{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T12:30:48Z","timestamp":1790944248042,"version":"4.1.0"},"reference-count":229,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2022,3,8]],"date-time":"2022-03-08T00:00:00Z","timestamp":1646697600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Most neurodegenerative diseases such as Alzheimer\u2019s disease, type 2 diabetes, Parkinson\u2019s disease, etc. are caused by inclusions and plaques containing misfolded protein aggregates. These protein aggregates are essentially formed by the interactions of either the same (homologous) or different (heterologous) sequences. Several experimental pieces of evidence have revealed the presence of cross-seeding in amyloid proteins, which results in a multicomponent assembly; however, the molecular and structural details remain less explored. Here, we discuss the amyloid proteins and the cross-seeding phenomena in detail. Data suggest that targeting the common epitope of the interacting amyloid proteins may be a better therapeutic option than targeting only one species. We also examine the dual inhibitors that target the amyloid proteins participating in the cross-seeding events. The future scopes and major challenges in understanding the mechanism and developing therapeutics are also considered. Detailed knowledge of the amyloid cross-seeding will stimulate further research in the practical aspects and better designing anti-amyloid therapeutics.<\/jats:p>","DOI":"10.3390\/molecules27061776","type":"journal-article","created":{"date-parts":[[2022,3,9]],"date-time":"2022-03-09T01:53:54Z","timestamp":1646790834000},"page":"1776","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":113,"title":["Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition"],"prefix":"10.3390","volume":"27","author":[{"given":"Sushma","family":"Subedi","sequence":"first","affiliation":[{"name":"Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0204-0263","authenticated-orcid":false,"given":"Santanu","family":"Sasidharan","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, National Institute of Technology Warangal, Warangal 506004, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1236-9289","authenticated-orcid":false,"given":"Niharika","family":"Nag","sequence":"additional","affiliation":[{"name":"Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7211-0581","authenticated-orcid":false,"given":"Prakash","family":"Saudagar","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, National Institute of Technology Warangal, Warangal 506004, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5559-289X","authenticated-orcid":false,"given":"Timir","family":"Tripathi","sequence":"additional","affiliation":[{"name":"Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,3,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"58","DOI":"10.3390\/biology1010058","article-title":"The Surprising Role of Amyloid Fibrils in HIV Infection","volume":"1","author":"Castellano","year":"2012","journal-title":"Biology"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"e24888","DOI":"10.7554\/eLife.24888","article-title":"Semen amyloids participate in spermatozoa selection and clearance","volume":"6","author":"Roan","year":"2017","journal-title":"eLife"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1126\/science.1173155","article-title":"Functional amyloids as natural storage of peptide hormones in pituitary secretory granules","volume":"325","author":"Maji","year":"2009","journal-title":"Science"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade","volume":"86","author":"Fabrizio","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1006\/jmbi.1997.1348","article-title":"Common core structure of amyloid fibrils by synchrotron X-ray diffraction","volume":"273","author":"Sunde","year":"1997","journal-title":"J. Mol. Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1038\/nature03680","article-title":"Structure of the cross-beta spine of amyloid-like fibrils","volume":"435","author":"Nelson","year":"2005","journal-title":"Nature"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"16742","DOI":"10.1073\/pnas.262663499","article-title":"A structural model for Alzheimer\u2019s beta -amyloid fibrils based on experimental constraints from solid state NMR","volume":"99","author":"Petkova","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"4443","DOI":"10.1073\/pnas.1111305109","article-title":"Antiparallel \u03b2-sheet architecture in Iowa-mutant \u03b2-amyloid fibrils","volume":"109","author":"Qiang","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"6072","DOI":"10.1021\/bi9002666","article-title":"Evidence for novel beta-sheet structures in Iowa mutant beta-amyloid fibrils","volume":"48","author":"Tycko","year":"2009","journal-title":"Biochemistry"},{"key":"ref_10","first-page":"1127","article-title":"Amyloids: From pathogenesis to function","volume":"80","author":"Nizhnikov","year":"2015","journal-title":"Biochemistry"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"25945","DOI":"10.1074\/jbc.274.36.25945","article-title":"Amyloid \u03b2-protein fibrillogenesis: Structure and biological activity of protofibrillar intermediates","volume":"274","author":"Walsh","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"363","DOI":"10.2174\/187152709789541998","article-title":"Cross currents in protein misfolding disorders: Interactions and therapy","volume":"8","author":"Morales","year":"2009","journal-title":"CNS Neurol. Disord. Drug Targets"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1038\/nrn3549","article-title":"Parkinson\u2019s disease dementia: Convergence of \u03b1-synuclein, tau and amyloid-\u03b2 pathologies","volume":"14","author":"Irwin","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"a033118","DOI":"10.1101\/cshperspect.a033118","article-title":"Clinical neurology and epidemiology of the major neurodegenerative diseases","volume":"10","author":"Erkkinen","year":"2018","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/S1474-4422(05)70284-2","article-title":"Risk of dementia in diabetes mellitus: A systematic review","volume":"5","author":"Biessels","year":"2006","journal-title":"Lancet Neurol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1001\/archneur.64.4.570","article-title":"Relation of diabetes to mild cognitive impairment","volume":"64","author":"Luchsinger","year":"2007","journal-title":"Arch. Neurol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"e108591","DOI":"10.15252\/embj.2021108591","article-title":"Heterotypic Amyloid \u03b2 interactions facilitate amyloid assembly and modify amyloid structure","volume":"41","author":"Konstantoulea","year":"2022","journal-title":"EMBO J."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S0065-3233(08)60320-4","article-title":"The structure of amyloid fibrils by electron microscopy and X-ray diffraction","volume":"50","author":"Sunde","year":"1997","journal-title":"Adv. Protein Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1146\/annurev-biochem-061516-045104","article-title":"Structural studies of amyloid proteins at the molecular level","volume":"86","author":"Eisenberg","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1006\/jmbi.1998.2299","article-title":"Watching amyloid fibrils grow by time-lapse atomic force microscopy","volume":"285","author":"Goldsbury","year":"1999","journal-title":"J. Mol. Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1093\/emboj\/18.4.815","article-title":"Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing","volume":"18","author":"Guijarro","year":"1999","journal-title":"EMBO J."