{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T14:34:30Z","timestamp":1790087670979,"version":"4.0.1"},"reference-count":96,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2017,8,1]],"date-time":"2017-08-01T00:00:00Z","timestamp":1501545600000},"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":["Journal of Structural Biology"],"published-print":{"date-parts":[[2017,8]]},"DOI":"10.1016\/j.jsb.2017.06.002","type":"journal-article","created":{"date-parts":[[2017,6,14]],"date-time":"2017-06-14T22:33:37Z","timestamp":1497479617000},"page":"140-152","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"title":["Tracking the amyloidogenic core of IAPP amyloid fibrils: Insights from micro-Raman spectroscopy"],"prefix":"10.1016","volume":"199","author":[{"given":"Nikolaos N.","family":"Louros","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paraskevi L.","family":"Tsiolaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fotis A.","family":"Baltoumas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Georgios D.","family":"Chryssikos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vassilis","family":"Gionis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stavros J.","family":"Hamodrakas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vassiliki A.","family":"Iconomidou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jsb.2017.06.002_b0005","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.jmb.2005.10.052","article-title":"Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP?","volume":"355","author":"Abedini","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2017.06.002_b0010","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1093\/protein\/gzp036","article-title":"A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides","volume":"22","author":"Abedini","year":"2009","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.jsb.2017.06.002_b0015","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/0021-9991(83)90014-1","article-title":"Rattle: a \u201cvelocity\u201d version of the shake algorithm for molecular dynamics calculations","volume":"52","author":"Andersen","year":"1983","journal-title":"J. Comput. Phys."},{"key":"10.1016\/j.jsb.2017.06.002_b0020","doi-asserted-by":"crossref","first-page":"34156","DOI":"10.1074\/jbc.M102883200","article-title":"Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation","volume":"276","author":"Azriel","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jsb.2017.06.002_b0025","doi-asserted-by":"crossref","first-page":"3943","DOI":"10.1016\/S0040-4039(00)99290-6","article-title":"Darstellung gesch\u00fctzter peptid-fragmente unter einsatz substituierter triphenylmethyl-harze","volume":"30","author":"Barlos","year":"1989","journal-title":"Tetrahedron Lett."},{"key":"10.1016\/j.jsb.2017.06.002_b0030","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1093\/protein\/gzs031","article-title":"Aggregation gatekeepers modulate protein homeostasis of aggregating sequences and affect bacterial fitness","volume":"25","author":"Beerten","year":"2012","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.jsb.2017.06.002_b0035","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/0014-5793(89)81467-X","article-title":"Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species","volume":"251","author":"Betsholtz","year":"1989","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jsb.2017.06.002_b0040","doi-asserted-by":"crossref","first-page":"2026","DOI":"10.1016\/j.bbamem.2007.07.001","article-title":"Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes","volume":"1768","author":"Brender","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jsb.2017.06.002_b0045","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 Am Chem Soc"},{"key":"10.1016\/j.jsb.2017.06.002_b0050","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1021\/ar200189b","article-title":"Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective","volume":"45","author":"Brender","year":"2012","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.jsb.2017.06.002_b0055","doi-asserted-by":"crossref","first-page":"8908","DOI":"10.1039\/c3cp44696d","article-title":"Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20\u201329) fragments","volume":"15","author":"Brender","year":"2013","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.jsb.2017.06.002_b0060","series-title":"Biochemical Applications of Raman and Resonance Raman Spectroscopies","author":"Carey","year":"1982"},{"key":"10.1016\/j.jsb.2017.06.002_b0065","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1111\/cbdd.12172","article-title":"Pinpointing proline substitution to be responsible for the loss of amyloidogenesis in IAPP","volume":"82","author":"Chakraborty","year":"2013","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.jsb.2017.06.002_b0070","doi-asserted-by":"crossref","first-page":"11141","DOI":"10.1021\/ja00103a033","article-title":"N-methylacetamide and its hydrogen-bonded water molecules are vibrationally coupled","volume":"116","author":"Chen","year":"1994","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jsb.2017.06.002_b0075","doi-asserted-by":"crossref","first-page":"092501","DOI":"10.1063\/1.4921073","article-title":"Fibrillar dimer formation of islet amyloid polypeptides","volume":"5","author":"Chiu","year":"2015","journal-title":"AIP Adv."