{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,8,7]],"date-time":"2025-08-07T20:35:39Z","timestamp":1754598939291,"version":"3.41.2"},"reference-count":219,"publisher":"Elsevier","isbn-type":[{"type":"print","value":"9780443293405"}],"license":[{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024]]},"DOI":"10.1016\/bs.pmbts.2024.03.008","type":"book-chapter","created":{"date-parts":[[2024,4,4]],"date-time":"2024-04-04T00:35:52Z","timestamp":1712190952000},"page":"341-388","source":"Crossref","is-referenced-by-count":2,"title":["Therapeutic approaches in proteinopathies"],"prefix":"10.1016","member":"78","reference":[{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib1","first-page":"97","article-title":"Misfolded structures|A brief insight into protein aggregation criteria, which may lead to proteopathy diseases","volume":"3","author":"Abbasbeigi","year":"2020","journal-title":"J Chem Rev"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib2","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/nrd769","article-title":"Therapeutic strategies for human amyloid diseases","volume":"1","author":"Sacchettini","year":"2002","journal-title":"Nat Rev Drug Discov"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib3","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1146\/annurev-biochem-061516-044518","article-title":"Protein misfolding diseases","volume":"86","author":"Hartl","year":"2017","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40035-017-0077-5","article-title":"Protein misfolding in neurodegenerative diseases: implications and strategies","volume":"6","author":"Sweeney","year":"2017","journal-title":"Transl Neurodegener"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib5","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.bbamcr.2013.03.012","article-title":"Proteostasis and neurodegeneration: the roles of proteasomal degradation and autophagy","volume":"1843","author":"Tanaka","year":"2014","journal-title":"Biochimica et Biophysica Acta (BBA)-Mol\u00a0Cell Res"},{"issue":"20","key":"10.1016\/bs.pmbts.2024.03.008_bib6","doi-asserted-by":"crossref","first-page":"3459","DOI":"10.1038\/emboj.2010.225","article-title":"Heat shock factor 1 ameliorates proteotoxicity in cooperation with the transcription factor NFAT","volume":"29","author":"Hayashida","year":"2010","journal-title":"Embo J"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib7","doi-asserted-by":"crossref","first-page":"3676","DOI":"10.1007\/s12035-018-1334-z","article-title":"Cellular proteostasis in neurodegeneration","volume":"56","author":"Kurtishi","year":"2019","journal-title":"Mol Neurobiol"},{"issue":"9","key":"10.1016\/bs.pmbts.2024.03.008_bib8","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1016\/j.tcb.2014.05.003","article-title":"Proteostasis impairment in protein-misfolding and-aggregation diseases","volume":"24","author":"Hipp","year":"2014","journal-title":"Trends Cell Biol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib9","first-page":"1","article-title":"Molecular mechanisms of proteinopathies across neurodegenerative disease: a review","volume":"1","author":"Marsh","year":"2019","journal-title":"Neurological Res Pract"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib10","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.euroneuro.2013.03.007","article-title":"Proteinopathies, a core concept for understanding and ultimately treating degenerative disorders?","volume":"25","author":"Bayer","year":"2015","journal-title":"Eur Neuropsychopharmacol"},{"issue":"6","key":"10.1016\/bs.pmbts.2024.03.008_bib11","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1038\/nsmb.1591","article-title":"Converging concepts of protein folding in vitro and in vivo","volume":"16","author":"Hartl","year":"2009","journal-title":"Nat Struct Mol Biol"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib12","doi-asserted-by":"crossref","first-page":"44","DOI":"10.3390\/ph11020044","article-title":"Old drugs as new treatments for neurodegenerative diseases","volume":"11","author":"Dur\u00e3es","year":"2018","journal-title":"Pharmaceuticals"},{"issue":"8","key":"10.1016\/bs.pmbts.2024.03.008_bib13","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1038\/nrd1468","article-title":"Drug repositioning: identifying and developing new uses for existing drugs","volume":"3","author":"Ashburn","year":"2004","journal-title":"Nat Rev Drug Discov"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib14","first-page":"385","article-title":"The future of drug repositioning: old drugs, new opportunities","volume":"46","author":"Doan","year":"2011","journal-title":"Annu\u00a0Rep\u00a0Med\u00a0Chem"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib15","first-page":"416","article-title":"Modern approaches to cardiovascular amyloidosis treatment","volume":"10","author":"Morozkina","year":"2021","journal-title":"Russ\u00a0Open Med J"},{"issue":"3","key":"10.1016\/bs.pmbts.2024.03.008_bib16","doi-asserted-by":"crossref","first-page":"184","DOI":"10.2174\/1566523220999200716111502","article-title":"Gene therapy, a novel therapeutic tool for neurological disorders: current progress, challenges and future prospective","volume":"20","author":"Iqubal","year":"2020","journal-title":"Curr Gene Ther"},{"issue":"17","key":"10.1016\/bs.pmbts.2024.03.008_bib17","doi-asserted-by":"crossref","first-page":"2920","DOI":"10.1093\/hmg\/ddaa179","article-title":"Gene therapy for Alzheimer\u2019s disease targeting CD33 reduces amyloid beta accumulation and neuroinflammation","volume":"29","author":"Griciuc","year":"2020","journal-title":"Hum Mol Genet"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib18","first-page":"40","article-title":"Natural product-based amyloid inhibitors","volume":"139","author":"Velander","year":"2017","journal-title":"Biochem\u00a0Pharmacol"},{"issue":"3","key":"10.1016\/bs.pmbts.2024.03.008_bib19","first-page":"444","article-title":"Current status, issues and future prospects of personalized medicine for each disease","volume":"12","author":"Yamamoto","year":"2022","journal-title":"J Pers\u00a0Med"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib20","first-page":"1","article-title":"Diagnostic biomarkers of amyloid and tau pathology in Alzheimer\u2019s disease: an overview of tests for clinical practice in the United States and Europe","author":"Iaccarino","year":"2023","journal-title":"J Prev Alzheimer\u2019s Dis"},{"issue":"49","key":"10.1016\/bs.pmbts.2024.03.008_bib21","doi-asserted-by":"crossref","first-page":"13018","DOI":"10.1073\/pnas.1713215114","article-title":"Amyloid polymorphisms constitute distinct clouds of conformational variants in different etiological subtypes of Alzheimer\u2019s disease","volume":"114","author":"Rasmussen","year":"2017","journal-title":"Proc Natl Acad Sci"},{"issue":"19","key":"10.1016\/bs.pmbts.2024.03.008_bib22","first-page":"2918","article-title":"How I treat AL amyloidosis","volume":"139","author":"Palladini","year":"2022","journal-title":"Blood, J Am Soc Hematol"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib23","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/s13024-023-00637-0","article-title":"Anti-amyloid therapies for Alzheimer disease: Finally, good news for patients","volume":"18","author":"Ramanan","year":"2023","journal-title":"Mol Neurodegener"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib24","doi-asserted-by":"crossref","first-page":"2739","DOI":"10.1007\/s11010-021-04120-6","article-title":"Mechanistic insights into the pathogenesis of neurodegenerative diseases: towards the development of effective therapy","volume":"476","author":"Nazam","year":"2021","journal-title":"Mol Cell Biochem"},{"issue":"6","key":"10.1016\/bs.pmbts.2024.03.008_bib25","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1097\/NRL.0b013e318158e47d","article-title":"Medications for Parkinson\u2019s disease","volume":"13","author":"Whitney","year":"2007","journal-title":"Neurologist"},{"issue":"12","key":"10.1016\/bs.pmbts.2024.03.008_bib26","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1080\/14728222.2017.1398235","article-title":"Emerging therapeutic targets currently under investigation for the treatment of systemic amyloidosis","volume":"21","author":"Nuvolone","year":"2017","journal-title":"Expert Opin Therap\u00a0Targets"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib27","doi-asserted-by":"crossref","DOI":"10.1002\/btm2.10367","article-title":"Alzheimer\u2019s and Parkinson\u2019s disease therapies in the clinic","volume":"8","author":"Chopade","year":"2023","journal-title":"Bioeng Transl