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.ymeth.2018.03.014","article-title":"3D structure determination of amyloid fibrils using solid-state NMR spectroscopy","volume":"138","author":"Loquet","year":"2018","journal-title":"Methods"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1146\/annurev-physchem-032210-103539","article-title":"Solid-State NMR Studies of Amyloid Fibril Structure","volume":"62","author":"Robert","year":"2011","journal-title":"Annu. Rev. Phys. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/s41580-018-0060-8","article-title":"A new era for understanding amyloid structures and disease","volume":"19","author":"Iadanza","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nature23002","article-title":"Cryo-EM structures of tau filaments from Alzheimer\u2019s disease","volume":"547","author":"Fitzpatrick","year":"2017","journal-title":"Nature"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1038\/s41586-019-1026-5","article-title":"Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules","volume":"568","author":"Falcon","year":"2019","journal-title":"Nature"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"e36402","DOI":"10.7554\/eLife.36402","article-title":"Cryo-EM structure of alpha-synuclein fibrils","volume":"7","author":"Taylor","year":"2018","journal-title":"eLife"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"6561","DOI":"10.1021\/cr400514h","article-title":"Introducing Protein Intrinsic Disorder","volume":"114","author":"Habchi","year":"2014","journal-title":"Chem. Rev."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"10003","DOI":"10.1021\/acsomega.9b01017","article-title":"Portrait of the Intrinsically Disordered Side of the HTLV-1 Proteome","volume":"4","author":"Lyngdoh","year":"2019","journal-title":"ACS Omega"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1002\/1097-0134(20001115)41:3<415::AID-PROT130>3.0.CO;2-7","article-title":"Why are \u201cnatively unfolded\u201d proteins unstructured under physiologic conditions?","volume":"41","author":"Uversky","year":"2000","journal-title":"Proteins"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1146\/annurev-biochem-072711-164947","article-title":"Intrinsically disordered proteins and intrinsically disordered protein regions","volume":"83","author":"Oldfield","year":"2014","journal-title":"Annu. Rev. Biochem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1016\/j.str.2010.08.009","article-title":"Biology of amyloid: Structure, function, and regulation","volume":"18","author":"Greenwald","year":"2010","journal-title":"Structure"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.conb.2020.01.010","article-title":"The molecular processes underpinning prion-like spreading and seed amplification in protein aggregation","volume":"61","author":"Meisl","year":"2020","journal-title":"Curr. Opin. Neurobiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1016\/j.cell.2012.02.022","article-title":"The amyloid state of proteins in human diseases","volume":"148","author":"Eisenberg","year":"2012","journal-title":"Cell"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"6692","DOI":"10.1039\/C3CS60431D","article-title":"Differences between amyloid-\u03b2 aggregation in solution and on the membrane: Insights into elucidation of the mechanistic details of Alzheimer\u2019s disease","volume":"43","author":"Kotler","year":"2014","journal-title":"Chem. Soc. Rev."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.sbi.2019.09.001","article-title":"Amyloid Structures: Much More than Just a Cross-\u03b2 Fold","volume":"60","author":"Gallardo","year":"2020","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"11541","DOI":"10.1021\/acs.jpcb.0c07598","article-title":"The dynamism of intrinsically disordered proteins: Binding-induced folding, amyloid formation, and phase separation","volume":"124","author":"Mukhopadhyay","year":"2020","journal-title":"J. Phys. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1038\/s41467-017-00794-z","article-title":"Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy","volume":"8","author":"Theint","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.cell.2005.01.034","article-title":"Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids","volume":"121","author":"Jones","year":"2005","journal-title":"Cell"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.tibs.2007.03.003","article-title":"Functional Amyloid\u2014From Bacteria to Humans","volume":"32","author":"Fowler","year":"2007","journal-title":"Trends Biochem. Sci."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"954","DOI":"10.1016\/j.bbapap.2019.05.010","article-title":"Bacterial Functional Amyloids: Order from Disorder","volume":"1867","author":"Jain","year":"2019","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"a033860","DOI":"10.1101\/cshperspect.a033860","article-title":"Functional Amyloids","volume":"11","author":"Otzen","year":"2019","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1202","DOI":"10.1038\/ncb3600","article-title":"Reversible protein aggregation is a protective mechanism to ensure cell cycle restart after stress","volume":"19","author":"Saad","year":"2017","journal-title":"Nat. Cell Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1016\/0092-8674(93)90635-4","article-title":"Seeding \u201cone-dimensional crystallization\u201d of amyloid: A pathogenic mechanism in Alzheimer\u2019s disease and scrapie?","volume":"73","author":"Jarrett","year":"1993","journal-title":"Cell"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1007\/s12551-017-0353-8","article-title":"Recent progress on understanding the mechanisms of amyloid nucleation","volume":"10","author":"Chatani","year":"2018","journal-title":"Biophys. Rev."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Morales, R., Moreno-Gonzalez, I., and Soto, C. (2013). Cross-seeding of misfolded proteins: Implications for etiology and pathogenesis of protein misfolding diseases. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003537"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"2334","DOI":"10.1110\/ps.073164107","article-title":"Protein aggregation processes: In search of the mechanism","volume":"16","author":"Frieden","year":"2007","journal-title":"Protein Sci."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2309","DOI":"10.1021\/cb500505m","article-title":"Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity","volume":"10","author":"Mannini","year":"2014","journal-title":"ACS Chem. Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/nn.3028","article-title":"The toxic abeta oligomer and Alzheimer\u2019s disease: An emperor in need of clothes","volume":"15","author":"Benilova","year":"2012","journal-title":"Nat. Neurosci."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"282","DOI":"10.3390\/biom5020282","article-title":"Seeking a mechanism for the toxicity of oligomeric alphasynuclein","volume":"5","author":"Roberts","year":"2015","journal-title":"Biomolecules"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/s00401-017-1709-7","article-title":"Interactions of pathological proteins in neurodegenerative diseases","volume":"134","author":"Attems","year":"2017","journal-title":"Acta Neuropathol."},{"key":"ref_52","first-page":"7267","article-title":"Fundamentals of cross-seeding of amyloid proteins: An introduction","volume":"7","author":"Ren","year":"2019","journal-title":"J. Mater. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1007\/s00401-015-1525-x","article-title":"Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo","volume":"131","author":"Vasconcelos","year":"2016","journal-title":"Acta Neuropathol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1111\/j.1471-4159.2012.07847.x","article-title":"Cross-seeding effects of amyloid-\u03b2-protein and \u03b1-synuclein","volume":"122","author":"Ono","year":"2012","journal-title":"J. Neurochem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"7604","DOI":"10.1523\/JNEUROSCI.0297-11.2011","article-title":"Induction of intracellular tau aggregation is promoted by \u03b1-synuclein seeds and provides novel insights into the hyperphosphorylation of tau","volume":"31","author":"Waxman","year":"2011","journal-title":"J. Neurosci."