"Bulone","year":"2001","journal-title":"Biophys. Chem."},{"issue":"8","key":"10.1016\/j.bpc.2020.106522_bb0365","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1002\/ddr.21368","article-title":"Psychotropic drug development strategies that target neuropsychiatric Etiologies in Alzheimer\u2019s and Parkinson\u2019s diseases","volume":"77","author":"Van der Schyf","year":"2016","journal-title":"Drug Dev. Res."},{"key":"10.1016\/j.bpc.2020.106522_bb0370","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.bpc.2018.02.005","article-title":"Inhibition of amyloid fibrillation of lysozyme by bisdemethoxycurcumin and diacetylbisdemethoxycurcumin","volume":"235","author":"Mohammadi","year":"2018","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bpc.2020.106522_bb0375","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.ejmech.2015.02.055","article-title":"Blood\u2013brain barrier permeable anticholinesterase aurones: synthesis, structure\u2013activity relationship, and drug-like properties","volume":"94","author":"Liew","year":"2015","journal-title":"Eur. J. Med. Chem."}],"container-title":["Biophysical Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462220302301?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462220302301?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T07:57:58Z","timestamp":1759564678000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0301462220302301"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,2]]},"references-count":75,"alternative-id":["S0301462220302301"],"URL":"https:\/\/doi.org\/10.1016\/j.bpc.2020.106522","relation":{},"ISSN":["0301-4622"],"issn-type":[{"value":"0301-4622","type":"print"}],"subject":[],"published":{"date-parts":[[2021,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Synthesis and in vitro quantification of amyloid fibrils by barbituric and thiobarbituric acid-based chromene derivatives","name":"articletitle","label":"Article Title"},{"value":"Biophysical Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpc.2020.106522","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"106522"}}