{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,22]],"date-time":"2026-01-22T01:20:53Z","timestamp":1769044853118,"version":"3.49.0"},"reference-count":73,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[1997,5,1]],"date-time":"1997-05-01T00:00:00Z","timestamp":862444800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":5921,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Structure"],"published-print":{"date-parts":[[1997,5]]},"DOI":"10.1016\/s0969-2126(97)00215-3","type":"journal-article","created":{"date-parts":[[2004,6,8]],"date-time":"2004-06-08T18:49:43Z","timestamp":1086720583000},"page":"595-600","source":"Crossref","is-referenced-by-count":183,"title":["Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases"],"prefix":"10.1016","volume":"5","author":[{"given":"Jeffery W","family":"Kelly","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S0969-2126(97)00215-3_BIB1","doi-asserted-by":"crossref","first-page":"6865","DOI":"10.1021\/bi00145a001","article-title":"In pursuit of the molecular structure of the amyloid plaque: new technology provides unexpected and critical information","volume":"31","author":"Lansbury","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB2","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1016\/S0969-2126(96)00104-9","article-title":"Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous \u03b2-sheet helix","volume":"4","author":"Blake","year":"1996","journal-title":"Structure"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB3","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1002\/anie.199500931","article-title":"Structural and thermodynamic basis for the formation of self-assembled peptide nanotubes","volume":"34","author":"Ghadiri","year":"1995","journal-title":"Angew. Chem. Int. Ed"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB4","doi-asserted-by":"crossref","first-page":"3127","DOI":"10.1073\/pnas.91.8.3127","article-title":"Domain swapping: entangling alliances between proteins","volume":"91","author":"Bennett","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB5","doi-asserted-by":"crossref","first-page":"2455","DOI":"10.1002\/pro.5560041202","article-title":"3D-domain swapping: a mechanism for oligomer assembly","volume":"4","author":"Bennett","year":"1995","journal-title":"Protein Sci"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB6","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/S0959-440X(96)80089-3","article-title":"Alternative conformations of amyloidogenic proteins govern their behavior","volume":"6","author":"Kelly","year":"1996","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB7","doi-asserted-by":"crossref","first-page":"186","DOI":"10.3109\/13506129409148451","article-title":"A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation","volume":"1","author":"Kelly","year":"1994","journal-title":"Amyloid\u2014Int. J. Exp. Clin. Invest"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB8","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/S0092-8674(00)80143-9","article-title":"For protein misassembly, its the \u201cI\u201d decade","volume":"86","author":"Wetzel","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB9","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1016\/0092-8674(93)90635-4","article-title":"Seeding \u201cone-dimensional crystallization\u201d of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?","volume":"73","author":"Jarrett","year":"1993","journal-title":"Cell"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB10","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1016\/S0968-0004(00)89100-8","article-title":"Defective protein folding as a cause of human disease","volume":"20","author":"Thomas","year":"1995","journal-title":"Trends Biochem. Sci"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB11","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/385787a0","article-title":"Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis","volume":"385","author":"Booth","year":"1997","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB12","doi-asserted-by":"crossref","first-page":"5446","DOI":"10.1073\/pnas.91.12.5446","article-title":"A role for destabilizing amino acid replacements in light chain amyloidosis","volume":"91","author":"Hurle","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB13","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/1074-5521(95)90074-8","article-title":"The chemistry of the scrapie infection: implications of the ICE 9 metaphor","volume":"2","author":"Lansbury","year":"1995","journal-title":"Chem. Biol"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB14","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\/S0969-2126(97)00215-3_BIB15","doi-asserted-by":"crossref","first-page":"3923","DOI":"10.1073\/pnas.92.9.3923","article-title":"Species specificity in the cell free conversion of prion protein to protease-resistant forms: a model for the scrapies species barrier","volume":"9","author":"Kocisko","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB16","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1006\/jmbi.1995.0395","article-title":"Conformational transitions on peptides containing two putative alpha-helices of the prion