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1038\/mp.2016.230","article-title":"Molecular interaction between type 2 diabetes and Alzheimer\u2019s disease through cross-seeding of protein misfolding","volume":"22","author":"Edwards","year":"2017","journal-title":"Mol. Psychiatry"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"4528","DOI":"10.1523\/JNEUROSCI.5924-09.2010","article-title":"Molecular cross talk between misfolded proteins in animal models of Alzheimer\u2019s and prion diseases","volume":"30","author":"Morales","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1021\/acsomega.6b00559","article-title":"Seed-induced heterogeneous cross-seeding self-assembly of human and rat islet polypeptides","volume":"2","author":"Hu","year":"2017","journal-title":"ACS Omega"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"7212","DOI":"10.1523\/JNEUROSCI.1450-06.2006","article-title":"Synapse formation and function is modulated by the amyloid precursor protein","volume":"26","author":"Priller","year":"2006","journal-title":"J. Neurosci."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0301-0082(03)00089-3","article-title":"Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory","volume":"70","author":"Turner","year":"2003","journal-title":"Prog. Neurobiol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1016\/j.cell.2010.08.014","article-title":"Iron-export ferroxidase activity of \u03b2-amyloid precursor protein is inhibited by zinc in Alzheimer\u2019s disease","volume":"142","author":"Duce","year":"2010","journal-title":"Cell"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1016\/S0006-291X(84)80190-4","article-title":"Alzheimer\u2019s disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein","volume":"120","author":"Glenner","year":"1984","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2757","DOI":"10.1002\/j.1460-2075.1985.tb04000.x","article-title":"Neuronal origin of a cerebral amyloid: Neurofibrillary tangles of Alzheimer\u2019s disease contain the same protein as the amyloid of plaque cores and blood vessels","volume":"4","author":"Masters","year":"1985","journal-title":"EMBO J."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"4245","DOI":"10.1073\/pnas.82.12.4245","article-title":"Amyloid plaque core protein in Alzheimer disease and Down syndrome","volume":"82","author":"Masters","year":"1985","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"8830","DOI":"10.1039\/D0CC02463E","article-title":"Mixing A\u03b2(1\u201340) and A\u03b2(1\u201342) peptides generates unique amyloid fibrils","volume":"56","author":"Cerofolini","year":"2020","journal-title":"Chem. Commun."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"17342","DOI":"10.1073\/pnas.0506723102","article-title":"3D structure of Alzheimer\u2019s amyloid-beta(1-42) fibrils","volume":"102","author":"Ritter","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"6011","DOI":"10.1523\/JNEUROSCI.1189-06.2006","article-title":"Different conformations of amyloid \u03b2 induce neurotoxicity by distinct mechanisms in human cortical neurons","volume":"26","author":"Deshpande","year":"2006","journal-title":"J. Neurosci."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"311","DOI":"10.3233\/JAD-2010-1221","article-title":"Alzheimer\u2019s disease and the amyloid-\u03b2 peptide","volume":"19","author":"Murphy","year":"2010","journal-title":"J. Alzheimers Dis."},{"key":"ref_69","first-page":"330","article-title":"Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through","volume":"100","author":"Teplow","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/j.neurobiolaging.2004.08.002","article-title":"Mean age of onset in familial Alzheimer\u2019s disease is determined by amyloid beta 42","volume":"26","author":"Duering","year":"2005","journal-title":"Neurobiol. Aging"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0169-328X(86)90033-1","article-title":"Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2","volume":"1","author":"Neve","year":"1986","journal-title":"Mol. Brain Res."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1858","DOI":"10.1073\/pnas.72.5.1858","article-title":"A protein factor essential for microtubule assembly","volume":"72","author":"Weingarten","year":"1975","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1002\/j.1460-2075.1989.tb03390.x","article-title":"Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain","volume":"8","author":"Goedert","year":"1989","journal-title":"EMBO J."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"204","DOI":"10.3389\/fnagi.2019.00204","article-title":"Role of tau as a microtubule-associated protein: Structural and functional aspects","volume":"11","author":"Barbier","year":"2019","journal-title":"Front. Aging Neurosci."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1186\/gb-2004-6-1-204","article-title":"The MAP2\/Tau family of microtubule-associated proteins","volume":"6","author":"Dehmelt","year":"2005","journal-title":"Genome Biol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1126\/science.1141736","article-title":"Reducing endogenous tau ameliorates amyloid \u00df-induced deficits in an Alzheimer\u2019s disease mouse model","volume":"316","author":"Roberson","year":"2007","journal-title":"Science"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"24374","DOI":"10.1016\/S0021-9258(20)80536-5","article-title":"Microtubule-associated protein tau\u2014Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease","volume":"268","author":"Tung","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"a006247","DOI":"10.1101\/cshperspect.a006247","article-title":"Biochemistry and cell biology of tau protein in neurofibrillary degeneration","volume":"2","author":"Mandelkow","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1586\/14789450.5.2.207","article-title":"Biochemistry of Tau in Alzheimer\u2019s disease and related neurological disorders","volume":"5","author":"Sergeant","year":"2008","journal-title":"Expert Rev. Proteom."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0165-0173(00)00019-9","article-title":"Tau protein isoforms, phosphorylation and role in neurodegenerative disorders","volume":"33","author":"Delacourte","year":"2000","journal-title":"Brain Res. Rev."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"7679","DOI":"10.1074\/jbc.270.13.7679","article-title":"Microtubule-associated Protein\/Microtubule Affinity-regulating Kinase (p110mark): A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262","volume":"270","author":"Meyer","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1570","DOI":"10.1096\/fasebj.9.15.8529836","article-title":"Phosphorylation of paired helical filament tau in Alzheimer\u2019s disease neurofibrillary lesions: Focusing on phosphatases","volume":"9","author":"Trojanowski","year":"1995","journal-title":"FASEB J."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"5562","DOI":"10.1073\/pnas.91.12.5562","article-title":"Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease","volume":"91","author":"Alonso","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"4854","DOI":"10.1074\/jbc.270.9.4854","article-title":"Dephosphorylation of Alzheimer Paired Helical Filaments by Protein Phosphatase-2A and -2B","volume":"270","author":"Wang","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1083\/jcb.124.5.769","article-title":"Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau","volume":"124","author":"Goode","year":"1994","journal-title":"J. Cell Biol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/ncomms1255","article-title":"The acetylation of tau inhibits its function and promotes pathological tau aggregation","volume":"2","author":"Cohen","year":"2011","journal-title":"Nat. Commun."