{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,31]],"date-time":"2026-10-31T05:04:29Z","timestamp":1793423069335,"version":"4.5.0"},"reference-count":71,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,8,29]],"date-time":"2023-08-29T00:00:00Z","timestamp":1693267200000},"content-version":"am","delay-in-days":332,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Pharmacological Research"],"published-print":{"date-parts":[[2022,10]]},"DOI":"10.1016\/j.phrs.2022.106409","type":"journal-article","created":{"date-parts":[[2022,8,19]],"date-time":"2022-08-19T22:12:03Z","timestamp":1660947123000},"page":"106409","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":19,"special_numbering":"C","title":["Catechol-containing compounds are a broad class of protein aggregation inhibitors: Redox state is a key determinant of the inhibitory activities"],"prefix":"10.1016","volume":"184","author":[{"given":"Paul","family":"Velander","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ling","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sherry B.","family":"Hildreth","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nancy J.","family":"Vogelaar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Biswarup","family":"Mukhopadhyay","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard F.","family":"Helm","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shijun","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bin","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.phrs.2022.106409_bib1","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1152\/physrev.00042.2009","article-title":"Islet amyloid polypeptide, islet amyloid, and diabetes mellitus","volume":"91","author":"Westermark","year":"2011","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.phrs.2022.106409_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.phrs.2022.106409_bib3","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein misfolding, functional amyloid, 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.phrs.2022.106409_bib4","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1038\/s41467-018-08130-9","article-title":"Early preclinical detection of prions in the skin of prion-infected animals","volume":"10","author":"Wang","year":"2019","journal-title":"Nat. Commun."},{"issue":"4","key":"10.1016\/j.phrs.2022.106409_bib5","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1021\/acsptsci.1c00028","article-title":"Rosmarinic acid potently detoxifies amylin amyloid and ameliorates diabetic pathology in a transgenic rat model of type 2 diabetes","volume":"4","author":"Wu","year":"2021","journal-title":"ACS Pharm. Transl. Sci."},{"key":"10.1016\/j.phrs.2022.106409_bib6","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1016\/j.cell.2012.02.022","article-title":"The amyloid state of proteins in human diseases","volume":"148","author":"Eisenberg","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.phrs.2022.106409_bib7","doi-asserted-by":"crossref","first-page":"595","DOI":"10.15252\/emmm.201606210","article-title":"The amyloid hypothesis of Alzheimer's disease at 25 years","volume":"8","author":"Selkoe","year":"2016","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.phrs.2022.106409_bib8","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1038\/nrd.2017.155","article-title":"Tau-based therapies in neurodegeneration: opportunities and challenges","volume":"16","author":"Li","year":"2017","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.phrs.2022.106409_bib9","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nature23002","article-title":"Cryo-EM structures of tau filaments from Alzheimer's disease","volume":"547","author":"Fitzpatrick","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.phrs.2022.106409_bib10","first-page":"6","article-title":"Atomic structures of fibrillar segments of hIAPP suggest tightly mated \u03b2-sheets are important for cytotoxicity","author":"Krotee","year":"2017","journal-title":"Elife"},{"key":"10.1016\/j.phrs.2022.106409_bib11","article-title":"Atomic structures of fibrillar segments of hIAPP suggest tightly mated \u03b2-sheets are important for cytotoxicity","author":"Li","year":"2017","journal-title":"Elife"},{"key":"10.1016\/j.phrs.2022.106409_bib12","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1038\/nchem.2889","article-title":"Structure-based inhibitors of tau aggregation","volume":"10","author":"Seidler","year":"2018","journal-title":"Nat. Chem."