{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T02:31:48Z","timestamp":1792809108688,"version":"4.5.0"},"reference-count":340,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,3,1]],"date-time":"2022-03-01T00:00:00Z","timestamp":1646092800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,3,1]],"date-time":"2022-03-01T00:00:00Z","timestamp":1646092800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,3,1]],"date-time":"2022-03-01T00:00:00Z","timestamp":1646092800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,3,1]],"date-time":"2022-03-01T00:00:00Z","timestamp":1646092800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,3,1]],"date-time":"2022-03-01T00:00:00Z","timestamp":1646092800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,3,1]],"date-time":"2022-03-01T00:00:00Z","timestamp":1646092800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,3,1]],"date-time":"2022-03-01T00:00:00Z","timestamp":1646092800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2022,3]]},"DOI":"10.1016\/j.ijbiomac.2022.01.115","type":"journal-article","created":{"date-parts":[[2022,1,22]],"date-time":"2022-01-22T01:49:28Z","timestamp":1642816168000},"page":"593-617","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":32,"special_numbering":"C","title":["The amyloid state of proteins: A boon or bane?"],"prefix":"10.1016","volume":"200","author":[{"given":"Md Nadir","family":"Hassan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Faisal","family":"Nabi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Asra Nasir","family":"Khan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Murtaza","family":"Hussain","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Waseem A.","family":"Siddiqui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vladimir N.","family":"Uversky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rizwan Hasan","family":"Khan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0005","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1006\/jsbi.2000.4221","article-title":"Review: history of the amyloid fibril","volume":"130","author":"Sipe","year":"2000","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0010","doi-asserted-by":"crossref","first-page":"1","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."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0015","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1080\/13506129.2016.1257986","article-title":"Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines","volume":"23","author":"Sipe","year":"2016","journal-title":"Amyloid"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0020","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1146\/annurev.publhealth.23.100901.140525","article-title":"The public health impact of Alzheimer\u2019s disease, 2000\u20132050: potential implication of treatment advances","volume":"23","author":"Sloane","year":"2002","journal-title":"Annu. Rev. Public Health"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0025","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1038\/nrm3810","article-title":"The amyloid state and its association with protein misfolding diseases","volume":"15","author":"Knowles","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0030","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade","volume":"86","author":"Chiti","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0035","doi-asserted-by":"crossref","first-page":"3448","DOI":"10.1529\/biophysj.106.098608","article-title":"A three-stage kinetic model of amyloid fibrillation","volume":"92","author":"Lee","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0040","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1126\/science.aad2033","article-title":"Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA","volume":"351","author":"Woerner","year":"2016","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0045","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1016\/j.cell.2017.12.030","article-title":"In situ structure of neuronal C9orf72 poly-GA aggregates reveals proteasome recruitment","volume":"172","author":"Guo","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0050","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1038\/418291a","article-title":"Neurodegenerative disease: amyloid pores from pathogenic mutations","volume":"418","author":"Lashuel","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0055","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-020-16074-2","article-title":"Increased mitochondrial calcium levels associated with neuronal death in a mouse model of Alzheimer\u2019s disease","volume":"11","author":"Calvo-Rodriguez","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0060","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40035-020-00197-z","article-title":"Mitochondria as a target for neuroprotection: role of methylene blue and photobiomodulation","volume":"9","author":"Yang","year":"2020","journal-title":"Transl. Neurodegener."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0065","doi-asserted-by":"crossref","first-page":"1440","DOI":"10.1126\/science.aan6160","article-title":"Structural basis of membrane disruption and cellular toxicity by a-synuclein oligomers","volume":"358","author":"Fusco","year":"2017","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0070","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1042\/bse0560207","article-title":"Functional amyloid: widespread in nature, diverse in purpose","volume":"56","author":"Pham","year":"2014","journal-title":"Essays Biochem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0075","doi-asserted-by":"crossref","first-page":"256","DOI":"10.4161\/pri.4.4.13676","article-title":"Functional amyloid: turning swords into plowshares","volume":"4","author":"Otzen","year":"2010","journal-title":"Prion"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0080","doi-asserted-by":"crossref","unstructured":"S.A. Levkovich E. Gazit D. Laor Bar-Yosef , Two Decades of Studying Functional Amyloids in Microorganisms, Elsevier Ltd, . doi:10.1016\/j.tim.2020.09.005.","DOI":"10.1016\/j.tim.2020.09.005"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0085","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 (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0090","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/biom7030046","article-title":"Functional amyloids in reproduction","volume":"7","author":"Hewetson","year":"2017","journal-title":"Biomolecules"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0095","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.devcel.2016.09.002","article-title":"Adaptation to stressors by systemic protein amyloidogenesis","volume":"39","author":"Audas","year":"2016","journal-title":"Dev. Cell"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0100","series-title":"Functional Mammalian Amyloids and Amyloid-like Proteins","author":"Rubel","year":"2020"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0105","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0036394","article-title":"Nonpathological extracellular amyloid is present during normal epididymal sperm maturation","volume":"7","author":"Whelly","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0110","doi-asserted-by":"crossref","first-page":"1775","DOI":"10.1016\/j.bpj.2011.01.072","article-title":"Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link","volume":"100","author":"Jang","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0115","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1016\/j.chom.2011.10.010","article-title":"Peptides released by physiological cleavage of semen coagulum proteins form amyloids that enhance HIV infection","volume":"10","author":"Roan","year":"2011","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0120","first-page":"1","article-title":"Functional amyloids germinate in plants","volume":"xx","author":"Santos","year":"2020","journal-title":"Trends Plant Sci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0125","series-title":"Systematic Analysis of Nucleation-dependent Polymerization Reveals New Insights Into the Mechanism of Amyloid Self-assembly","author":"Xue","year":"2008"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0130","series-title":"HHS Public Access","first-page":"632","volume":"86","author":"Tycko","year":"2016"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0135","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/j.jmb.2012.01.024","article-title":"A molecular history of the amyloidoses","volume":"421","author":"Buxbaum","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0140","doi-asserted-by":"crossref","DOI":"10.1186\/1750-1326-2-18","article-title":"Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers","volume":"2","author":"Kayed","year":"2007","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0145","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1073\/pnas.022662599","article-title":"Conformational abs recognizing a generic amyloid fibril epitope","volume":"99","author":"O\u2019Nuallain","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0150","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1021\/ar300282r","article-title":"Molecular structures of amyloid and prion fibrils","volume":"46","author":"Tycko","year":"2013","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0155","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.ijbiomac.2016.06.052","article-title":"Kinetics of protein fibril formation: methods and mechanisms","volume":"100","author":"Kumar","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0160","series-title":"Correlation of Structure and Infectivity of the HET-s Prion","author":"Ritter","year":"2005"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0165","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1038\/nature06108","article-title":"The structural basis of yeast prion strain variants","volume":"449","author":"Toyama","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0170","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1146\/annurev-biochem-090908-120656","article-title":"Amyloid structure: conformational diversity and consequences","volume":"80","author":"Toyama","year":"2011","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0175","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fnmol.2019.00025","article-title":"Molecular mechanisms of TDP-43 misfolding and pathology in amyotrophic lateral sclerosis","volume":"12","author":"Prasad","year":"2019","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0180","doi-asserted-by":"crossref","unstructured":"P.T. Nguyen X. Zottig M. Sebastiao A.A. Arnold I. Marcotte S. Bourgault , Diversity of amyloid assemblies, Commun. Biol. (n.d.). doi:10.1038\/s42003-021-02466-7.","DOI":"10.1038\/s42003-021-02466-7"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0185","series-title":"Amyloid Prefibrillar Oligomers : The Surprising Commonalities in Their Structure and Activity","author":"Diociaiuti","year":"2021"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0190","series-title":"Proteins in Membranes","first-page":"1","volume":"30","author":"Lomize","year":"2007"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0195","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1007\/s00109-003-0464-5","article-title":"Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution","volume":"81","author":"Stefani","year":"2003","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0200","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1038\/nchembio.283","article-title":"A causative link between the structure of aberrant protein oligomers and their toxicity","volume":"6","author":"Campioni","year":"2010","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0205","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1038\/aps.2017.28","article-title":"Amyloid beta: structure, biology and structure-based therapeutic development","volume":"38","author":"Chen","year":"2017","journal-title":"Acta Pharmacol. Sin."