{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,26]],"date-time":"2026-01-26T02:38:54Z","timestamp":1769395134300,"version":"3.49.0"},"reference-count":97,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2019,3,14]],"date-time":"2019-03-14T00:00:00Z","timestamp":1552521600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100008530","name":"European Regional Development Fund","doi-asserted-by":"publisher","award":["Norte-01-0145-FEDER-000008"],"award-info":[{"award-number":["Norte-01-0145-FEDER-000008"]}],"id":[{"id":"10.13039\/501100008530","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Transthyretin (TTR) amyloidoses (ATTR amyloidosis) are diseases associated with transthyretin (TTR) misfolding, aggregation and extracellular deposition in tissues as amyloid. Clinical manifestations of the disease are variable and include mainly polyneuropathy and\/or cardiomyopathy. The reasons why TTR forms aggregates and amyloid are related with amino acid substitutions in the protein due to mutations, or with environmental alterations associated with aging, that make the protein more unstable and prone to aggregation. According to this model, several therapeutic approaches have been proposed for the diseases that range from stabilization of TTR, using chemical chaperones, to clearance of the aggregated protein deposited in tissues in the form of oligomers or small aggregates, by the action of disruptors or by activation of the immune system. Interestingly, different studies revealed that curcumin presents anti-amyloid properties, targeting multiple steps in the ATTR amyloidogenic cascade. The effects of curcumin on ATTR amyloidosis will be reviewed and discussed in the current work in order to contribute to knowledge of the molecular mechanisms involved in TTR amyloidosis and propose more efficient drugs for therapy.<\/jats:p>","DOI":"10.3390\/ijms20061287","type":"journal-article","created":{"date-parts":[[2019,3,15]],"date-time":"2019-03-15T04:12:09Z","timestamp":1552623129000},"page":"1287","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":39,"title":["Uncovering the Neuroprotective Mechanisms of Curcumin on Transthyretin Amyloidosis"],"prefix":"10.3390","volume":"20","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0305-9097","authenticated-orcid":false,"given":"Nelson","family":"Ferreira","sequence":"first","affiliation":[{"name":"Danish Research Institute of Translational Neuroscience, Nordic EMBL Partnership for Molecular Medicine, Department of Biomedicine, Aarhus University, 8000 Aarhus C, Denmark"}]},{"given":"Maria Jo\u00e3o","family":"Saraiva","sequence":"additional","affiliation":[{"name":"Molecular Neurobiology Group, IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, 4200-135 Porto, Portugal"},{"name":"Instituto de Investiga\u00e7\u00e3o e Inova\u00e7\u00e3o em Sa\u00fade (I3S), Universidade do Porto, 4200-135 Porto, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9289-3835","authenticated-orcid":false,"given":"Maria Ros\u00e1rio","family":"Almeida","sequence":"additional","affiliation":[{"name":"Molecular Neurobiology Group, IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, 4200-135 Porto, Portugal"},{"name":"Instituto de Investiga\u00e7\u00e3o e Inova\u00e7\u00e3o em Sa\u00fade (I3S), Universidade do Porto, 4200-135 Porto, Portugal"},{"name":"Molecular Biology Department, ICBAS-Instituto de Ci\u00eancias Biom\u00e9dicas Abel Salazar, Universidade do Porto, 4050-313 Porto, Portugal"}]}],"member":"1968","published-online":{"date-parts":[[2019,3,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3230","DOI":"10.1016\/S0021-9258(18)93118-2","article-title":"The interaction of thyroxine with human plasma prealbumin and with the prealbumin-retinol-binding protein complex","volume":"244","author":"Raz","year":"1969","journal-title":"J. Biol. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/S0022-2275(20)32074-5","article-title":"Transthyretin in high density lipoproteins: Association with apolipoprotein A-I","volume":"41","author":"Sousa","year":"2000","journal-title":"J. Lipid Res."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1038\/labinvest.3780116","article-title":"Interaction of the receptor for advanced glycation end products (RAGE) with transthyretin triggers nuclear transcription factor kB (NF-kB) activation","volume":"80","author":"Sousa","year":"2000","journal-title":"Lab. Investig."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2244","DOI":"10.1021\/bi7016377","article-title":"Transthyretin interacts with metallothionein 2","volume":"47","author":"Quintela","year":"2008","journal-title":"Biochemistry"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1096\/fj.05-4106fje","article-title":"Transthyretin knockouts are a new mouse model for increased neuropeptide Y","volume":"20","author":"Nunes","year":"2006","journal-title":"FASEB J."