Med"},{"issue":"3","key":"10.1016\/bs.pmbts.2024.03.008_bib28","doi-asserted-by":"crossref","first-page":"247","DOI":"10.7861\/clinmedicine.16-3-247","article-title":"Drug treatments in Alzheimer\u2019s disease","volume":"16","author":"Briggs","year":"2016","journal-title":"Clin Med"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib29","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1055\/s-0039-1678581","article-title":"Current and future treatments in Alzheimer\u2019s disease","volume":"39","author":"Livingston","year":"2019","journal-title":"Semin Neurol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib30","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejphar.2020.173554","article-title":"Alzheimer\u2019s disease: recent treatment strategies","volume":"887","author":"Vaz","year":"2020","journal-title":"Eur J Pharmacol"},{"issue":"3","key":"10.1016\/bs.pmbts.2024.03.008_bib31","first-page":"307","article-title":"Evaluating the completeness of ClinicalTrials. gov","volume":"53","author":"Stergiopoulos","year":"2019","journal-title":"Therap\u00a0Innov\u00a0Regul\u00a0Sci"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib32","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1097\/NAN.0b013e31826579aa","article-title":"Biologic therapy","volume":"35","author":"Eisenberg","year":"2012","journal-title":"J Infus Nurs"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib33","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1080\/17460441.2018.1437142","article-title":"The development of biological therapies for neurological diseases: moving on from previous failures","volume":"13","author":"Qosa","year":"2018","journal-title":"Expert Opin Drug Discov"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib34","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.cbpa.2018.05.018","article-title":"Therapeutic strategies for targeting neurodegenerative protein misfolding disorders","volume":"44","author":"Scannevin","year":"2018","journal-title":"Curr Opin\u00a0Chem Biol"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib35","first-page":"663","article-title":"Preclinical and clinical development of noncoding RNA therapeutics for cardiovascular disease","volume":"126","author":"Huang","year":"2020","journal-title":"Circ\u00a0Res"},{"issue":"9","key":"10.1016\/bs.pmbts.2024.03.008_bib36","doi-asserted-by":"crossref","first-page":"1397","DOI":"10.3390\/pharmaceutics13091397","article-title":"New RNA-based breakthroughs in Alzheimer\u2019s disease diagnosis and therapeutics","volume":"13","author":"Riscado","year":"2021","journal-title":"Pharmaceutics"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib37","doi-asserted-by":"crossref","first-page":"5","DOI":"10.2217\/nmt-2018-0033","article-title":"Patisiran, an RNAi therapeutic for the treatment of hereditary transthyretin-mediated amyloidosis","volume":"9","author":"Kristen","year":"2019","journal-title":"Neurodegener\u00a0Dis Manag"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib38","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2021.685143","article-title":"Long noncoding RNAs in neurodegenerative diseases: pathogenesis and potential implications as clinical biomarkers","volume":"14","author":"Zhang","year":"2021","journal-title":"Front Mol Neurosci"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib39","doi-asserted-by":"crossref","first-page":"137","DOI":"10.3390\/cells9010137","article-title":"RNA-based therapeutics: from antisense oligonucleotides to miRNAs","volume":"9","author":"Bajan","year":"2020","journal-title":"Cells"},{"issue":"24","key":"10.1016\/bs.pmbts.2024.03.008_bib40","doi-asserted-by":"crossref","first-page":"2307","DOI":"10.1056\/NEJMoa1900907","article-title":"Targeting huntingtin expression in patients with Huntington\u2019s disease","volume":"380","author":"Tabrizi","year":"2019","journal-title":"N Engl J Med"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib41","first-page":"36","article-title":"Potent and sustained huntingtin lowering via AAV5 encoding miRNA preserves striatal volume and cognitive function in a humanized mouse model of Huntington disease","volume":"48","author":"Caron","year":"2020","journal-title":"Nucleic Acids Res"},{"issue":"6","key":"10.1016\/bs.pmbts.2024.03.008_bib42","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"},{"issue":"6","key":"10.1016\/bs.pmbts.2024.03.008_bib43","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1021\/acs.biochem.5b01168","article-title":"Stabilization of-synuclein fibril clusters prevents fragmentation and reduces seeding activity and toxicity","volume":"55","author":"Lam","year":"2016","journal-title":"Biochemistry"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib44","article-title":"Myeloperoxidase: mechanisms, reactions and inhibition as a therapeutic strategy in inflammatory diseases","volume":"218","author":"Davies","year":"2021","journal-title":"Pharmacol\u00a0Therap"},{"issue":"26","key":"10.1016\/bs.pmbts.2024.03.008_bib45","first-page":"2748","article-title":"The therapeutical potential of alpha-synuclein antiaggregatory agents for dementia with Lewy bodies","volume":"15","author":"Beyer","year":"2008","journal-title":"Curr Med\u00a0Chem"},{"issue":"3","key":"10.1016\/bs.pmbts.2024.03.008_bib46","doi-asserted-by":"crossref","first-page":"839","DOI":"10.3390\/pharmaceutics15030839","article-title":"Development of small molecules targeting \u03b1-synuclein aggregation: a promising strategy to treat Parkinson\u2019s disease","volume":"15","author":"Pe\u00f1a-D\u00edaz","year":"2023","journal-title":"Pharmaceutics"},{"issue":"7","key":"10.1016\/bs.pmbts.2024.03.008_bib47","doi-asserted-by":"crossref","first-page":"1416","DOI":"10.1002\/mds.29016","article-title":"A randomized first\u2010in\u2010human study with UB\u2010312, a UBITh\u00ae \u03b1\u2010synuclein peptide vaccine","volume":"37","author":"Yu","year":"2022","journal-title":"Mov Disord"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib48","doi-asserted-by":"crossref","first-page":"1210","DOI":"10.3390\/molecules27041210","article-title":"Amyloidosis in Alzheimer\u2019s disease: pathogeny, etiology, and related therapeutic directions","volume":"27","author":"Ma","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib49","unstructured":"National Institutes of Health.\u00a0What happens to the brain in Alzheimer\u2019s disease. May;2017."},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib50","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3233\/JAD-201027","article-title":"Selective secretase targeting for Alzheimer\u2019s disease therapy","volume":"81","author":"Miranda","year":"2021","journal-title":"J Alzheimer\u2019s Dis"},{"issue":"3","key":"10.1016\/bs.pmbts.2024.03.008_bib51","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1007\/s40263-019-00613-7","article-title":"A close look at BACE1 inhibitors for Alzheimer\u2019s disease treatment","volume":"33","author":"Das","year":"2019","journal-title":"CNS drugs"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib52","doi-asserted-by":"crossref","first-page":"178","DOI":"10.3389\/fchem.2018.00178","article-title":"Highlights in BACE1 inhibitors for Alzheimer\u2019s disease treatment","volume":"6","author":"Coimbra","year":"2018","journal-title":"Front Chem"},{"issue":"12","key":"10.1016\/bs.pmbts.2024.03.008_bib53","doi-asserted-by":"crossref","first-page":"2444","DOI":"10.1038\/s41591-022-02132-3","article-title":"11 clinical trials that will shape medicine in 2023","volume":"28","author":"Arnold","year":"2022","journal-title":"Nat Med"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib54","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1056\/NEJMoa1210951","article-title":"A phase 3 trial of semagacestat for treatment of Alzheimer\u2019s disease","volume":"369","author":"Doody","year":"2013","journal-title":"N Engl J Med"},{"issue":"10","key":"10.1016\/bs.pmbts.2024.03.008_bib55","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1517\/14656560903044982","article-title":"Development of semagacestat (LY450139), a functional \u03b3-secretase inhibitor, for the treatment of Alzheimer\u2019s disease","volume":"10","author":"Henley","year":"2009","journal-title":"Expert Opin Pharmacother"},{"issue":"6","key":"10.1016\/bs.pmbts.2024.03.008_bib56","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1007\/s12192-021-01231-3","article-title":"The PI3K\/Akt signaling axis in Alzheimer\u2019s disease: a valuable target to stimulate or suppress?","volume":"26","author":"Razani","year":"2021","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib57","doi-asserted-by":"crossref","DOI":"10.1177\/1179573520907397","article-title":"Current