},{"key":"10.1016\/j.phrs.2022.106409_bib13","doi-asserted-by":"crossref","first-page":"14503","DOI":"10.1002\/anie.201802979","article-title":"Designed macrocyclic peptides as nanomolar amyloid inhibitors based on minimal recognition elements","volume":"57","author":"Spanopoulou","year":"2018","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.phrs.2022.106409_bib14","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.46924","article-title":"Structure-based inhibitors of amyloid beta core suggest a common interface with tau","volume":"8","author":"Griner","year":"2019","journal-title":"Elife"},{"key":"10.1016\/j.phrs.2022.106409_bib15","doi-asserted-by":"crossref","first-page":"12837","DOI":"10.1002\/anie.202000148","article-title":"The human host-defense peptide cathelicidin LL-37 is a nanomolar inhibitor of amyloid self-assembly of islet amyloid polypeptide (IAPP)","volume":"59","author":"Armiento","year":"2020","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.phrs.2022.106409_bib16","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.bcp.2017.04.004","article-title":"Natural product-based amyloid inhibitors","volume":"139","author":"Velander","year":"2017","journal-title":"Biochem Pharm."},{"key":"10.1016\/j.phrs.2022.106409_bib17","doi-asserted-by":"crossref","first-page":"3372","DOI":"10.1002\/anie.201906908","article-title":"Peptide-based molecular strategies to interfere with protein misfolding, aggregation, and cell degeneration","volume":"59","author":"Armiento","year":"2020","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.phrs.2022.106409_bib18","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.jmb.2011.12.060","article-title":"The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug","volume":"421","author":"Johnson","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.phrs.2022.106409_bib19","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1038\/nsmb.1437","article-title":"EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers","volume":"15","author":"Ehrnhoefer","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.phrs.2022.106409_bib20","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.jmb.2008.08.039","article-title":"Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein","volume":"383","author":"Hong","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.phrs.2022.106409_bib21","doi-asserted-by":"crossref","first-page":"7710","DOI":"10.1073\/pnas.0910723107","article-title":"EGCG remodels mature \u03b1-synuclein and amyloid-\u03b2 fibrils and reduces cellular toxicity","volume":"107","author":"Bieschke","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.phrs.2022.106409_bib22","doi-asserted-by":"crossref","first-page":"28511","DOI":"10.1038\/srep28511","article-title":"Effect of curcumin analogs on alpha-synuclein aggregation and cytotoxicity","volume":"6","author":"Jha","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.phrs.2022.106409_bib23","doi-asserted-by":"crossref","first-page":"2670","DOI":"10.1021\/bi2015162","article-title":"Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols","volume":"51","author":"Cao","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.phrs.2022.106409_bib24","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.10935","article-title":"Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain","volume":"4","author":"Brumshtein","year":"2015","journal-title":"Elife"},{"key":"10.1016\/j.phrs.2022.106409_bib25","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/S1474-4422(13)70090-5","article-title":"Tau pathology and neurodegeneration","volume":"12","author":"Spillantini","year":"2013","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.phrs.2022.106409_bib26","doi-asserted-by":"crossref","first-page":"3492","DOI":"10.1073\/pnas.93.8.3492","article-title":"Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide","volume":"93","author":"Verchere","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.phrs.2022.106409_bib27","doi-asserted-by":"crossref","first-page":"4255","DOI":"10.1021\/acs.biochem.6b00578","article-title":"Amylin amyloid inhibition by flavonoid baicalein: key roles of its vicinal dihydroxyl groups of the catechol moiety","volume":"55","author":"Velander","year":"2016","journal-title":"Biochemistry"},{"key":"10.1016\/j.phrs.2022.106409_bib28","doi-asserted-by":"crossref","first-page":"5035","DOI":"10.1021\/acs.biochem.7b00199","article-title":"Olive component oleuropein promotes beta-cell insulin secretion and protects beta-cells from amylin amyloid-induced cytotoxicity","volume":"56","author":"Wu","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.phrs.2022.106409_bib29","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2022.945875","article-title":"Selective detection of misfolded tau from post-mortem Alzheimer\u2019s diease brains","volume":"14","author":"Wu","year":"2022","journal-title":"Front Aging Neurosci."