},{"key":"ref_87","first-page":"731526","article-title":"Structure and pathology of tau protein in Alzheimer disease","volume":"2012","author":"Kolarova","year":"2012","journal-title":"Int. J. Alzheimer\u2019s Dis."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"4884","DOI":"10.1073\/pnas.85.13.4884","article-title":"Structural characterization of the core of the paired helical filament of Alzheimer disease","volume":"85","author":"Wischik","year":"1988","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S0891-0618(01)00096-5","article-title":"Accumulation of C-terminally truncated tau protein associated with vulnerability of the perforant pathway in early stages of neurofibrillary pathology in Alzheimer\u2019s disease","volume":"22","author":"Wischik","year":"2001","journal-title":"J. Chem. Neuroanat."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.3389\/fneur.2020.590754","article-title":"Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target","volume":"11","author":"Oakley","year":"2020","journal-title":"Front. Neurol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1007\/s00401-021-02294-3","article-title":"Cryo-EM structures of tau filaments from Alzheimer\u2019s disease with PET ligand APN-1607","volume":"141","author":"Shi","year":"2021","journal-title":"Acta Neuropathol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1007\/s00401-007-0302-x","article-title":"\u03b1-Synucleinopathy models and human neuropathology: Similarities and differences","volume":"115","author":"Kahle","year":"2008","journal-title":"Acta Neuropathol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"a009399","DOI":"10.1101\/cshperspect.a009399","article-title":"\u03b1-Synuclein in Parkinson\u2019s disease","volume":"2","author":"Stefanis","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1376","DOI":"10.1021\/acschemneuro.0c00216","article-title":"A Master Regulator of \u03b1-Synuclein Aggregation","volume":"11","author":"Tripathi","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1073\/pnas.97.2.571","article-title":"Acceleration of oligomerization, not fibrillization, is a shared property of both \u03b1-synuclein mutations linked to early-onset Parkinson\u2019s disease: Implications for pathogenesis and therapy","volume":"97","author":"Conway","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"7107","DOI":"10.1021\/bi7000246","article-title":"The impact of the E46K mutation on the properties of \u03b1-synuclein in its monomeric and oligomeric states","volume":"46","author":"Fredenburg","year":"2007","journal-title":"Biochemistry"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1186\/s13024-019-0329-1","article-title":"Alpha-synuclein structure and Parkinson\u2019s disease\u2013lessons and emerging principles","volume":"14","author":"Meade","year":"2019","journal-title":"Mol. Neurodegener."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1038\/nn1443","article-title":"\u03b1-Synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease","volume":"8","author":"Chen","year":"2005","journal-title":"Nat. Neurosci."},{"key":"ref_99","first-page":"3257","article-title":"Tyrosine and serine phosphorylation of \u03b1-synuclein have opposing effects on neurotoxicity and soluble oligomer formation","volume":"119","author":"Chen","year":"2009","journal-title":"J. Clin. Investig."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"6963","DOI":"10.1523\/JNEUROSCI.6513-10.2011","article-title":"Enhanced phosphatase activity attenuates \u03b1-synucleinopathy in a mouse model","volume":"31","author":"Lee","year":"2011","journal-title":"J. Neurosci."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"3121","DOI":"10.1016\/j.bbamem.2012.08.012","article-title":"Probing ion channel activity of human islet amyloid polypeptide (amylin)","volume":"1818","author":"Zhao","year":"2012","journal-title":"Biochim. Biophys. Acta (BBA)\u2014Biomembr."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"5036","DOI":"10.1073\/pnas.87.13.5036","article-title":"Islet amyloid polypeptide: Pinpointing amino acid residues linked to amyloid fibril formation","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"11012","DOI":"10.1021\/ja00076a078","article-title":"Interspecies sequence variations affect the kinetics and thermodynamics of amyloid formation: Peptide models of pancreatic amyloid","volume":"115","author":"Ashburn","year":"1993","journal-title":"J. Am. Chem. Soc."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bpc.2012.05.003","article-title":"A mechanistic insight into the amyloidogenic structure of hIAPP peptide revealed from sequence analysis and molecular dynamics simulation","volume":"168","author":"Chakraborty","year":"2012","journal-title":"Biophys. Chem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"7606","DOI":"10.1039\/C4CP05563B","article-title":"On the lag phase in amyloid fibril formation","volume":"17","author":"Arosio","year":"2015","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"11970","DOI":"10.1074\/jbc.M109541200","article-title":"Biophysical properties of the synucleins and their propensities to fibrillate: Inhibition of \u03b1-synuclein assembly by \u03b2-and \u03b3-synucleins","volume":"277","author":"Uversky","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.ijbiomac.2018.10.205","article-title":"Repulsive interaction induces fibril formation and their growth","volume":"123","author":"Khatun","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1515\/hsz-2020-0174","article-title":"Human islet amyloid polypeptide (hIAPP)-a curse in type II diabetes mellitus: Insights from structure and toxicity studies","volume":"402","author":"Bishoyi","year":"2021","journal-title":"Biol. Chem."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.jmb.2005.02.029","article-title":"The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin","volume":"348","author":"Kajava","year":"2005","journal-title":"J. Mol. Biol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"2118","DOI":"10.1002\/anie.200804198","article-title":"Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy","volume":"48","author":"Nielsen","year":"2009","journal-title":"Angew Chem."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/s41594-020-0435-3","article-title":"Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils","volume":"27","author":"Cao","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1152\/physrev.00006.2009","article-title":"Prions: Protein aggregation and infectious diseases","volume":"89","author":"Aguzzi","year":"2009","journal-title":"Physiol. Rev."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1126\/science.6801762","article-title":"Novel proteinaceous infectious particles cause scrapie","volume":"216","author":"Prusiner","year":"1982","journal-title":"Science"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1006\/jmbi.1994.0030","article-title":"Prion protein gene variation among primates","volume":"245","author":"Taylor","year":"1995","journal-title":"J. Mol. Biol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1006\/jmbi.1999.2831","article-title":"Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein","volume":"289","author":"Wopfner","year":"1999","journal-title":"J. Mol. Biol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"169","DOI":"10.3389\/fnmol.2019.00169","article-title":"Recent advances in understanding mammalian prion structure: A mini review","volume":"12","author":"Terry","year":"2019","journal-title":"Front. Mol. Neurosci."