and future treatments in Alzheimer disease: an update","volume":"12","author":"Yiannopoulou","year":"2020","journal-title":"J Cent Nerv Syst Dis"},{"issue":"6","key":"10.1016\/bs.pmbts.2024.03.008_bib58","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.3390\/pharmaceutics14061117","article-title":"Therapeutic approach to Alzheimer\u2019s disease: current treatments and new perspectives","volume":"14","author":"Pardo-Moreno","year":"2022","journal-title":"Pharmaceutics"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib59","doi-asserted-by":"crossref","first-page":"401","DOI":"10.3233\/JAD-160965","article-title":"A randomized, double-blind, placebo-controlled, phase II study of oral ELND005 (scyllo-inositol) in young adults with down syndrome without dementia","volume":"58","author":"Rafii","year":"2017","journal-title":"J Alzheimer\u2019s Dis"},{"issue":"13","key":"10.1016\/bs.pmbts.2024.03.008_bib60","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1212\/WNL.0b013e3182309fa5","article-title":"A phase 2 randomized trial of ELND005, scyllo-inositol, in mild to moderate Alzheimer disease","volume":"77","author":"Salloway","year":"2011","journal-title":"Neurology"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib61","doi-asserted-by":"crossref","first-page":"87","DOI":"10.2165\/00126839-200607020-00003","article-title":"\u03b3-secretase inhibitors for Alzheimer\u2019s disease: balancing efficacy and toxicity","volume":"7","author":"Barten","year":"2006","journal-title":"Drugs R&D"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib62","doi-asserted-by":"crossref","first-page":"102","DOI":"10.5114\/aoms.2011.20612","article-title":"Tramiprosate in mild-to-moderate Alzheimer\u2019s disease\u2013a randomized, double-blind, placebo-controlled, multi-centre study (the Alphase study)","volume":"7","author":"Aisen","year":"2011","journal-title":"Arch Med Sci"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib63","doi-asserted-by":"crossref","first-page":"577","DOI":"10.3233\/JAD-180184","article-title":"Improvement of main cognitive functions in patients with alzheimer\u2019s disease after treatment with coconut oil enriched mediterranean diet: a pilot study","volume":"65","author":"De La Rubia Ort\u00ed","year":"2018","journal-title":"J Alzheimer\u2019s Dis"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib64","unstructured":"De Sousa Loureiro J.A.\u00a0The Relevance of Natural Compounds in the Alzheimer\u2019s Disease. Universidade Fernando Pessoa (Portugal); 2018."},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib65","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1124\/jpet.114.219352","article-title":"Complex disposition of methylthioninium redox forms determines efficacy in tau aggregation inhibitor therapy for Alzheimer\u2019s disease","volume":"352","author":"Baddeley","year":"2015","journal-title":"J Pharmacol\u00a0Exp Therap"},{"issue":"10062","key":"10.1016\/bs.pmbts.2024.03.008_bib66","doi-asserted-by":"crossref","first-page":"2873","DOI":"10.1016\/S0140-6736(16)31275-2","article-title":"Efficacy and safety of tau-aggregation inhibitor therapy in patients with mild or moderate Alzheimer\u2019s disease: a randomised, controlled, double-blind, parallel-arm, phase 3 trial","volume":"388","author":"Gauthier","year":"2016","journal-title":"Lancet"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib67","doi-asserted-by":"crossref","first-page":"435","DOI":"10.3233\/JAD-170560","article-title":"Potential of low dose leuco-methylthioninium bis (hydromethanesulphonate)(LMTM) monotherapy for treatment of mild Alzheimer\u2019s disease: Cohort analysis as modified primary outcome in a phase III clinical trial","volume":"61","author":"Wilcock","year":"2018","journal-title":"J Alzheimer\u2019s Dis"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib68","doi-asserted-by":"crossref","unstructured":"Ritter R.RC. Gastrointest peptides control food intakeGastrointestinal Peptides and the Control of Food Intake. In: (Koob GF, LeMoal M, Thompson RF, eds. Encyclopedia of Behavioral Neuroscience. 2010:559\u2013568. https:\/\/doi.org\/10.1016\/B978-0-08-045396-5.00191-3.","DOI":"10.1016\/B978-0-08-045396-5.00191-3"},{"issue":"8","key":"10.1016\/bs.pmbts.2024.03.008_bib69","doi-asserted-by":"crossref","first-page":"2207","DOI":"10.3390\/jcm11082207","article-title":"Mediators of amylin action in metabolic control","volume":"11","author":"Boyle","year":"2022","journal-title":"J Clin Med"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib70","doi-asserted-by":"crossref","first-page":"17","DOI":"10.3389\/fmolb.2016.00017","article-title":"Historical and current concepts of fibrillogenesis and in vivo amyloidogenesis: implications of amyloid tissue targeting","volume":"3","author":"Kisilevsky","year":"2016","journal-title":"Front Mol Biosci"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib71","first-page":"16","article-title":"Alzheimer\u2019s amyloid fibrils: structure and assembly","volume":"1502","author":"Serpell","year":"2000","journal-title":"Biochim\u00a0Biophys\u00a0Acta (BBA)-Mol\u00a0Basis Dis"},{"issue":"10","key":"10.1016\/bs.pmbts.2024.03.008_bib72","doi-asserted-by":"crossref","first-page":"1286","DOI":"10.1161\/CIRCULATIONAHA.111.078915","article-title":"Transthyretin (TTR) cardiac amyloidosis","volume":"126","author":"Ruberg","year":"2012","journal-title":"Circulation"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib73","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1007\/978-94-007-5416-4_21","article-title":"Familial amyloidotic polyneuropathy and transthyretin","volume":"65","author":"Nagasaka","year":"2012","journal-title":"Subcell Biochems"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib74","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1111\/febs.15339","article-title":"Tolcapone, a potent aggregation inhibitor for the treatment of familial leptomeningeal amyloidosis","volume":"288","author":"Pinheiro","year":"2021","journal-title":"FEBS J"},{"issue":"14","key":"10.1016\/bs.pmbts.2024.03.008_bib75","doi-asserted-by":"crossref","first-page":"1924","DOI":"10.1200\/JCO.2010.32.2271","article-title":"Amyloidosis: pathogenesis and new therapeutic options","volume":"29","author":"Merlini","year":"2011","journal-title":"J Clin Oncol"},{"issue":"24","key":"10.1016\/bs.pmbts.2024.03.008_bib76","doi-asserted-by":"crossref","first-page":"9629","DOI":"10.1073\/pnas.1121005109","article-title":"Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade","volume":"109","author":"Bulawa","year":"2012","journal-title":"Proc Natl Acad Sci"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib77","doi-asserted-by":"crossref","first-page":"79","DOI":"10.3109\/13506129.2014.997872","article-title":"Safety and efficacy of long-term diflunisal administration in hereditary transthyretin (ATTR) amyloidosis","volume":"22","author":"Sekijima","year":"2015","journal-title":"Amyloid"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib78","doi-asserted-by":"crossref","first-page":"10787","DOI":"10.1038\/ncomms10787","article-title":"Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity","volume":"7","author":"Sant\u2019Anna","year":"2016","journal-title":"Nat Commun"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib79","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1111\/j.1742-4658.2010.07956.x","article-title":"Activation, regulation, and inhibition of DYRK1A","volume":"278","author":"Becker","year":"2011","journal-title":"FEBS J"},{"issue":"9","key":"10.1016\/bs.pmbts.2024.03.008_bib80","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2016072118","article-title":"A circulating, disease-specific, mechanism-linked biomarker for ATTR polyneuropathy diagnosis and response to therapy prediction","volume":"118","author":"Jiang","year":"2021","journal-title":"Proc Natl Acad Sci"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib81","first-page":"1","article-title":"The use of diflunisal for transthyretin cardiac amyloidosis: a review","author":"Ibrahim","year":"2022","journal-title":"Heart Fail Rev"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib82","article-title":"The structural understanding of transthyretin misfolding and the inspired drug approaches for the treatment of heart failure associated with transthyretin amyloidosis","volume":"12","author":"He","year":"2021","journal-title":"Front Pharmacol"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib83","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1053\/berh.1999.0049","article-title":"Amyloid precursors and amyloidosis in rheumatoid