},{"key":"10.1016\/j.phrs.2022.106409_bib30","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1016\/j.febslet.2011.03.046","article-title":"Inhibition and disaggregation of a-synuclein oligomers by natural polyphenolic compounds","volume":"585","author":"Caruana","year":"2011","journal-title":"FEBS Lett."},{"key":"10.1016\/j.phrs.2022.106409_bib31","doi-asserted-by":"crossref","first-page":"23212","DOI":"10.1074\/jbc.M113.464222","article-title":"Site-specific inhibitory mechanism for amyloid beta42 aggregation by catechol-type flavonoids targeting the Lys residues","volume":"288","author":"Sato","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2022.106409_bib32","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1021\/acscombsci.5b00129","article-title":"Method of creating small-molecule libraries to target the aggregation of intrinsically disordered proteins","volume":"18","author":"Joshi","year":"2016","journal-title":"ACS Comb. Sci."},{"key":"10.1016\/j.phrs.2022.106409_bib33","doi-asserted-by":"crossref","first-page":"3628","DOI":"10.1074\/jbc.M410984200","article-title":"Anthraquinones inhibit tau aggregation and dissolve Alzheimer's paired helical filaments in vitro and in cells","volume":"280","author":"Pickhardt","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2022.106409_bib34","doi-asserted-by":"crossref","first-page":"5648","DOI":"10.1038\/srep05648","article-title":"Effects of several quinones on insulin aggregation","volume":"4","author":"Gong","year":"2014","journal-title":"Sci. Rep."},{"key":"10.1016\/j.phrs.2022.106409_bib35","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1016\/S0014-5793(00)02380-2","article-title":"Anti-amyloidogenic activity of tetracyclines: studies in vitro","volume":"487","author":"Forloni","year":"2001","journal-title":"FEBS Lett."},{"key":"10.1016\/j.phrs.2022.106409_bib36","doi-asserted-by":"crossref","first-page":"2121","DOI":"10.1074\/jbc.M110.178376","article-title":"Effect of tetracyclines on the dynamics of formation and destructuration of beta2-microglobulin amyloid fibrils","volume":"286","author":"Giorgetti","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2022.106409_bib37","doi-asserted-by":"crossref","DOI":"10.1098\/rsos.160696","article-title":"Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation","volume":"4","author":"Xue","year":"2017","journal-title":"R. Soc. Open Sci."},{"key":"10.1016\/j.phrs.2022.106409_bib38","doi-asserted-by":"crossref","first-page":"7732","DOI":"10.1021\/bi9006435","article-title":"Identification of aminothienopyridazine inhibitors of tau assembly by quantitative high-throughput screening","volume":"48","author":"Crowe","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.phrs.2022.106409_bib39","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1002\/pro.2023","article-title":"Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers","volume":"21","author":"Noor","year":"2012","journal-title":"Protein Sci."},{"key":"10.1016\/j.phrs.2022.106409_bib40","doi-asserted-by":"crossref","first-page":"7503","DOI":"10.1021\/ja3115696","article-title":"Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils","volume":"135","author":"Palhano","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.phrs.2022.106409_bib41","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1093\/ilar.47.3.225","article-title":"Islet amyloid polypeptide (IAPP) transgenic rodents as models for type 2 diabetes","volume":"47","author":"Matveyenko","year":"2006","journal-title":"ILAR J."},{"key":"10.1016\/j.phrs.2022.106409_bib42","doi-asserted-by":"crossref","first-page":"2106","DOI":"10.2337\/db05-1672","article-title":"Beta-cell deficit due to increased apoptosis in the human islet amyloid polypeptide transgenic (HIP) rat recapitulates the metabolic defects present in type 2 diabetes","volume":"55","author":"Matveyenko","year":"2006","journal-title":"Diabetes"},{"key":"10.1016\/j.phrs.2022.106409_bib43","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1002\/ana.24992","article-title":"Brain microvascular injury and white matter disease provoked by diabetes-associated hyperamylinemia","volume":"82","author":"Ly","year":"2017","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.phrs.2022.106409_bib44","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.2337\/diabetes.53.6.1509","article-title":"Diabetes due to a progressive defect in beta-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): a new model for type 