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1038\/45574","article-title":"Transmissible and genetic prion diseases share a common pathway of neurodegeneration","volume":"402","author":"Hegde","year":"1999","journal-title":"Nature"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"529","DOI":"10.2174\/138920309789352056","article-title":"Copper binding extrinsic to the octarepeat region in the prion protein","volume":"10","author":"Walter","year":"2009","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"12229","DOI":"10.1021\/ja2045259","article-title":"Copper redox cycling in the prion protein depends critically on binding mode","volume":"133","author":"Liu","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/bs.pmbts.2017.06.018","article-title":"Cell biology of prion protein","volume":"150","author":"Sarnataro","year":"2017","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"36139","DOI":"10.1074\/jbc.M304002200","article-title":"Post-translational import of the prion protein into the endoplasmic reticulum interferes with cell viability: A critical role for the putative transmembrane domain","volume":"278","author":"Heller","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"9678","DOI":"10.1073\/pnas.90.20.9678","article-title":"Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro","volume":"90","author":"Tagliavini","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1038\/sj.emboj.7601510","article-title":"Lethal recessive myelin toxicity of prion protein lacking its central domain","volume":"26","author":"Baumann","year":"2007","journal-title":"EMBO J."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"3356","DOI":"10.1091\/mbc.e06-01-0083","article-title":"Association of Bcl-2 with misfolded prion protein is linked to the toxic potential of cytosolic PrP","volume":"17","author":"Rambold","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"10962","DOI":"10.1073\/pnas.90.23.10962","article-title":"Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins","volume":"90","author":"Pan","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1038\/s41594-020-0403-y","article-title":"Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core","volume":"27","author":"Glynn","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"13363","DOI":"10.1073\/pnas.95.23.13363","article-title":"Prions","volume":"95","author":"Prusiner","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/0092-8674(95)90236-8","article-title":"Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein","volume":"83","author":"Telling","year":"1995","journal-title":"Cell"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/ncomms1282","article-title":"Rapid cell-surface prion protein conversion revealed using a novel cell system","volume":"2","author":"Goold","year":"2011","journal-title":"Nat. Commun."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Marijanovic, Z., Caputo, A., Campana, V., and Zurzolo, C. (2009). Identification of an intracellular site of prion conversion. PLoS Pathol., 5.","DOI":"10.1371\/journal.ppat.1000426"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"14367","DOI":"10.1073\/pnas.0602348103","article-title":"Normal-repeat-length polyglutamine peptides accelerate aggregation nucleation and cytotoxicity of expanded polyglutamine proteins","volume":"103","author":"Slepko","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"19509","DOI":"10.1074\/jbc.274.28.19509","article-title":"\u03b1-Synuclein Fibrillogenesis Is Nucleation-dependent: Implications for the pathogenesis of Parkinson\u2019 s disease","volume":"274","author":"Wood","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1002\/ijch.201600103","article-title":"Oligomer Formation and Cross-Seeding: The New Frontier","volume":"57","author":"Farmer","year":"2017","journal-title":"Isr. J. Chem."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"8001","DOI":"10.1021\/bi501333q","article-title":"Evidence of rapid coaggregation of globular proteins during amyloid formation","volume":"53","author":"Dubey","year":"2014","journal-title":"Biochemistry"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1428","DOI":"10.1016\/j.ijbiomac.2017.10.004","article-title":"Mechanism of co-aggregation in a protein mixture with small additives","volume":"107","author":"Oki","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2781","DOI":"10.1021\/jacs.7b13660","article-title":"E22G pathogenic mutation of \u03b2-amyloid (A\u03b2) enhances misfolding of A\u03b240 by unexpected prion-like cross talk between A\u03b242 and A\u03b240","volume":"140","author":"Yoo","year":"2018","journal-title":"J. Am. Chem. Soc."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"2888","DOI":"10.1074\/jbc.M117.806109","article-title":"Common fibrillar spines of amyloid-\u03b2 and human islet amyloid polypeptide revealed by microelectron diffraction and structure-based inhibitors","volume":"293","author":"Krotee","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1038\/nature25158","article-title":"Microglia-derived ASC specks cross-seed amyloid-\u03b2 in Alzheimer\u2019s disease","volume":"552","author":"Venegas","year":"2017","journal-title":"Nature"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1016\/j.bbadis.2014.01.002","article-title":"Exogenous amyloidogenic proteins function as seeds in amyloid \u03b2-protein aggregation","volume":"1842","author":"Ono","year":"2014","journal-title":"Biochim. Biophys. Acta (BBA)\u2014Mol. Basis Dis."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"3276","DOI":"10.1021\/acs.jpclett.5b01447","article-title":"A\u03b2 \u201cstretching-and-packing\u201d cross-seeding mechanism can trigger tau protein aggregation","volume":"6","author":"Qi","year":"2015","journal-title":"J. Phys. Chem. Lett."},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Raz, Y., and Miller, Y. (2013). Interactions between A\u03b2 and mutated Tau lead to polymorphism and induce aggregation of A\u03b2-mutated tau oligomeric complexes. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0073303"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1021\/acschemneuro.6b00357","article-title":"Alzheimer\u2019s Protective Cross-Interaction between Wild-Type and A2T Variants Alters A\u03b242 Dimer Structure","volume":"8","author":"Das","year":"2017","journal-title":"ACS Chem. Neurosci."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"5172","DOI":"10.1021\/bi200400u","article-title":"Synergistic interactions between repeats in tau protein and A\u03b2 amyloids may be responsible for accelerated aggregation via polymorphic states","volume":"50","author":"Miller","year":"2011","journal-title":"Biochemistry"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"14950","DOI":"10.1074\/jbc.M112.340794","article-title":"Cross-seeding and conformational selection between three-and four-repeat human Tau proteins","volume":"287","author":"Yu","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.1021\/cn400141x","article-title":"In silico cross seeding of A\u03b2 and amylin fibril-like oligomers","volume":"4","author":"Berhanu","year":"2013","journal-title":"ACS Chem. Neurosci."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"1628","DOI":"10.1021\/acs.jcim.5b00166","article-title":"Polymorphic associations and structures of the cross-seeding of A\u03b21\u201342 and hIAPP1\u201337 polypeptides","volume":"55","author":"Zhang","year":"2015","journal-title":"J. Chem. Inf. Model."