arthritis","volume":"13","author":"Cunnane","year":"1999","journal-title":"Best Pract\u00a0Res\u00a0Clin Rheumatol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib84","doi-asserted-by":"crossref","DOI":"10.1016\/j.xkme.2022.100504","article-title":"AA Amyloid kidney disease: presentation, diagnosis, and management","author":"Thorne","year":"2022","journal-title":"Kidney Med"},{"issue":"11","key":"10.1016\/bs.pmbts.2024.03.008_bib85","doi-asserted-by":"crossref","first-page":"10148","DOI":"10.1021\/acsomega.2c07468","article-title":"Partial destabilization of amyloid-\u03b2 protofibril by methionine photo-oxidation: a molecular dynamic simulation study","volume":"8","author":"Maghsoodi","year":"2023","journal-title":"ACS Omega"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib86","doi-asserted-by":"crossref","first-page":"1382","DOI":"10.1002\/anie.201308001","article-title":"Attenuation of the aggregation and neurotoxicity of amyloid\u2010\u03b2 peptides by catalytic photooxygenation","volume":"53","author":"Taniguchi","year":"2014","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib87","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2022.945017","article-title":"Photo-oxygenation as a new therapeutic strategy for neurodegenerative proteinopathies by enhancing the clearance of amyloid proteins","volume":"14","author":"Tomizawa","year":"2022","journal-title":"Front Aging Neurosci"},{"issue":"8","key":"10.1016\/bs.pmbts.2024.03.008_bib88","doi-asserted-by":"crossref","first-page":"a004374","DOI":"10.1101\/cshperspect.a004374","article-title":"Cellular strategies of protein quality control","volume":"3","author":"Chen","year":"2011","journal-title":"Cold Spring Harb Perspect Biol"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib89","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.cell.2005.11.039","article-title":"Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells","volume":"124","author":"Albanese","year":"2006","journal-title":"Cell"},{"issue":"7","key":"10.1016\/bs.pmbts.2024.03.008_bib90","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1001100","article-title":"Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes","volume":"9","author":"Alamo","year":"2011","journal-title":"PLoS Biol"},{"issue":"3","key":"10.1016\/bs.pmbts.2024.03.008_bib91","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1016\/j.celrep.2014.09.042","article-title":"A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease","volume":"9","author":"Brehme","year":"2014","journal-title":"Cell Rep"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib92","doi-asserted-by":"crossref","first-page":"823","DOI":"10.3390\/ijms24010823","article-title":"Chaperone-Dependent mechanisms as a pharmacological target for neuroprotection","volume":"24","author":"Voronin","year":"2023","journal-title":"Int J Mol Sci"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib93","first-page":"142","article-title":"Molecular chaperones and neuronal proteostasis","volume":"40","author":"Smith","year":"2015","journal-title":"Semin\u00a0Cell\u00a0Develop\u00a0Biol"},{"issue":"7","key":"10.1016\/bs.pmbts.2024.03.008_bib94","doi-asserted-by":"crossref","first-page":"1794","DOI":"10.1093\/hmg\/ddt570","article-title":"DNAJC13 mutations in Parkinson disease","volume":"23","author":"Vilari\u00f1o-G\u00fcell","year":"2014","journal-title":"Hum Mol Genet"},{"issue":"13","key":"10.1016\/bs.pmbts.2024.03.008_bib95","doi-asserted-by":"crossref","first-page":"8447","DOI":"10.1074\/jbc.M114.627463","article-title":"Functional significance of point mutations in stress chaperone mortalin and their relevance to Parkinson disease","volume":"290","author":"Wadhwa","year":"2015","journal-title":"J Biol Chem"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib96","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1016\/j.neuron.2010.11.036","article-title":"Exome sequencing reveals VCP mutations as a cause of familial ALS","volume":"68","author":"Johnson","year":"2010","journal-title":"Neuron"},{"issue":"6","key":"10.1016\/bs.pmbts.2024.03.008_bib97","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.1021\/acschembio.6b00195","article-title":"Pharmacological chaperones: design and development of new therapeutic strategies for the treatment of conformational diseases","volume":"11","author":"Convertino","year":"2016","journal-title":"ACS Chem Biol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib98","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.phrs.2015.12.028","article-title":"Linking HSP90 target occupancy to HSP70 induction and efficacy in mouse brain","volume":"104","author":"Thirstrup","year":"2016","journal-title":"Pharmacol Res"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib99","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1016\/S1474-4422(04)00757-4","article-title":"Arimoclomol delays progression in ALS mouse model","volume":"3","author":"Love","year":"2004","journal-title":"Lancet Neurol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib100","first-page":"1","article-title":"Fighting against amyotrophic lateral sclerosis (ALS) with flavonoids: a computational approach to inhibit superoxide dismutase (SOD1) mutant aggregation","author":"Noorbakhsh Varnosfaderani","year":"2023","journal-title":"J Biomol\u00a0Struct\u00a0Dyn"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib101","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1016\/j.cell.2012.09.038","article-title":"Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients","volume":"151","author":"DeSantis","year":"2012","journal-title":"Cell"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib102","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1016\/j.biocel.2011.01.022","article-title":"Heat shock protein 104 inhibited the fibrillization of prion peptide 106\u2013126 and disassembled prion peptide 106\u2013126 fibrils in vitro","volume":"43","author":"Liu","year":"2011","journal-title":"Int J Biochem Cell Biol"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib103","doi-asserted-by":"crossref","first-page":"197","DOI":"10.4161\/pri.28938","article-title":"The therapeutic potential of chemical chaperones in protein folding diseases","volume":"8","author":"Cortez","year":"2014","journal-title":"Prion"},{"issue":"9","key":"10.1016\/bs.pmbts.2024.03.008_bib104","doi-asserted-by":"crossref","first-page":"4831","DOI":"10.1074\/jbc.273.9.4831","article-title":"Forcing thermodynamically unfolded proteins to fold","volume":"273","author":"Baskakov","year":"1998","journal-title":"J Biol Chem"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib105","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S0014-5793(01)03121-0","article-title":"Trimethylamine-N-oxide-induced folding of \u03b1-synuclein","volume":"509","author":"Uversky","year":"2001","journal-title":"FEBS Lett"},{"issue":"46","key":"10.1016\/bs.pmbts.2024.03.008_bib106","doi-asserted-by":"crossref","first-page":"32970","DOI":"10.1074\/jbc.274.46.32970","article-title":"Manipulating the amyloid-\u03b2 aggregation pathway with chemical chaperones","volume":"274","author":"Yang","year":"1999","journal-title":"J Biol Chem"},{"issue":"8","key":"10.1016\/bs.pmbts.2024.03.008_bib107","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1194\/jlr.R900007-JLR200","article-title":"Bile acids as regulatory molecules","volume":"50","author":"Hylemon","year":"2009","journal-title":"J\u00a0Lipid Res"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib108","first-page":"46","article-title":"GSK-3\u03b2, a pivotal kinase in Alzheimer disease","volume":"7","author":"Llorens-Mar\u00edtin","year":"2014","journal-title":"Front Mol Neurosci"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib109","first-page":"255","article-title":"The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases","volume":"3","author":"Wang","year":"2006","journal-title":"Cell Mol Immunol"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib110","doi-asserted-by":"crossref","first-page":"60","DOI":"10.3390\/biom11010060","article-title":"The ubiquitin\u2013proteasome system in immune cells","volume":"11","author":"\u00c7etin","year":"2021","journal-title":"Biomolecules"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib111","doi-asserted-by":"crossref","DOI":"10.1007\/s13577-023-00996-2","article-title":"Autophagy induced by Helicobacter pylori infection can lead to gastric cancer dormancy, metastasis, and recurrence: new insights","volume":"15","author":"Akbari","year":"2023","journal-title":"Hum Cell"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib112","first-page":"1","article-title":"Natural