2 diabetes","volume":"53","author":"Butler","year":"2004","journal-title":"Diabetes"},{"key":"10.1016\/j.phrs.2022.106409_bib45","doi-asserted-by":"crossref","first-page":"2557","DOI":"10.2353\/ajpath.2009.090417","article-title":"Phenolic compounds prevent Alzheimer\u2019s pathology through different effects on the amyloid-beta aggregation pathway","volume":"175","author":"Hamaguchi","year":"2009","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.phrs.2022.106409_bib46","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1186\/1750-1326-9-30","article-title":"Neuroinflammation and neurologic deficits in diabetes linked to brain accumulation of amylin","volume":"9","author":"Srodulski","year":"2014","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.phrs.2022.106409_bib47","doi-asserted-by":"crossref","first-page":"3689","DOI":"10.1016\/0006-2952(84)90158-8","article-title":"Kinetic study and intermediates identification of noradrenaline oxidation by tyrosinase","volume":"33","author":"Jimenez","year":"1984","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.phrs.2022.106409_bib48","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1021\/tx700254q","article-title":"Oxidation chemistry of norepinephrine: partitioning of the O-quinone between competing cyclization and chain breakdown pathways and their roles in melanin formation","volume":"20","author":"Manini","year":"2007","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.phrs.2022.106409_bib49","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1096\/fj.03-0770fje","article-title":"Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease","volume":"18","author":"Li","year":"2004","journal-title":"FASEB J."},{"key":"10.1016\/j.phrs.2022.106409_bib50","doi-asserted-by":"crossref","first-page":"10216","DOI":"10.1038\/ncomms10216","article-title":"Toxic tau oligomer formation blocked by capping of cysteine residues with 1,2-dihydroxybenzene groups","volume":"6","author":"Soeda","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.phrs.2022.106409_bib51","series-title":"Laboratory Tests and Diagnostic Procedures","first-page":"302","article-title":"Catecholamines - plasma","author":"Chernecky","year":"2013"},{"key":"10.1016\/j.phrs.2022.106409_bib52","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1021\/cn300158p","article-title":"Chemical gradients within brain extracellular space measured using low flow push-pull perfusion sampling in vivo","volume":"4","author":"Slaney","year":"2013","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.phrs.2022.106409_bib53","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1002\/jnr.20602","article-title":"Variations in extracellular levels of dopamine, noradrenaline, glutamate, and aspartate across the sleep--wake cycle in the medial prefrontal cortex and nucleus accumbens of freely moving rats","volume":"81","author":"L\u00e9na","year":"2005","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.phrs.2022.106409_bib54","doi-asserted-by":"crossref","first-page":"8206","DOI":"10.1021\/bi900506b","article-title":"Molecular mechanisms underlying the flavonoid-induced inhibition of alpha-synuclein fibrillation","volume":"48","author":"Meng","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.phrs.2022.106409_bib55","doi-asserted-by":"crossref","first-page":"26846","DOI":"10.1074\/jbc.M403129200","article-title":"The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils","volume":"279","author":"Zhu","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2022.106409_bib56","doi-asserted-by":"crossref","first-page":"3650","DOI":"10.1021\/jp2121577","article-title":"Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286)","volume":"116","author":"Popovych","year":"2012","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.phrs.2022.106409_bib57","doi-asserted-by":"crossref","first-page":"14631","DOI":"10.1074\/jbc.M111.325456","article-title":"Phenolic compounds prevent amyloid \u03b2-protein oligomerization and synaptic dysfunction by site-specific binding","volume":"287","author":"Ono","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2022.106409_bib58","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/978-3-319-18365-7_4","article-title":"Natural phenolic compounds as therapeutic and preventive agents for cerebral amyloidosis","volume":"863","author":"Yamada","year":"2015","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.phrs.2022.106409_bib59","doi-asserted-by":"crossref","first-page":"2719","DOI":"10.1021\/jm901137j","article-title":"New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays","volume":"53","author":"Baell","year":"2010","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.phrs.2022.106409_bib60","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1021\/acs.jnatprod.5b00947","article-title":"Feeling