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"23245","DOI":"10.1039\/C5CP03329B","article-title":"Polymorphic cross-seeding amyloid assemblies of amyloid-\u03b2 and human islet amyloid polypeptide","volume":"17","author":"Zhang","year":"2015","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"3373","DOI":"10.1016\/j.celrep.2016.08.053","article-title":"Molecular and biological compatibility with host alpha-synuclein influences fibril pathogenicity","volume":"16","author":"Luk","year":"2016","journal-title":"Cell Rep."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"13910","DOI":"10.1074\/jbc.RA118.001862","article-title":"The effect of truncation on prion-like properties of \u03b1-synuclein","volume":"293","author":"Terada","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"3847","DOI":"10.1016\/j.jmb.2018.08.002","article-title":"Quinolinic acid amyloid-like fibrillar assemblies seed \u03b1-synuclein aggregation","volume":"430","author":"Tavassoly","year":"2018","journal-title":"J. Mol. Biol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1021\/acschemneuro.5b00204","article-title":"Non-amyloid-\u03b2 component of human \u03b1-synuclein oligomers induces formation of new A\u03b2 oligomers: Insight into the mechanisms that link Parkinson\u2019s and Alzheimer\u2019s diseases","volume":"7","author":"Miller","year":"2016","journal-title":"ACS Chem. Neurosci."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1002\/pro.3421","article-title":"Seeding and cross-seeding fibrillation of N-terminal prion protein peptides PrP (120\u2013144)","volume":"27","author":"Wang","year":"2018","journal-title":"Protein Sci."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Katorcha, E., Makarava, N., Lee, Y.J., Lindberg, I., Monteiro, M.J., Kovacs, G.G., and Baskakov, I.V. (2017). Cross-seeding of prions by aggregated \u03b1-synuclein leads to transmissible spongiform encephalopathy. PLoS Pathol., 13.","DOI":"10.1371\/journal.ppat.1006563"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"9685","DOI":"10.1021\/jacs.8b05925","article-title":"Hetero-oligomeric amyloid assembly and mechanism: Prion fragment PrP (106\u2013126) catalyzes the islet amyloid polypeptide \u03b2-hairpin","volume":"140","author":"Ilitchev","year":"2018","journal-title":"J. Am. Chem. Soc."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"1134","DOI":"10.1002\/prot.25060","article-title":"Replica exchange molecular dynamics simulation of cross-fibrillation of IAPP and PrP106-126","volume":"84","author":"Chua","year":"2016","journal-title":"Proteins Struct. Funct. Bioinform."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"1759","DOI":"10.1021\/acschemneuro.5b00192","article-title":"Cross-seeding interaction between \u03b2-amyloid and human islet amyloid polypeptide","volume":"6","author":"Hu","year":"2015","journal-title":"ACS Chem. Neurosci."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"10373","DOI":"10.1039\/C4CP05658B","article-title":"Interfacial interaction and lateral association of cross-seeding assemblies between hIAPP and rIAPP oligomers","volume":"17","author":"Zhang","year":"2015","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"7026","DOI":"10.1021\/jp5022246","article-title":"Structural and energetic insight into the cross-seeding amyloid assemblies of human IAPP and rat IAPP","volume":"118","author":"Zhang","year":"2014","journal-title":"J. Phys. Chem. B"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1021\/acschemneuro.6b00247","article-title":"Molecular understanding of A\u03b2-hIAPP cross-seeding assemblies on lipid membranes","volume":"8","author":"Zhang","year":"2017","journal-title":"ACS Chem. Neurosci."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"14673","DOI":"10.1021\/jacs.5b07849","article-title":"N-terminal extensions retard A\u03b242 fibril formation but allow cross-seeding and coaggregation with A\u03b242","volume":"137","author":"Szczepankiewicz","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1002\/1873-3468.12526","article-title":"Cross-seeding between A\u03b240 and A\u03b242 in Alzheimer\u2019s disease","volume":"591","author":"Tran","year":"2017","journal-title":"FEBS Lett."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1523\/JNEUROSCI.4849-06.2007","article-title":"A\u03b240 inhibits amyloid deposition in vivo","volume":"27","author":"Kim","year":"2007","journal-title":"J. Neurosci."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1038\/s41467-017-00579-4","article-title":"Seed-induced acceleration of amyloid-\u03b2 mediated neurotoxicity in vivo","volume":"8","author":"Sowade","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"S10","DOI":"10.1038\/nm1066","article-title":"Protein aggregation and neurodegenerative disease","volume":"10","author":"Ross","year":"2004","journal-title":"Nat. Med."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1126\/science.1062097","article-title":"Formation of neurofibrillary tangles in P301L tau transgenic mice induced by A\u03b242 fibrils","volume":"293","author":"Chen","year":"2001","journal-title":"Science"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"1953","DOI":"10.1073\/pnas.0509386103","article-title":"A\u03b2 and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer\u2019s disease","volume":"103","author":"Guo","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1038\/nchem.2889","article-title":"Structure-based inhibitors of tau aggregation","volume":"10","author":"Seidler","year":"2018","journal-title":"Nat. Chem."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"e46924","DOI":"10.7554\/eLife.46924","article-title":"Structure-based inhibitors of amyloid beta core suggest a common interface with tau","volume":"8","author":"Griner","year":"2019","journal-title":"eLife"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1021\/acs.biochem.9b01087","article-title":"Direct Interaction between the \u03b2-Amyloid Core and Tau Facilitates Cross-Seeding: A Novel Target for Therapeutic Intervention","volume":"59","author":"Tripathi","year":"2020","journal-title":"Biochemistry"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1016\/j.neurobiolaging.2014.02.009","article-title":"Differential aggregation properties of alpha-synuclein isoforms","volume":"35","author":"Bungeroth","year":"2014","journal-title":"Neurobiol. Aging"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.neulet.2014.01.009","article-title":"Alpha-synuclein transcript isoforms in three different brain regions from Parkinson\u2019s disease and healthy subjects in relation to the SNCA rs356165\/rs11931074 polymorphisms","volume":"562","author":"Cardo","year":"2014","journal-title":"Neurosci. Lett."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1046\/j.1471-4159.2001.00301.x","article-title":"Interaction of \u03b1-synuclein and synphilin-1: Effect of Parkinson\u2019s disease-associated mutations","volume":"77","author":"Kawamata","year":"2001","journal-title":"J. Neurochem."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1038\/8820","article-title":"Synphilin-1 associates with \u03b1-synuclein and promotes the formation of cytosolic inclusions","volume":"22","author":"Engelender","year":"1999","journal-title":"Nat. Genet."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1007\/s00018-007-7343-0","article-title":"Synphilin-1 isoforms in Parkinson\u2019s disease: Regulation by phosphorylation and ubiquitylation","volume":"65","author":"Szargel","year":"2008","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/bpa.12344","article-title":"Lewy Bodies and the Mechanisms of Neuronal Cell Death in Parkinson\u2019s Disease and Dementia with Lewy Bodies","volume":"27","author":"Power","year":"2017","journal-title":"Brain Pathol"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1186\/s13024-021-00465-0","article-title":"Extracellular protein components of amyloid plaques and their roles in Alzheimer\u2019s disease pathology","volume":"16","author":"Rahman","year":"2021","journal-title":"Mol. Neurodegener."