{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T22:26:37Z","timestamp":1781130397805,"version":"3.54.1"},"reference-count":82,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2017,2,1]],"date-time":"2017-02-01T00:00:00Z","timestamp":1485907200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"published-print":{"date-parts":[[2017,2]]},"DOI":"10.1016\/j.bbapap.2016.11.006","type":"journal-article","created":{"date-parts":[[2016,11,17]],"date-time":"2016-11-17T08:00:14Z","timestamp":1479369614000},"page":"176-185","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":26,"title":["Insights into amyloid-like aggregation of H2 region of the C-terminal domain of nucleophosmin"],"prefix":"10.1016","volume":"1865","author":[{"given":"Anna","family":"Russo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlo","family":"Diaferia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara","family":"La Manna","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cinzia","family":"Giannini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Teresa","family":"Sibillano","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonella","family":"Accardo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giancarlo","family":"Morelli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ettore","family":"Novellino","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6618-2949","authenticated-orcid":false,"given":"Daniela","family":"Marasco","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2016.11.006_bb0005","doi-asserted-by":"crossref","first-page":"2595","DOI":"10.1016\/j.bpj.2012.03.057","article-title":"Characterizing intermolecular interactions that initiate native-like protein aggregation","volume":"102","author":"Bemporad","year":"2012","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0010","doi-asserted-by":"crossref","first-page":"4431","DOI":"10.1021\/acs.biochem.5b00605","article-title":"Molecular mechanism of the misfolding and oligomerization of the prion protein: current understanding and its implications","volume":"54","author":"Singh","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0015","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0020","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1021\/ar050067x","article-title":"Sequence and structural determinants of amyloid fibril formation","volume":"39","author":"Bemporad","year":"2006","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0025","doi-asserted-by":"crossref","first-page":"1033","DOI":"10.1006\/jmbi.2000.3908","article-title":"The protofilament substructure of amyloid fibrils","volume":"300","author":"Serpell","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0030","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/j.bbapap.2016.01.011","article-title":"Structural remodeling during amyloidogenesis of physiological N(alpha)-acetylated alpha-synuclein","volume":"1864","author":"Gallea","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0035","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1080\/07391102.2015.1052849","article-title":"Molecular dynamics studies on the buffalo prion protein","volume":"34","author":"Zhang","year":"2016","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0040","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"Dobson","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0045","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.bbapap.2016.11.006_bb0050","doi-asserted-by":"crossref","first-page":"5971","DOI":"10.1111\/j.1742-4658.2005.05022.x","article-title":"Mechanisms of amyloid fibril self-assembly and inhibition. Model short peptides as a key research tool","volume":"272","author":"Gazit","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0055","doi-asserted-by":"crossref","first-page":"14689","DOI":"10.1074\/jbc.M109.082156","article-title":"Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates","volume":"285","author":"Pagano","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0060","doi-asserted-by":"crossref","first-page":"5699","DOI":"10.1074\/jbc.M310605200","article-title":"Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy","volume":"279","author":"Olofsson","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0065","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/nsb935","article-title":"Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS","volume":"10","author":"Elam","year":"2003","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0070","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1016\/j.str.2006.03.014","article-title":"Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus","volume":"14","author":"Plakoutsi","year":"2006","journal-title":"Structure"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0075","doi-asserted-by":"crossref","first-page":"26430","DOI":"10.1074\/jbc.R115.653097","article-title":"Specific chaperones and regulatory domains in control of amyloid formation","volume":"290","author":"Landreh","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0080","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.bbapap.2016.11.006_bb0085","first-page":"1470","article-title":"Nucleolar phosphoproteins of normal rat liver and Novikoff hepatoma ascites cells","volume":"35","author":"Kang","year":"1975","journal-title":"Cancer Res."