nature's PAINS: natural products, natural product drugs, and pan assay interference compounds (PAINS)","volume":"79","author":"Baell","year":"2016","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.phrs.2022.106409_bib61","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1021\/acschembio.7b00903","article-title":"Seven year itch: pan-assay interference compounds (PAINS) in 2017-utility and limitations","volume":"13","author":"Baell","year":"2018","journal-title":"ACS Chem. Biol."},{"issue":"41","key":"10.1016\/j.phrs.2022.106409_bib62","doi-asserted-by":"crossref","first-page":"8154","DOI":"10.1021\/bi3012548","article-title":"Alternative pathways of human islet amyloid polypeptide aggregation distinguished by (19)f nuclear magnetic resonance-detected kinetics of monomer consumption","volume":"51","author":"Suzuki","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.phrs.2022.106409_bib63","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1038\/nsmb.1643","article-title":"Molecular mechanisms for protein-encoded inheritance","volume":"16","author":"Wiltzius","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.phrs.2022.106409_bib64","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.neuron.2015.03.017","article-title":"Amyloid polymorphism: structural basis and neurological relevance","volume":"86","author":"Tycko","year":"2015","journal-title":"Neuron"},{"key":"10.1016\/j.phrs.2022.106409_bib65","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1038\/nature20814","article-title":"Structural variation in amyloid-\u03b2 fibrils from Alzheimer's disease clinical subtypes","volume":"541","author":"Qiang","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.phrs.2022.106409_bib66","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1038\/s41594-018-0045-5","article-title":"Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2","volume":"25","author":"Guenther","year":"2018","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.phrs.2022.106409_bib67","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1038\/s41594-019-0248-4","article-title":"Cryo-EM structures of four polymorphic TDP-43 amyloid cores","volume":"26","author":"Cao","year":"2019","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.phrs.2022.106409_bib68","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/j.cell.2020.01.027","article-title":"Posttranslational modifications mediate the structural diversity of tauopathy strains","volume":"180","author":"Arakhamia","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.phrs.2022.106409_bib69","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1038\/nrn2786","article-title":"Prion-like mechanisms in neurodegenerative diseases","volume":"11","author":"Frost","year":"2010","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.phrs.2022.106409_bib70","doi-asserted-by":"crossref","first-page":"10323","DOI":"10.1073\/pnas.1408900111","article-title":"Serial propagation of distinct strains of A\u03b2 prions from Alzheimer's disease patients","volume":"111","author":"Watts","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.phrs.2022.106409_bib71","doi-asserted-by":"crossref","first-page":"2408","DOI":"10.1074\/jbc.M117.815357","article-title":"Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathies","volume":"293","author":"Strang","year":"2018","journal-title":"J. Biol. Chem."}],"container-title":["Pharmacological Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1043661822003541?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1043661822003541?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T22:35:37Z","timestamp":1760913337000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1043661822003541"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,10]]},"references-count":71,"alternative-id":["S1043661822003541"],"URL":"https:\/\/doi.org\/10.1016\/j.phrs.2022.106409","relation":{},"ISSN":["1043-6618"],"issn-type":[{"value":"1043-6618","type":"print"}],"subject":[],"published":{"date-parts":[[2022,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Catechol-containing compounds are a broad class of protein aggregation inhibitors: Redox state is a key determinant of the inhibitory activities","name":"articletitle","label":"Article Title"},{"value":"Pharmacological Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.phrs.2022.106409","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"106409"}}