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Chem. Soc."},{"key":"10.1016\/j.bpj.2012.11.3811_bib72","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1074\/jbc.M109.024190","article-title":"Calcium-activated calpain-2 is a mediator of \u03b2 cell dysfunction and apoptosis in type 2 diabetes","volume":"285","author":"Huang","year":"2010","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2012.11.3811_bib73","doi-asserted-by":"crossref","first-page":"8973","DOI":"10.1021\/ja1007867","article-title":"Role of zinc in human islet amyloid polypeptide aggregation","volume":"132","author":"Brender","year":"2010","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2012.11.3811_bib74","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1085\/jgp.79.3.387","article-title":"Calcium-induced inactivation of alamethicin in asymmetric lipid bilayers","volume":"79","author":"Hall","year":"1982","journal-title":"J.\u00a0Gen. Physiol."},{"key":"10.1016\/j.bpj.2012.11.3811_bib75","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1007\/BF00262322","article-title":"Effects of calcium on the\u00a0gramicidin A single channel in phosphatidylserine membranes. Screening and blocking","volume":"14","author":"Gambale","year":"1987","journal-title":"Eur. Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2012.11.3811_bib76","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1016\/j.jmb.2011.04.045","article-title":"Membrane integrity and amyloid cytotoxicity: a model study involving mitochondria and lysozyme fibrillation products","volume":"409","author":"Meratan","year":"2011","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.bpj.2012.11.3811_bib77","doi-asserted-by":"crossref","first-page":"14369","DOI":"10.1021\/bi701275p","article-title":"Helical \u03b1-synuclein forms highly conductive ion channels","volume":"46","author":"Zakharov","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2012.11.3811_bib78","doi-asserted-by":"crossref","first-page":"10427","DOI":"10.1073\/pnas.0502066102","article-title":"Amyloid ion channels: a common structural link for protein-misfolding disease","volume":"102","author":"Quist","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2012.11.3811_bib79","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1007\/978-1-4419-6327-7_13","article-title":"Amyloid peptide pores and the \u03b2 sheet conformation","volume":"677","author":"Kagan","year":"2010","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.bpj.2012.11.3811_bib80","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.bpj.2012.11.3811_bib81","article-title":"Amyloid peptide channels are inhibited by Congo Red and blocked by zinc","volume":"76","author":"Hirakura","year":"1999","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2012.11.3811_bib82","doi-asserted-by":"crossref","first-page":"1529","DOI":"10.1016\/j.bbamem.2006.07.001","article-title":"Detergent-like actions of linear amphipathic cationic antimicrobial peptides","volume":"1758","author":"Bechinger","year":"2006","journal-title":"Biochim. Biophys. 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