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0090","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1016\/S0014-5793(01)02939-8","article-title":"Function of nucleophosmin\/B23, a nucleolar acidic protein, as a histone chaperone","volume":"506","author":"Okuwaki","year":"2001","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0095","doi-asserted-by":"crossref","first-page":"519","DOI":"10.3324\/haematol.11007","article-title":"Translocations and mutations involving the nucleophosmin (NPM1) gene in lymphomas and leukemias","volume":"92","author":"Falini","year":"2007","journal-title":"Haematologica"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0100","doi-asserted-by":"crossref","first-page":"1731","DOI":"10.1038\/leu.2009.124","article-title":"Altered nucleophosmin transport in acute myeloid leukaemia with mutated NPM1: molecular basis and clinical implications","volume":"23","author":"Falini","year":"2009","journal-title":"Leukemia"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0105","doi-asserted-by":"crossref","first-page":"2149","DOI":"10.1016\/j.str.2004.09.017","article-title":"The structure and function of Xenopus NO38-core, a histone chaperone in the nucleolus","volume":"12","author":"Namboodiri","year":"2004","journal-title":"Structure"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0110","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1002\/prot.21504","article-title":"Crystal structure of human nucleophosmin-core reveals plasticity of the pentamer-pentamer interface","volume":"69","author":"Lee","year":"2007","journal-title":"Proteins"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0115","doi-asserted-by":"crossref","first-page":"4466","DOI":"10.1073\/pnas.1321007111","article-title":"Structural polymorphism in the N-terminal oligomerization domain of NPM1","volume":"111","author":"Mitrea","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0120","doi-asserted-by":"crossref","first-page":"7394","DOI":"10.3390\/ijms16047394","article-title":"Identification of inhibitors of biological interactions involving intrinsically disordered proteins","volume":"16","author":"Marasco","year":"2015","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0125","doi-asserted-by":"crossref","first-page":"21230","DOI":"10.1074\/jbc.M114.565010","article-title":"Synergic role of nucleophosmin three-helix bundle and a flanking unstructured tail in the interaction with G-quadruplex DNA","volume":"289","author":"Arcovito","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0130","doi-asserted-by":"crossref","first-page":"2050","DOI":"10.1016\/j.bbagen.2014.02.017","article-title":"G-quadruplex DNA recognition by nucleophosmin: new insights from protein dissection","volume":"1840","author":"Scognamiglio","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0135","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1186\/s12867-016-0073-9","article-title":"Nucleophosmin: from structure and function to disease development","volume":"17","author":"Box","year":"2016","journal-title":"BMC Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0140","doi-asserted-by":"crossref","first-page":"23326","DOI":"10.1074\/jbc.M801706200","article-title":"Structural consequences of nucleophosmin mutations in acute myeloid leukemia","volume":"283","author":"Grummitt","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0145","doi-asserted-by":"crossref","first-page":"2360","DOI":"10.1096\/fj.08-128306","article-title":"Folding mechanism of the C-terminal domain of nucleophosmin: residual structure in the denatured state and its pathophysiological significance","volume":"23","author":"Scaloni","year":"2009","journal-title":"FASEB J."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0150","doi-asserted-by":"crossref","first-page":"5447","DOI":"10.1073\/pnas.0910516107","article-title":"Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain","volume":"107","author":"Scaloni","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0155","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.bbrc.2013.04.038","article-title":"The folding pathway of a functionally competent C-terminal domain of nucleophosmin: protein stability and denatured state residual structure","volume":"435","author":"Chiarella","year":"2013","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0160","doi-asserted-by":"crossref","first-page":"2595","DOI":"10.1038\/onc.2010.646","article-title":"Nucleophosmin and its complex network: a possible therapeutic target in hematological diseases","volume":"30","author":"Colombo","year":"2011","journal-title":"Oncogene"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0165","doi-asserted-by":"crossref","first-page":"3096","DOI":"10.1182\/blood-2010-09-309674","article-title":"Targeting levels or oligomerization of nucleophosmin 1 induces differentiation and