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.neuron.2019.10.010","article-title":"Amyloid-Beta (A\u03b2) Plaques Promote Seeding and Spreading of Alpha-Synuclein and Tau in a Mouse Model of Lewy Body Disorders with A\u03b2 Pathology","volume":"105","author":"Bassil","year":"2020","journal-title":"Neuron"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1046\/j.1471-4159.2001.00408.x","article-title":"Identification of the region of non -A\u03b2 component (NAC) of Alzheimer\u2019s disease amyloid responsible for its aggregation and toxicity","volume":"78","author":"Bodles","year":"2001","journal-title":"J. Neurochem."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1007\/s11064-006-9140-9","article-title":"Interaction between A\u03b2 Peptide and \u03b1-Synuclein: Molecular Mechanisms in Overlapping Pathology of Alzheimer\u2019s and Parkinson\u2019s in Dementia with Lewy Body Disease","volume":"31","author":"Mandal","year":"2006","journal-title":"Neurochem. Res."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"10356","DOI":"10.1038\/s41598-020-66602-9","article-title":"Amylin and beta amyloid proteins interact to form amorphous heterocomplexes with enhanced toxicity in neuronal cells","volume":"10","author":"Bharadwaj","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1016\/j.ajpath.2014.11.016","article-title":"In Vivo Seeding and Cross-Seeding of Localized Amyloidosis: A Molecular Link between Type 2 Diabetes and Alzheimer Disease","volume":"185","author":"Oskarsson","year":"2015","journal-title":"Am. J. Pathol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1002\/1531-8249(199903)45:3<353::AID-ANA11>3.0.CO;2-4","article-title":"Antibodies to alpha-synuclein detect Lewy bodies in many Down\u2019s syndrome brains with Alzheimer\u2019s disease","volume":"45","author":"Lippa","year":"1999","journal-title":"Ann. Neurol."},{"key":"ref_183","doi-asserted-by":"crossref","unstructured":"Badiola, N., de Oliveira, R.M., Herrera, F., Guardia-Laguarta, C., Gon\u00e7alves, S.A., Pera, M., Su\u00e1rez-Calvet, M., Clarimon, J., Outeiro, T.F., and Lle\u00f3, A. (2011). Tau enhances \u03b1-synuclein aggregation and toxicity in cellular models of synucleinopathy. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0026609"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/j.biopsych.2017.12.018","article-title":"\u03b1-Synuclein Oligomers Induce a Unique Toxic Tau Strain","volume":"84","author":"Sengupta","year":"2018","journal-title":"Biol. Psychiatry"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"741662","DOI":"10.3389\/fcell.2021.741662","article-title":"Interactions and Cytotoxicity of Human Neurodegeneration\u2014Associated Proteins Tau and \u03b1-Synuclein in the Simple Model Dictyostelium discoideum","volume":"9","author":"Mroczek","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.nbd.2010.05.026","article-title":"Neurodegenerative models in Drosophila: Polyglutamine disorders, Parkinson disease, and amyotrophic lateral sclerosis","volume":"40","author":"Ambegaokar","year":"2010","journal-title":"Neurobiol. Dis."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"e20192193","DOI":"10.1084\/jem.20192193","article-title":"\u03b1-Synuclein modulates tau spreading in mouse brains","volume":"218","author":"Bassil","year":"2021","journal-title":"J. Exp. Med."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1007\/s00401-018-1832-0","article-title":"Interaction of amyloidogenic proteins in pancreatic \u03b2 cells from subjects with synucleinopathies","volume":"135","author":"Marcilla","year":"2018","journal-title":"Acta Neuropathol."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"20438","DOI":"10.1038\/s41598-020-77409-z","article-title":"\u03b1-Synuclein promotes IAPP fibril formation in vitro and \u03b2-cell amyloid formation in vivo in mice","volume":"10","author":"Mucibabic","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1002\/pro.4247","article-title":"A new strategy to reconcile amyloid cross-seeding and amyloid prevention in a binary system of \u03b1-synuclein fragmental peptide and hIAPP","volume":"31","author":"Tang","year":"2022","journal-title":"Protein Sci."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"3300","DOI":"10.1039\/D0TB02958K","article-title":"Dual amyloid cross-seeding reveals steric zipper-facilitated fibrillization and pathological links between protein misfolding diseases","volume":"9","author":"Zhang","year":"2021","journal-title":"J. Mater. Chem. B"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"2057","DOI":"10.1021\/acschemneuro.1c00235","article-title":"Dual Inhibitors of Amyloid-\u03b2 and Tau Aggregation with Amyloid-\u03b2 Disaggregating Properties: Extended In Cellulo, In Silico, and Kinetic Studies of Multifunctional Anti-Alzheimer\u2019s Agents","volume":"12","author":"Pasieka","year":"2021","journal-title":"ACS Chem. Neurosci."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"15095","DOI":"10.1074\/jbc.M110.199356","article-title":"Amyloid-\u03b242 interacts mainly with insoluble prion protein in the Alzheimer brain","volume":"286","author":"Zou","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"10050","DOI":"10.1038\/s41598-017-10236-x","article-title":"\u03b1-Synuclein amyloids hijack prion protein to gain cell entry, facilitate cell-to-cell spreading and block prion replication","volume":"7","author":"Masperone","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"10168","DOI":"10.1073\/pnas.97.18.10168","article-title":"Genetic influence on the structural variations of the abnormal prion protein","volume":"97","author":"Parchi","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1056\/NEJMc1610003","article-title":"Variant Creutzfeldt\u2013Jakob disease in a patient with heterozygosity at PRNP codon 129","volume":"376","author":"Mok","year":"2017","journal-title":"N. Engl. J. Med."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"fcaa030","DOI":"10.1093\/braincomms\/fcaa030","article-title":"Prion protein codon 129 polymorphism in mild cognitive impairment and dementia: The Rotterdam Study","volume":"2","author":"Ahmad","year":"2020","journal-title":"Brain Commun."},{"key":"ref_198","first-page":"342","article-title":"Homozygous prion protein genotype predisposes to sporadic Creutzfeld-Jakob disease","volume":"352","author":"Palmer","year":"1991","journal-title":"Nature"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"2132","DOI":"10.1093\/brain\/awl153","article-title":"Semantic impairment in stroke aphasia versus semantic dementia: A case-series comparison","volume":"129","author":"Jefferies","year":"2006","journal-title":"Brain"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1097\/WNR.0b013e328318edfa","article-title":"Effects of human PrPSc type and PRNP genotype in an in-vitro conversion assay","volume":"19","author":"Jones","year":"2008","journal-title":"Neuroreport"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.3201\/eid1512.090194","article-title":"Molecular model of prion transmission to humans","volume":"15","author":"Jones","year":"2009","journal-title":"Emerg. Infect. Dis."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"5153","DOI":"10.1523\/JNEUROSCI.0783-09.2009","article-title":"Cross-Seeding Fibrillation of Q\/N-Rich Proteins Offers New Pathomechanism of Polyglutamine Diseases","volume":"29","author":"Furukawa","year":"2009","journal-title":"J. Neurosci."},{"key":"ref_203","first-page":"606172","article-title":"The aggregation of huntingtin and \u03b1-synuclein","volume":"2012","year":"2012","journal-title":"J. Biophys."