products and the balancing act of autophagy-dependent\/independent ferroptosis in cancer therapy","author":"Rahimipour Anaraki","year":"2023","journal-title":"Naunyn-Schmiedeberg\u2019s Arch Pharmacol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib113","doi-asserted-by":"crossref","first-page":"70","DOI":"10.3389\/fnmol.2014.00070","article-title":"The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution","volume":"7","author":"Dantuma","year":"2014","journal-title":"Front Mol Neurosci"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib114","doi-asserted-by":"crossref","first-page":"6609","DOI":"10.1038\/ncomms7609","article-title":"The Parkinson\u2019s-associated protein DJ-1 regulates the 20S proteasome","volume":"6","author":"Moscovitz","year":"2015","journal-title":"Nat Commun"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib115","first-page":"337","article-title":"The ubiquitin proteasome system as a potential therapeutic target for treatment of neurodegenerative diseases","volume":"34","author":"Opattova","year":"2015","journal-title":"Gen Physiol Biophys"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib116","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1038\/nm.4011","article-title":"Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling","volume":"22","author":"Myeku","year":"2016","journal-title":"Nat Med"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib117","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1038\/nrneurol.2011.200","article-title":"Control of autophagy as a therapy for neurodegenerative disease","volume":"8","author":"Harris","year":"2012","journal-title":"Nat Rev Neurol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib118","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.semcdb.2015.03.005","article-title":"Autophagy in neurodegenerative diseases: from pathogenic dysfunction to therapeutic modulation","volume":"40","author":"Martinez-Vicente","year":"2015","journal-title":"Semin Cell Develop Biol"},{"issue":"9363","key":"10.1016\/bs.pmbts.2024.03.008_bib119","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1016\/S0140-6736(03)12914-5","article-title":"Gene therapy with neprilysin reduces amyloid deposits in mice","volume":"361","author":"Senior","year":"2003","journal-title":"Lancet"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib120","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1515\/revneuro-2020-0065","article-title":"Patient-derived iPSCs, a reliable in vitro model for the investigation of Alzheimer\u2019s disease","volume":"32","author":"Amponsah","year":"2021","journal-title":"Rev Neurosci"},{"issue":"18","key":"10.1016\/bs.pmbts.2024.03.008_bib121","doi-asserted-by":"crossref","first-page":"2891","DOI":"10.1016\/j.febslet.2012.07.029","article-title":"Clearance of extracellular misfolded proteins in systemic amyloidosis: experience with transthyretin","volume":"586","author":"Almeida","year":"2012","journal-title":"FEBS Lett"},{"issue":"10","key":"10.1016\/bs.pmbts.2024.03.008_bib122","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1038\/s41593-018-0235-9","article-title":"Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases","volume":"21","author":"Soto","year":"2018","journal-title":"Nat Neurosci"},{"issue":"6","key":"10.1016\/bs.pmbts.2024.03.008_bib123","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1016\/j.neuron.2014.12.064","article-title":"Immunotherapeutic approaches for Alzheimer\u2019s disease","volume":"85","author":"Wisniewski","year":"2015","journal-title":"Neuron"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib124","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.nbd.2018.10.016","article-title":"Development of an aggregate-selective, human-derived \u03b1-synuclein antibody BIIB054 that ameliorates disease phenotypes in Parkinson\u2019s disease models","volume":"124","author":"Weihofen","year":"2019","journal-title":"Neurobiol Dis"},{"issue":"8","key":"10.1016\/bs.pmbts.2024.03.008_bib125","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1002\/mds.27738","article-title":"Randomized phase I clinical trial of anti\u2013\u03b1\u2010synuclein antibody BIIB054","volume":"34","author":"Brys","year":"2019","journal-title":"Mov Disord"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib126","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1080\/19336896.2015.1011887","article-title":"Regulating extracellular proteostasis capacity through the unfolded protein response","volume":"9","author":"Genereux","year":"2015","journal-title":"Prion"},{"issue":"6","key":"10.1016\/bs.pmbts.2024.03.008_bib127","doi-asserted-by":"crossref","first-page":"5383","DOI":"10.3390\/ijms24065383","article-title":"New pathways identify novel drug targets for the prevention and treatment of Alzheimer\u2019s disease","volume":"24","author":"Penke","year":"2023","journal-title":"Int J Mol Sci"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib128","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40035-022-00292-3","article-title":"Immunotherapy for Alzheimer\u2019s disease: targeting \u03b2-amyloid and beyond","volume":"11","author":"Song","year":"2022","journal-title":"Transl Neurodegener"},{"issue":"6740","key":"10.1016\/bs.pmbts.2024.03.008_bib129","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1038\/22124","article-title":"Immunization with amyloid-\u03b2 attenuates Alzheimer-disease-like pathology in the PDAPP mouse","volume":"400","author":"Schenk","year":"1999","journal-title":"Nature"},{"issue":"7","key":"10.1016\/bs.pmbts.2024.03.008_bib130","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/S1474-4422(12)70140-0","article-title":"Safety, tolerability, and antibody response of active A\u03b2 immunotherapy with CAD106 in patients with Alzheimer\u2019s disease: randomised, double-blind, placebo-controlled, first-in-human study","volume":"11","author":"Winblad","year":"2012","journal-title":"Lancet Neurol"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib131","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.3233\/JAD-150376","article-title":"Two phase 2 multiple ascending\u2013dose studies of vanutide cridificar (ACC-001) and QS-21 adjuvant in mild-to-moderate Alzheimer\u2019s disease","volume":"51","author":"Pasquier","year":"2016","journal-title":"J Alzheimer\u2019s Dis"},{"issue":"11","key":"10.1016\/bs.pmbts.2024.03.008_bib132","doi-asserted-by":"crossref","first-page":"4923","DOI":"10.1523\/JNEUROSCI.4672-12.2013","article-title":"Immunogenicity, efficacy, safety, and mechanism of action of epitope vaccine (Lu AF20513) for Alzheimer\u2019s disease: prelude to a clinical trial","volume":"33","author":"Davtyan","year":"2013","journal-title":"J Neurosci"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib133","first-page":"1","article-title":"Aducanumab, gantenerumab, BAN2401, and ALZ-801\u2014the first wave of amyloid-targeting drugs for Alzheimer\u2019s disease with potential for near term approval","volume":"12","author":"Tolar","year":"2020","journal-title":"Alzheimer\u2019s Res Ther"},{"issue":"10","key":"10.1016\/bs.pmbts.2024.03.008_bib134","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1007\/s40265-021-01546-6","article-title":"Current status of clinical trials on tau immunotherapies","volume":"81","author":"Ji","year":"2021","journal-title":"Drugs"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib135","first-page":"611","article-title":"Passive tau-based immunotherapy for tauopathies","volume":"vol. 196","author":"Panza","year":"2023"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib136","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S1474-4422(16)30331-3","article-title":"Safety and immunogenicity of the tau vaccine AADvac1 in patients with Alzheimer\u2019s disease: a randomised, double-blind, placebo-controlled, phase 1 trial","volume":"16","author":"Novak","year":"2017","journal-title":"Lancet Neurol"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib137","first-page":"1","article-title":"FUNDAMANT: an interventional 72-week phase 1 follow-up study of AADvac1, an active immunotherapy against tau protein pathology in Alzheimer\u2019s disease","volume":"10","author":"Novak","year":"2018","journal-title":"Alzheimer\u2019s Res Ther"},{"issue":"6","key":"10.1016\/bs.pmbts.2024.03.008_bib138","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1080\/13543784.2019.1619694","article-title":"Tau immunotherapies for Alzheimer\u2019s disease","volume":"28","author":"Hoskin","year":"2019","journal-title":"Expert Opin