},{"key":"10.1016\/j.jsb.2017.06.002_b0080","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1016\/j.bpj.2013.07.029","article-title":"Effect of proline mutations on the monomer conformations of amylin","volume":"105","author":"Chiu","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.jsb.2017.06.002_b0085","doi-asserted-by":"crossref","first-page":"1890","DOI":"10.1016\/j.bbapap.2015.08.005","article-title":"Scaffolded multimers of hIAPP(20\u201329) peptide fragments fibrillate faster and lead to different fibrils compared to the free hIAPP(20\u201329) peptide fragment","volume":"1854","author":"Christoffersen","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jsb.2017.06.002_b0090","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/S0140-6736(87)90825-7","article-title":"Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes","volume":"2","author":"Clark","year":"1987","journal-title":"Lancet"},{"key":"10.1016\/j.jsb.2017.06.002_b0095","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/1471-2105-8-65","article-title":"AGGRESCAN: a server for the prediction and evaluation of \u201chot spots\u201d of aggregation in polypeptides","volume":"8","author":"Conchillo-Sole","year":"2007","journal-title":"BMC Bioinf."},{"key":"10.1016\/j.jsb.2017.06.002_b0100","doi-asserted-by":"crossref","first-page":"8628","DOI":"10.1073\/pnas.84.23.8628","article-title":"Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients","volume":"84","author":"Cooper","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.jsb.2017.06.002_b0105","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1016\/j.bpj.2013.08.026","article-title":"Cyclic N-terminal loop of amylin forms non amyloid fibers","volume":"105","author":"Cope","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.jsb.2017.06.002_b0110","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bpc.2016.09.007","article-title":"Amyloidogenesis of the amylin analogue pramlintide","volume":"219","author":"da Silva","year":"2016","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.jsb.2017.06.002_b0115","first-page":"1808","article-title":"Sur les proprietes optiques de l'amyloide","volume":"97","author":"Divry","year":"1927","journal-title":"C. R. Soc. Biol."},{"key":"10.1016\/j.jsb.2017.06.002_b0120","doi-asserted-by":"crossref","first-page":"e47150","DOI":"10.1371\/journal.pone.0047150","article-title":"Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation","volume":"7","author":"Duan","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.jsb.2017.06.002_b0125","doi-asserted-by":"crossref","first-page":"7240","DOI":"10.1021\/ja1081537","article-title":"The amyloid formation mechanism in human IAPP: dimers have \u03b2-strand monomer\u2013monomer interfaces","volume":"133","author":"Dupuis","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jsb.2017.06.002_b0130","doi-asserted-by":"crossref","first-page":"4613","DOI":"10.1063\/1.470648","article-title":"Constant pressure molecular dynamics simulation: the Langevin piston method","volume":"103","author":"Feller","year":"1995","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.jsb.2017.06.002_b0135","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.jsb.2017.06.002_b0140","doi-asserted-by":"crossref","first-page":"7783","DOI":"10.1021\/bi100337p","article-title":"Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity","volume":"49","author":"Fox","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsb.2017.06.002_b0145","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1016\/S0022-2836(02)01377-3","article-title":"Full-length rat amylin forms fibrils following substitution of single residues from human amylin","volume":"326","author":"Green","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2017.06.002_b0150","doi-asserted-by":"crossref","first-page":"3366","DOI":"10.1021\/jp5111357","article-title":"Distinct helix propensities and membrane interactions of human and rat IAPP(1\u201319) monomers in anionic lipid bilayers","volume":"119","author":"Guo","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jsb.2017.06.002_b0155","doi-asserted-by":"crossref","first-page":"2135","DOI":"10.1002\/jcc.23354","article-title":"CHARMM36 all-atom additive protein force field: validation based on comparison to NMR data","volume":"34","author":"Huang","year":"2013","journal-title":"J. Comput. Chem."