protein","volume":"250","author":"Zhang","year":"1995","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB17","doi-asserted-by":"crossref","first-page":"10962","DOI":"10.1073\/pnas.90.23.10962","article-title":"Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins","volume":"90","author":"Pan","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB18","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1126\/science.273.5275.622","article-title":"Support for the prion hypothesis for inheritance of a phenotypic trait in yeast","volume":"273","author":"Patino","year":"1996","journal-title":"Science"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB19","first-page":"376","article-title":"Mad cows meet mad yeast: the prion hypothesis","volume":"1","author":"Lindquist","year":"1996","journal-title":"Mol. Psychiatry"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB20","first-page":"in press","article-title":"Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis","author":"Lindquist","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB21","series-title":"Stability of Protein Pharmaceuticals: in vivo Pathways of Degradation and Strategies for Protein Stabilization","first-page":"43","article-title":"Protein aggregation in vivo: bacterial inclusion bodies and mammalian amyloid","author":"Wetzel","year":"1992"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB22","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/0167-7799(94)90082-5","article-title":"Mutations and off-pathway aggregation of proteins","volume":"12","author":"Wetzel","year":"1994","journal-title":"Trends in Biotech"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB23","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0065-3233(08)60287-9","article-title":"Sickle cell hemoglobin polymerization","volume":"40","author":"Eaton","year":"1990","journal-title":"Adv. Protein Chem"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB24","series-title":"Electron Microscopy of Proteins","first-page":"165","article-title":"Electron microscopy of amyloid","author":"Cohen","year":"1982"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB25","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1111\/j.1365-2559.1994.tb00001.x","article-title":"Amyloidosis","volume":"25","author":"Tan","year":"1994","journal-title":"Histopathology"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB26","series-title":"Applications of Enzyme Biotechnology","first-page":"99","article-title":"Transthyretin acid induced denaturation is required for amyloid fibril formation in vitro","author":"Colon","year":"1991"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB27","doi-asserted-by":"crossref","first-page":"8654","DOI":"10.1021\/bi00151a036","article-title":"Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro","volume":"31","author":"Colon","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB28","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1016\/0006-291X(91)91687-8","article-title":"Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro","volume":"175","author":"Gustavsson","year":"1991","journal-title":"Biochem. Biophys. Res. Comm"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB29","doi-asserted-by":"crossref","first-page":"6470","DOI":"10.1021\/bi952501g","article-title":"The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate which can self-assemble into amyloid","volume":"35","author":"Lai","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB30","first-page":"in press","article-title":"Characterization of the transthyretin acid denaturation pathway by analytical ultracentrifugation: implications for amyloid fibril formation","author":"Lai","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB31","first-page":"in press","article-title":"GdnHCl induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers","author":"Lai","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB32","series-title":"Protein Misassembly","article-title":"Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid: a new therapeutic strategy based on preventing the amyloidogenic conformational changes","author":"Colon","year":"1997"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB33","doi-asserted-by":"crossref","first-page":"13527","DOI":"10.1021\/bi00041a032","article-title":"Comparison of lethal and non-lethal transthyretin variants and their relationship to amyloid disease","volume":"34","author":"McCutchen","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB34","doi-asserted-by":"crossref","first-page":"12119","DOI":"10.1021\/bi00096a024","article-title":"Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity","volume":"32","author":"McCutchen","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB35","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1073\/pnas.93.3.1125","article-title":"On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantification of rate constants","volume":"93","author":"Lomakin","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB36","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.1016\/S0006-3495(94)80591-0","article-title":"Amyloid-beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths","volume":"67","author":"Snyder","year":"1994","journal-title":"Biophys. J"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB37","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1016\/S0006-3495(95)79940-4","article-title":"Solvent effects on self-assembly of