loss of survival of human AML cells with mutant NPM1","volume":"118","author":"Balusu","year":"2011","journal-title":"Blood"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0170","doi-asserted-by":"crossref","first-page":"1999","DOI":"10.1182\/blood-2006-03-007013","article-title":"Immunohistochemistry predicts nucleophosmin (NPM) mutations in acute myeloid leukemia","volume":"108","author":"Falini","year":"2006","journal-title":"Blood"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0175","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1056\/NEJMoa041974","article-title":"Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal karyotype","volume":"352","author":"Falini","year":"2005","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0180","doi-asserted-by":"crossref","first-page":"874","DOI":"10.1182\/blood-2006-07-012252","article-title":"Acute myeloid leukemia carrying cytoplasmic\/mutated nucleophosmin (NPMc+ AML): biologic and clinical features","volume":"109","author":"Falini","year":"2007","journal-title":"Blood"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0185","doi-asserted-by":"crossref","first-page":"4861","DOI":"10.1093\/nar\/gks162","article-title":"Function of homo- and hetero-oligomers of human nucleoplasmin\/nucleophosmin family proteins NPM1, NPM2 and NPM3 during sperm chromatin remodeling","volume":"40","author":"Okuwaki","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0190","doi-asserted-by":"crossref","first-page":"1909","DOI":"10.1056\/NEJMoa074306","article-title":"Mutations and treatment outcome in cytogenetically normal acute myeloid leukemia","volume":"358","author":"Schlenk","year":"2008","journal-title":"N. Engl. J. Med."},{"issue":"28","key":"10.1016\/j.bbapap.2016.11.006_bb0195","doi-asserted-by":"crossref","first-page":"44821","DOI":"10.18632\/oncotarget.8599","article-title":"Molecules that target nucleophosmin for cancer treatment: an update","volume":"7","author":"Di Matteo","year":"2016","journal-title":"Oncotarget"},{"issue":"5","key":"10.1016\/j.bbapap.2016.11.006_bb0200","doi-asserted-by":"crossref","first-page":"3228","DOI":"10.1093\/nar\/gkt001","article-title":"Nucleophosmin mutations alter its nucleolar localization by impairing G-quadruplex binding at ribosomal DNA","volume":"41","author":"Chiarella","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0205","doi-asserted-by":"crossref","first-page":"144","DOI":"10.7150\/ijbs.13382","article-title":"Nucleophosmin mutants promote adhesion, migration and invasion of human leukemia THP-1 cells through MMPs up-regulation via Ras\/ERK MAPK signaling","volume":"12","author":"Xian","year":"2016","journal-title":"Int. J. Biol. Sci."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0210","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M116.723015","article-title":"Regulation of neuronal survival by nucleophosmin 1 (NPM1) is dependent on its expression level, subcellular localization and oligomerization status","author":"Pfister","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0215","doi-asserted-by":"crossref","DOI":"10.1096\/fj.14-269522","article-title":"Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions","author":"Di Natale","year":"2015","journal-title":"FASEB J."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0220","doi-asserted-by":"crossref","DOI":"10.18632\/oncotarget.10991","article-title":"Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia","author":"Scognamiglio","year":"2016","journal-title":"Oncotarget"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0225","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1073\/pnas.1014796108","article-title":"Natural tri- to hexapeptides self-assemble in water to amyloid beta-type fiber aggregates by unexpected alpha-helical intermediate structures","volume":"108","author":"Hauser","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0230","doi-asserted-by":"crossref","first-page":"W301","DOI":"10.1093\/nar\/gku399","article-title":"PASTA 2.0: an improved server for protein aggregation prediction","volume":"42","author":"Walsh","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0235","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1038\/sj.emboj.7601953","article-title":"Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice","volume":"27","author":"Martins","year":"2008","journal-title":"EMBO J."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0240","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1096\/fj.01-0442hyp","article-title":"A possible role for pi-stacking in the self-assembly of amyloid fibrils","volume":"16","author":"Gazit","year":"2002","journal-title":"FASEB J."