},{"issue":"33\u201338","key":"10.1016\/j.jsb.2017.06.002_b0160","first-page":"27","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."},{"key":"10.1016\/j.jsb.2017.06.002_b0165","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1006\/jsbi.2000.4307","article-title":"Secondary structure of chorion proteins of the teleostean fish Dentex dentex by ATR FT-IR and FT-Raman spectroscopy","volume":"132","author":"Iconomidou","year":"2000","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jsb.2017.06.002_b0170","doi-asserted-by":"crossref","first-page":"1010","DOI":"10.1007\/s13361-016-1347-7","article-title":"Human islet amyloid polypeptide N-terminus fragment self-assembly: effect of conserved disulfide bond on aggregation propensity","volume":"27","author":"Ilitchev","year":"2016","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"10.1016\/j.jsb.2017.06.002_b0175","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S0925-4439(01)00078-3","article-title":"Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology","volume":"1537","author":"Jaikaran","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jsb.2017.06.002_b0180","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1006\/jmbi.2001.4593","article-title":"Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis","volume":"308","author":"Jaikaran","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2017.06.002_b0185","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"10.1016\/j.jsb.2017.06.002_b0190","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.jmb.2005.02.029","article-title":"The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin","volume":"348","author":"Kajava","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2017.06.002_b0195","doi-asserted-by":"crossref","first-page":"W469","DOI":"10.1093\/nar\/gkp351","article-title":"NetCSSP: web application for predicting chameleon sequences and amyloid fibril formation","volume":"37","author":"Kim","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jsb.2017.06.002_b0200","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1110\/ps.041051205","article-title":"Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid","volume":"14","author":"Koo","year":"2005","journal-title":"Protein Sci."},{"key":"10.1016\/j.jsb.2017.06.002_b0205","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1093\/protein\/gzm076","article-title":"Amide inequivalence in the fibrillar assembly of islet amyloid polypeptide","volume":"21","author":"Koo","year":"2008","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.jsb.2017.06.002_b0210","doi-asserted-by":"crossref","first-page":"3146","DOI":"10.1021\/jp108870q","article-title":"Structure and thermodynamics of amylin dimer studied by Hamiltonian-temperature replica exchange molecular dynamics simulations","volume":"115","author":"Laghaei","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jsb.2017.06.002_b0215","series-title":"Evolving Methods for Macromolecular Crystallography","first-page":"41","article-title":"Processing diffraction data with mosflm","author":"Leslie","year":"2007"},{"key":"10.1016\/j.jsb.2017.06.002_b0220","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1021\/bi301525e","article-title":"Comparative molecular dynamics study of human islet amyloid polypeptide (IAPP) and rat IAPP oligomers","volume":"52","author":"Liang","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsb.2017.06.002_b0225","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1021\/bi301525e","article-title":"Comparative Molecular Dynamics Study of Human Islet Amyloid Polypeptide (IAPP) and Rat IAPP Oligomers","volume":"52","author":"Liang","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsb.2017.06.002_b0230","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.febslet.2013.10.049","article-title":"An N-terminal pro-atrial natriuretic peptide (NT-proANP) 'aggregation-prone' segment involved in isolated atrial amyloidosis","volume":"588","author":"Louros","year":"2014","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jsb.2017.06.002_b0235","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1016\/j.ijbiomac.2015.05.032","article-title":"Chameleon \u2018aggregation-prone\u2019 segments of apoA-I: a model of amyloid fibrils formed in apoA-I amyloidosis","volume":"79","author":"Louros","year":"2015","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.jsb.2017.06.002_b0240","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1002\/bip.22650","article-title":"Structural studies and cytotoxicity assays of \u201caggregation-prone\u201d IAPP(8\u201316) and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin","volume":"104","author":"Louros","year":"2015","journal-title":"Biopolymers"},{"key":"10.1016\/j.jsb.2017.06.002_b0245","doi-asserted-by":"crossref","first-page":"13505","DOI":"10.1021\/bi701427q","article-title":"Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR","volume":"46","author":"Luca","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsb.2017.06.002_b0250","first-page":"R1475","article-title":"The role of amylin in the control of energy homeostasi","volume":"298","author":"Lutz","year":"2010","journal-title":"Am. J. Physiol."