beta-peptide","volume":"69","author":"Shen","year":"1995","journal-title":"Biophys. J"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB38","doi-asserted-by":"crossref","first-page":"1238","DOI":"10.1016\/S0006-3495(94)80593-4","article-title":"Effect of acid predissolution on fibril size and fibril flexibility of synthetic beta-amyloid peptide","volume":"67","author":"Shen","year":"1995","journal-title":"Biophys. J"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB39","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S1074-5521(97)90255-6","article-title":"Observation of metastable A-beta amyloid protofibrils by atomic force microscopy","volume":"4","author":"Harper","year":"1997","journal-title":"Chem. Biol"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB40","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1007\/BF01887400","article-title":"The nanometer-scale structure of amyloid-beta visualized by atomic force microscopy","volume":"15","author":"Stine","year":"1996","journal-title":"J. Prot. Chem"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB41","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/978-1-4684-5958-6_2","article-title":"Genetic aspects of amyloidosis","volume":"20","author":"Jacobson","year":"1991","journal-title":"Adv. Hum. Genet"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB42","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/0272-6386(95)90647-9","article-title":"Treatment of amyloidosis","volume":"26","author":"Tan","year":"1995","journal-title":"Am. J. Kidney Dis"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB43","series-title":"Immunological Diseases","first-page":"631","article-title":"Amyloidosis","author":"Pepys","year":"1988"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB44","series-title":"Amyloidosis in the Metabolic Basis of Inherited Disease","first-page":"2439","author":"Benson","year":"1989"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB45","first-page":"88","article-title":"Familial amyloidotic polyneuropathy","volume":"12","author":"Benson","year":"1989","journal-title":"Trends Biochem. Sci"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB46","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1146\/annurev.bi.61.070192.004503","article-title":"Amyloidosis","volume":"61","author":"Sipe","year":"1992","journal-title":"Ann. Rev. Biochem"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB47","doi-asserted-by":"crossref","first-page":"325","DOI":"10.3109\/10408369409084679","article-title":"Amyloidosis","volume":"31","author":"Sipe","year":"1994","journal-title":"Crit. Rev. Clin. Lab. Sci"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB48","first-page":"189","article-title":"Transthyretin (prealbumin) in familial amyloidotic polyneuropathy: genetic and functional aspects","volume":"48","author":"Saraiva","year":"1988","journal-title":"Adv. Neurol"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB49","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1016\/0006-291X(88)90188-X","article-title":"Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin","volume":"154","author":"Cornwell","year":"1988","journal-title":"Biochem. Biophys. Res. Comm"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB50","doi-asserted-by":"crossref","first-page":"2843","DOI":"10.1073\/pnas.87.7.2843","article-title":"Fibril in senile systemic amyloidosis is derived from normal transthyretin","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB51","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1172\/JCI111390","article-title":"Amyloid fibril protein in familial polyneuropathy, portuguese type: definition of molecular abnormality in transthyretin (prealbumin)","volume":"74","author":"Saravia","year":"1984","journal-title":"J. Clin Inv"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB52","first-page":"161","article-title":"Human transthyretin (prealbumin) gene and molecular genetics of familial amyloid polyneuropathy","volume":"6","author":"Sakaki","year":"1989","journal-title":"Mol. Biol. Med"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB53","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1002\/humu.1380050302","article-title":"Transthyretin Mutations in Health and Disease","volume":"5","author":"Saraiva","year":"1995","journal-title":"Human Mutation"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB54","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1146\/annurev.bi.62.070193.001035","article-title":"Structural and genetic analysis of protein stability","volume":"62","author":"Matthews","year":"1993","journal-title":"Ann. Rev. Biochem"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB55","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0022-2836(74)90291-5","article-title":"Structure of human plasma prealbumin at 2.5 angstrom resolution","volume":"88","author":"Blake","year":"1974","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB56","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/0022-2836(78)90368-6","article-title":"Structure of prealbumin: secondary, tertiary and quaternary interactions determined by fourier refinement at 1.8 Angstroms","volume":"121","author":"Blake","year":"1978","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB57","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1002\/j.1460-2075.1993.tb05707.x","article-title":"Crystral structure of recombinant Met30 transthyretin suggests a