Invest\u00a0Drugs"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib139","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1038\/s41375-021-01317-y","article-title":"A randomized phase 3 study of ixazomib\u2013dexamethasone versus physician\u2019s choice in relapsed or refractory AL amyloidosis","volume":"36","author":"Dispenzieri","year":"2022","journal-title":"Leukemia"},{"issue":"18","key":"10.1016\/bs.pmbts.2024.03.008_bib140","first-page":"1517","article-title":"Daratumumab for systemic AL amyloidosis: prognostic factors and adverse outcome with nephrotic-range albuminuria","volume":"135","author":"Kimmich","year":"2020","journal-title":"Blood, J Am Soc Hematol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib141","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.ceb.2013.12.006","article-title":"Sorting out the trash: the spatial nature of eukaryotic protein quality control","volume":"26","author":"Sontag","year":"2014","journal-title":"Curr Opin\u00a0Cell Biol"},{"issue":"3","key":"10.1016\/bs.pmbts.2024.03.008_bib142","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1523\/JNEUROSCI.2642-12.2013","article-title":"Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer\u2019s-like tauopathy","volume":"33","author":"Iba","year":"2013","journal-title":"J Neurosci"},{"issue":"11","key":"10.1016\/bs.pmbts.2024.03.008_bib143","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.3390\/vaccines9111278","article-title":"Peptide-based vaccines for neurodegenerative diseases: recent endeavors and future perspectives","volume":"9","author":"Vassilakopoulou","year":"2021","journal-title":"Vaccines"},{"issue":"3","key":"10.1016\/bs.pmbts.2024.03.008_bib144","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1038\/sj.jcbfm.9600364","article-title":"Subthalamic glutamic acid decarboxylase gene therapy: changes in motor function and cortical metabolism","volume":"27","author":"Emborg","year":"2007","journal-title":"J Cereb Blood Flow\u00a0Metab"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib145","article-title":"Bidirectional regulation of motor circuits using magnetogenetic gene therapy","author":"Unda","year":"2023","journal-title":"bioRxiv"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib146","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1042\/BST20180025","article-title":"Mitochondrial dysfunction and neurodegenerative proteinopathies: mechanisms and prospects for therapeutic intervention","volume":"46","author":"Briston","year":"2018","journal-title":"Biochem\u00a0Soc Trans"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib147","first-page":"147","article-title":"Differential expression of oxidative phosphorylation genes in patients with Alzheimer\u2019s disease: implications for early mitochondrial dysfunction and oxidative damage","volume":"5","author":"Manczak","year":"2004","journal-title":"Neuromol\u00a0Med"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib148","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1007\/s10571-009-9398-y","article-title":"Amyloid-beta leads to impaired cellular respiration, energy production and mitochondrial electron chain complex activities in human neuroblastoma cells","volume":"29","author":"Rhein","year":"2009","journal-title":"Cell Mol Neurobiol"},{"issue":"8","key":"10.1016\/bs.pmbts.2024.03.008_bib149","doi-asserted-by":"crossref","first-page":"2191","DOI":"10.1111\/bph.12476","article-title":"Mitochondrial dysfunction in amyotrophic lateral sclerosis\u2013a valid pharmacological target?","volume":"171","author":"Muyderman","year":"2014","journal-title":"Br J Pharmacol"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib150","first-page":"357","article-title":"Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress","volume":"255","author":"Crompton","year":"1988","journal-title":"Biochem\u00a0J"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib151","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.REV120.014294","article-title":"Targeting mitophagy in Parkinson\u2019s disease","volume":"296","author":"Clark","year":"2021","journal-title":"J Biol Chem"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib152","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1007\/s00109-013-1112-3","article-title":"Nilotinib-induced autophagic changes increase endogenous parkin level and ubiquitination, leading to amyloid clearance","volume":"92","author":"Lonskaya","year":"2014","journal-title":"J Mol Med"},{"issue":"38","key":"10.1016\/bs.pmbts.2024.03.008_bib153","doi-asserted-by":"crossref","first-page":"16691","DOI":"10.1073\/pnas.1006083107","article-title":"Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin\u2019s ubiquitination and protective function","volume":"107","author":"Ko","year":"2010","journal-title":"Proc Natl Acad Sci"},{"issue":"7505","key":"10.1016\/bs.pmbts.2024.03.008_bib154","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1038\/nature13418","article-title":"The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy","volume":"510","author":"Bingol","year":"2014","journal-title":"Nature"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib155","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1091\/mbc.e07-11-1103","article-title":"Regulation of mitochondrial morphology by USP30, a deubiquitinating enzyme present in the mitochondrial outer membrane","volume":"19","author":"Nakamura","year":"2008","journal-title":"Mol Biol Cell"},{"issue":"21","key":"10.1016\/bs.pmbts.2024.03.008_bib156","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.15252\/embj.201489729","article-title":"USP 8 regulates mitophagy by removing K 6\u2010linked ubiquitin conjugates from parkin","volume":"33","author":"Durcan","year":"2014","journal-title":"Embo J"},{"issue":"13","key":"10.1016\/bs.pmbts.2024.03.008_bib157","doi-asserted-by":"crossref","first-page":"2973","DOI":"10.1093\/hmg\/dds128","article-title":"Mitochondria-targeted catalase reduces abnormal APP processing, amyloid \u03b2 production and BACE1 in a mouse model of Alzheimer\u2019s disease: implications for neuroprotection and lifespan extension","volume":"21","author":"Mao","year":"2012","journal-title":"Hum Mol Genet"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib158","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/j.freeradbiomed.2014.02.019","article-title":"Neuroprotective effects of the mitochondria-targeted antioxidant MitoQ in a model of inherited amyotrophic lateral sclerosis","volume":"70","author":"Miquel","year":"2014","journal-title":"Free Radic Biol Med"},{"issue":"12","key":"10.1016\/bs.pmbts.2024.03.008_bib159","doi-asserted-by":"crossref","first-page":"3337","DOI":"10.3390\/cells10123337","article-title":"Protein aggregation in the ER: calm behind the storm","volume":"10","author":"Li","year":"2021","journal-title":"Cells"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib160","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/j.ceb.2009.04.004","article-title":"Peripheral ER structure and function","volume":"21","author":"English","year":"2009","journal-title":"Curr Opin\u00a0Cell Biol"},{"issue":"10","key":"10.1016\/bs.pmbts.2024.03.008_bib161","doi-asserted-by":"crossref","first-page":"3171","DOI":"10.1083\/jcb.201906047","article-title":"Protein quality control in the secretory pathway","volume":"218","author":"Sun","year":"2019","journal-title":"J Cell Biol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib162","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.mam.2015.01.001","article-title":"Proinsulin misfolding and endoplasmic reticulum stress during the development and progression of diabetes","volume":"42","author":"Sun","year":"2015","journal-title":"Mol Asp Med"},{"issue":"7586","key":"10.1016\/bs.pmbts.2024.03.008_bib163","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1038\/nature17041","article-title":"Protein misfolding in the endoplasmic reticulum as a conduit to human disease","volume":"529","author":"Wang","year":"2016","journal-title":"Nature"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib164","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.molcel.2017.12.003","article-title":"Molecular mechanism of J-domain-triggered ATP hydrolysis by Hsp70 chaperones","volume":"69","author":"Kityk","year":"2018","journal-title":"Mol Cell"},{"issue":"7","key":"10.1016\/bs.pmbts.2024.03.008_bib165","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1016\/j.tcb.2005.05.007","article-title":"The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags","volume":"15","author":"Hebert","year":"2005","journal-title":"Trends Cell Biol"},{"issue":"16","key":"10.1016\/bs.pmbts.2024.03.008_bib166","doi-asserted-by":"crossref","first-page":"10221","DOI":"10.1074\/jbc.R700048200","article-title":"Getting