},{"key":"10.1016\/j.jsb.2017.06.002_b0255","doi-asserted-by":"crossref","first-page":"14990","DOI":"10.1021\/ja802483d","article-title":"Structural insights into the polymorphism of amyloid-like fibrils formed by region 20\u201329 of amylin revealed by solid-state NMR and X-ray fiber diffraction","volume":"130","author":"Madine","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jsb.2017.06.002_b0260","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1016\/j.talanta.2015.11.012","article-title":"New insights into side effect of solvents on the aggregation of human islet amyloid polypeptide 11\u201320","volume":"148","author":"Mao","year":"2016","journal-title":"Talanta"},{"key":"10.1016\/j.jsb.2017.06.002_b0265","doi-asserted-by":"crossref","first-page":"3255","DOI":"10.1021\/bi0621967","article-title":"Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology","volume":"46","author":"Marek","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsb.2017.06.002_b0270","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1016\/S0022-2836(02)00887-2","article-title":"Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide","volume":"322","author":"Mazor","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2017.06.002_b0275","doi-asserted-by":"crossref","first-page":"9742","DOI":"10.1021\/ja00026a005","article-title":"Ab initio vibrational analysis of hydrogen-bonded trans- and cis-N-methylacetamide","volume":"113","author":"Mirkin","year":"1991","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jsb.2017.06.002_b0280","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1002\/jcc.540130805","article-title":"Settle: an analytical version of the SHAKE and RATTLE algorithm for rigid water models","volume":"13","author":"Miyamoto","year":"1992","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jsb.2017.06.002_b0285","doi-asserted-by":"crossref","first-page":"1811","DOI":"10.1021\/bi981658g","article-title":"Effects of sequential proline substitutions on amyloid formation by human amylin20-29","volume":"38","author":"Moriarty","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsb.2017.06.002_b0290","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/0022-2836(74)90174-0","article-title":"Letter: conformation of the cystine linkages in bovine alpha-lactalbumin as revealed by its Raman effect","volume":"89","author":"Nakanishi","year":"1974","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2017.06.002_b0295","doi-asserted-by":"crossref","first-page":"8252","DOI":"10.1021\/ja9010095","article-title":"Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy","volume":"131","author":"Nanga","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jsb.2017.06.002_b0300","doi-asserted-by":"crossref","first-page":"2337","DOI":"10.1016\/j.bbamem.2011.06.012","article-title":"Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment","volume":"1808","author":"Nanga","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jsb.2017.06.002_b0305","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.ymeth.2004.03.012","article-title":"Techniques to study amyloid fibril formation in vitro","volume":"34","author":"Nilsson","year":"2004","journal-title":"Methods"},{"key":"10.1016\/j.jsb.2017.06.002_b0310","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.bpc.2007.03.012","article-title":"Analysis of insulin amyloid fibrils by Raman spectroscopy","volume":"128","author":"Ortiz","year":"2007","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.jsb.2017.06.002_b0315","series-title":"Chrysalis promotions","author":"Oxford diffraction","year":"2009"},{"key":"10.1016\/j.jsb.2017.06.002_b0320","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1002\/psc.913","article-title":"Self-assembly of the octapeptide lanreotide and lanreotide-based derivatives: the role of the aromatic residues","volume":"14","author":"Pandit","year":"2008","journal-title":"J. Peptide Sci."},{"key":"10.1016\/j.jsb.2017.06.002_b0325","doi-asserted-by":"crossref","first-page":"1864","DOI":"10.1021\/jz5001775","article-title":"In search of aggregation pathways of IAPP and other amyloidogenic proteins: finding answers through NMR spectroscopy","volume":"5","author":"Patel","year":"2014","journal-title":"J. Phys. Chem. Lett."},{"key":"10.1016\/j.jsb.2017.06.002_b0330","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/jcc.20289","article-title":"Scalable molecular dynamics with NAMD","volume":"26","author":"Phillips","year":"2005","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jsb.2017.06.002_b0335","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1111\/j.1464-5491.2004.01319.x","article-title":"Amylin replacement with pramlintide as an adjunct to insulin therapy improves long-term glycaemic and weight control in Type 1 diabetes mellitus: a 1-year, randomized controlled trial","volume":"21","author":"Ratner","year":"2004","journal-title":"Diabetic Med."