molecular basis for amyloidogenesis in familiar amyloidotic polyneuropathy (FAP)","volume":"12","author":"Terry","year":"1993","journal-title":"EMBO J"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB58","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/0925-4439(92)90075-X","article-title":"Alteration in molecular structure which results in disease: the Met-30 variant of human plasma transthyretin","volume":"1139","author":"Hamilton","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB59","doi-asserted-by":"crossref","first-page":"966","DOI":"10.1107\/S0907444996003307","article-title":"Structure of the Val122lle variant transthyretin-A cardiomyopathic mutant","volume":"52","author":"Damas","year":"1996","journal-title":"Acta Cryst. D"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB60","doi-asserted-by":"crossref","first-page":"2425","DOI":"10.1016\/S0021-9258(18)53793-5","article-title":"X-ray crystal structure of the Ala-109-Thr variant of human transthyretin which produces euthyroid hyperthyroxinemia","volume":"268","author":"Steinrauf","year":"1993","journal-title":"J. Biol. Chem"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB61","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1126\/science.8100365","article-title":"To fold or not to fold (the box model)","volume":"260","author":"Agard","year":"1993","journal-title":"Science"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB62","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1038\/nbt0486-297","article-title":"Genetic analysis of protein folding pathways","volume":"4","author":"King","year":"1986","journal-title":"Bio\/Technology"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB63","series-title":"Cellular Organelles","first-page":"216","article-title":"Lysosomes","author":"Holtzman","year":"1989"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB64","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1021\/bi00058a003","article-title":"Structure and dynamics of the acid denatured molten globule state of \u03b1-lactalbumin: a two-dimensional NMR study","volume":"32","author":"Alexandrescu","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB65","doi-asserted-by":"crossref","first-page":"1559","DOI":"10.1126\/science.1523410","article-title":"NMR determination of residual structure in a urea denatured protein, the 434 Trp-repressor","volume":"257","author":"Neri","year":"1992","journal-title":"Science"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB66","doi-asserted-by":"crossref","first-page":"1573","DOI":"10.1021\/bi00057a023","article-title":"Structural characterization of monellin in the alcohol denatured state by NMR: evidence for \u03b2-sheet to \u03b1-helix conversion","volume":"32","author":"Fan","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB67","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1006\/jmbi.1995.0604","article-title":"Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs","volume":"254","author":"Serpell","year":"1995","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB68","series-title":"The Nature and Origin Of Amyloid Fibrils","first-page":"6","article-title":"A molecular model of the amyloid fibril","author":"Blake","year":"1996"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB69","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1038\/382180a0","article-title":"NMR Structure of the mouse prion protein domain PRP (121\u2013231)","volume":"382","author":"Riek","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB70","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1038\/nsb1195-990","article-title":"Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel beta-sheet comprising a C-terminal peptide","volume":"2","author":"Lansbury","year":"1995","journal-title":"Nat. Struct. Biol"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB71","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/S0006-3495(93)81393-6","article-title":"Structure of beta-crystallites assemblies formed by the Alzheimer beta-amyloid protein analogs: analysis by X-ray diffraction","volume":"64","author":"Inouye","year":"1993","journal-title":"Biophys. J"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB72","doi-asserted-by":"crossref","first-page":"15051","DOI":"10.1073\/pnas.93.26.15051","article-title":"Inhibiting transthyretin amyloid fibril formation via protein stabilization","volume":"93","author":"Miroy","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(97)00215-3_BIB73","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1021\/jm00349a004","article-title":"Computer graphics in drug design: molecular modeling of thyroid hormone-prealbumin interactions","volume":"25","author":"Blaney","year":"1982","journal-title":"J. Med. Chem"}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212697002153?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212697002153?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,23]],"date-time":"2021-06-23T01:09:27Z","timestamp":1624410567000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212697002153"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,5]]},"references-count":73,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1997,5]]}},"alternative-id":["S0969212697002153"],"URL":"https:\/\/doi.org\/10.1016\/s0969-2126(97)00215-3","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[1997,5]]}}}