in and out from calnexin\/calreticulin cycles","volume":"283","author":"Caramelo","year":"2008","journal-title":"J Biol Chem"},{"issue":"11","key":"10.1016\/bs.pmbts.2024.03.008_bib167","doi-asserted-by":"crossref","first-page":"a013219","DOI":"10.1101\/cshperspect.a013219","article-title":"Disulfide bond formation in the mammalian endoplasmic reticulum","volume":"4","author":"Bulleid","year":"2012","journal-title":"Cold Spring Harb Perspect Biol"},{"issue":"4","key":"10.1016\/bs.pmbts.2024.03.008_bib168","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.molcel.2014.01.004","article-title":"Protein disulfide isomerase A6 controls the decay of IRE1\u03b1 signaling via disulfide-dependent association","volume":"53","author":"Eletto","year":"2014","journal-title":"Mol Cell"},{"issue":"8","key":"10.1016\/bs.pmbts.2024.03.008_bib169","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1038\/s41580-020-0250-z","article-title":"Mechanisms, regulation and functions of the unfolded protein response","volume":"21","author":"Hetz","year":"2020","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"7","key":"10.1016\/bs.pmbts.2024.03.008_bib170","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1000415","article-title":"BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response","volume":"8","author":"Pincus","year":"2010","journal-title":"PLoS Biol"},{"issue":"6051","key":"10.1016\/bs.pmbts.2024.03.008_bib171","doi-asserted-by":"crossref","first-page":"1891","DOI":"10.1126\/science.1209126","article-title":"Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response","volume":"333","author":"Gardner","year":"2011","journal-title":"Science"},{"issue":"5888","key":"10.1016\/bs.pmbts.2024.03.008_bib172","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1126\/science.1159293","article-title":"ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER","volume":"321","author":"Ushioda","year":"2008","journal-title":"Science"},{"issue":"20","key":"10.1016\/bs.pmbts.2024.03.008_bib173","doi-asserted-by":"crossref","first-page":"3155","DOI":"10.1091\/mbc.e13-03-0138","article-title":"Glycosylation-independent ERAD pathway serves as a backup system under ER stress","volume":"24","author":"Ushioda","year":"2013","journal-title":"Mol Biol Cell"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib174","first-page":"59","article-title":"Endoplasmic reticulum protein quality control in \u03b2 cells","volume":"103","author":"Shrestha","year":"2020","journal-title":"Semin\u00a0Cell\u00a0Develop\u00a0Biol"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib175","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.molcel.2013.12.014","article-title":"Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy","volume":"53","author":"Rogov","year":"2014","journal-title":"Mol Cell"},{"issue":"8","key":"10.1016\/bs.pmbts.2024.03.008_bib176","doi-asserted-by":"crossref","first-page":"1382","DOI":"10.15252\/embr.201643587","article-title":"Structural and functional analysis of the GABARAP interaction motif (GIM)","volume":"18","author":"Rogov","year":"2017","journal-title":"EMBO Rep"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib177","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.tcb.2020.02.001","article-title":"ER-phagy: quality control and turnover of endoplasmic reticulum","volume":"30","author":"Chino","year":"2020","journal-title":"Trends Cell Biol"},{"issue":"7","key":"10.1016\/bs.pmbts.2024.03.008_bib178","first-page":"949","article-title":"ER-phagy responses in yeast, plants, and mammalian cells and their crosstalk with UPR and ERAD","volume":"56","author":"Molinari","year":"2021","journal-title":"Develop\u00a0Cell"},{"issue":"8","key":"10.1016\/bs.pmbts.2024.03.008_bib179","doi-asserted-by":"crossref","first-page":"a033928","DOI":"10.1101\/cshperspect.a033928","article-title":"Chaperoning endoplasmic reticulum\u2013associated degradation (ERAD) and protein conformational diseases","volume":"11","author":"Needham","year":"2019","journal-title":"Cold Spring Harb Perspect Biol"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib180","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1038\/nrm3565","article-title":"Signals from the lysosome: a control centre for cellular clearance and energy metabolism","volume":"14","author":"Settembre","year":"2013","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"7","key":"10.1016\/bs.pmbts.2024.03.008_bib181","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1007\/s00109-020-01935-6","article-title":"Lysosomal storage diseases: current therapies and future alternatives","volume":"98","author":"Leal","year":"2020","journal-title":"J Mol Med"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib182","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1186\/s13041-019-0504-x","article-title":"Autophagic and endo-lysosomal dysfunction in neurodegenerative disease","volume":"12","author":"Malik","year":"2019","journal-title":"Mol Brain"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib183","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2020.615740","article-title":"The role of Cathepsin B in the degradation of A\u03b2 and in the production of A\u03b2 peptides starting with Ala2 in cultured astrocytes","volume":"13","author":"Oberstein","year":"2021","journal-title":"Front Mol Neurosci"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib184","first-page":"10","article-title":"Cathepsin D: a candidate link between amyloid \u03b2-protein and tauopathy in Alzheimer disease","volume":"2","author":"Suire","year":"2021","journal-title":"J Exp Neurol"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib185","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1111\/jnc.13935","article-title":"Endo\u2010lysosomal and autophagic dysfunction: a driving factor in Alzheimer\u2019s disease?","volume":"140","author":"Whyte","year":"2017","journal-title":"J Neurochem"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib186","article-title":"Cathepsin D variants associated with neurodegenerative diseases show dysregulated functionality and modified \u03b1-synuclein degradation properties","volume":"9","author":"Bunk","year":"2021","journal-title":"Front Cell Develop\u00a0Biol"},{"issue":"5","key":"10.1016\/bs.pmbts.2024.03.008_bib187","doi-asserted-by":"crossref","first-page":"1478","DOI":"10.1091\/mbc.e08-07-0726","article-title":"Mutant huntingtin impairs post-Golgi trafficking to lysosomes by delocalizing optineurin\/Rab8 complex from the Golgi apparatus","volume":"20","author":"Del Toro","year":"2009","journal-title":"Mol Biol Cell"},{"issue":"21","key":"10.1016\/bs.pmbts.2024.03.008_bib188","doi-asserted-by":"crossref","first-page":"15613","DOI":"10.3390\/ijms242115613","article-title":"The role of cysteine protease cathepsins B, H, C, and X\/Z in neurodegenerative diseases and cancer","volume":"24","author":"Stoka","year":"2023","journal-title":"Int J Mol Sci"},{"issue":"12","key":"10.1016\/bs.pmbts.2024.03.008_bib189","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1038\/s41573-019-0036-1","article-title":"Lysosomes as a therapeutic target","volume":"18","author":"Bonam","year":"2019","journal-title":"Nat Rev Drug Discovery"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib190","unstructured":"El-Daher M.-T.Huntingtin Proteolysis and Toxicity. Universit\u00e9 Paris Sud-Paris XI;\u00a02013."