},{"key":"10.1016\/j.jsb.2017.06.002_b0340","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.jsb.2017.06.002_b0345","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1007\/BF00544254","article-title":"Selective differentiation between amyloid and connective tissue structures based on the collagen specific topo-optical staining reaction with congo red","volume":"354","author":"Romhanyi","year":"1971","journal-title":"Virchows Arch."},{"key":"10.1016\/j.jsb.2017.06.002_b0350","doi-asserted-by":"crossref","first-page":"2247","DOI":"10.1021\/bm049717v","article-title":"Study of protein conformation and orientation in silkworm and spider silk fibers using Raman microspectroscopy","volume":"5","author":"Rousseau","year":"2004","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.jsb.2017.06.002_b0355","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0021-9991(77)90098-5","article-title":"Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes","volume":"23","author":"Ryckaert","year":"1977","journal-title":"J. Comput. Phys."},{"key":"10.1016\/j.jsb.2017.06.002_b0360","doi-asserted-by":"crossref","first-page":"2101","DOI":"10.1016\/S0002-9440(10)64848-1","article-title":"S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin","volume":"157","author":"Sakagashira","year":"2000","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.jsb.2017.06.002_b0365","doi-asserted-by":"crossref","first-page":"28324","DOI":"10.1074\/jbc.M114.563981","article-title":"The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses","volume":"289","author":"Sant'Anna","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jsb.2017.06.002_b0370","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/j.bpj.2016.05.050","article-title":"The role of cholesterol in driving IAPP-membrane interactions","volume":"111","author":"Sciacca","year":"2016","journal-title":"Biophys. J."},{"key":"10.1016\/j.jsb.2017.06.002_b0375","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/S1047-8477(02)00630-5","article-title":"Identification of minimal peptide sequences in the (8\u201320) domain of human islet amyloid polypeptide involved in fibrillogenesis","volume":"141","author":"Scrocchi","year":"2003","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jsb.2017.06.002_b0380","doi-asserted-by":"crossref","first-page":"11312","DOI":"10.1021\/jacs.5b07535","article-title":"Structural organization of insulin fibrils based on polarized Raman spectroscopy: evaluation of existing models","volume":"137","author":"Sereda","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jsb.2017.06.002_b0385","doi-asserted-by":"crossref","first-page":"6614","DOI":"10.1073\/pnas.0805957106","article-title":"Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution","volume":"106","author":"Shim","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.jsb.2017.06.002_b0390","doi-asserted-by":"crossref","first-page":"4870","DOI":"10.1021\/bi00693a014","article-title":"Interpretation of the doublet at 850 and 830 cm-1 in the Raman spectra of tyrosyl residues in proteins and certain model compounds","volume":"14","author":"Siamwiza","year":"1975","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsb.2017.06.002_b0395","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1016\/0584-8539(75)80116-4","article-title":"Normal vibrations and molecular conformations of dialkyl disulfides","volume":"31","author":"Sugeta","year":"1975","journal-title":"Spectrochim. Acta, Part A"},{"key":"10.1016\/j.jsb.2017.06.002_b0400","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1246\/cl.1972.83","article-title":"S-S and C\u2013S stretching vibrations and molecular conformations of dialkyl disulfides and cystine","volume":"1","author":"Sugeta","year":"1972","journal-title":"Chem. Lett."},{"key":"10.1016\/j.jsb.2017.06.002_b0405","doi-asserted-by":"crossref","first-page":"3407","DOI":"10.1246\/bcsj.46.3407","article-title":"Vibrational spectra and molecular conformations of dialkyl disulfides","volume":"46","author":"Sugeta","year":"1973","journal-title":"Bull. Chem. Soc. Jpn."},{"issue":"Suppl. 1","key":"10.1016\/j.jsb.2017.06.002_b0410","doi-asserted-by":"crossref","first-page":"S45","DOI":"10.1186\/1471-2105-10-S1-S45","article-title":"Prediction of amyloid fibril-forming segments based on a support vector machine","volume":"10","author":"Tian","year":"2009","journal-title":"BMC Bioinf."