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0245","doi-asserted-by":"crossref","first-page":"5960","DOI":"10.1111\/j.1742-4658.2009.07307.x","article-title":"The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds","volume":"276","author":"Hudson","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0250","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1016\/j.jmb.2014.09.026","article-title":"The CamSol method of rational design of protein mutants with enhanced solubility","volume":"427","author":"Sormanni","year":"2015","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0255","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/j.jmb.2016.01.009","article-title":"Comparison of the aggregation of homologous beta2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation","volume":"428","author":"Pashley","year":"2016","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0260","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.1039\/b706784b","article-title":"The Zyggregator method for predicting protein aggregation propensities","volume":"37","author":"Tartaglia","year":"2008","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0265","doi-asserted-by":"crossref","first-page":"20075","DOI":"10.1073\/pnas.1320626110","article-title":"Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation","volume":"110","author":"Crick","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0270","doi-asserted-by":"crossref","first-page":"1984","DOI":"10.1021\/jz500794d","article-title":"How to get insight into amyloid structure and formation from infrared spectroscopy","volume":"5","author":"Moran","year":"2014","journal-title":"J. Phys. Chem. Lett."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0275","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/0003-2697(91)90155-M","article-title":"Protein secondary structure from Fourier transform infrared spectroscopy: a data base analysis","volume":"194","author":"Sarver","year":"1991","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0280","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1016\/0032-3861(85)90108-9","article-title":"The spherulitic and lamellar morphology of melt-crystallized isotactic polypropylene","volume":"26","author":"Norton","year":"1985","journal-title":"Polymer"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0285","doi-asserted-by":"crossref","first-page":"14420","DOI":"10.1073\/pnas.0405933101","article-title":"The formation of spherulites by amyloid fibrils of bovine insulin","volume":"101","author":"Krebs","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0290","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1016\/j.jinorgbio.2010.05.012","article-title":"Human pro-islet amyloid polypeptide (ProIAPP(1\u201348)) forms amyloid fibrils and amyloid spherulites in vitro","volume":"104","author":"Exley","year":"2010","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0295","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.bpc.2009.01.008","article-title":"Self assembly of a model amphiphilic phenylalanine peptide\/polyethylene glycol block copolymer in aqueous solution","volume":"141","author":"Castelletto","year":"2009","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0300","doi-asserted-by":"crossref","first-page":"4213","DOI":"10.1021\/bm301481v","article-title":"Self-assembly of ovalbumin into amyloid and non-amyloid fibrils","volume":"13","author":"Lara","year":"2012","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0305","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/S0925-4439(00)00029-6","article-title":"Alzheimer's amyloid fibrils: structure and assembly","volume":"1502","author":"Serpell","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0310","doi-asserted-by":"crossref","first-page":"7003","DOI":"10.1002\/adfm.201502458","article-title":"Peptide materials obtained by aggregation of polyphenylalanine conjugates as gadolinium-based magnetic resonance imaging contrast agents","volume":"25","author":"Diaferia","year":"2015","journal-title":"Adv. Funct. Mater."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0315","article-title":"Self-assembly of PEGylated tetra-phenylalanine derivatives: structural insights from solution and solid state studies","volume":"6","author":"M.F.A.","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0320","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0968-0004(99)01445-0","article-title":"Protein misfolding, evolution and disease","volume":"24","author":"Dobson","year":"1999","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0325","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.jmb.2004.06.088","article-title":"A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins","volume":"342","author":"Linding","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0330","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1038\/nbt1012","article-title":"Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins","volume":"22","author":"Fernandez-Escamilla","year":"2004","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0340","doi-asserted-by":"crossref","first-page":"9619","DOI":"10.1021\/ja021047i","article-title":"pH as a trigger of peptide beta-sheet self-assembly and reversible switching between nematic and isotropic phases","volume":"125","author":"Aggeli","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0345","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1021\/bm000080z","article-title":"Structure and dynamics of self-assembling