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0210","series-title":"Cellular Regulation of Amyloid Formation in Aging and Disease","first-page":"1","volume":"11","author":"Stroo","year":"2017"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0215","doi-asserted-by":"crossref","first-page":"1727","DOI":"10.1371\/journal.pcbi.0030173","article-title":"Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils","volume":"3","author":"Cheon","year":"2007","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0220","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.cell.2010.11.050","article-title":"Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions","volume":"144","author":"Olzscha","year":"2011","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0225","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1021\/ja3103567","article-title":"Single molecule characterization of the interactions between amyloid-\u03b2 peptides and the membranes of hippocampal cells","volume":"135","author":"Narayan","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0230","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1038\/nm.3457","article-title":"Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases","volume":"20","author":"Guo","year":"2014","journal-title":"Nat. Med."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0235","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/416507a","article-title":"Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases","volume":"416","author":"Bucciantini","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0240","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/nature01891","article-title":"Rationalization of the effects of mutations on peptide and protein aggregation rates","volume":"424","author":"Chiti","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0245","series-title":"Factors Affecting the Physical Stability ( Aggregation ) of Peptide Therapeutics","author":"Zapadka","year":"2017"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0250","first-page":"1","article-title":"Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of alzheimer-associated a \u03b2 -peptide","author":"Meisl","year":"2016","journal-title":"Nat. Publ. Group"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0255","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.jmb.2005.04.016","article-title":"Prediction of \u201caggregation-prone\u201d and \u201caggregation- susceptible\u201d regions in proteins associated with neurodegenerative diseases","volume":"350","author":"Pawar","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0260","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/j.jmb.2008.05.013","article-title":"Prediction of aggregation-prone regions in structured proteins","volume":"380","author":"Tartaglia","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0265","doi-asserted-by":"crossref","DOI":"10.1039\/D0MO00085J","article-title":"Cleaning the molecular machinery of cells via proteostasis, proteolysis and endocytosis selectively, effectively, and precisely: intracellular self-defense and cellular perturbations","author":"Kumar","year":"2021","journal-title":"Mol. Omi."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0270","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1038\/nature05291","article-title":"The roles of intracellular protein-degradation pathways in neurodegeneration","volume":"443","author":"Rubinsztein","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0275","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1038\/nature06639","article-title":"Autophagy fights disease through cellular self-digestion","volume":"451","author":"Mizushima","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0280","series-title":"Molecular Chaperone Functions in Protein Folding and Proteostasis","author":"Kim","year":"2013"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0285","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1038\/nsmb.2191","article-title":"The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-\u03b2 1\u201340 peptide","volume":"19","author":"Narayan","year":"2012","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0290","series-title":"Molecular Chaperones : A Double-Edged Sword in Neurodegenerative Diseases","first-page":"1","volume":"12","author":"Tittelmeier","year":"2020"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0295","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13024-019-0333-5","article-title":"The neuropathological diagnosis of Alzheimer\u2019s disease","volume":"14","author":"Deture","year":"2019","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0300","first-page":"1","volume":"11","author":"Oakley","year":"2020"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0305","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1038\/nn.3606","article-title":"Molecular drivers and cortical spread of lateral entorhinal cortex dysfunction in preclinical Alzheimer\u2019s disease","volume":"17","author":"Khan","year":"2014","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0310","doi-asserted-by":"crossref","first-page":"595","DOI":"10.15252\/emmm.201606210","article-title":"The amyloid hypothesis of Alzheimer\u2019s disease at 25 years","volume":"8","author":"Selkoe","year":"2016","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0315","series-title":"Amyloid Precursor Protein ( APP ) Metabolites APP Intracellular Fragment ( AICD ), A \u2424 42 , and Tau in Nuclear Roles *","first-page":"23515","volume":"290","author":"Multhaup","year":"2015"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0320","series-title":"NIH Public Access","first-page":"185","volume":"1987","author":"Manuscript","year":"2011"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0325","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1038\/nm.4443","article-title":"Amyloid-\u03b2 plaques enhance Alzheimer\u2019s brain tau-seeded pathologies by facilitating neuritic plaque tau aggregation","volume":"24","author":"He","year":"2018","journal-title":"Nat. Med."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0330","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/nn.3028","article-title":"The toxic A\u03b2 oligomer and Alzheimer\u2019s disease: an emperor in need of clothes","volume":"15","author":"Benilova","year":"2012","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0335","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1016\/j.cell.2013.08.035","article-title":"XMolecular structure of \u03b2-amyloid fibrils in alzheimer\u2019s disease brain tissue","volume":"154","author":"Lu","year":"2013","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0340","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1038\/nature20814","article-title":"Structural variation in amyloid-\u03b2 fibrils from Alzheimer\u2019s disease clinical subtypes","volume":"541","author":"Qiang","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0345","series-title":"Structure and Function of the \u03b3 - Secretase Complex","first-page":"2953","volume":"58","author":"Wolfe","year":"2019"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0350","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1126\/science.aao2825","article-title":"Fibril structure of amyloid- b (1 \u2013 42) by cryo \u2013 electron microscopy","volume":"119","author":"Gremer","year":"2017","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0355","doi-asserted-by":"crossref","DOI":"10.1155\/2015\/151979","article-title":"Tau hyperphosphorylation and oxidative stress, a critical vicious circle in neurodegenerative Tauopathies?","volume":"2015","author":"Alavi Naini","year":"2015","journal-title":"Oxidative Med. Cell. Longev."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0360","doi-asserted-by":"crossref","first-page":"3661","DOI":"10.1002\/j.1460-2075.1985.tb04132.x","article-title":"Image reconstruction of the alzheimer paired helical filament","volume":"4","author":"Crowther","year":"1985","journal-title":"EMBO J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0365","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1111\/j.1750-3639.2007.00053.x","article-title":"Structural principles of tau and the paired helical filaments of Alzheimer\u2019s disease","author":"Mandelkow","year":"2007","journal-title":"Brain Pathol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0370","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":"10.1016\/j.ijbiomac.2022.01.115_bb0375","doi-asserted-by":"crossref","first-page":"9316","DOI":"10.1074\/jbc.REV119.008031","article-title":"Elucidating tau function and dysfunction in the era of cryo-EM","volume":"294","author":"Lippens","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0380","doi-asserted-by":"crossref","first-page":"E4976","DOI":"10.1073\/pnas.1600749113","article-title":"Atomic-resolution structure of a disease-relevant A\u03b2(1\u201342) amyloid fibril","volume":"113","author":"W\u00e4lti","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0385","doi-asserted-by":"crossref","first-page":"9663","DOI":"10.1021\/jacs.6b05129","article-title":"Atomic resolution structure of monomorphic A\u03b242 amyloid fibrils","volume":"138","author":"Colvin","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0390","series-title":"Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids","author":"Willbold","year":"2021"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0395","series-title":"The Elusive Tau Molecular Structures : Can we Translate the Recent Breakthroughs Into New Targets for Intervention ?","first-page":"1","author":"Fichou","year":"2019"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0400","series-title":"Apolipoprotein E Immunoreactivity in Cerebral Amyloid Deposits and Neurofibrillary Tangles in Alzheimer\u2019s Disease and Kuru Plaque Amyloid in Creutzfeldt-Jakob Disease","author":"Namba","year":"1991"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0405","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1194\/jlr.R075481","article-title":"Apolipoprotein E and Alzheimer\u2019s disease: the influence of apolipoprotein E on amyloid-\u03b2 and other amyloidogenic proteins","volume":"58","author":"Huynh","year":"2017","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0410","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1084\/jem.20171265","article-title":"ApoE facilitates the microglial response to amyloid plaque pathology","volume":"215","author":"Ulrich","year":"2018","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0415","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/S0304-3940(99)00101-9","article-title":"Alzheimer\u2019s amyloid \u03b2-peptide associated free radicals increase rat embryonic neuronal polyamine uptake and ornithine decarboxylase activity: protective effect of vitamin E","volume":"263","author":"Yatin","year":"1999","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0420","doi-asserted-by":"crossref","first-page":"1899","DOI":"10.1046\/j.1471-4159.1995.65041899.x","article-title":"Enhancement of beta-amyloid peptide A beta(1\u201340)-mediated neurotoxicity by glutamine synthetase","volume":"65","author":"Aksenov","year":"1995","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0425","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1083\/jcb.200207030","article-title":"Mitochondrial targeting and a novel transmembrane arrest of Alzheimer\u2019s amyloid precursor protein impairs mitochondrial function in neuronal cells","volume":"161","author":"Anandatheerthavarada","year":"2003","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0430","doi-asserted-by":"crossref","first-page":"9057","DOI":"10.1523\/JNEUROSCI.1469-06.2006","article-title":"Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer\u2019s disease brain is associated with mitochondrial dysfunction","volume":"26","author":"Devi","year":"2006","journal-title":"J. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0435","series-title":"Emergent Therapeutic Strategies","first-page":"1","author":"Guo","year":"2017"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0440","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.3233\/JAD-215065","article-title":"A primer on the evolution of aducanumab: the first antibody approved for treatment of Alzheimer\u2019s disease","volume":"83","author":"Mukhopadhyay","year":"2021","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0445","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/s13195-021-00838-z","article-title":"Aducanumab produced a clinically meaningful benefit in association with amyloid lowering","volume":"13","author":"Cummings","year":"2021","journal-title":"Alzheimers Res. Ther."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0450","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jocn.2020.03.047","article-title":"A review of possible therapies for Parkinson\u2019s disease","volume":"76","author":"Chakraborty","year":"2020","journal-title":"J. Clin. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0455","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fncel.2020.00159","article-title":"Pathogenic mutations differentially regulate cell-to-cell transmission of \u03b1-synuclein","volume":"14","author":"Guan","year":"2020","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0460","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1111\/j.1749-6632.2009.05118.x","article-title":"The progression of pathology in Parkinson\u2019s disease","volume":"1184","author":"Halliday","year":"2010","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0465","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1002\/mds.25952","article-title":"Stage-dependent nigral neuronal loss in incidental lewy body and parkinson\u2019s disease","volume":"29","author":"Dijkstra","year":"2014","journal-title":"Mov. Disord."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0470","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1093\/brain\/122.8.1437","article-title":"The substantia nigra of the human brain: II. Patterns of loss of dopamine-containing neurons in Parkinson\u2019s disease","volume":"122","author":"Damier","year":"1999","journal-title":"Brain"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0475","doi-asserted-by":"crossref","first-page":"2283","DOI":"10.1093\/brain\/114.5.2283","article-title":"Ageing and parkinson\u2019s disease: substantia nigra regional selectivity","volume":"114","author":"Fearnley","year":"1991","journal-title":"Brain"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0480","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1007\/s00441-004-0956-9","article-title":"Stages in the development of Parkinson\u2019s disease-related pathology","volume":"318","author":"Braak","year":"2004","journal-title":"Cell Tissue Res."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0485","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1111\/jnc.13845","article-title":"Cross-linking for the analysis of \u03b1-synuclein in the enteric nervous system","volume":"139","author":"Corbill\u00e9","year":"2016","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0490","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1007\/s00401-010-0664-3","article-title":"Multi-organ distribution of phosphorylated \u03b1-synuclein histopathology in subjects with lewy body disorders","volume":"119","author":"Beach","year":"2010","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0495","series-title":"The New Mutation, E46K, of-Synuclein Causes Parkinson and Lewy Body Dementia","author":"Zarranz","year":"2004"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0500","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1111\/jnc.12806","article-title":"Divergent effects of the H50Q and G51D SNCA mutations on the aggregation of \u03b1-synuclein","volume":"131","author":"Rutherford","year":"2014","journal-title":"J. Neurochem."},{"issue":"2180","key":"10.1016\/j.ijbiomac.2022.01.115_bb0505","article-title":"A novel \u03b1-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson\u2019s disease-type pathology","volume":"35","author":"Pasanen","year":"2014","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0510","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1038\/33416","article-title":"Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism","volume":"392","author":"Kitada","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0515","series-title":"Heterozygosity for a Mutation in the","author":"Foroud","year":"2003"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0520","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1002\/mds.27352","article-title":"Genotype-phenotype relations for the Parkinson\u2019s disease genes parkin, PINK1, DJ1: MDSGene systematic review","volume":"33","author":"Kasten","year":"2018","journal-title":"Mov. Disord."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0525","first-page":"261","article-title":"\u03b1-synuclein misfolding and Parkinson\u2019s disease","volume":"2012","author":"Breydo","year":"1822","journal-title":"Biochim. Biophys. Acta Mol. basis Dis."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0530","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/nature10324","article-title":"\u03b1-synuclein occurs physiologically as a helically folded tetramer that resists aggregation","volume":"477","author":"Bartels","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0535","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/nature12125","article-title":"Properties of native brain \u03b1-synuclein","volume":"498","author":"Burr\u00e9","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0540","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1002\/1873-3468.13047","article-title":"Refolding of helical soluble \u03b1-synuclein through transient interaction with lipid interfaces","volume":"592","author":"Rovere","year":"2018","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0545","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/nchembio.1750","article-title":"Lipid vesicles trigger \u03b1-synuclein aggregation by stimulating primary nucleation","volume":"11","author":"Galvagnion","year":"2015","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0550","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1038\/nature15368","article-title":"Structure of the toxic core of \u03b1-synuclein from invisible crystals","volume":"525","author":"Rodriguez","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0555","doi-asserted-by":"crossref","DOI":"10.1186\/s13024-019-0329-1","article-title":"Alpha-synuclein structure and Parkinson\u2019s disease - lessons and emerging principles","volume":"14","author":"Meade","year":"2019","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0560","doi-asserted-by":"crossref","first-page":"3435","DOI":"10.1093\/bioinformatics\/bti537","article-title":"FoldIndex\u00a9: a simple tool to predict whether a given protein sequence is intrinsically unfolded","volume":"21","author":"Prilusky","year":"2005","journal-title":"Bioinformatics"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0565","doi-asserted-by":"crossref","first-page":"2380","DOI":"10.1074\/jbc.M008919200","article-title":"A hydrophobic stretch of 12 amino acid residues in the middle of \u03b1-synuclein is essential for filament assembly","volume":"276","author":"Giasson","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0570","series-title":"A Peptide Motif Consisting of Glycine, Alanine, and Valine Is Required for the Fibrillization and Cytotoxicity of Human R-Synuclein \u2020","author":"Du","year":"2003"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0575","first-page":"1","article-title":"Cryo-EM of full-length \u03b1-synuclein reveals fibril polymorphs with a common structural kernel","volume":"9","author":"Li","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0580","unstructured":"R. Guerrero-Ferreira N.M.I. Taylor D. Mona P. Ringler M.E. Lauer R. Riek M. Britschgi H. Stahlberg , Cryo-EM Structure of Alpha-synuclein Fibrils, n.d."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0585","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1038\/nsmb.3194","article-title":"Solid-state NMR structure of a pathogenic fibril of full-length human \u03b1-synuclein","volume":"23","author":"Tuttle","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0590","series-title":"A Seat at the Table for People With Parkinson\u2019s Disease","author":"Morgan","year":"2015"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0595","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2019.01399","article-title":"Alpha-synuclein physiology and pathology: a perspective on cellular structures and organelles","volume":"13","author":"Bernal-Conde","year":"2020","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0600","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.abb.2018.04.018","article-title":"Alpha-synuclein mitochondrial interaction leads to irreversible translocation and complex I impairment","volume":"651","author":"Mart\u00ednez","year":"2018","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0605","doi-asserted-by":"crossref","first-page":"15685","DOI":"10.1002\/chem.201803933","article-title":"Alpha-synuclein modulates the physical properties of DNA","volume":"24","author":"Jiang","year":"2018","journal-title":"Chem. Eur. J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0610","doi-asserted-by":"crossref","first-page":"4441","DOI":"10.1093\/hmg\/ddx331","article-title":"Alpha-synuclein induces the unfolded protein response in Parkinson\u2019s disease SNCA triplication iPSC-derived neurons","volume":"26","author":"Heman-Ackah","year":"2017","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0615","doi-asserted-by":"crossref","first-page":"11835","DOI":"10.1523\/JNEUROSCI.0983-17.2017","article-title":"Human astrocytes transfer aggregated alpha-synuclein via tunneling nanotubes","volume":"37","author":"Rostami","year":"2017","journal-title":"J. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0620","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1126\/science.1090278","article-title":"\u03b1-Synuclein locus triplication causes Parkinson\u2019s disease","volume":"302","author":"Singleton","year":"2003","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0625","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. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0630","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/s00401-010-0735-5","article-title":"Molecular pathology of human prion disease","volume":"121","author":"Wadsworth","year":"2011","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0635","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1093\/ilar\/ilv008","article-title":"The transmissible spongiform encephalopathies of livestock","volume":"56","author":"Greenlee","year":"2015","journal-title":"ILAR J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0640","series-title":"Handb. Clin. Neurol","first-page":"135","article-title":"Chronic wasting disease: an evolving prion disease of cervids","author":"Benestad","year":"2018"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0645","doi-asserted-by":"crossref","DOI":"10.3390\/v11040309","article-title":"Understanding prion strains: evidence from studies of the disease forms affecting humans","volume":"11","author":"Rossi","year":"2019","journal-title":"Viruses"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0650","doi-asserted-by":"crossref","first-page":"930","DOI":"10.1126\/science.1138718","article-title":"A general model of prion strains and their pathogenicity","volume":"318","author":"Collinge","year":"2007","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0655","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0065-3233(01)57018-7","article-title":"Three-dimensional structures of prion proteins","volume":"57","author":"W\u00fcthrich","year":"2001","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0660","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a031336","article-title":"Toward the atomic structure of PrPSc","volume":"9","author":"Rodriguez","year":"2017","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0665","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1093\/abbs\/gmt027","article-title":"Conformational conversion of prion protein in prion diseases","volume":"45","author":"Zhou","year":"2013","journal-title":"Acta Biochim. Biophys. Sin. Shanghai"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0670","series-title":"Biochemistry and Structure of PrP C and PrP Sc","first-page":"21","author":"Riesner","year":"2003"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0675","series-title":"Predicted a-Helical Regions of the Prion Protein When Synthesized as Peptides Form Amyloid (scrapie\/13-sheet\/proteln secondary structure\/amylold flbrils)","author":"Gasset","year":"1992"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0680","series-title":"Recombinant Scrapie-like Prion Protein of 106 Amino Acids is Soluble (Prion Diseasesprotein Solubilityprion Protein Structureprotein Aggregationprion Replication)","author":"Muramoto","year":"1996"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0685","doi-asserted-by":"crossref","first-page":"8342","DOI":"10.1073\/pnas.0402254101","article-title":"Evidence for assembly of prions with left-handed \u03b2-helices into trimers","volume":"101","author":"Govaerts","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0690","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1146\/annurev-genet-110711-155524","article-title":"Biology and genetics of prions causing neurodegeneration","volume":"47","author":"Prusiner","year":"2013","journal-title":"Annu. Rev. Genet."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0695","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.nbd.2017.07.018","article-title":"Distinct \u03b1-synuclein strains and implications for heterogeneity among \u03b1-synucleinopathies","volume":"109","author":"Peng","year":"2018","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0700","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1038\/nature20415","article-title":"Mammalian prions and their wider relevance in neurodegenerative diseases","volume":"539","author":"Collinge","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0705","doi-asserted-by":"crossref","DOI":"10.1002\/psc.3216","article-title":"Prion protein\u2014semisynthetic prion protein (PrP) variants with posttranslational modifications","volume":"25","author":"Hackl","year":"2019","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0710","doi-asserted-by":"crossref","first-page":"1240","DOI":"10.1093\/emboj\/21.3.202","article-title":"Erratum: post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration (The EMBO journal (2002) 21 (202\u2013210))","volume":"21","author":"Mallucci","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0715","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1016\/j.neuron.2016.02.003","article-title":"The biology of huntingtin","volume":"89","author":"Saudou","year":"2016","journal-title":"Neuron"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0720","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1007\/978-3-642-45106-5_14","article-title":"Huntington\u2019s disease","volume":"220","author":"Zuccato","year":"2015","journal-title":"Handb. Exp. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0725","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1093\/hmg\/ddl440","article-title":"The first 17 amino acids of huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis","volume":"16","author":"Rockabrand","year":"2007","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0730","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1093\/hmg\/ddh162","article-title":"Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release","volume":"13","author":"Choo","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0735","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1038\/nn884","article-title":"Early mitochondrial calcium defects in Huntington\u2019s disease are a direct effect of polyglutamines","volume":"5","author":"Panov","year":"2002","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0740","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1186\/1750-1172-5-40","article-title":"Huntington\u2019s disease: a clinical review","volume":"5","author":"Roos","year":"2010","journal-title":"Orphanet J. Rare Dis."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0745","article-title":"Huntington disease","volume":"1","author":"Bates","year":"2015","journal-title":"Nat. Rev. Dis. Prim."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0750","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1111\/j.1471-4159.2005.03348.x","article-title":"Purification of neuronal inclusions of patients with Huntington\u2019s disease reveals a broad range of N-terminal fragments of expanded huntingtin and insoluble polymers","volume":"95","author":"Hoffher","year":"2005","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0755","series-title":"Truncated N-terminal Fragments of Huntingtin With Expanded Glutamine Repeats Form Nuclear and Cytoplasmic Aggregates in Cell Culture","author":"Cooper","year":"1998"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0760","doi-asserted-by":"crossref","first-page":"3765","DOI":"10.1021\/ac400038b","article-title":"Structure of inclusions of huntington\u2019s disease brain revealed by synchrotron infrared microspectroscopy: polymorphism and relevance to cytotoxicity","volume":"85","author":"Andr\u00e9","year":"2013","journal-title":"Anal. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0765","doi-asserted-by":"crossref","first-page":"9679","DOI":"10.1073\/pnas.0812083106","article-title":"Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity","volume":"106","author":"Nekooki-Machida","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0770","doi-asserted-by":"crossref","first-page":"3188","DOI":"10.1074\/jbc.M008099200","article-title":"Isolation of a 40-kDa huntingtin-associated protein","volume":"276","author":"Peters","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0775","doi-asserted-by":"crossref","first-page":"23686","DOI":"10.1074\/jbc.M513507200","article-title":"Huntingtin phosphorylation sites mapped by mass spectrometry: modulation of cleavage and toxicity","volume":"281","author":"Schilling","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0780","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1038\/nature25502","article-title":"The cryo-electron microscopy structure of huntingtin","volume":"555","author":"Guo","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0785","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2021.105476","article-title":"HAP40 protein levels are huntingtin-dependent and decrease in Huntington disease","volume":"158","author":"Huang","year":"2021","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0790","article-title":"Amyotrophic lateral sclerosis","volume":"3","author":"Hardiman","year":"2017","journal-title":"Nat. Rev. Dis. Primers."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0795","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/nature20413","article-title":"Decoding ALS: from genes to mechanism","volume":"539","author":"Taylor","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0800","doi-asserted-by":"crossref","DOI":"10.3389\/fncel.2020.581907","article-title":"Amyotrophic lateral sclerosis: proteins, proteostasis, prions, and promises","volume":"14","author":"McAlary","year":"2020","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0805","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1126\/science.1134108","article-title":"Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"314","author":"Neumann","year":"2006","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0810","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1267\/ahc.26.619","article-title":"Immunohistochemical demonstration of cu\/zn superoxide dismutase in the spinal cord of patients with familial amyotro-phic lateral sclerosis","volume":"26","author":"Shibata","year":"1993","journal-title":"Acta Histochem. Cytochem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0815","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1126\/science.1165942","article-title":"Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6","volume":"323","author":"Vance","year":"2009","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0820","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1016\/j.neuron.2013.07.033","article-title":"Converging mechanisms in als and FTD: disrupted RNA and protein homeostasis","volume":"79","author":"Ling","year":"2013","journal-title":"Neuron"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0825","doi-asserted-by":"crossref","first-page":"E3935","DOI":"10.1073\/pnas.1613854114","article-title":"Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS","volume":"114","author":"Ciryam","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0830","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2019.00262","article-title":"Prion-like propagation of protein misfolding and aggregation in amyotrophic lateral sclerosis","volume":"12","author":"McAlary","year":"2019","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0835","doi-asserted-by":"crossref","DOI":"10.1017\/S003358351900012X","article-title":"The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis","volume":"52","author":"Wright","year":"2019","journal-title":"Q. Rev. Biophys."