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A."},{"key":"ref41","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1002\/(SICI)1521-1878(199802)20:2<156::AID-BIES8>3.0.CO;2-R","article-title":"Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding proteins","volume":"20","author":"RE Hileman","year":"1998","journal-title":"Bioessays"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"8800","DOI":"10.1021\/bi401398k","article-title":"Characterization of amyloid formation by glucagon-like peptides: role of basic residues in heparin-mediated aggregation","volume":"52","author":"NN Jha","year":"2013","journal-title":"Biochemistry"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/S0076-6879(99)09020-5","article-title":"Quantification of \u03b2-sheet amyloid fibril structures with thioflavin T","volume":"309","author":"H LeVine 3rd","year":"1999","journal-title":"Methods Enzymol"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/S0076-6879(99)09021-7","article-title":"Quantifying amyloid by congo red spectral shift assay","volume":"309","author":"WE Klunk","year":"1999","journal-title":"Methods Enzymol"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"3775","DOI":"10.1021\/la404739f","article-title":"Complexation of amyloid fibrils with charged conjugated polymers","volume":"30","author":"D Ghosh","year":"2014","journal-title":"Langmuir"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"16884","DOI":"10.1074\/jbc.M114.548354","article-title":"Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretion","volume":"289","author":"A Anoop","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref47","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1007\/s12013-012-9364-z","article-title":"Amyloid-like fibril formation by tachykinin neuropeptides and its relevance to amyloid \u03b2-protein aggregation and toxicity","volume":"64","author":"PK Singh","year":"2012","journal-title":"Cell Biochem. Biophys."},{"key":"ref48","doi-asserted-by":"crossref","first-page":"2586","DOI":"10.1021\/bi802127h","article-title":"Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation","volume":"48","author":"G Klocek","year":"2009","journal-title":"Biochemistry"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1021\/cb1001203","article-title":"ANS binding reveals common features of cytotoxic amyloid species","volume":"5","author":"B Bolognesi","year":"2010","journal-title":"ACS Chem. Biol."},{"key":"ref50","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":"S Campioni","year":"2010","journal-title":"Nat. Chem. Biol."},{"key":"ref51","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/0003-2697(87)90157-6","article-title":"Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces","volume":"167","author":"DL Sackett","year":"1987","journal-title":"Anal. Biochem."},{"key":"ref52","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/0003-2697(91)90084-7","article-title":"Use of nile red as a fluorescent probe for the study of the hydrophobic properties of protein-sodium dodecyl sulfate complexes in solution","volume":"199","author":"JR Daban","year":"1991","journal-title":"Anal. 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