beta-sheet peptide tapes by dynamic light scattering","volume":"2","author":"Aggeli","year":"2001","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0350","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1038\/81937","article-title":"A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils","volume":"7","author":"Fezoui","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0355","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1016\/j.jmb.2009.09.039","article-title":"The common architecture of cross-beta amyloid","volume":"395","author":"Jahn","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0360","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S0065-3233(08)60320-4","article-title":"The structure of amyloid fibrils by electron microscopy and X-ray diffraction","volume":"50","author":"Sunde","year":"1997","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0365","doi-asserted-by":"crossref","first-page":"13940","DOI":"10.1039\/c3cp52595c","article-title":"Determination of orientations of aromatic groups in self-assembled peptide fibrils by polarised Raman spectroscopy","volume":"15","author":"Rodriguez-Perez","year":"2013","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0370","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nature05695","article-title":"Atomic structures of amyloid cross-beta spines reveal varied steric zippers","volume":"447","author":"Sawaya","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0375","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.tibs.2014.04.001","article-title":"Prion-like aggregation of mutant p53 in cancer","volume":"39","author":"Silva","year":"2014","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0380","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a023614","article-title":"Aggregation and prion-like properties of misfolded tumor suppressors: is cancer a prion disease?","volume":"8","author":"Costa","year":"2016","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0385","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.ccell.2015.12.002","article-title":"A designed inhibitor of p53 aggregation rescues p53 tumor suppression in ovarian carcinomas","volume":"29","author":"Soragni","year":"2016","journal-title":"Cancer Cell"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0390","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1111\/j.1399-3011.1990.tb00939.x","article-title":"Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids","volume":"35","author":"Fields","year":"1990","journal-title":"Int. J. Pept. Protein Res."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0395","doi-asserted-by":"crossref","first-page":"1615","DOI":"10.1007\/s00726-012-1237-7","article-title":"Dakin-West reaction on 1-thyminyl acetic acid for the synthesis of 1,3-bis(1-thyminyl)-2-propanone, a heteroaromatic compound with nucleopeptide-binding properties","volume":"43","author":"Roviello","year":"2012","journal-title":"Amino Acids"},{"key":"10.1016\/j.bbapap.2016.11.006_bb0400","doi-asserted-by":"crossref","first-page":"14140","DOI":"10.1039\/C5RA25809J","article-title":"Solid phase synthesis and RNA-binding activity of an arginine-containing nucleopeptide","volume":"6","author":"Roviello","year":"2016","journal-title":"RSC Adv."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0405","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1006\/jmbi.1997.1348","article-title":"Common core structure of amyloid fibrils by synchrotron X-ray diffraction","volume":"273","author":"Sunde","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0410","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1107\/S0021889812025733","article-title":"X-ray microimaging laboratory (XMI-LAB)","volume":"45","author":"Altamura","year":"2012","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.bbapap.2016.11.006_bb0415","doi-asserted-by":"crossref","DOI":"10.1038\/srep06985","article-title":"An optimized table-top small-angle X-ray scattering set-up for the nanoscale structural analysis of soft matter","volume":"4","author":"Sibillano","year":"2014","journal-title":"Sci. Rep."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963916302333?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963916302333?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,8,20]],"date-time":"2023-08-20T23:24:21Z","timestamp":1692573861000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963916302333"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,2]]},"references-count":82,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2017,2]]}},"alternative-id":["S1570963916302333"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2016.11.006","relation":{},"ISSN":["1570-9639"],"issn-type":[{"value":"1570-9639","type":"print"}],"subject":[],"published":{"date-parts":[[2017,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Insights into amyloid-like aggregation of H2 region of the C-terminal domain of nucleophosmin","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbapap.2016.11.006","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}