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0840","doi-asserted-by":"crossref","first-page":"30624","DOI":"10.1074\/jbc.M115.666503","article-title":"The disulfide bond, but not zinc or dimerization, controls initiation and seeded growth in amyotrophic lateral sclerosis-linked cu, zn superoxide dismutase (SOD1) fibrillation","volume":"290","author":"Chattopadhyay","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0845","doi-asserted-by":"crossref","first-page":"10934","DOI":"10.1073\/pnas.1309613110","article-title":"Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy","volume":"110","author":"Chan","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0850","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2016.00499","article-title":"Susceptibility of mutant SOD1 to form a destabilized monomer predicts cellular aggregation and toxicity but not in vitro aggregation propensity","volume":"10","author":"McAlary","year":"2016","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0855","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1016\/j.jmb.2010.04.019","article-title":"Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants","volume":"399","author":"M\u00fcnch","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0860","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-018-32835-y","article-title":"Tryptophan 32-mediated SOD1 aggregation is attenuated by pyrimidine-like compounds in living cells","volume":"8","author":"Pokrishevsky","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0865","doi-asserted-by":"crossref","first-page":"3620","DOI":"10.1073\/pnas.1312245111","article-title":"Intercellular propagated misfolding of wild-type Cu\/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms","volume":"111","author":"Grad","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0870","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1002\/pro.3391","article-title":"Atomic structures of corkscrew-forming segments of SOD1 reveal varied oligomer conformations","volume":"27","author":"Sangwan","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0875","doi-asserted-by":"crossref","first-page":"16329","DOI":"10.1074\/jbc.M610119200","article-title":"Tryptophan 32 potentiates aggregation and cytotoxicity of a copper\/zinc superoxide dismutase mutant associated with familial amyotrophic lateral sclerosis","volume":"282","author":"Taylor","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0880","doi-asserted-by":"crossref","first-page":"37572","DOI":"10.1074\/jbc.M505557200","article-title":"TDP-43 binds heterogeneous nuclear ribonucleoprotein A\/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing","volume":"280","author":"Buratti","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0885","doi-asserted-by":"crossref","first-page":"6000","DOI":"10.1093\/nar\/gki897","article-title":"Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene","volume":"33","author":"Mercado","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0890","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.1111\/febs.13651","article-title":"The TDP-43 N-terminal domain structure at high resolution","volume":"283","author":"Mompe\u00e1n","year":"2016","journal-title":"FEBS J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0895","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.brainres.2012.01.016","article-title":"The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease","volume":"1462","author":"King","year":"2012","journal-title":"Brain Res."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0900","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1038\/s41594-018-0064-2","article-title":"Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation","volume":"25","author":"Guenther","year":"2018","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0905","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nature05695","article-title":"Atomic structures of amyloid cross-\u03b2 spines reveal varied steric zippers","volume":"447","author":"Sawaya","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0910","series-title":"The Amyloid State of Proteins in Human Diseases","author":"Eisenberg","year":"2012"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0915","doi-asserted-by":"crossref","first-page":"18619","DOI":"10.1073\/pnas.1413994112","article-title":"TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA","volume":"111","author":"Qin","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0920","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.bbrc.2012.07.071","article-title":"The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity","volume":"425","author":"Ke Chang","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0925","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-017-00062-0","article-title":"Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation","volume":"8","author":"Afroz","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0930","doi-asserted-by":"crossref","first-page":"9049","DOI":"10.1074\/jbc.M112.438564","article-title":"The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates","volume":"288","author":"Wang","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0935","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.neulet.2004.12.071","article-title":"Delocalization of the multifunctional RNA splicing factor TLS\/FUS in hippocampal neurones: exclusion from the nucleus and accumulation in dendritic granules and spine heads","volume":"379","author":"Belly","year":"2005","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0940","doi-asserted-by":"crossref","DOI":"10.1186\/1471-2121-9-37","article-title":"The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response","volume":"9","author":"Andersson","year":"2008","journal-title":"BMC Cell Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0945","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/S0378-1119(98)00463-6","article-title":"Genomic structure of the human RBP56\/hTAF(II)68 and FUS\/TLS genes","volume":"221","author":"Morohoshi","year":"1998","journal-title":"Gene"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0950","doi-asserted-by":"crossref","first-page":"44834","DOI":"10.1074\/jbc.M408552200","article-title":"Domain architectures and characterization of an RNA-binding protein, TLS","volume":"279","author":"Iko","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0955","doi-asserted-by":"crossref","first-page":"7128","DOI":"10.1074\/jbc.TM118.001190","article-title":"Prion-like low-complexity sequences: key regulators of protein solubility and phase behavior","volume":"294","author":"Franzmann","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0960","doi-asserted-by":"crossref","first-page":"1","DOI":"10.5607\/en.2015.24.1.1","article-title":"Prion-like mechanism in amyotrophic lateral sclerosis: are protein aggregates the key?","volume":"24","author":"Lee","year":"2015","journal-title":"Exp. Neurobiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0965","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1007\/s00401-013-1089-6","article-title":"Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid","volume":"125","author":"Bigio","year":"2013","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0970","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1007\/s00401-012-1055-8","article-title":"TDP-43 skeins show properties of amyloid in a subset of ALS cases","volume":"125","author":"Robinson","year":"2013","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0975","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1038\/nn.3584","article-title":"State of play in amyotrophic lateral sclerosis genetics HHS public access author manuscript","volume":"17","author":"Renton","year":"2014","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0980","doi-asserted-by":"crossref","first-page":"20329","DOI":"10.1074\/jbc.M109.010264","article-title":"TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity","volume":"284","author":"Johnson","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0985","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1101\/cshperspect.a024554","article-title":"Biology and pathobiology of TDP-43 and emergent therapeutic strategies","volume":"7","author":"Guo","year":"2017","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0990","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1152\/physrev.00042.2009","article-title":"Islet amyloid polypeptide, islet amyloid, and diabetes mellitus","volume":"91","author":"Westermark","year":"2011","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb0995","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.12977","article-title":"Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics","volume":"5","author":"Abedini","year":"2016","journal-title":"elife"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1000","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7554\/eLife.19273","article-title":"Atomic structures of fibrillar segments of hIAPP suggest tightly mated \u03b2-sheets are important for cytotoxicity","volume":"6","author":"Krotee","year":"2017","journal-title":"elife"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1005","doi-asserted-by":"crossref","first-page":"2641","DOI":"10.1016\/S0140-6736(15)01274-X","article-title":"Systemic amyloidosis","volume":"387","author":"Wechalekar","year":"2016","journal-title":"Lancet"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1010","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-019-12683-8","article-title":"Cryo-EM structure and polymorphism of A\u03b2 amyloid fibrils purified from Alzheimer\u2019s brain tissue","volume":"10","author":"Kollmer","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1015","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nsmb.2991","article-title":"A\u03b2(1\u201342) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer\u2019s disease","volume":"22","author":"Xiao","year":"2015","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1020","doi-asserted-by":"crossref","first-page":"3592","DOI":"10.1073\/pnas.1917914117","article-title":"The \u03b1-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure","volume":"117","author":"Boyer","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1025","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":"10.1016\/j.ijbiomac.2022.01.115_bb1030","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1038\/s41594-020-0441-5","article-title":"Cryo-EM structure of an amyloid fibril formed by full-length human prion protein","volume":"27","author":"Wang","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1035","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s42003-021-02360-2","article-title":"Cryo-electron tomography provides topological insights into mutant huntingtin exon 1 and polyQ aggregates","volume":"4","author":"Galaz-Montoya","year":"2021","journal-title":"Commun. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1040","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-019-13038-z","article-title":"Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis","volume":"10","author":"Schmidt","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1045","doi-asserted-by":"crossref","first-page":"16748","DOI":"10.1073\/pnas.252625999","article-title":"Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril","volume":"99","author":"Jaroniec","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1050","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1002\/pro.3420","article-title":"Crystal structures of amyloidogenic segments of human transthyretin","volume":"27","author":"Saelices","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1055","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/j.jmb.2005.07.040","article-title":"Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme","volume":"352","author":"Johnson","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1060","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.sbi.2020.05.011","article-title":"Cryo-EM structures of tau filaments","volume":"64","author":"Scheres","year":"2020","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1065","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-018-06761-6","article-title":"The structure of a \u03b22-microglobulin fibril suggests a molecular basis for its amyloid polymorphism","volume":"9","author":"Iadanza","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1070","doi-asserted-by":"crossref","first-page":"15870","DOI":"10.1021\/jacs.0c06143","article-title":"Interpenetrating cubes in the X-ray crystallographic structure of a peptide derived from Medin19-36","volume":"142","author":"Howitz","year":"2020","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1075","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1038\/s41594-020-0442-4","article-title":"Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-\u03b2 fibrils","volume":"27","author":"R\u00f6der","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1080","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":"10.1016\/j.ijbiomac.2022.01.115_bb1085","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1110\/ps.036509.108","article-title":"Atomic structure of the cross-\u03b2 spine of islet amyloid polypeptide (amylin)","volume":"17","author":"Wiltzius","year":"2008","journal-title":"Protein Sci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1090","doi-asserted-by":"crossref","first-page":"9196","DOI":"10.1073\/pnas.142459399","article-title":"The protofilament structure of insulin amyloid fibrils","volume":"99","author":"Jim\u00e9nez","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1095","doi-asserted-by":"crossref","first-page":"3187","DOI":"10.1016\/j.bpj.2009.09.042","article-title":"Molecular modeling of the misfolded insulin subunit and amyloid fibril","volume":"97","author":"Choi","year":"2009","journal-title":"Biophys. J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1100","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1107\/S0907444902004183","article-title":"Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties","volume":"58","author":"Bourne","year":"2002","journal-title":"Acta Crystallogr. Sect. D: Biol. Crystallogr."