},{"issue":"21","key":"10.1016\/bs.pmbts.2024.03.008_bib191","doi-asserted-by":"crossref","first-page":"17471","DOI":"10.1074\/jbc.M112.352781","article-title":"Cathepsins L and Z are critical in degrading polyglutamine-containing proteins within lysosomes","volume":"287","author":"Bhutani","year":"2012","journal-title":"J Biol Chem"},{"issue":"9","key":"10.1016\/bs.pmbts.2024.03.008_bib192","doi-asserted-by":"crossref","first-page":"2355","DOI":"10.1084\/jem.20172158","article-title":"TFEB enhances astroglial uptake of extracellular tau species and reduces tau spreading","volume":"215","author":"Martini-Stoica","year":"2018","journal-title":"J Exp Med"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib193","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2022.105855","article-title":"TFEB in Alzheimer\u2019s disease: from molecular mechanisms to therapeutic implications","author":"Gu","year":"2022","journal-title":"Neurobiol Dis"},{"issue":"3","key":"10.1016\/bs.pmbts.2024.03.008_bib194","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1111\/jnc.13411","article-title":"The contribution of neuroinflammation to amyloid toxicity in Alzheimer\u2019s disease","volume":"136","author":"Minter","year":"2016","journal-title":"J Neurochem"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib195","doi-asserted-by":"crossref","first-page":"1008","DOI":"10.3389\/fphar.2019.01008","article-title":"Neuroinflammation as a common feature of neurodegenerative disorders","volume":"10","author":"Guzman-Martinez","year":"2019","journal-title":"Front Pharmacol"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib196","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1186\/1742-2094-5-37","article-title":"Neuro-inflammation induced by lipopolysaccharide causes cognitive impairment through enhancement of beta-amyloid generation","volume":"5","author":"Lee","year":"2008","journal-title":"J Neuroinflamm"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib197","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1007\/s40263-017-0483-3","article-title":"Targeting neuroinflammation to treat Alzheimer\u2019s disease","volume":"31","author":"Ardura-Fabregat","year":"2017","journal-title":"CNS Drugs"},{"issue":"36","key":"10.1016\/bs.pmbts.2024.03.008_bib198","doi-asserted-by":"crossref","first-page":"8240","DOI":"10.1523\/JNEUROSCI.1808-05.2005","article-title":"Microglial phagocytosis induced by fibrillar \u03b2-amyloid and IgGs are differentially regulated by proinflammatory cytokines","volume":"25","author":"Koenigsknecht-Talboo","year":"2005","journal-title":"J Neurosci"},{"issue":"44","key":"10.1016\/bs.pmbts.2024.03.008_bib199","doi-asserted-by":"crossref","first-page":"9838","DOI":"10.1523\/JNEUROSCI.2557-04.2004","article-title":"Microglial phagocytosis of fibrillar \u03b2-amyloid through a \u03b21 integrin-dependent mechanism","volume":"24","author":"Koenigsknecht","year":"2004","journal-title":"J Neurosci"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib200","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1750-1326-6-45","article-title":"Microglial phagocytosis induced by fibrillar \u03b2-amyloid is attenuated by oligomeric \u03b2-amyloid: implications for Alzheimer\u2019s disease","volume":"6","author":"Pan","year":"2011","journal-title":"Mol Neurodegener"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib201","doi-asserted-by":"crossref","DOI":"10.3389\/fncel.2023.1264402","article-title":"VEGF controls microglial phagocytic response to amyloid-\u03b2","volume":"17","author":"De Gea","year":"2023","journal-title":"Front Cell Neurosci"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib202","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1742-2094-7-61","article-title":"Distinct modulation of microglial amyloid \u03b2 phagocytosis and migration by neuropeptidesi","volume":"7","author":"Fleisher-Berkovich","year":"2010","journal-title":"J Neuroinflamm"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib203","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1002\/glia.22350","article-title":"Microglia and neurodegeneration: the role of systemic inflammation","volume":"61","author":"Cunningham","year":"2013","journal-title":"Glia"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib204","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1002\/jnr.24419","article-title":"Microglial phagocytosis in aging and Alzheimer\u2019s disease","volume":"98","author":"Gaband\u00e9\u2010Rodr\u00edguez","year":"2020","journal-title":"J Neurosci Res"},{"issue":"7","key":"10.1016\/bs.pmbts.2024.03.008_bib205","doi-asserted-by":"crossref","first-page":"2026","DOI":"10.1021\/acs.accounts.9b00248","article-title":"Metal ions in Alzheimer\u2019s disease: a key role or not?","volume":"52","author":"Liu","year":"2019","journal-title":"ACC Chem Res"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib206","doi-asserted-by":"crossref","first-page":"25","DOI":"10.3389\/fnins.2018.00025","article-title":"Reconsideration of amyloid hypothesis and tau hypothesis in Alzheimer\u2019s disease","volume":"12","author":"Kametani","year":"2018","journal-title":"Front Neurosci"},{"issue":"1","key":"10.1016\/bs.pmbts.2024.03.008_bib207","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40035-020-00189-z","article-title":"Current understanding of metal ions in the pathogenesis of Alzheimer\u2019s disease","volume":"9","author":"Wang","year":"2020","journal-title":"Transl Neurodegener"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib208","article-title":"The metal ion hypothesis of Alzheimer\u2019s disease and the anti-neuroinflammatory effect of metal chelators","volume":"131","author":"Chen","year":"2023","journal-title":"Bioorg\u00a0Chem"},{"issue":"2","key":"10.1016\/bs.pmbts.2024.03.008_bib209","doi-asserted-by":"crossref","first-page":"335","DOI":"10.3390\/biomedicines11020335","article-title":"The future of precision medicine in the cure of Alzheimer\u2019s disease","volume":"11","author":"Arafah","year":"2023","journal-title":"Biomedicines"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib210","unstructured":"U.S. Food and Drug Administration.\u00a0FDA converts novel Alzheimer\u2019s disease treatment to traditional approval; 2023."},{"key":"10.1016\/bs.pmbts.2024.03.008_bib211","first-page":"1","article-title":"Special FDA designations for drug development: orphan, fast track, accelerated approval, priority review, and breakthrough therapy","author":"Michaeli","year":"2023","journal-title":"Eur J Health Econ"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib212","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1007\/s00228-018-2431-7","article-title":"A comparison of new drugs approved by the FDA, the EMA, and Swissmedic: an assessment of the international harmonization of drugs","volume":"74","author":"Zeukeng","year":"2018","journal-title":"Eur J Clin Pharmacol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib213","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1016\/j.ijbiomac.2021.07.056","article-title":"Mechanisms of amyloid proteins aggregation and their inhibition by antibodies, small molecule inhibitors, nano-particles and nano-bodies","volume":"186","author":"Salahuddin","year":"2021","journal-title":"Int J Biol Macromol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib214","doi-asserted-by":"crossref","first-page":"S44","DOI":"10.1016\/j.amjmed.2022.01.002","article-title":"Developing therapy for transthyretin amyloidosis","volume":"135","author":"Campbell","year":"2022","journal-title":"Am J Med"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib215","doi-asserted-by":"crossref","DOI":"10.1093\/braincomms\/fcad175","article-title":"Key questions for the evaluation of anti-amyloid immunotherapies for Alzheimer\u2019s disease","author":"Liu","year":"2023","journal-title":"Brain Commun"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib216","doi-asserted-by":"crossref","DOI":"10.1016\/j.jsps.2022.10.004","article-title":"An update on the novel and approved drugs for Alzheimer disease","author":"Alhazmi","year":"2022","journal-title":"Saudi Pharm J"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib217","doi-asserted-by":"crossref","first-page":"2980","DOI":"10.3389\/fimmu.2019.02980","article-title":"Amyloids in site-specific autoimmune reactions and inflammatory responses","volume":"10","author":"Huang","year":"2020","journal-title":"Front Immunol"},{"key":"10.1016\/bs.pmbts.2024.03.008_bib218","article-title":"Novel anti-amyloid-beta (A\u03b2) monoclonal antibody lecanemab for Alzheimer\u2019s disease: a systematic review","volume":"37","author":"Chowdhury","year":"2023","journal-title":"Int J Immunopathol\u00a0Pharmacol"},{"issue":"12","key":"10.1016\/bs.pmbts.2024.03.008_bib219","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1002\/acn3.469","article-title":"Efficacy and safety of anti\u2010amyloid\u2010\u03b2 immunotherapy for Alzheimer\u2019s disease: a systematic review and network meta\u2010analysis","volume":"4","author":"Mo","year":"2017","journal-title":"Ann Clin Transl Neurol"}],"container-title":["Progress in Molecular Biology and Translational Science","The Hidden World of Protein Aggregation"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1877117324000632?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1877117324000632?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,7,24]],"date-time":"2025-07-24T07:21:36Z","timestamp":1753341696000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1877117324000632"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024]]},"ISBN":["9780443293405"],"references-count":219,"URL":"https:\/\/doi.org\/10.1016\/bs.pmbts.2024.03.008","relation":{},"ISSN":["1877-1173"],"issn-type":[{"type":"print","value":"1877-1173"}],"subject":[],"published":{"date-parts":[[2024]]}}}