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1016\/j.febslet.2008.02.034","article-title":"Transthyretin binding to A-Beta peptide--impact on A-Beta fibrillogenesis and toxicity","volume":"582","author":"Costa","year":"2008","journal-title":"FEBS Lett."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1002\/iub.340","article-title":"Aboard transthyretin: From transport to cleavage","volume":"62","author":"Liz","year":"2010","journal-title":"IUBMB Life"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"587","DOI":"10.2174\/156800705774322076","article-title":"Small transthyretin (TTR) ligands as possible therapeutic agents in TTR amyloidoses","volume":"4","author":"Almeida","year":"2005","journal-title":"Curr. Drug Targets CNS Neurol. Disord."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/0014-5793(95)00095-Q","article-title":"A yellow component associated with human transthyretin has properties like a pterin derivative, 7,8-dihydropterin-6-carboxaldehyde","volume":"360","author":"Pettersson","year":"1995","journal-title":"FEBS Lett."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/0009-2797(93)90081-9","article-title":"Structure-dependent, competitive interaction of hydroxy-polychlorobiphenyls, -dibenzo-p-dioxins and -dibenzofurans with human transthyretin","volume":"88","author":"Lans","year":"1993","journal-title":"Chem. Biol. Interact."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.1016\/S0968-0896(99)00066-8","article-title":"Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid","volume":"7","author":"Baures","year":"1999","journal-title":"Bioorg. Med. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.bbrc.2011.07.093","article-title":"Erratum to \u201cMechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs\u201d [Biochem. Biophys. Res. Commun. 410 (2011) 707\u2013713]","volume":"412","author":"Bourgault","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.jsb.2012.07.008","article-title":"Flavonoid interactions with human transthyretin: Combined structural and thermodynamic analysis","volume":"180","author":"Trivella","year":"2012","journal-title":"J. Struct. Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"8928","DOI":"10.1021\/jm500997m","article-title":"Inhibitory activities of propolis and its promising component, caffeic acid phenethyl ester, against amyloidogenesis of human transthyretin","volume":"57","author":"Yokoyama","year":"2014","journal-title":"J. Med. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.nbt.2014.09.002","article-title":"Transthyretin complexes with curcumin and bromo-estradiol: Evaluation of solubilizing multicomponent mixtures","volume":"32","author":"Ciccone","year":"2015","journal-title":"New Biotechnol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1177\/31.5.6341455","article-title":"Localization of human prealbumin in choroid plexus epithelium","volume":"31","author":"Aleshire","year":"2017","journal-title":"J. Histochem. Cytochem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"8214","DOI":"10.1016\/S0021-9258(17)39583-2","article-title":"Rat transthyretin (prealbumin). Molecular cloning, nucleotide sequence, and gene expression in liver and brain","volume":"260","author":"Dickson","year":"1985","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0074-7696(07)58003-4","article-title":"Cell and molecular biology of transthyretin and thyroid hormones","volume":"258","author":"Richardson","year":"2007","journal-title":"Int. Rev. Cytol."},{"key":"ref_19","first-page":"497","article-title":"The retinal pigment epithelium is the unique site of transthyretin synthesis in the rat eye","volume":"31","author":"Cavallaro","year":"1990","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"5342","DOI":"10.1111\/j.1742-4658.2009.07244.x","article-title":"Evolutionary changes to transthyretin: Evolution of transthyretin biosynthesis","volume":"276","author":"Richardson","year":"2009","journal-title":"FEBS J."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/0022-2836(78)90368-6","article-title":"Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A","volume":"121","author":"Blake","year":"1978","journal-title":"J. Mol. Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1016\/S0021-9258(18)53792-3","article-title":"The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution","volume":"268","author":"Hamilton","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"505","DOI":"10.18388\/abp.1997_4400","article-title":"Crystal structure of rat transthyretin at 2.5 A resolution: First report on a unique tetrameric structure","volume":"44","author":"Wojtczak","year":"1997","journal-title":"Acta Biochim. Pol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2324","DOI":"10.2174\/092986712800269335","article-title":"Nearly 200 X-ray crystal structures of transthyretin: What do they tell us about this protein and the design of drugs for TTR amyloidoses?","volume":"19","author":"Palaninathan","year":"2012","journal-title":"Curr. Med. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1002\/mus.20821","article-title":"The molecular biology and clinical features of amyloid neuropathy","volume":"36","author":"Benson","year":"2007","journal-title":"Muscle Nerve"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.1136\/jnnp-2014-308724","article-title":"Transthyretin (ATTR) amyloidosis: Clinical spectrum, molecular pathogenesis and disease-modifying treatments","volume":"86","author":"Sekijima","year":"2015","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.pneurobio.2003.11.002","article-title":"Neurodegeneration in familial amyloid polyneuropathy: From pathology to molecular signaling","volume":"71","author":"Sousa","year":"2003","journal-title":"Prog. Neurobiol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1111\/joim.12383","article-title":"Cardiac amyloidosis: Where are we today?","volume":"278","author":"Patel","year":"2015","journal-title":"J. Intern. Med."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1172\/JCI111390","article-title":"Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin)","volume":"74","author":"Saraiva","year":"1984","journal-title":"J. Clin. Investig."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1016\/B978-0-444-52902-2.00038-2","article-title":"Transthyretin familial amyloid polyneuropathy","volume":"115","author":"Kerschen","year":"2013","journal-title":"Handb. Clin. Neurol."},{"key":"ref_31","first-page":"127","article-title":"A homozygous transthyretin variant associated with senile systemic amyloidosis: Evidence for a late-onset disease of genetic etiology","volume":"47","author":"Jacobson","year":"1990","journal-title":"Am. J. Hum. Genet."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1111\/j.1365-3083.1990.tb02928.x","article-title":"Cardiac amyloidosis: Report of a patient heterozygous for the transthyretin isoleucine 122 variant","volume":"32","author":"Saraiva","year":"1990","journal-title":"Scand. J. Immunol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2451","DOI":"10.1016\/j.jacc.2015.09.075","article-title":"Diagnosis, Prognosis, and Therapy of Transthyretin Amyloidosis","volume":"66","author":"Gertz","year":"2015","journal-title":"J. Am. Coll. Cardiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1111\/jns.12153","article-title":"\u201cRed-flag\u201d symptom clusters in transthyretin familial amyloid polyneuropathy","volume":"21","author":"Obici","year":"2016","journal-title":"J. Peripher. Nerv. Syst."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1186\/1750-1172-8-31","article-title":"Guideline of transthyretin-related hereditary amyloidosis for clinicians","volume":"8","author":"Ando","year":"2013","journal-title":"Orphanet J. Rare Dis."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1212\/01.WNL.0000132966.36437.12","article-title":"Pathology of early- vs. late-onset TTR Met30 familial amyloid polyneuropathy","volume":"63","author":"Koike","year":"2004","journal-title":"Neurology"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1007\/s00415-017-8708-4","article-title":"Transthyretin familial amyloid polyneuropathy: An update","volume":"265","year":"2018","journal-title":"J. Neurol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1016\/0140-6736(93)93127-M","article-title":"Clinical improvement and amyloid regression after liver transplantation in hereditary transthyretin amyloidosis","volume":"341","author":"Holmgren","year":"1993","journal-title":"Lancet"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1002\/lt.24058","article-title":"Liver transplantation in transthyretin amyloidosis: Issues and challenges","volume":"21","author":"Carvalho","year":"2015","journal-title":"Liver Transpl."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1212\/WNL.0b013e3181ea15d4","article-title":"Progression of transthyretin amyloid neuropathy after liver transplantation","volume":"75","author":"Liepnieks","year":"2010","journal-title":"Neurology"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"200","DOI":"10.3109\/13506129.2011.615872","article-title":"Development of cardiomyopathy after liver transplantation in Swedish hereditary transthyretin amyloidosis (ATTR) patients","volume":"18","author":"Okamoto","year":"2011","journal-title":"Amyloid"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1847","DOI":"10.1097\/TP.0000000000000574","article-title":"Liver Transplantation for Hereditary Transthyretin Amyloidosis: After 20 Years Still the Best Therapeutic Alternative?","volume":"99","author":"Ericzon","year":"2015","journal-title":"Transplantation"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"15051","DOI":"10.1073\/pnas.93.26.15051","article-title":"Inhibiting transthyretin amyloid fibril formation via protein stabilization","volume":"93","author":"Miroy","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1021\/ar020073i","article-title":"Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses","volume":"38","author":"Johnson","year":"2005","journal-title":"Acc. Chem. Res."