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/microorganisms8121951","article-title":"Functional amyloids are the rule rather than the exception in cellular biology","volume":"8","author":"Balistreri","year":"2020","journal-title":"Microorganisms"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1110","doi-asserted-by":"crossref","first-page":"15806","DOI":"10.1073\/pnas.0604035103","article-title":"Characterization of the nanoscale properties of individual amyloid fibrils","volume":"103","author":"Smith","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1115","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.tibs.2007.03.003","article-title":"Functional amyloid - from bacteria to humans","volume":"32","author":"Fowler","year":"2007","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1120","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":"10.1016\/j.ijbiomac.2022.01.115_bb1125","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1126\/science.1067484","article-title":"Role of Escherichia coli curli operons in directing amyloid fiber formation","volume":"295","author":"Chapman","year":"2002","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1130","doi-asserted-by":"crossref","first-page":"2696","DOI":"10.1073\/pnas.052709699","article-title":"Microcin E492, a channel-forming bacteriocin from Klebsiella pneumoniae, induces apoptosis in some human cell lines","volume":"99","author":"Hetz","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1135","doi-asserted-by":"crossref","first-page":"13601","DOI":"10.1074\/jbc.M602576200","article-title":"Amyloidogenesis of type III-dependent harpins from plant pathogenic bacteria","volume":"282","author":"Oh","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1140","doi-asserted-by":"crossref","first-page":"1714","DOI":"10.1101\/gad.264303","article-title":"A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils","volume":"17","author":"Claessen","year":"2003","journal-title":"Genes Dev."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1145","doi-asserted-by":"crossref","DOI":"10.1038\/srep25425","article-title":"Functional amyloids as inhibitors of plasmid DNA replication","volume":"6","author":"Molina-Garc\u00eda","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1150","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1128\/EC.00068-09","article-title":"Yeast cell adhesion molecules have functional amyloid-forming sequences","volume":"9","author":"Ramsook","year":"2010","journal-title":"Eukaryot. Cell"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1155","doi-asserted-by":"crossref","DOI":"10.1038\/s41522-019-0094-5","article-title":"Candida albicans biofilm development is governed by cooperative attachment and adhesion maintenance proteins","volume":"5","author":"McCall","year":"2019","journal-title":"Npj Biofilms Microbiomes"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1160","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep23370","article-title":"Amyloid formation of growth hormone in presence of zinc: relevance to its storage in secretory granules","volume":"6","author":"Jacob","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1165","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1021\/mp200419b","article-title":"Antimicrobial properties of amyloid peptides","volume":"9","author":"Kagan","year":"2012","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1170","series-title":"Amyloids Protect the Silkmoth Oocyte and Embryo","author":"Iconomidou","year":"2000"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1175","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.4315\/0362-028X-70.6.1339","article-title":"Influence of curli expression by Escherichia coli O157:H7 on the cell\u2019s overall hydrophobicity, charge, and ability to attach to lettuce","volume":"70","author":"Boyer","year":"2007","journal-title":"J. Food Prot."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1180","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1111\/j.1365-2672.2005.02499.x","article-title":"Role of curli fimbriae in mediating the cells of enterohaemorrhagic Escherichia coli to attach to abiotic surfaces","volume":"99","author":"Pawar","year":"2005","journal-title":"J. Appl. Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1185","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.tim.2011.11.005","article-title":"Diversity, biogenesis and function of microbial amyloids","volume":"20","author":"Blanco","year":"2012","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1190","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1146\/annurev.micro.60.080805.142106","article-title":"Plaque assay for detecting lysogeny","volume":"60","author":"Barnhart","year":"2010","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1195","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1016\/j.resmic.2005.02.005","article-title":"Role of bacterial cell surface structures in Escherichia coli biofilm formation","volume":"156","author":"Van Houdt","year":"2005","journal-title":"Res. Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1200","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1111\/j.1348-0421.2005.tb03678.x","article-title":"Curli fibers are required for development of biofilm architecture in Escherichia coli K-12 and enhance bacterial adherence to human uroepithelial cells","volume":"49","author":"Kikuchi","year":"2005","journal-title":"Microbiol. Immunol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1205","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1126\/sciadv.1600998","article-title":"Adhesion mechanisms of curli subunit CsgA to abiotic surfaces","volume":"2","author":"DeBenedictis","year":"2016","journal-title":"Sci. Adv."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1210","series-title":"The Curli Nucleator Protein, CsgB, Contains an Amyloidogenic Domain That DIRECTS CSGA Polymerization","author":"Hammer","year":"2007"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1215","doi-asserted-by":"crossref","first-page":"25065","DOI":"10.1074\/jbc.M109.007054","article-title":"The functional curli amyloid is not based on in-register parallel \u03b2-sheet structure","volume":"284","author":"Shewmaker","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1220","doi-asserted-by":"crossref","first-page":"1841","DOI":"10.4315\/0362-028X-72.9.1841","article-title":"Molecular characterization of biofilm formation and attachment of salmonella enterica serovar typhimurium DT104 on food contact surfaces","volume":"72","author":"Kim","year":"2009","journal-title":"J. Food Prot."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1225","doi-asserted-by":"crossref","first-page":"7130","DOI":"10.1073\/pnas.1607222113","article-title":"Solution NMR structure of CsgE: structural insights into a chaperone and regulator protein important for functional amyloid formation","volume":"113","author":"Shu","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1230","doi-asserted-by":"crossref","first-page":"E5439","DOI":"10.1073\/pnas.1411942111","article-title":"Structure of the nonameric bacterial amyloid secretion channel","volume":"111","author":"Cao","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1235","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1038\/nature13768","article-title":"Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG","volume":"516","author":"Goyal","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1240","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1002\/1873-3468.13002","article-title":"Structural and functional characterization of the curli adaptor protein CsgF","volume":"592","author":"Schubeis","year":"2018","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1245","doi-asserted-by":"crossref","first-page":"6562","DOI":"10.1073\/pnas.93.13.6562","article-title":"Nucleator-dependent intercellular assembly of adhesive curli organelles in escherichia coli","volume":"93","author":"Hammar","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1250","doi-asserted-by":"crossref","first-page":"6502","DOI":"10.1073\/pnas.1204161109","article-title":"The E. coli CsgB nucleator of curli assembles to \u03b2-sheet oligomers that alter the CsgA fibrillization mechanism","volume":"109","author":"Shu","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1255","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1111\/j.1365-2958.2011.07706.x","article-title":"CsgE is a curli secretion specificity factor that prevents amyloid fibre aggregation","volume":"81","author":"Nenninger","year":"2011","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1260","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1111\/j.1365-2958.2005.04997.x","article-title":"Secretion of curli fibre subunits is mediated by the outer membrane-localized CsgG protein","volume":"59","author":"Robinson","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1265","doi-asserted-by":"crossref","first-page":"900","DOI":"10.1073\/pnas.0812143106","article-title":"Localized and efficient curli nucleation requires the chaperone-like amyloid assembly protein CsgF","volume":"106","author":"Nenninger","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1270","first-page":"1551","article-title":"Curli biogenesis: order out of disorder","volume":"2014","author":"Evans","year":"1843","journal-title":"Biochim. Biophys. Acta, Mol. Cell Res."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1275","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.tim.2015.07.010","article-title":"Bacterial amyloid formation: structural insights into curli biogensis","volume":"23","author":"Van Gerven","year":"2015","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1280","doi-asserted-by":"crossref","first-page":"3685","DOI":"10.1016\/j.jmb.2018.05.004","article-title":"Ecology and biogenesis of functional amyloids in pseudomonas","volume":"430","author":"Rouse","year":"2018","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1285","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0076630","article-title":"Evolutionary insight into the functional amyloids of the pseudomonads","volume":"8","author":"Dueholm","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1290","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fmicb.2015.01099","article-title":"Functional bacterial amyloid increases pseudomonas biofilm hydrophobicity and stiffness","volume":"6","author":"Zeng","year":"2015","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1295","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1002\/mbo3.81","article-title":"Expression of fap amyloids in Pseudomonas aeruginosa, P. Fluorescens, and P. Putida results in aggregation and increased biofilm formation","volume":"2","author":"Dueholm","year":"2013","journal-title":"Microbiologyopen."