},{"key":"10.1016\/j.jsb.2017.06.002_b0415","doi-asserted-by":"crossref","first-page":"e54175","DOI":"10.1371\/journal.pone.0054175","article-title":"A consensus method for the prediction of 'aggregation-prone' peptides in globular proteins","volume":"8","author":"Tsolis","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jsb.2017.06.002_b0420","doi-asserted-by":"crossref","first-page":"1520","DOI":"10.1016\/j.bpj.2013.12.052","article-title":"Mutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formation","volume":"106","author":"Tu","year":"2014","journal-title":"Biophys. J."},{"key":"10.1016\/j.jsb.2017.06.002_b0425","doi-asserted-by":"crossref","first-page":"1823","DOI":"10.1021\/j100557a016","article-title":"Raman spectra of strained disulfides. Effect of rotation about sulfur-sulfur bonds on sulfur-sulfur stretching frequencies","volume":"80","author":"Van Wart","year":"1976","journal-title":"J. Phys. Chem."},{"key":"10.1016\/j.jsb.2017.06.002_b0430","doi-asserted-by":"crossref","first-page":"2619","DOI":"10.1073\/pnas.70.9.2619","article-title":"Disulfide bond dihedral angles from Raman spectroscopy","volume":"70","author":"Van Wart","year":"1973","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jsb.2017.06.002_b0435","doi-asserted-by":"crossref","first-page":"4131","DOI":"10.1002\/smll.201500562","article-title":"Nanoscale heterogeneity of the molecular structure of individual hIAPP amyloid fibrils revealed with tip-enhanced Raman spectroscopy","volume":"11","author":"vandenAkker","year":"2015","journal-title":"Small"},{"key":"10.1016\/j.jsb.2017.06.002_b0440","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1002\/cjoc.201100413","article-title":"Structural effects of L16Q, S20G, and L16Q\u2013S20G mutations on hIAPP: a comparative molecular dynamics study","volume":"30","author":"Wang","year":"2012","journal-title":"Chin. J. Chem."},{"key":"10.1016\/j.jsb.2017.06.002_b0445","doi-asserted-by":"crossref","first-page":"6704","DOI":"10.1021\/acs.biochem.5b00567","article-title":"Analysis of the ability of pramlintide to inhibit amyloid formation by human islet amyloid polypeptide reveals a balance between optimal recognition and reduced amyloidogenicity","volume":"54","author":"Wang","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsb.2017.06.002_b0450","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1007\/BF01219652","article-title":"The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus","volume":"15","author":"Westermark","year":"1978","journal-title":"Diabetologia"},{"key":"10.1016\/j.jsb.2017.06.002_b0455","first-page":"414","article-title":"Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone","volume":"127","author":"Westermark","year":"1987","journal-title":"A. J. Pathol."},{"key":"10.1016\/j.jsb.2017.06.002_b0460","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1073\/pnas.84.11.3881","article-title":"Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells","volume":"84","author":"Westermark","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.jsb.2017.06.002_b0465","doi-asserted-by":"crossref","first-page":"5036","DOI":"10.1073\/pnas.87.13.5036","article-title":"Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.jsb.2017.06.002_b0470","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1110\/ps.062486907","article-title":"Direct detection of transient alpha-helical states in islet amyloid polypeptide","volume":"16","author":"Williamson","year":"2007","journal-title":"Protein Sci."},{"key":"10.1016\/j.jsb.2017.06.002_b0475","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1110\/ps.036509.108","article-title":"Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin)","volume":"17","author":"Wiltzius","year":"2008","journal-title":"Protein Sci."},{"key":"10.1016\/j.jsb.2017.06.002_b0480","doi-asserted-by":"crossref","first-page":"7308","DOI":"10.1021\/jp8106827","article-title":"Conformation preorganization: effects of S20G mutation on the structure of human islet amyloid polypeptide segment","volume":"113","author":"Xu","year":"2009","journal-title":"J. Phys. Chem. B"}],"container-title":["Journal of Structural Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1047847717300965?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1047847717300965?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,8,31]],"date-time":"2018-08-31T21:59:12Z","timestamp":1535752752000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1047847717300965"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,8]]},"references-count":96,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2017,8]]}},"alternative-id":["S1047847717300965"],"URL":"https:\/\/doi.org\/10.1016\/j.jsb.2017.06.002","relation":{},"ISSN":["1047-8477"],"issn-type":[{"value":"1047-8477","type":"print"}],"subject":[],"published":{"date-parts":[[2017,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Tracking the amyloidogenic core of IAPP amyloid fibrils: Insights from micro-Raman spectroscopy","name":"articletitle","label":"Article Title"},{"value":"Journal of Structural Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jsb.2017.06.002","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}