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1141","DOI":"10.1210\/jcem-68-6-1141","article-title":"Drug competition for thyroxine binding to transthyretin (prealbumin): Comparison with effects on thyroxine-binding globulin","volume":"68","author":"Munro","year":"1989","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1021\/jm030347n","article-title":"Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis","volume":"47","author":"Palaninathan","year":"2004","journal-title":"J. Med. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1038\/labinvest.3700059","article-title":"Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants","volume":"84","author":"Miller","year":"2004","journal-title":"Lab. Investig."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/j.neures.2006.08.014","article-title":"Diflunisal stabilizes familial amyloid polyneuropathy-associated transthyretin variant tetramers in serum against dissociation required for amyloidogenesis","volume":"56","author":"Tojo","year":"2006","journal-title":"Neurosci. Res."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1080\/13506120600960882","article-title":"Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis","volume":"13","author":"Sekijima","year":"2006","journal-title":"Amyloid"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1021\/jm0708735","article-title":"Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors","volume":"51","author":"Johnson","year":"2008","journal-title":"J. Med. Chem."},{"key":"ref_51","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":"ref_52","doi-asserted-by":"crossref","first-page":"2802","DOI":"10.1007\/s00415-013-7051-7","article-title":"Long-term effects of tafamidis for the treatment of transthyretin familial amyloid polyneuropathy","volume":"260","author":"Coelho","year":"2013","journal-title":"J. Neurol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1517\/14656566.2016.1145664","article-title":"TTR kinetic stabilizers and TTR gene silencing: A new era in therapy for familial amyloidotic polyneuropathies","volume":"17","author":"Adams","year":"2016","journal-title":"Expert Opin. Pharmacother."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1007\/s13311-013-0256-8","article-title":"Molecular tweezers targeting transthyretin amyloidosis","volume":"11","author":"Ferreira","year":"2014","journal-title":"Neurotherapeutics"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1042\/CS20160413","article-title":"Transthyretin amyloidosis: An under-recognized neuropathy and cardiomyopathy","volume":"131","author":"Galant","year":"2017","journal-title":"Clin. Sci."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1002\/mnfr.201400290","article-title":"Natural polyphenols binding to amyloid: A broad class of compounds to treat different human amyloid diseases","volume":"59","author":"Ngoungoure","year":"2014","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2119\/molmed.2016.00124","article-title":"Resveratrol Administration Increases Transthyretin Protein Levels, Ameliorating AD Features: The Importance of Transthyretin Tetrameric Stability","volume":"22","author":"Santos","year":"2016","journal-title":"Mol. Med."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"2424","DOI":"10.1016\/j.febslet.2011.06.030","article-title":"Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation","volume":"585","author":"Ferreira","year":"2011","journal-title":"FEBS Lett."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"29769","DOI":"10.1074\/jbc.M115.690172","article-title":"Transthyretin Binding Heterogeneity and Anti-amyloidogenic Activity of Natural Polyphenols and Their Metabolites","volume":"290","author":"Florio","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.1002\/cmdc.201600092","article-title":"Targeting Different Transthyretin Binding Sites with Unusual Natural Compounds","volume":"11","author":"Ortore","year":"2016","journal-title":"ChemMedChem"},{"key":"ref_61","first-page":"123","article-title":"Transthyretin chemical chaperoning by flavonoids: Structure-activity insights towards the design of potent amyloidosis inhibitors","volume":"3","author":"Ferreira","year":"2015","journal-title":"Biochem. Biophys. Rep."