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1300","doi-asserted-by":"crossref","first-page":"3657","DOI":"10.1016\/j.jmb.2018.07.010","article-title":"The role of functional amyloids in bacterial virulence","volume":"430","author":"Van Gerven","year":"2018","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1305","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-017-00361-6","article-title":"A new class of hybrid secretion system is employed in pseudomonas amyloid biogenesis","volume":"8","author":"Rouse","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1310","doi-asserted-by":"crossref","first-page":"2232","DOI":"10.1016\/j.jmb.2020.01.044","article-title":"Predicted loop regions promote aggregation: a study of amyloidogenic domains in the functional amyloid FapC","volume":"432","author":"Nagaraj","year":"2020","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1315","doi-asserted-by":"crossref","first-page":"1727","DOI":"10.1101\/gad.264403","article-title":"The chaplins: a family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor","volume":"17","author":"Elliot","year":"2003","journal-title":"Genes Dev."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1320","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0018839","article-title":"The assembly of individual chaplin peptides from streptomyces coelicolor into functional amyloid fibrils","volume":"6","author":"Sawyer","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1325","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1111\/j.1365-2958.2004.04143.x","article-title":"The formation of the rodlet layer of streptomycetes is the result of the interplay between rodlins and chaplins","volume":"53","author":"Claessen","year":"2004","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1330","first-page":"1","article-title":"The propensity of the bacterial rodlin protein RdlB to form amyloid fibrils determines its function in Streptomyces coelicolor","volume":"7","author":"Yang","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1335","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1111\/j.1365-2958.2009.06838.x","article-title":"Attachment of Streptomyces coelicolor is mediated by amyloida fimbriae that are anchored to the cell surface via cellulose","volume":"73","author":"De Jong","year":"2009","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1340","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1016\/j.febslet.2009.07.003","article-title":"Structure-activity relationship of amyloid fibrils","volume":"583","author":"Maji","year":"2009","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1345","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.febslet.2004.09.075","article-title":"Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers","volume":"577","author":"Sparr","year":"2004","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1350","doi-asserted-by":"crossref","first-page":"6297","DOI":"10.1073\/pnas.0407035102","article-title":"Raft lipids as common components of human extracellular amyloid fibrils","volume":"102","author":"Gellermann","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1355","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12915-017-0347-9","article-title":"Amyloid-like aggregation of provasopressin in diabetes insipidus and secretory granule sorting","volume":"15","author":"Beuret","year":"2017","journal-title":"BMC Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1360","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1038\/nature03680","article-title":"Structure of the cross-\u03b2 spine of amyloid-like fibrils","volume":"435","author":"Nelson","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1365","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/j.mib.2006.09.001","article-title":"Non-self recognition and programmed cell death in filamentous fungi","volume":"9","author":"Glass","year":"2006","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1370","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1210\/er.2011-1002","article-title":"Prolactin and growth hormone aggregates in secretory granules: the need to understand the structure of the aggregate","volume":"33","author":"Dannies","year":"2012","journal-title":"Endocr. Rev."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1375","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1021\/jacs.5b08694","article-title":"Dynamic assembly and disassembly of functional \u03b2-endorphin amyloid fibrils","volume":"138","author":"Nespovitaya","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1380","article-title":"EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation","volume":"2","author":"Pearson","year":"2017","journal-title":"Nat. Microbiol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1385","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.semcancer.2006.11.009","article-title":"Cell death by incompatibility in the fungus podospora","volume":"17","author":"Pinan-Lucarr\u00e9","year":"2007","journal-title":"Semin. Cancer Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1390","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1007\/BF00282475","article-title":"Two allelic genes responsible for vegetative incompatibility in the fungus podospora anserina are not essential for cell viability","volume":"228","author":"Turcq","year":"1991","journal-title":"Mol. Gen. Genet."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1395","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1001451","article-title":"The mechanism of toxicity in HET-S\/HET-s prion incompatibility","volume":"10","author":"Seuring","year":"2012","journal-title":"PLoS Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1400","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1016\/j.molcel.2010.05.019","article-title":"The mechanism of prion inhibition by HET-S","volume":"38","author":"Greenwald","year":"2010","journal-title":"Mol. Cell"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1405","doi-asserted-by":"crossref","first-page":"2071","DOI":"10.1093\/emboj\/cdg213","article-title":"Domain organization and structure-function relationship of the HET-s prion protein of podospora anserina","volume":"22","author":"Balguerie","year":"2003","journal-title":"EMBO J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1410","doi-asserted-by":"crossref","first-page":"6616","DOI":"10.1073\/pnas.1030058100","article-title":"Sexual transmission of the [Het-s] prion leads to meiotic drive in podospora anserina","volume":"100","author":"Dalstra","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1415","doi-asserted-by":"crossref","first-page":"1523","DOI":"10.1126\/science.1151839","article-title":"Amyloid fibrils of the HET-s(218-289) prion form a \u03b2 solenoid with a triangular hydrophobic core","volume":"319","author":"Wasmer","year":"2008","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1420","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1038\/nature03793","article-title":"Correlation of structural elements and infectivity of the HET-s prion","volume":"435","author":"Ritter","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1425","doi-asserted-by":"crossref","DOI":"10.3390\/ijms17091438","article-title":"PMEL amyloid fibril formation: the bright steps of pigmentation","volume":"17","author":"Bissig","year":"2016","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1430","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1083\/jcb.200302072","article-title":"Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis","volume":"161","author":"Berson","year":"2003","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1435","doi-asserted-by":"crossref","first-page":"2296","DOI":"10.1074\/jbc.M808904200","article-title":"Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for \u03b3-secretase","volume":"284","author":"Kummer","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1440","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1002286","article-title":"Mutations in or near the transmembrane domain alter PMEL amyloid formation from functional to pathogenic","volume":"7","author":"Watt","year":"2011","journal-title":"PLoS Genet."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1445","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1534\/genetics.104.027995","article-title":"The dominant white, dun and smoky color variants in chicken are associated with insertion\/deletion polymorphisms in the PMEL17 gene","volume":"168","author":"Kerje","year":"2004","journal-title":"Genetics"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1450","doi-asserted-by":"crossref","first-page":"9321","DOI":"10.1074\/jbc.M110.168088","article-title":"Proprotein convertases process Pmel17 during secretion","volume":"286","author":"Leonhardt","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1455","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1111\/pcmr.12067","article-title":"PMEL: a pigment cell-specific model for functional amyloid formation","volume":"26","author":"Watt","year":"2013","journal-title":"Pigment Cell Melanoma Res."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1460","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1111\/j.1600-0749.2005.00269.x","article-title":"The silver locus product Pmel17\/gp100\/Silv\/ME20: controversial in name and in function","volume":"18","author":"Theos","year":"2005","journal-title":"Pigment Cell Res."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1465","doi-asserted-by":"crossref","first-page":"964","DOI":"10.1091\/mbc.e12-10-0742","article-title":"Critical residues in the PMEL\/Pmel17 N-terminus direct the hierarchical assembly of melanosomal fibrils","volume":"24","author":"Leonhardt","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1470","doi-asserted-by":"crossref","first-page":"21198","DOI":"10.1074\/jbc.M601643200","article-title":"The repeat domain of the melanosomal matrix protein PMEL17\/GP100 is required for the formation of organellar fibers","volume":"281","author":"Hoashi","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1475","doi-asserted-by":"crossref","DOI":"10.1038\/srep44064","article-title":"Melanosomal formation of PMEL core amyloid is driven by aromatic residues","volume":"7","author":"Hee","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1480","series-title":"Structural Insights Into a Yeast Prion Illuminate Nucleation and Strain Diversity","author":"Krishnan","year":"2005"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1485","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005835","article-title":"The structural architecture of an infectious mammalian prion using electron cryomicroscopy","volume":"12","author":"V\u00e1zquez-Fern\u00e1ndez","year":"2016","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1490","doi-asserted-by":"crossref","first-page":"13731","DOI":"10.1073\/pnas.0906509106","article-title":"The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis","volume":"106","author":"McGlinchey","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1495","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1002285","article-title":"Inactivation of PMEL alters melanosome shape but has only a subtle effect on visible pigmentation","volume":"7","author":"Hellstr\u00f6m","year":"2011","journal-title":"PLoS Genet."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1500","first-page":"0100","article-title":"Functional amyloid formation within mammalian tissue","volume":"4","author":"Fowler","year":"2006","journal-title":"PLoS Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1505","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1111\/j.1432-1033.1996.t01-1-00180.x","article-title":"Polymerization of 5,6-dihydroxyindole-2-carboxylic acid to melanin by the pmel 17\/silver locus protein","volume":"236","author":"Chakraborty","year":"1996","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1510","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1111\/j.1755-148X.2009.00610.x","article-title":"Current challenges in understanding melanogenesis: bridging chemistry, biological control, morphology, and function","volume":"22","author":"Simon","year":"2009","journal-title":"Pigment Cell Melanoma Res."