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1093\/hmg\/ddr507","article-title":"\u03b1-Synuclein accumulates in huntingtin inclusions but forms independent filaments and its deficiency attenuates early phenotype in a mouse model of Huntington\u2019s disease","volume":"21","author":"Ferrer","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1021\/acschemneuro.2c00083","article-title":"Cross-Seeding with Homologous Sequences Alters Amyloid Aggregation Kinetics and Fibril Structure","volume":"13","author":"Nag","year":"2022","journal-title":"ACS Chem. Neurosci."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1111\/j.1399-0004.1991.tb03085.x","article-title":"Biochemical effect of liver transplantation in two Swedish patients with familial amyloidotic polyneuropathy (FAP-met30)","volume":"40","author":"Holmgren","year":"1991","journal-title":"Clin. Genet."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1097\/00007890-199806150-00016","article-title":"Domino hepatic transplantation using the liver from a patient with familial amyloid polyneuropathy","volume":"65","author":"Stangou","year":"1998","journal-title":"Transplantation"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1136\/jnnp.2010.218958","article-title":"Systemic but asymptomatic transthyretin amyloidosis 8 years after domino liver transplantation","volume":"82","author":"Koike","year":"2011","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"e1587","DOI":"10.1212\/WNL.0000000000008360","article-title":"Characteristics of acquired transthyretin amyloidosis: A case series and review of the literature","volume":"93","author":"Misumi","year":"2019","journal-title":"Neurology"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1111\/j.1600-6143.2006.01585.x","article-title":"Progressive wild-type transthyretin deposition after liver transplantation preferentially occurs onto myocardium in FAP patients","volume":"7","author":"Yazaki","year":"2007","journal-title":"Am. J. Transplant."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1080\/13506120701614032","article-title":"Progression of cardiac amyloid deposition in hereditary transthyretin amyloidosis patients after liver transplantation","volume":"14","author":"Liepnieks","year":"2007","journal-title":"Amyloid"},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"2133","DOI":"10.2169\/internalmedicine.47.1399","article-title":"Evaluation of myocardial changes in familial amyloid polyneuropathy after liver transplantation","volume":"47","author":"Okamoto","year":"2008","journal-title":"Intern. Med."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1097\/00007890-200301150-00018","article-title":"Factors influencing liver regeneration following living-donor liver transplantation of the right hepatic lobe","volume":"75","author":"Maetani","year":"2003","journal-title":"Transplantation"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"313","DOI":"10.3233\/JAD-161017","article-title":"PE859, a novel curcumin derivative, inhibits amyloid-\u03b2 and tau aggregation, and ameliorates cognitive dysfunction in senescence-accelerated mouse prone 8","volume":"59","author":"Okuda","year":"2017","journal-title":"J. Alzheimers Dis."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"e50","DOI":"10.1002\/ctm2.50","article-title":"A natural BACE1 and GSK3\u03b2 dual inhibitor Notopterol effectively ameliorates the cognitive deficits in APP\/PS1 Alzheimer\u2019s mice by attenuating amyloid-\u03b2 and tau pathology","volume":"10","author":"Jiang","year":"2020","journal-title":"Clin. Transl. Med."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.2147\/DDDT.S289473","article-title":"Epigallocatechin-3-Gallate Provides Protection Against Alzheimer\u2019s Disease-Induced Learning and Memory Impairments in Rats","volume":"13","author":"Nan","year":"2021","journal-title":"Drug Des. Dev. Ther."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"11024","DOI":"10.1074\/jbc.M112.436006","article-title":"Aminothienopyridazines and Methylene Blue Affect Tau Fibrillization via Cysteine Oxidation","volume":"288","author":"Crowe","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"1677","DOI":"10.3233\/JAD-181001","article-title":"Methylene Blue Inhibits Formation of Tau Fibrils but not of Granular Tau Oligomers: A Plausible Key to Understanding Failure of a Clinical Trial for Alzheimer\u2019s Disease","volume":"68","author":"Soeda","year":"2019","journal-title":"J. Alzheimers Dis."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"474","DOI":"10.2337\/diabetes.53.2.474","article-title":"Increased risk of type 2 diabetes in Alzheimer disease","volume":"53","author":"Janson","year":"2004","journal-title":"Diabetes"},{"key":"ref_220","first-page":"493","article-title":"High affinity amylin binding sites in rat brain","volume":"44","author":"Beaumont","year":"1993","journal-title":"Mol. Pharmacol."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"3081","DOI":"10.1002\/anie.200904902","article-title":"Identification of Hot Regions of the A\u03b2-IAPP Interaction Interface as High-Affinity Binding Sites in both Cross- and Self-Association","volume":"49","author":"Andreetto","year":"2011","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"25929","DOI":"10.1039\/D0RA04949B","article-title":"Bleomycin modulates amyloid aggregation in \u03b2-amyloid and hIAPP","volume":"10","author":"Kumari","year":"2020","journal-title":"RSC Adv."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1021\/acschemneuro.8b00039","article-title":"Genistein: A Dual Inhibitor of Both Amyloid \u03b2 and Human Islet Amylin Peptides","volume":"9","author":"Ren","year":"2018","journal-title":"ACS Chem. Neurosci."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"34","DOI":"10.3109\/13506129.2012.762761","article-title":"IAPP aggregation and cellular toxicity are inhibited by 1,2,3,4,6-penta-O-galloyl-\u03b2-d-glucose","volume":"20","author":"Bruno","year":"2013","journal-title":"Amyloid"},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.ijms.2016.09.018","article-title":"1,2,3,4,6-penta-O-galloyl-\u03b2-d-glucopyranose binds to the N-terminal metal binding region to inhibit amyloid \u03b2-protein oligomer and fibril formation","volume":"420","author":"Do","year":"2017","journal-title":"Int. J. Mass Spectrom."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1039\/C7TB02538F","article-title":"Tanshinones inhibit hIAPP aggregation, disaggregate preformed hIAPP fibrils, and protect cultured cells","volume":"6","author":"Ren","year":"2018","journal-title":"J. Mater. Chem. B"},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"14941","DOI":"10.1074\/jbc.M109.080390","article-title":"Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity","volume":"285","author":"Eleuteri","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1111\/j.1471-4159.2006.03707.x","article-title":"Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for \u03b1-synuclein fibrils in vitro","volume":"97","author":"Ono","year":"2006","journal-title":"J. Neurochem."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"2051","DOI":"10.1021\/acschemneuro.0c00281","article-title":"Dual Targeting of Monomeric Tau and \u03b1-Synuclein Aggregation: A New Multitarget Therapeutic Strategy for Neurodegeneration","volume":"11","author":"Gabr","year":"2020","journal-title":"ACS Chem. Neurosci."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/27\/6\/1776\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T22:34:13Z","timestamp":1760135653000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/27\/6\/1776"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,3,8]]},"references-count":229,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2022,3]]}},"alternative-id":["molecules27061776"],"URL":"https:\/\/doi.org\/10.3390\/molecules27061776","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,3,8]]}}}