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"3569","DOI":"10.1016\/j.febslet.2009.10.062","article-title":"Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity","volume":"583","author":"Ferreira","year":"2009","journal-title":"FEBS Lett."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"6104","DOI":"10.1021\/bi1004409","article-title":"The crystal structure of the green tea polyphenol (\u2212)-epigallocatechin gallate-transthyretin complex reveals a novel binding site distinct from the thyroxine binding site","volume":"49","author":"Miyata","year":"2010","journal-title":"Biochemistry"},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Ferreira, N., Saraiva, M.J., and Almeida, M.R. (2012). Epigallocatechin-3-gallate as a potential therapeutic drug for TTR-related amyloidosis: \u201cin vivo\u201d evidence from FAP mice models. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0029933"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1007\/s00392-012-0463-z","article-title":"Green tea halts progression of cardiac transthyretin amyloidosis: An observational report","volume":"101","author":"Kristen","year":"2012","journal-title":"Clin. Res. Cardiol."},{"key":"ref_66","first-page":"6319","article-title":"Green tea extract as a treatment for patients with wild-type transthyretin amyloidosis: An observational study","volume":"9","author":"Bauer","year":"2015","journal-title":"Drug Des. Dev. Ther."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1007\/s11739-018-1887-x","article-title":"Epigallocatechin-3-gallate tolerability and impact on survival in a cohort of patients with transthyretin-related cardiac amyloidosis. A single-center retrospective study","volume":"13","author":"Cappelli","year":"2018","journal-title":"Intern. Emerg. Med."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.abb.2009.02.013","article-title":"Binding and stabilization of transthyretin by curcumin","volume":"485","author":"Pullakhandam","year":"2009","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.jsb.2016.01.007","article-title":"A new crystal form of human transthyretin obtained with a curcumin derived ligand","volume":"194","author":"Polsinelli","year":"2016","journal-title":"J. Struct. Biol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1038\/srep26623","article-title":"Curcumin: A multi-target disease-modifying agent for late-stage transthyretin amyloidosis","volume":"6","author":"Ferreira","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1021\/acschemneuro.5b00214","article-title":"Curcumin Attenuates Amyloid-\u03b2 Aggregate Toxicity and Modulates Amyloid-\u03b2 Aggregation Pathway","volume":"7","author":"Thapa","year":"2015","journal-title":"ACS Chem. Neurosci."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"999","DOI":"10.3233\/JAD-170351","article-title":"Curcumin Inhibits Tau Aggregation and Disintegrates Preformed Tau Filaments in vitro","volume":"60","author":"Rane","year":"2017","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1021\/cn3001203","article-title":"Curcumin modulates \u03b1-synuclein aggregation and toxicity","volume":"4","author":"Singh","year":"2013","journal-title":"ACS Chem. Neurosci."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"5892","DOI":"10.1074\/jbc.M404751200","article-title":"Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo","volume":"280","author":"Yang","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1111\/j.1471-4159.2007.04613.x","article-title":"Curcumin labels amyloid pathology in vivo, disrupts existing plaques, and partially restores distorted neurites in an Alzheimer mouse model","volume":"102","author":"Borrelli","year":"2007","journal-title":"J. Neurochem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1007\/s00418-016-1464-1","article-title":"A comparative study of dietary curcumin, nanocurcumin, and other classical amyloid-binding dyes for labeling and imaging of amyloid plaques in brain tissue of 5\u00d7-familial Alzheimer\u2019s disease mice","volume":"146","author":"Maiti","year":"2016","journal-title":"Histochem. Cell Biol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"5967","DOI":"10.1016\/j.bmc.2011.08.052","article-title":"Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid \u03b2-protein fibrils","volume":"19","author":"Masuda","year":"2011","journal-title":"Bioorg. Med. Chem."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Maiti, P., and Dunbar, G.L. (2018). Use of Curcumin, a Natural Polyphenol for Targeting Molecular Pathways in Treating Age-Related Neurodegenerative Diseases. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19061637"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.bbadis.2012.10.007","article-title":"Dietary curcumin counteracts extracellular transthyretin deposition: Insights on the mechanism of amyloid inhibition","volume":"1832","author":"Ferreira","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"18736","DOI":"10.1038\/srep18736","article-title":"Curcumin modulates cell death and is protective in Huntington\u2019s disease model","volume":"6","author":"Chongtham","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"31752","DOI":"10.1074\/jbc.M113.469858","article-title":"Transthyretin proteins regulate angiogenesis by conferring different molecular identities to endothelial cells","volume":"288","author":"Nunes","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"2220","DOI":"10.1212\/WNL.0000000000003362","article-title":"Schwann cell and endothelial cell damage in transthyretin familial amyloid polyneuropathy","volume":"87","author":"Koike","year":"2016","journal-title":"Neurology"},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Koike, H., and Katsuno, M. (2019). Ultrastructure in Transthyretin Amyloidosis: From Pathophysiology to Therapeutic Insights. Biomedicines, 7.","DOI":"10.3390\/biomedicines7010011"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"2462","DOI":"10.2174\/1381612823666170222122822","article-title":"Curcumin and Endothelial Function: Evidence and Mechanisms of Protective Effects","volume":"23","author":"Karimian","year":"2017","journal-title":"Curr. Pharm. Des."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"345","DOI":"10.5483\/BMBRep.2017.50.7.069","article-title":"Therapeutic implication of autophagy in neurodegenerative diseases","volume":"50","author":"Rahman","year":"2017","journal-title":"BMB Rep."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"255","DOI":"10.3389\/fnins.2018.00255","article-title":"Association Between Autophagy and Neurodegenerative Diseases","volume":"12","author":"Fujikake","year":"2018","journal-title":"Front. Neurosci."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1042\/CS20160075","article-title":"Impairment of autophagy by TTR V30M aggregates: In vivo reversal by TUDCA and curcumin","volume":"130","author":"Teixeira","year":"2016","journal-title":"Clin. Sci."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"e2003","DOI":"10.1038\/cddis.2015.343","article-title":"Curcumin hormesis mediates a cross-talk between autophagy and cell death","volume":"6","author":"Rainey","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"15017","DOI":"10.1038\/cddiscovery.2015.17","article-title":"Curcumin induces crosstalk between autophagy and apoptosis mediated by calcium release from the endoplasmic reticulum, lysosomal destabilization and mitochondrial events","volume":"1","author":"Moustapha","year":"2015","journal-title":"Cell Death Discov."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"165","DOI":"10.2217\/fnl.12.6","article-title":"Clearance of amyloid-\u03b2 peptides by microglia and macrophages: The issue of what, when and where","volume":"7","author":"Lai","year":"2012","journal-title":"Future Neurol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3233\/JAD-2006-10101","article-title":"Curcuminoids enhance amyloid-\u03b2 uptake by macrophages of Alzheimer\u2019s disease patients","volume":"10","author":"Zhang","year":"2006","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"703","DOI":"10.3233\/JAD-2009-1080","article-title":"1\u03b1,25-dihydroxyvitamin D3 Interacts with Curcuminoids to Stimulate Amyloid-\u03b2 Clearance by Macrophages of Alzheimer\u2019s Disease Patients","volume":"17","author":"Masoumi","year":"2009","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"135","DOI":"10.3233\/JAD-2011-101950","article-title":"MGAT3 mRNA: A Biomarker for Prognosis and Therapy of Alzheimer\u2019s Disease by Vitamin D and Curcuminoids","volume":"25","author":"Fiala","year":"2011","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Hewlings, S.J., and Kalman, D.S. (2017). Curcumin: A Review of Its\u2019 Effects on Human Health. Foods, 6.","DOI":"10.3390\/foods6100092"},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Lao, C.D., Ruffin, M.T., Normolle, D., Heath, D.D., Murray, S.I., Bailey, J.M., Boggs, M.E., Crowell, J., Rock, C.L., and Brenner, D.E. (2006). Dose escalation of a curcuminoid formulation. BMC Complement. Altern. Med., 6.","DOI":"10.1186\/1472-6882-6-10"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1056\/NEJMoa1716153","article-title":"Patisiran, an RNAi Therapeutic, for Hereditary Transthyretin Amyloidosis","volume":"379","author":"Adams","year":"2018","journal-title":"N. Engl. J. Med."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1056\/NEJMoa1716793","article-title":"Inotersen Treatment for Patients with Hereditary Transthyretin Amyloidosis","volume":"379","author":"Benson","year":"2018","journal-title":"N. Engl. J. 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