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1515","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1111\/j.1600-0854.2006.00425.x","article-title":"The quest for the mechanism of melanin transfer","volume":"7","author":"Van Den Bossche","year":"2006","journal-title":"Traffic"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1520","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1016\/S0092-8674(03)01021-3","article-title":"A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia","volume":"115","author":"Si","year":"2003","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1525","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1016\/S0092-8674(03)01020-1","article-title":"A neuronal isoform of the aplysia CPEB has prion-like properties","volume":"115","author":"Si","year":"2003","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1530","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1016\/j.neuron.2015.05.021","article-title":"The persistence of hippocampal-based memory requires protein synthesis mediated by the prion-like protein CPEB3","volume":"86","author":"Fioriti","year":"2015","journal-title":"Neuron"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1535","doi-asserted-by":"crossref","first-page":"1694","DOI":"10.1016\/j.celrep.2015.04.061","article-title":"SUMOylation is an inhibitory constraint that regulates the prion-like aggregation and activity of CPEB3","volume":"11","author":"Drisaldi","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1540","doi-asserted-by":"crossref","first-page":"2015","DOI":"10.1016\/j.jmb.2013.03.009","article-title":"The C-terminal region of cytoplasmic polyadenylation element binding protein is a ZZ domain with potential for protein-protein interactions","volume":"425","author":"Merkel","year":"2013","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1545","doi-asserted-by":"crossref","first-page":"17008","DOI":"10.1523\/JNEUROSCI.3043-13.2013","article-title":"Deletion of CPEB3 enhances hippocampus-dependent memory via increasing expressions of PSD95 and NMDA receptors","volume":"33","author":"Chao","year":"2013","journal-title":"J. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1550","doi-asserted-by":"crossref","first-page":"4865","DOI":"10.1038\/sj.emboj.7601322","article-title":"CPEB3 and CPEB4 in neurons: analysis of RNA-binding specificity and translational control of AMPA receptor GluR2 mRNA","volume":"25","author":"Huang","year":"2006","journal-title":"EMBO J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1555","doi-asserted-by":"crossref","first-page":"1772","DOI":"10.1016\/j.celrep.2015.04.060","article-title":"The CPEB3 protein is a functional prion that interacts with the actin cytoskeleton","volume":"11","author":"Stephan","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1560","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13041-016-0271-x","article-title":"ApCPEB4, a non-prion domain containing homolog of ApCPEB, is involved in the initiation of long-term facilitation","volume":"9","author":"Lee","year":"2016","journal-title":"Mol. Brain"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1565","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1002361","article-title":"Molecular basis of Orb2 amyloidogenesis and blockade of memory consolidation","volume":"14","author":"Herv\u00e1s","year":"2016","journal-title":"PLoS Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1570","doi-asserted-by":"crossref","DOI":"10.1186\/s12915-021-00967-9","article-title":"Divergent CPEB prion-like domains reveal different assembly mechanisms for a generic amyloid-like fold","volume":"19","author":"Herv\u00e1s","year":"2021","journal-title":"BMC Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1575","series-title":"Molecular Determinants of Liquid Demixing and Amyloidogenesis in Human CPEB3","author":"de Mingo","year":"2020"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1580","doi-asserted-by":"crossref","first-page":"1866","DOI":"10.1016\/j.celrep.2015.05.034","article-title":"MicroRNA-22 gates long-term heterosynaptic plasticity in aplysia through presynaptic regulation of CPEB and downstream targets","volume":"11","author":"Fiumara","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1585","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fnmol.2021.670513","article-title":"Structures of pathological and functional amyloids and prions, a solid-state NMR perspective","volume":"14","author":"Daskalov","year":"2021","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1590","doi-asserted-by":"crossref","first-page":"2624","DOI":"10.1128\/MCB.00073-14","article-title":"Functional amyloids in the mouse sperm acrosome","volume":"34","author":"Guyonnet","year":"2014","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1595","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/j.cell.2012.06.019","article-title":"The RIP1\/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis","volume":"150","author":"Li","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1600","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":"10.1016\/j.ijbiomac.2022.01.115_bb1605","doi-asserted-by":"crossref","first-page":"2079","DOI":"10.1126\/science.274.5295.2079","article-title":"Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity","volume":"274","author":"Telling","year":"1996","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1610","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1038\/375698a0","article-title":"Non-genetic propagation of strain-specific properties of scrapie prion protein","volume":"375","author":"Bessen","year":"1995","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1615","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1146\/annurev.biochem.72.121801.161837","article-title":"Emerging principles of conformation-based prion inheritance","volume":"73","author":"Chien","year":"2004","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1620","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1126\/science.1105850","article-title":"Self-propagating, molecular-level polymorphism in Alzheimer\u2019s \u03b2-amyloid fibrils","volume":"307","author":"Petkova","year":"2005","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1625","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1126\/science.1131864","article-title":"Exogenous induction of cerebral \u03b2-amyloidogenesis is governed bf agent and host","volume":"313","author":"Meyer-Luehmann","year":"2006","journal-title":"Science (80-.)"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1630","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1038\/s41594-018-0050-8","article-title":"Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation","volume":"25","author":"Luo","year":"2018","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1635","doi-asserted-by":"crossref","first-page":"4591","DOI":"10.1111\/j.1742-4658.2010.07888.x","article-title":"Amyloid structure - one but not the same: the many levels of fibrillar polymorphism","volume":"277","author":"Pedersen","year":"2010","journal-title":"FEBS J."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1640","series-title":"A Structural Analysis of Amyloid Polymorphism in Disease: Clues for Selective Vulnerability?","author":"Kant","year":"2021"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1645","series-title":"Functional Amyloids","author":"Otzen","year":"2019"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1650","doi-asserted-by":"crossref","first-page":"3595","DOI":"10.1074\/jbc.M115.692442","article-title":"The kringle-like domain facilitates post-endoplasmic reticulum changes to premelanosome protein (PMEL) oligomerization and disulfide bond configuration and promotes amyloid formation","volume":"291","author":"Ho","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1655","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1073\/pnas.0908714107","article-title":"Gatekeeper residues in the major curlin subunit modulate bacterial amyloid fiber biogenesis","volume":"107","author":"Wang","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1660","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/mBio.02279-18","article-title":"Physical determinants of amyloid assembly in biofilm formation","volume":"10","author":"Andreasen","year":"2019","journal-title":"MBio"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1665","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1016\/j.chembiol.2013.07.017","article-title":"Modulation of curli assembly and pellicle biofilm formation by chemical and protein chaperones","volume":"20","author":"Andersson","year":"2013","journal-title":"Chem. Biol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1670","doi-asserted-by":"crossref","DOI":"10.3390\/biom9110659","article-title":"Plant polyphenols inhibit functional amyloid and biofilm formation in pseudomonas strains by directing monomers to off-pathway oligomers","volume":"9","author":"Najarzadeh","year":"2019","journal-title":"Biomolecules"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1675","doi-asserted-by":"crossref","first-page":"1794","DOI":"10.1016\/j.ijbiomac.2020.08.080","article-title":"Date palm (Phoenix dactylifera L.) fruit\u2019s polyphenols as potential inhibitors for human amylin fibril formation and toxicity in type 2 diabetes","volume":"164","author":"Chaari","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1680","doi-asserted-by":"crossref","DOI":"10.1016\/j.neuint.2020.104806","article-title":"The effect of three polyphenols and some other antioxidant substances on amyloid fibril formation by human cystatin C","volume":"140","author":"Jahi\u0107","year":"2020","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1685","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.molliq.2019.04.059","article-title":"Gallic acid: a naturally occurring bifunctional inhibitor of amyloid and metal induced aggregation with possible implication in metal-based therapy","volume":"285","author":"Khan","year":"2019","journal-title":"J. Mol. Liq."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1690","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.tibs.2017.11.005","article-title":"Organization and function of non-dynamic biomolecular condensates","volume":"43","author":"Woodruff","year":"2018","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1695","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1080\/15384101.2018.1480220","article-title":"Reversible, functional amyloids: towards an understanding of their regulation in yeast and humans","volume":"17","author":"Cereghetti","year":"2018","journal-title":"Cell Cycle"},{"key":"10.1016\/j.ijbiomac.2022.01.115_bb1700","doi-asserted-by":"crossref","first-page":"4857","DOI":"10.1016\/j.cell.2021.08.013","article-title":"Ll the expanding amyloid family : structure, stability, function, and pathogenesis","volume":"184","author":"Sawaya","year":"2021","journal-title":"Cell"}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813022001301?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813022001301?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T09:24:16Z","timestamp":1758878656000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813022001301"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,3]]},"references-count":340,"alternative-id":["S0141813022001301"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2022.01.115","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2022,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The amyloid state of proteins: A boon or bane?","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2022.01.115","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}